1. (-)-(S)-Proline
2. (-)-2-Pyrrolidinecarboxylate
3. (-)-2-Pyrrolidinecarboxylic acid
4. (-)-Proline
5. (S)-(-)-Proline
6. (S)-(-)-Pyrrolidine-2-carboxylate
7. (S)-(-)-Pyrrolidine-2-carboxylic acid
8. (S)-2-Carboxypyrrolidine
9. (S)-2-Pyrralidinecarboxylate
10. (S)-2-Pyrralidinecarboxylic acid
11. (S)-2-Pyrrolidinecarboxylate
12. (S)-2-Pyrrolidinecarboxylic acid
13. (S)-Proline
14. 2-Pyrrolidinecarboxylate
15. 2-Pyrrolidinecarboxylic acid
16. Proline

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• Cytoplasm
• endoplasmic reticulum
• Extracellular
• lysosome
• mitochondria

• Blood
• Cerebrospinal Fluid
• Saliva
• Urine

• 104300 (Alzheimer's disease)

1. Deng C, Shang C, Hu Y, Zhang X: Rapid diagnosis of phenylketonuria and other aminoacidemias by quantitative analysis of amino acids in neonatal blood spots by gas chromatography-mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jul 25;775(1):115-20. [PubMed ]
2. Azizi M, Junot C, Ezan E, Menard J: Angiotensin I-converting enzyme and metabolism of the haematological peptide N-acetyl-seryl-aspartyl-lysyl-proline. Clin Exp Pharmacol Physiol. 2001 Dec;28(12):1066-9. [PubMed ]
3. Roesel RA, Blankenship PR, Mobley EB, Coryell ME: Increased excretion of histidyl-L-proline diketopiperazine by infants receiving Pregestimil and Nutramigen formulas. Clin Chem. 1986 May;32(5):865-7. [PubMed ]
4. Chambers ST, Kunin CM: Osmoprotective activity for Escherichia coli in mammalian renal inner medulla and urine. Correlation of glycine and proline betaines and sorbitol with response to osmotic loads. J Clin Invest. 1987 Nov;80(5):1255-60. [PubMed ]
5. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed ]
6. Azizi M, Ezan E, Reny JL, Wdzieczak-Bakala J, Gerineau V, Menard J: Renal and metabolic clearance of N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) during angiotensin-converting enzyme inhibition in humans. Hypertension. 1999 Mar;33(3):879-86. [PubMed ]
7. Hart W, van den Hamer CJ, van der Sluys Veer J: The use of hydroxy-DL-proline-2-(14)C in the investigation of hydroxyproline metabolism in normal subjects and in patients with renal insufficiency. Clin Nephrol. 1976 Sep;6(3):379-87. [PubMed ]
8. Kanwar YS, Krakower CA, Manaligod JR, Justice P, Wong PW: Biochemical, morphological and hybrid studies in hyperprolinemic mice. Biomedicine. 1975 May;22(3):209-16. [PubMed ]
9. Simila S: Hydroxyproline metabolism in type II hyperprolinaemia. Ann Clin Biochem. 1979 Jul;16(4):177-81. [PubMed ]
10. Lu SH, Ohshima H, Fu HM, Tian Y, Li FM, Blettner M, Wahrendorf J, Bartsch H: Urinary excretion of N-nitrosamino acids and nitrate by inhabitants of high- and low-risk areas for esophageal cancer in Northern China: endogenous formation of nitrosoproline and its inhibition by vitamin C. Cancer Res. 1986 Mar;46(3):1485-91. [PubMed ]
11. Hausmann D: [Post-traumatic imbalances of plasma amino acids--interference factors or defense mechanisms? A study of protein metabolism in severe craniocerebral trauma] Anasth Intensivther Notfallmed. 1988 Feb;23(1):14-21. [PubMed ]
12. Scriver CR, McInnes RR, Mohyuddin F: Role of epithelial architecture and intracellular metabolism in proline uptake and transtubular reclamation in PRO/re mouse kidney. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1431-5. [PubMed ]
13. Boden G, Rezvani I, Owen OE: Effects of glucagon on plasma amino acids. J Clin Invest. 1984 Mar;73(3):785-93. [PubMed ]
14. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed ]
15. Feldman JM, Plonk JW, Admiraal J, Sidbury, JB: Plasma amino acids in patients with the carcinoid syndrome. Cancer. 1976 Nov;38(5):2127-31. [PubMed ]
16. Humbertclaude V, Rivier F, Roubertie A, Echenne B, Bellet H, Vallat C, Morin D: Is hyperprolinemia type I actually a benign trait? Report of a case with severe neurologic involvement and vigabatrin intolerance. J Child Neurol. 2001 Aug;16(8):622-3. [PubMed ]
17. Wikipedia

1. Prolyl 4-hydroxylase subunit alpha-2 precursor
2. Pyrroline-5-carboxylate reductase 1
3. Prolyl 4-hydroxylase subunit alpha-1 precursor
4. Pyrroline-5-carboxylate reductase 2
5. Bifunctional aminoacyl-tRNA synthetase [Includes: Glutamyl-tRNA synthetase
6. Cytosol aminopeptidase
7. Proline oxidase, mitochondrial precursor
8. Pyrroline-5-carboxylate reductase-like variant
9. Sodium-dependent proline transporter
10. cDNA FLJ75752, highly similar to Homo sapiens pyrroline-5-carboxylate reductase family, member 2
11. Uncharacterized protein PRODH
12. Melastatin 1 splicing variant
13. Prolyl 3-hydroxylase 1 precursor
14. Prolyl 3-hydroxylase 2 precursor
15. Prolyl 3-hydroxylase 3 precursor
16. Prolyl 4-hydroxylase subunit alpha-3
17. Egl nine homolog 1
18. Egl nine homolog 2
19. Egl nine homolog 3
20. Putative HIF-prolyl hydroxylase PH-4
21. cDNA FLJ75964, highly similar to Homo sapiens prolyl-tRNA synthetase (mitochondrial)(putative) (PARS2), mRNA (Prolyl-tRNA synthetase (Mitochondrial)(Putative))
22. Probable proline racemase
23. Peptidyl-prolyl cis-trans isomerase, mitochondrial
24. Peptidyl-prolyl cis-trans isomerase A
25. Peptidyl-prolyl cis-trans isomerase B
26. Peptidyl-prolyl cis-trans isomerase G
27. Probable prolyl-tRNA synthetase, mitochondrial
28. Peptidyl-prolyl cis-trans isomerase H

1. 4-PH alpha-2
2. Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha-2 subunit

MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKS
WANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQR
QFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEG
DYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSH
ERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVK
LTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPK
LARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVAN
YGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKK
GTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD

• Arginine and Proline Metabolism (map00330 )

• procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2

• 2OG-FeII_Oxy (PF03171 )
• P4Ha_N (PF08336 )
• TPR_2 (PF07719 )

• 1-21

ATGAAACTCTGGGTGTCTGCATTGCTGATGGCCTGGTTTGGTGTCCTGAGCTGTGTGCAG
GCCGAATTCTTCACCTCTATTGGGCACATGACTGACCTGATTTATGCAGAGAAAGAGCTG
GTGCAGTCTCTGAAAGAGTACATCCTTGTGGAGGAAGCCAAGCTTTCCAAGATTAAGAGC
TGGGCCAACAAAATGGAAGCCTTGACTAGCAAGTCAGCTGCTGATGCTGAGGGCTACCTG
GCTCACCCTGTGAATGCCTACAAACTGGTGAAGCGGCTAAACACAGACTGGCCTGCGCTG
GAGGACCTTGTCCTGCAGGACTCAGCTGCAGGTTTTATCGCCAACCTCTCTGTGCAGCGG
CAGTTCTTCCCCACTGATGAGGACGAGATAGGAGCTGCCAAAGCCCTGATGAGACTTCAG
GACACATACAGGCTGGACCCAGGCACAATTTCCAGAGGGGAACTTCCAGGAACCAAGTAC
CAGGCAATGCTGAGTGTGGATGACTGCTTTGGGATGGGCCGCTCGGCCTACAATGAAGGG
GACTATTATCATACGGTGTTGTGGATGGAGCAGGTGCTAAAGCAGCTTGATGCCGGGGAG
GAGGCCACCACAACCAAGTCACAGGTGCTGGACTACCTCAGCTATGCTGTCTTCCAGTTG
GGTGATCTGCACCGTGCCCTGGAGCTCACCCGCCGCCTGCTCTCCCTTGACCCAAGCCAC
GAACGAGCTGGAGGGAATCTGCGGTACTTTGAGCAGTTATTGGAGGAAGAGAGAGAAAAA
ACGTTAACAAATCAGACAGAAGCTGAGCTAGCAACCCCAGAAGGCATCTATGAGAGGCCT
GTGGACTACCTGCCTGAGAGGGATGTTTACGAGAGCCTCTGTCGTGGGGAGGGTGTCAAA
CTGACACCCCGTAGACAGAAGAGGCTTTTCTGTAGGTACCACCATGGCAACAGGGCCCCA
CAGCTGCTCATTGCCCCCTTCAAAGAGGAGGACGAGTGGGACAGCCCGCACATCGTCAGG
TACTACGATGTCATGTCTGATGAGGAAATCGAGAGGATCAAGGAGATCGCAAAACCTAAA
CTTGCACGAGCCACCGTTCGTGATCCCAAGACAGGAGTCCTCACTGTCGCCAGCTACCGG
GTTTCCAAAAGCTCCTGGCTAGAGGAAGATGATGACCCTGTTGTGGCCCGAGTAAATCGT
CGGATGCAGCATATCACAGGGTTAACAGTAAAGACTGCAGAATTGTTACAGGTTGCAAAT
TATGGAGTGGGAGGACAGTATGAACCGCACTTCGACTTCTCTAGGAATGATGAGCGAGAT
ACTTTCAAGCATTTAGGGACGGGGAATCGTGTGGCTACTTTCTTAAACTACATGAGTGAT
GTAGAAGCTGGTGGTGCCACCGTCTTCCCTGATCTGGGGGCTGCAATTTGGCCTAAGAAG
GGTACAGCTGTGTTCTGGTACAACCTCTTGCGGAGCGGGGAAGGTGACTACCGAACAAGA
CATGCTGCCTGCCCTGTGCTTGTGGGCTGCAAGTGGGTCTCCAATAAGTGGTTCCATGAA
CGAGGACAGGAGTTCTTGAGACCTTGTGGATCAACAGAAGTTGACTGA

1. Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI: Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J Biol Chem. 1997 Jul 11;272(28):17342-8. [PubMed ]
2. Nokelainen M, Nissi R, Kukkola L, Helaakoski T, Myllyharju J: Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues. Eur J Biochem. 2001 Oct;268(20):5300-9. [PubMed ]
3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. P5CR 1
2. P5C reductase 1

MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDLATVSALRKMGVKLTPHNKETV
QHSDVLFLAVKPHIIPFILDEIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIRC
MTNTPVVVREGATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIH
ALHVLESGGFRSLLINAVEASCIRTRELQSMADQEQVSPAAIKKTILDKVKLDSPAGTAL
SPSGHTKLLPRSLAPAGKD

• Arginine and Proline Metabolism (map00330 )

• L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+

• F420_oxidored (PF03807 )

• 1-26

ATGAGCGTGGGCTTCATCGGCGCTGGCCAGCTGGCTTTTGCCCTGGCCAAGGGCTTCACA
GCAGCAGGCGTCTTGGCTGCCCACAAGATAATGGCTAGCTCCCCAGACATGGACCTGGCC
ACAGTTTCTGCTCTCAGGAAGATGGGGGTGAAGTTGACACCCCACAACAAGGAGACGGTG
CAGCACAGTGATGTGCTCTTCCTGGCTGTGAAGCCACACATCATCCCCTTCATCCTGGAT
GAAATAGGCGCCGACATTGAGGACAGACACATTGTGGTGTCCTGCGCGGCCGGCGTCACC
ATCAGCTCCATTGAGAAGAAGCTGTCAGCGTTTCGGCCAGCCCCCAGGGTCATCCGCTGC
ATGACCAACACTCCAGTCGTGGTGCGGGAGGGGGCCACCGTGTATGCCACAGGCACGCAC
GCCCAGGTGGAGGACGGGAGGCTCATGGAGCAGCTGCTGAGCACGGTGGGCTTCTGCACG
GAGGTGGAAGAGGACCTGATTGATGCCGTCACGGGGCTCAGTGGCAGCGGCCCCGCCTAC
GCATTCACAGCCCTGGATGCCCTGGCTGATGGGGGTGTGAAGATGGGACTTCCAAGGCGC
CTGGCAGTCCGCCTCGGGGCCCAGGCCCTCCTGGGGGCTGCCAAGATGCTGCTGCACTCA
GAACAGCACCCAGGCCAGCTCAAGGACAACGTCAGCTCTCCTGGTGGGGCCACCATCCAT
GCCTTGCATGTGCTGGAGAGTGGGGGCTTCCGCTCCCTGCTCATCAACGCTGTGGAGGCC
TCCTGCATCCGCACACGGGAGCTGCAGTCCATGGCTGACCAGGAGCAGGTGTCACCAGCC
GCCATCAAGAAGACCATCCTGGACAAGGTGAAGCTGGACTCCCCTGCAGGGACCGCTCTG
TCGCCTTCTGGCCACACCAAGCTGCTCCCCCGCAGCCTGGCCCCAGCGGGCAAGGATTGA

1. Dougherty KM, Brandriss MC, Valle D: Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae. J Biol Chem. 1992 Jan 15;267(2):871-5. [PubMed ]

1. 4-PH alpha-1
2. Procollagen-proline,2-oxoglutarate-4-dioxygenase alpha-1 subunit

MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE

• Arginine and Proline Metabolism (map00330 )

• procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2

• 2OG-FeII_Oxy (PF03171 )
• P4Ha_N (PF08336 )
• TPR_2 (PF07719 )

• 1-17

ATGATCTGGTATATATTAATTATAGGAATTCTGCTTCCCCAGTCTTTGGCTCATCCAGGC
TTTTTTACTTCAATTGGTCAGATGACTGATTTGATCCATACTGAGAAAGATCTGGTGACT
TCTCTGAAAGATTATATTAAGGCAGAAGAGGACAAGTTAGAACAAATAAAAAAATGGGCA
GAGAAGTTAGATCGGCTAACTAGTACAGCGACAAAAGATCCAGAAGGATTTGTTGGGCAT
CCAGTAAATGCATTCAAATTAATGAAACGTCTGAATACTGAGTGGAGTGAGTTGGAGAAT
CTGGTCCTTAAGGATATGTCAGATGGCTTTATCTCTAACCTAACCATTCAGAGACCAGTA
CTTTCTAATGATGAAGATCAGGTTGGGGCAGCCAAAGCTCTGTTACGTCTCCAGGATACC
TACAATTTGGATACAGATACCATCTCAAAGGGTAATCTTCCAGGAGTGAAACACAAATCT
TTTCTAACGGCTGAGGACTGCTTTGAGTTGGGCAAAGTGGCCTATACAGAAGCAGATTAT
TACCATACGGAACTGTGGATGGAACAAGCCCTAAGGCAACTGGATGAAGGCGAGATTTCT
ACCATAGATAAAGTCTCTGTTCTAGATTATTTGAGCTATGCGGTATATCAGCAGGGAGAC
CTGGATAAGGCACTTTTGCTCACAAAGAAGCTTCTTGAACTAGATCCTGAACATCAGAGA
GCTAATGGTAACTTAAAATATTTTGAGTATATAATGGCTAAAGAAAAAGATGTCAATAAG
TCTGCTTCAGATGACCAATCTGATCAGAAAACTACACCAAAGAAAAAAGGGGTTGCTGTG
GATTACCTGCCAGAGAGACAGAAGTACGAAATGCTGTGCCGTGGGGAGGGTATCAAAATG
ACCCCTCGGAGACAGAAAAAACTCTTTTGCCGCTACCATGATGGAAACCGTAATCCTAAA
TTTATTCTGGCTCCAGCTAAACAGGAGGATGAATGGGACAAGCCTCGTATTATTCGCTTC
CATGATATTATTTCTGATGCAGAAATTGAAATCGTCAAAGACCTAGCAAAACCAAGGCTG
AGCCGAGCTACAGTACATGACCCTGAGACTGGAAAATTGACCACAGCACAGTACAGAGTA
TCTAAGAGTGCCTGGCTCTCTGGCTATGAAAATCCTGTGGTGTCTCGAATTAATATGAGA
ATACAAGATCTAACAGGACTAGATGTTTCCACAGCAGAGGAATTACAGGTAGCAAATTAT
GGAGTTGGAGGACAGTATGAACCCCATTTTGACTTTGCACGGAAAGATGAGCCAGATGCT
TTCAAAGAGCTGGGGACAGGAAATAGAATTGCTACATGGCTGTTTTATATGAGTGATGTG
TCTGCAGGAGGAGCCACTGTTTTTCCTGAAGTTGGAGCTAGTGTTTGGCCCAAAAAAGGA
ACTGCTGTTTTCTGGTATAATCTGTTTGCCAGTGGAGAAGGAGATTATAGTACACGGCAT
GCAGCCTGTCCAGTGCTAGTTGGCAACAAATGGGTATCCAATAAATGGCTCCATGAACGT
GGACAAGAATTTCGAAGACCTTGTACGTTGTCAGAATTGGAATGA

1. Helaakoski T, Vuori K, Myllyla R, Kivirikko KI, Pihlajaniemi T: Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4392-6. [PubMed ]
2. Helaakoski T, Veijola J, Vuori K, Rehn M, Chow LT, Taillon-Miller P, Kivirikko KI, Pihlajaniemi T: Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues. J Biol Chem. 1994 Nov 11;269(45):27847-54. [PubMed ]

1. P5CR 2
2. P5C reductase 2

MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD

• Arginine and Proline Metabolism (map00330 )

• L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+

• F420_oxidored (PF03807 )

• 1-16

ATGAGCGTGGGCTTCATCGGGGCCGGCCAGCTGGCTAATGCTCTGGCGCGGGGCTTCACG
GCCGCAGCATTCCTGTCGGCTCACAAGATAATAGCCAGCTCCCCAGAAATGAACCTGCCC
ACGGTGTCCGCGCTCAGGAAGATGGGTGTGAACCTGACACGCAGCAACAAGGAGACGGTG
AAGCACAGCGACGTCCTGTTTCTGGCTGTGAAGCACATTATCATCCCCTTCATCCTGGAT
GAGATTGGGGCCGACGTGCAAGCCAGACACATCGTGGTCTCCTGTGCGGCTGGTGTCACC
ATCAGCTCTGTGGAGAAGAAGCTGATGGCATTCCAGCCAGCCCCCAAAGTGATTCGCTGC
ATGACCAACACACCTGTGGTAGTGCAGGAAGGCGCTACAGTGTACGCCACGGGCACCCAT
GCCCTGGTGGAGGATGGGCAGCTCCTGGAGCAGCTCATGAGCAGCGTGGGCTTCTGCACT
GAGGTGGAAGAGGACCTCATCGATGCCGTCACGGGGCTCAGTGGCAGCGGGCCTGCCTAT
GCATTCATGGCTCTGGACGCATTGGCTGATGGTGGGGTGAAGATGGGTTTGCCACGGCGC
CTGGCAATCCAACTCGGGGCCCAGGCTTTGCTGGGAGCTGCCAAGATGCTGCTGGACTCG
GAGCAGCATCCATGCCAGCTTAAGGACAATGTCTGCTCCCCTGGGGGAGCCACCATCCAC
GCCCTGCACTTTCTAGAGAGTGGGGGCTTCCGCTCTCTGCTCATCAATGCAGTTGAGGCC
TCCTGTATCCGAACACGAGAGCTACAGTCCATGGCCGACCAAGAAAAGATCTCCCCAGCT
GCCCTTAAGAAGACCCTCTTAGACAGAGTGAAGCTGGAATCCCCCACAGTCTCCACACTG
ACCCCCTCCAGCCCAGGGAAGCTCCTCACAAGAAGCCTGGCCCTGGGAGGCAAGAAGGAC
TAA

1. Glutamate--tRNA ligase
2. Prolyl-tRNA synthetase
3. Proline--tRNA ligase]

MEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNA
AWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPG
AEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVI
LEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHR
KNPIEKNLQMWEEMKKGSQFGHSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYN
VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTV
LSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKI
WAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFI
EGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKFNLENKDYKKTTKVTWLAE
TTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQL
QRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPF
KERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYK
EKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINE
AVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQG
EVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKS
EKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVI
TKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKT
HVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVR
WEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTE
KEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNS
WGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRR
RLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTV
AENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEID
CEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glutamate Metabolism (map00251 )
• Porphyrin Metabolism (map00860 )

• ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)

• HGTP_anticodon (PF03129 )
• ProRS-C_1 (PF09180 )
• tRNA-synt_1c (PF00749 )
• tRNA-synt_1c_C (PF03950 )
• tRNA-synt_2b (PF00587 )
• WHEP-TRS (PF00458 )

• None

• None

ATGGAACATACTGAGATTGATCACTGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGT
GATTCCTTTACTTCTACAATTAATGAACTCAATCATTGCCTGTCTCTGAGAACATACTTA
GTTGGAAACTCCTTGAGTTTAGCAGATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCT
GCCTGGCAAGAACAGTTGAAACAGAAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGC
TTTCTTGAAGCCCAGCAGGCCTTCCAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACC
AAAGCTCGAGTGGCACCTGAGAAAAAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGT
GCGGAGATGGGAAAGGTTACCGTCAGATTTCCTCCAGAGGCCAGTGGTTACTTACACATT
GGGCATGCAAAAGCTGCTCTTCTGAACCAGCACTACCAGGTTAACTTTAAAGGGAAACTG
ATCATGAGATTTGATGACACAAATCCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATC
TTGGAAGATGTTGCAATGTTGCATATCAAACCAGATCAATTTACTTATACTTCGGATCAT
TTTGAAACTATAATGAAGTATGCAGAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGAT
GATACTCCTGCTGAACAGATGAAAGCAGAACGTGAGCAGAGGATAGAATCTAAACATAGA
AAAAACCCTATTGAGAAGAATCTACAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTT
GGTCACTCCTGTTGTTTGCGAGCAAAAATTGACATGAGTAGTAACAATGGATGCATGAGA
GATCCAACCCTTTATCGCTGCAAAATTCAACCACATCCAAGAACTGGAAATAAATACAAT
GTTTATCCAACATATGATTTTGCCTGCCCCATAGTTGACAGCATCGAAGGTGTTACACAT
GCCCTGAGAACAACAGAATACCATGACAGAGATGAGCAGTTTTACTGGATTATTGAAGCT
TTAGGCATAAGAAAACCATATATTTGGGAATATAGTCGGCTAAATCTCAACAACACAGTG
CTATCCAAAAGAAAACTCACATGGTTTGTCAATGAAGGACTAGTAGATGGATGGGATGAC
CCAAGATTTCCTACGGTTCGTGGTGTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAA
CAGTTTATTGCTGCTCAGGGCTCCTCACGTTCAGTCGTGAACATGGAGTGGGACAAAATC
TGGGCGTTTAACAAAAAGGTTATTGACCCAGTGGCTCCACGATATGTTGCATTACTGAAG
AAAGAAGTGATCCCAGTGAATGTACCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAAA
CACCCAAAGAATCCTGAGGTTGGCTTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATT
GAAGGTGCTGATGCAGAGACTTTTTCGGAGGGTGAGATGGTTACATTTATAAATTGGGGC
AACCTCAACATTACAAAAATACACAAAAATGCAGATGGAAAAATCATATCTCTTGATGCA
AAGTTTAATTTGGAAAACAAAGACTACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAG
ACTACACATGCTCTTCCTATTCCAGTAATCTGTGTCACTTATGAGCACTTGATCACAAAG
CCAGTGCTAGGAAAAGACGAGGACTTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAA
GAGCTAATGCTAGGGGATCCCTGCCTTAAGGATTTGAAAAAAGGAGATATTATACAACTC
CAGAGAAGAGGATTCTTCATATGTGATCAACCTTATGAACCTGTTAGCCCATATAGTTGC
AAGGAAGCCCCGTGTGTTTTGATATACATTCCTGATGGGCACACAAAGGAAATGCCAACA
TCAGGGTCAAAGGAAAAGACCAAAGTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTT
AAGGAAAGACCAACACCTTCTCTGAATAATAATTGTACTACATCTGAGGATTCCTTGGTC
CTTTACAATAGAGTGGCTGTTCAAGGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCA
CCAAAGGAAGATGTAGATGCAGCTGTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAG
GAGAAAACTGGCCAGGAATATAAACCTGGAAACCCTCCTGCTGAAATAGGACAGAATATT
TCTTCTAATTCCTCAGCAAGTATTCTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCA
CAAGGGGAGGTGGTTCGTAAGCTAAAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAA
GCTGTAGAATGCTTACTGTCCCTGAAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTAC
ATACCTGGTCAGCCCCCATTATCTCAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAA
CCTGCTGGTTTAGAAACACCAGAAGCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGG
GAAGTAGTTCGGAAACTTAAAACTGAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTT
CAAGAACTCCTTCAGCTAAAGGCACAGTACAAGTCTTTGATAGGAGTAGAGTATAAGCCT
GTGTCGGCCACTGGAGCTGAGGACAAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCT
GAAAAGCAGAATAAGCCTCAGAAACAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAAC
CAAGGAGGTGGGCTCTCATCAAGTGGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACC
AGGTTGGGTCTTGAGGCAAAAAAAGAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATC
ACAAAGTCAGAAATGATTGAATACCATGACATAAGTGGCTGTTATATTCTTCGTCCCTGG
GCCTATGCCATTTGGGAAGCCATCAAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGT
GTTGAAAACTGCTACTTCCCCATGTTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACT
CATGTTGCTGACTTTGCCCCAGAGGTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTG
GCAGAACCAATTGCCATTCGTCCTACTAGTGAAACAGTAATGTATCCTGCATATGCAAAA
TGGGTACAATCACACAGAGACCTGCCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGT
TGGGAATTCAAGCATCCTCAGCCTTTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGG
CACAGTGCTTTTGCTACCATGGAAGAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTA
TATGCTCAGGTATATGAAGAACTCCTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAA
AAGGAAAAATTTGCAGGAGGAGACTATACAACTACAATAGAAGCATTTATATCTGCTAGT
GGAAGAGCTATCCAGGGAGGAACATCACATCATTTAGGGCAGAATTTTTCCAAAATGTTT
GAAATCGTTTTTGAAGATCCAAAGATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCC
TGGGGCCTGACAACTCGAACTATTGGTGTTATGACCATGGTTCATGGGGACAACATGGGT
TTAGTATTACCACCCCGTGTAGCATGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACC
AATGCACTTTCTGAAGAAGACAAAGAAGCGCTGATTGCAAAATGCAATGATTATCGAAGG
CGATTACTCAGTGTTAACATCCGCGTTAGAGCTGATTTACGAGATAATTATTCTCCAGGT
TGGAAATTCAATCACTGGGAGCTCAAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGT
GATATGAAGAGCTGTCAGTTTGTAGCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTT
GCTGAAAATGAGGCAGAGACTAAACTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTT
TTCACAAGGGCTTCTGAAGACCTTAAGACTCATATGGTTGTGGCTAATACAATGGAAGAC
TTTCAGAAGATACTAGATTCTGGAAAGATTGTTCAGATTCCATTCTGTGGGGAAATTGAC
TGTGAGGACTGGATCAAAAAGACCACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCA
TCCATGGGAGCTAAAAGCCTTTGCATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGA
GCCAAATGTGTCTGTGGCAAGAACCCTGCCAAGTACTACACCTTATTTGGTCGCAGCTAC
TGA

1. Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed ]
2. Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed ]
3. Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed ]
4. Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed ]
5. Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed ]

1. Leucine aminopeptidase
2. LAP
3. Leucyl aminopeptidase
4. Leucine aminopeptidase 3
5. Proline aminopeptidase
6. Prolyl aminopeptidase
7. Peptidase S

MFLLPLPAAGRVVVRRLAVRRFGSRSLSTADMTKGLVLGIYSKEKEDDVPQFTSAGENFD
KLLAGKLRETLNISGPPLKAGKTRTFYGLHQDFPSVVLVGLGKKAAGIDEQENWHEGKEN
IRAAVAAGCRQIQDLELSSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKMAVSAKLYGS
GDQEAWQKGVLFASGQNLARQLMETPANEMTPTRFAEIIEKNLKSASSKTEVHIRPKSWI
EEQAMGSFLSVAKGSDEPPVFLEIHYKGSPNANEPPLVFVGKGITFDSGGISIKASANMD
LMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRAKNGKTIQV
DNTDAEGRLILADALCYAHTFNPKVILNAATLTGAMDVALGSGATGVFTNSSWLWNKLFE
ASIETGDRVWRMPLFEHYTRQVVDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHL
DIAGVMTNKDEVPYLRKGMTGRPTRTLIEFLLRFSQDNA

• Arginine and Proline Metabolism (map00330 )

• Release of N-terminal proline from a peptide

• Peptidase_M17 (PF00883 )
• Peptidase_M17_N (PF02789 )

• 1-18

ATGTTCTTGCTGCCTCTTCCGGCTGCGGGGCGAGTAGTCGTCCGACGTCTGGCCGTAGTA
CGTTCTGGGAGCCGGAGTCTCTCCACCGCAGACATGACGAAGGGCCTTGTTTTAGGAATC
TATTCCAAAGAAAAAGAAGATGATGTGCCACAGTTCACAAGTGCAGGAGAGAATTTTGAT
AAATTGTTAGCTGGAAAGCTGAGAGAGACTTTGAACATATCTGGACCACCTCTGAAGGCA
GGGAAGACTCGAACCTTTTATGGTCTGCATCAGGACTTCCCCAGCGTGGTGCTAGTTGGC
CTCGGCAAAAAGGCAGCTGGAATCGACGAACAGGAAAACTGGCATGAAGGCAAAGAAAAC
ATCAGAGCTGCTGTTGCAGCGGGGTGCAGGCAGATTCAAGACCTGGAGCTCTCGTCTGTG
GAGGTGGATCCCTGTGGAGACGCTCAGGCTGCTGCGGAGGGAGCGGTGCTTGGTCTCTAT
GAATACGATGACCTAAAGCAAAAAAAGAAGATGGCTGTGTCGGCAAAGCTCTATGGAAGT
GGGGATCAGGAGGCCTGGCAGAAAGGAGTCCTGTTTGCTTCTGGGCAGAACTTGGCACGC
CAATTGATGGAGACGCCAGCCAATGAGATGACGCCAACCAGATTTGCCGAAATTATTGAG
AAGAATCTCAAAAGTGCTAGTAGTAAAACCGAGGTCCATATCAGACCCAAGTCTTGGATT
GAGGAACAGGCAATGGGATCATTCCTCAGTGTGGCCAAAGGATCTGACGAGCCCCCAGTC
TTCTTGGAAATTCACTACAAAGGCAGCCCCAATGCAAACGAACCACCCCTGGTGTTTGTT
GGGAAAGGAATTACCTTTGACAGTGGTGGTATCTCCATCAAGGCTTCTGCAAATATGGAC
CTCATGAGGGCTGACATGGGAGGAGCTGCAACTATATGCTCAGCCATCGTGTCTGCTGCA
AAGTTAAATTTGCCCATTAATATTATAGGTCTGGCCCCTCTTTGTGAAAATATGCCCAGC
GGCAAGGCCAACAAGCCGGGGGATGTTGTTAGAGCCAAAAACGGGAAGACCATCCAGGTT
GATAACACTGATGCTGAGGGGAGGCTCATACTGGCTGATGCGCTCTGTTACGCACACACG
TTTAACCCGAAGGTCATCCTCAATGCCGCCACCTTAACAGGTGCCATGGATGTAGCTTTG
GGATCAGGTGCCACTGGGGTCTTTACCAATTCATCCTGGCTCTGGAACAAACTCTTCGAG
GCCAGCATTGAAACAGGGGACCGTGTCTGGAGGATGCCTCTCTTCGAACATTATACAAGA
CAGGTTGTAGATTGCCAGCTTGCTGATGTTAACAACATTGGAAAATACAGATCTGCAGGA
GCATGTACAGCTGCAGCATTCCTGAAAGAATTCGTAACTCATCCTAAGTGGGCACATTTA
GACATAGCAGGCGTGATGACCAACAAAGATGAAGTTCCCTATCTACGGAAAGGCATGACT
GGGAGGCCCACAAGGACTCTCATTGAGTTCTTACTTCGTTTCAGTCAAGACAATGCTTAG

1. Matsushima M, Takahashi T, Ichinose M, Miki K, Kurokawa K, Takahashi K: Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1459-64. [PubMed ]

1. Proline dehydrogenase
2. Proline oxidase 2
3. P53-induced gene 6 protein

MLEFVMREWKKSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDY
GVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHRAFGDRRNGVISARTYFYAN
EAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVE
QGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSR
TKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQT
YFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRG
AYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVR
FALRRMEELGLHPADHQVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRR
ALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA

• Arginine and Proline Metabolism (map00330 )

• L-proline + acceptor + H2O = (S)-1-pyrroline-5-carboxylate + reduced acceptor

• Pro_dh (PF01619 )

• None

• None

ATGCTGGAATTTGTGATGAGAGAGTGGAAAAAATCCAGGAAACTTCTAGGACAGAGGCTA
TTCAACAAGCTCATGAAGATGACCTTCTATGGGCATTTTGTAGCCGGGGAGGACCAGGAG
TCCATCCAGCCCCTGCTTCGGCACTACAGGGCCTTCGGTGTCAGCGCCATCCTGGACTAT
GGAGTGGAGGAGGACCTGAGCCCCGAGGAGGCAGAGCACAAGGAGATGGAGTCCTGCTCC
TCGGCTGCGGAGAGGGATGGCAGTGGCACGAATAAGCGGGACAAGCAATACCAGGCCCAC
CGGGCTTTCGGGGACCGCAGGAATGGTGTCATCAGTGCCCGCACCTACTTCTACGCCAAT
GAGGCCAAGTGCGACAGCCACATGGAGACATTCTTGCGCTGCATCGAAGCCTCAGGTAGA
GTCAGCGATGACGGCTTCATAGCCATTAAGCTCACAGCACTGGGGAGACCCCAGTTTCTG
CTGCAGTTCTCAGAGGTGCTGGCCAAGTGGAGGTGCTTCTTTCACCAAATGGCTGTGGAG
CAAGGGCAGGCGGGCCTGGCTGCCATGGACACCAAGCTGGAGGTGGCGGTGCTGCAGGAA
AGTGTCGCAAAGTTGGGCATCGCATCCAGGGCTGAGATTGAGGACTGGTTCACGGCAGAG
ACCCTGGGAGTGTCTGGCACCATGGACCTGCTGGACTGGAGCAGCCTCATCGACAGCAGG
ACCAAGCTGTCCAAGCACCTGGTAGTCCCCAACGCACAGACAGGACAGCTGGAGCCCCTG
CTGTCCCGGTTCACTGAGGAGGAGGAGCTACAGATGACCAGGATGCTACAGCGGATGGAT
GTCCTGGCCAAGAAAGCCACAGAGATGGGCGTGCGGCTGATGGTGGATGCCGAGCAGACC
TACTTCCAGCCGGCCATCAGCCGCCTGACGCTGGAGATGCAGCGGAAGTTCAATGTGGAG
AAGCCGCTCATCTTCAACACATACCAGTGCTACCTCAAGGATGCCTATGACAATGTGACC
CTGGACGTGGAGCTGGCTCGCCGTGAGGGCTGGTGTTTTGGGGCCAAGCTGGTGCGGGGC
GCATACCTGGCCCAGGAGCGAGCCCGTGCGGCAGAGATCGGCTATGAGGACCCCATCAAC
CCCACGTACGAGGCCACCAACGCCATGTACCACAGGTGCCTGGACTACGTGTTGGAGGAG
CTGAAGCACAACGCCAAGGCCAAGGTGATGGTGGCCTCCCACAATGAGGACACAGTGCGC
TTCGCACTGCGCAGGATGGAGGAGCTGGGCCTGCATCCTGCTGACCACCAGGTGTACTTT
GGACAGCTGCTAGGCATGTGTGACCAGATCAGCTTCCCGCTGGGCCAGGCCGGCTACCCC
GTGTACAAGTACGTGCCCTATGGCCCCGTGATGGAGGTGCTGCCCTACTTGTCCCGCCGT
GCCCTGGAGAACAGCAGCCTCATGAAGGGCACCCATCGGGAGCGGCAGTTGCTGTGGCTG
GAGCTCTTGAGGCGGCTCCGAACTGGCAACCTCTTCCATCGCCCTGCCTAG

1. Campbell HD, Webb GC, Young IG: A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia. Hum Genet. 1997 Nov;101(1):69-74. [PubMed ]
2. Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M: The gene encoding proline dehydrogenase modulates sensorimotor gating in mice. Nat Genet. 1999 Apr;21(4):434-9. [PubMed ]
3. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed ]

MGGERSGVRGNKMAAAEPSPRRVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNL
CHFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGVSLS
TLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPEA
YVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPA
QLRSDVCTPGGTTIYGLHALALVWIQAPSFLPILSS

• F420_oxidored (PF03807 )

ATGGGCGGTGAGCGCAGCGGCGTCCGAGGCAACAAGATGGCAGCTGCGGAGCCGTCTCCG
CGGCGCGTGGGCTTCGTGGGCGCGGGCCGCATGGCGGGGGCCATCGCGCAGGGCCTCATC
AGAGCAGGAAAAGTGGAAGCTCAGCACATACTGGCCAGTGCACCAACAGACAGGAACCTA
TGTCACTTTCAAGCTCTGGGTTGCCGGACCACGCACTCCAACCAGGAGGTGCTGCAGAGC
TGCCTGCTCGTCATCTTTGCCACCAAGCCTCATGTGCTGCCAGCTGTCCTGGCAGAGGTG
GCTCCTGTGGTCACCACTGAACACATCTTGGTGTCCGTGGCTGCTGGGGTGTCTCTGAGC
ACCCTGGAGGAGCTGCTGCCCCCAAACACACGGGTGCTGCGGGTCTTGCCCAACCTGCCC
TGTGTGGTCCAGGAAGGGGCCATAGTGATGGCGCGGGGCCGCCACGTGGGGAGCAGCGAG
ACCAACCTCCTGCAGCATCTGCTGGAGGCCTGTGGGCGGTGTGAGGAGGTGCCTGAAGCC
TACGTCGACATCCACACTGGCCTCAGTGGCAGTGGCGTGGCCTTCGTGTGTGCATTCTCC
GAGGCCCTGGCTGAAGGAGCCGTCAAGATGGGCATGCCCAGCAGCCTGGCCCACCGCATC
GCTGCCCAGACCCTGCTGGGGACGGCCAAGATGCTGCTGCACGAGGGCCAACACCCAGCC
CAGCTGCGCTCAGACGTGTGCACCCCGGGTGGCACCACCATCTATGGACTCCACGCCCTG
GCTTTAGTCTGGATACAGGCTCCCTCTTTCCTCCCAATCCTAAGCTCCTGA

1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed ]
2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed ]

1. Solute carrier family 6 member 7

MKKLQGAHLRKPVTPDLLMTPSDQGDVDLDVDFAAHRGNWTGKLDFLLSCIGYCVGLGNV
WRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGA
AMLLIVGLVAIYYNMIIAYVLFYLFASLTSDLPWEHCGNWWNTELCLEHRVSKDGNGALP
LNLTCTVSPSEEYWSRYVLHIQGSQGIGSPGEIRWNLCLCLLLAWVIVFLCILKGVKSSG
KVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLG
VGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVA
KAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLR
PKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQ
RFCRDIHMMLGFKPGLYFRACWLFLSPATLLALLVYSIVKYQPSEYGSYRFPPWAELLGI
LMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQS
PKPLMVHMRKYGGITSFENTAIEVDREIAEEEESMM

• SNF (PF00209 )

• 1-238

• 46-66 74-93 117-137 215-233 242-259 295-312 324-345 378-397 425-443 459-479 500-519 538-556

1. Shafqat S, Velaz-Faircloth M, Henzi VA, Whitney KD, Yang-Feng TL, Seldin MF, Fremeau RT Jr: Human brain-specific L-proline transporter: molecular cloning, functional expression, and chromosomal localization of the gene in human and mouse genomes. Mol Pharmacol. 1995 Aug;48(2):219-29. [PubMed ]

1. PYCR2, mRNA
2. Pyrroline-5-carboxylate reductase family, member 2, isoform CRA_b

MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD

• None

• None

RHGSEARPARAAPLHSPLRPAVHGAGLPRAARSGPSGRARRWVGHGSAAAGARRGLRQRA
GGVPQPANLGAGAEPAGAALVRLARAAGAPRAAAVCFQETSRTEAIQQAHEDDLLWAFCS
RGGESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQ
YQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGR
PQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDW
FTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRML
QRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQPHPADAY
DNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDY
VLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHRVYFGQLLGMCDQISFPLGQ
AGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA

• Pro_dh (PF01619 )

• None

• None

1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

MYIRVSYDTKPDSLLHLMVKDWQLELPKLLISVHGGLQNFEMQPKLKQVFGKGLIKAAMT
TGAWIFTGGVSTGVISHVGDALKDHSSKSRGRVCAIGIAPWGIVENKEDLVGKDVTRVYQ
TMSNPLSKLSVLNNSHTHFILADNGTLGKYGAEVKLRRLLEKHISLQKINTRLGQGVPLV
GLVVEGGPNVVSIVLEYLQEEPPIPVVICDGSGRASDILSFAHKYCEEGG

• None

• None

1. Leucine- and proline- enriched proteoglycan 1
2. Leprecan-1
3. Growth suppressor 1

MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMER
ALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACL
RRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQ
QNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYE
ECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFL
PSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRE
SAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQE
IGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISD
HECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYN
VTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVC
VKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHG
VKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEP
AQESLSGSESKPKDEL

• procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218] ALL_REAC R03218

• 2OG-FeII_Oxy (PF03171 )

• 1-22

• None

ATGGCGGTACGCGCGTTGAAGCTGCTGACCACACTGCTGGCTGTCGTGGCCGCTGCCTCC
CAAGCCGAGGTCGAGTCCGAGGCAGGATGGGGCATGGTGACGCCTGATCTGCTCTTCGCC
GAGGGGACCGCAGCCTACGCGCGCGGGGACTGGCCCGGGGTGGTCCTGAGCATGGAACGG
GCGCTGCGCTCCCGGGCAGCCCTCCGCGCCCTTCGCCTGCGCTGCCGCACCCAGTGTGCC
GCCGACTTCCCGTGGGAGCTGGACCCCGACTGGTCCCCCAGCCCGGCCCAGGCCTCGGGC
GCCGGCGCCCTGCGCGACCTGAGCTTCTTCGGGGGCCTTCTGCGTCGCGCTGCCTGCCTG
CGCCGCTGCCTCGGGCCGCCGGCCGCCCACTCGCTCAGCGAAGAGATGGAGCTGGAGTTC
CGCAAGCGGAGCCCCTACAACTACCTGCAGGTCGCCTACTTCAAGATCAACAAGTTGGAG
AAAGCTGTTGCTGCAGCACACACCTTCTTCGTGGGCAATCCTGAGCACATGGAAATGCAG
CAGAACCTAGACTATTACCAAACCATGTCTGGAGTGAAGGAGGCCGACTTCAAGGATCTT
GAGACTCAACCCCATATGCAAGAATTTCGACTGGGAGTGCGACTCTACTCAGAGGAACAG
CCACAGGAAGCTGTGCCCCACCTAGAGGCGGCGCTGCAAGAATACTTTGTGGCCTATGAG
GAGTGCCGTGCCCTCTGCGAAGGGCCCTATGACTACGATGGCTACAACTACCTTGAGTAC
AACGCTGACCTCTTCCAGGCCATCACAGATCATTACATCCAGGTCCTCAACTGTAAGCAG
AACTGTGTCACGGAGCTTGCTTCCCACCCAAGTCGAGAGAAGCCCTTTGAAGACTTCCTC
CCATCGCATTATAATTATCTGCAGTTTGCCTACTATAACATTGGGAATTATACACAAGCT
GGTGAATGTGCCAAGACCTATCTTCTCTTCTTCCCCAATGACGAGGTGATGAACCAAAAT
TTGGCCTATTATGCAGCTATGCTTGGAGAAGAACACACCAGATCCATCGGCCCCCGTGAG
CAGGGCACCTAG

1. Kaul SC, Sugihara T, Yoshida A, Nomura H, Wadhwa R: Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan. Oncogene. 2000 Jul 27;19(32):3576-83. [PubMed ]

1. Leprecan-like protein 1
2. Myxoid liposarcoma-associated protein 4

MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDY
ERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCY
RSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPE
HMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREY
FVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSP
IENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPA
SIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGA
EVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELH
SVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARR
IVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAY
TFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKG
KRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL

• procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218] ALL_REAC R03218

• 2OG-FeII_Oxy (PF03171 )
• TPR_2 (PF07719 )

• 1-24

• None

ATGCGGGAGCGCATCTGGGCGCCGCCGCTGCTGCTGCTGCTGCCGCTGCTACTGCCGCCG
CCACTGTGGGGCGGCCCCCCGGACAGCCCACGCCGGGAGCTGGAGCTGGAGCCCGGGCCT
CTGCAGCCCTTCGACCTGCTCTACGCCAGCGGCGCGGCCGCCTACTACAGCGGAGACTAC
GAGCGAGCGGTGCGCGACTTGGAAGCGGCGCTGCGCAGCCACCGGCGCCTGCGGGAAATC
CGCACGCGCTGTGCCCGCCACTGCGCGGCGCGCCACCCGCTCCCGCCCCCGCCCCCCGGC
GAGGGCCCCGGCGCTGAGCTGCCCCTTTTCCGCTCCTTGTTGGGGCGGGCGCGCTGTTAT
CGCAGCTGTGAGACCCAGCGCCTCGGGGGCCCCGCATCCCGCCACCGCGTCAGCGAGGAT
GTGCGCAGCGACTTCCAGCGCAGAGTGCCCTACAACTACCTGCAGCGGGCCTACATCAAG
CTTAACCAGCTCGAAAAAGCAGTGGAAGCAGCTCACACATTTTTCGTGGCTAACCCTGAG
CACATGGAAATGCAGCAGAACATTGAGAATTACAGGGCGACAGCTGGTGTTGAAGCATTG
CAGTTGGTAGACAGAGAAGCCAAGCCACACATGGAGAGTTACAATGCAGGAGTTAAACAT
TATGAGGCTGATGACTTTGAGATGGCTATCAGGCATTTCGAACAAGCCTTAAGAGAATAT
TTCGTTGAAGATACAGAATGCCGGACCCTATGTGAGGGGCCTCAGAGATTTGAAGAATAT
GAGTATTTAGGGTATAAGGCTGGTCTGTATGAAGCTATTGCAGATCACTACATGCAGGTG
CTTGTTTGTCAGCATGAATGTGTGAGGGAACTTGCCACCCGCCCTGGCCGCCTCTCTCCC
ATCGAGAATTTTCTTCCTCTGCACTATGATTACCTACAGTTTGCCTACTATCGAGTTGGT
GAGTATGTGAAAGCCCTGGAGTGTGCCAAAGCCTATCTTCTATGCCATCCAGATGATGAG
GATGTCCTAGACAATGTGGATTACTATGAGAGTCTGCTGGATGATAGCATTGACCCGGCA
TCCATTGAGGCCAGAGAGGATTTAACAATGTTTGTGAAACGTCATAAGCTGGAGTCTGAG
CTGATAAAATCAGCTGCAGAAGGTCTGGGGTTTTCATACACTGAACCGAATTATTGGATC
AGATATGGAGGACGACAGGATGAGAATCGGGTCCCTTCAGGAGTGAACGTAGAGGGAGCA
GAAGTTCATGGATTCTCAATGGGAAAAAAGCTATCACCCAAGATAGATCGAGACCTAAGA
GAAGGTGGTCCTCTACTCTATGAGAACATCACATTCGTCTACAACTCGGAGCAGCTGAAC
GGGACTCAGCGGGTTCTCCTGGATAACGTCCTGTCGGAAGAACAGTGCCGGGAGCTCCAC
AGCGTGGCCAGTGGAATCATGCTTGTTGGTGATGGATACAGAGGAAAAACTTCACCCCAT
ACACCCAATGAAAAGTTTGAAGGTGCAACTGTCCTGAAAGCACTCAAATCTGGTTATGAA
GGTCGAGTCCCACTGAAGAGCGCTCGTCTGTTTTATGACATCAGCGAAAAGGCTCGAAGG
ATTGTAGAATCTTATTTTATGCTGAACTCAACTCTGTATTTTTCCTATACACACATGGTC
TGCCGAACAGCCCTGTCTGGTCAGCAGGATAGAAGAAATGACCTCAGTCATCCCATCCAT
GCTGACAACTGTTTGTTGGATCCAGAGGCCAACGAATGCTGGAAGGAGCCTCCTGCTTAC
ACATTTCGAGACTATAGTGCTCTCCTATATATGAATGATGACTTTGAAGGAGGAGAATTC
ATATTCACAGAGATGGATGCTAAGACTGTGACTGCCTCTATAAAACCAAAATGTGGGCGC
ATGATCAGCTTCTCATCTGGAGGAGAGAACCCTCATGGGGTGAAGGCAGTCACCAAGGGA
AAGAGGTGTGCTGTGGCTCTGTGGTTCACCTTGGACCCACTTTATAGAGAATTGGAGCGA
ATACAGGCTGATGAAGTGATTGCAATTCTGGATCAAGAACAGCAAGGGAAGCATGAACTG
AATATCAACCCTAAAGATGAGCTATAA

1. Leprecan-like protein 2
2. Protein B

MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALL
REALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALR
RADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTF
FVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLE
EALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGE
TATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQ
AQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREK
LREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGV
LLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSE
RVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWRE
PPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWA
VTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQ
RVQDKTGRAPRVREEL

• procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218] ALL_REAC R03218

• 2OG-FeII_Oxy (PF03171 )

• 1-20

• None

ATGCACCTGCAGATGCGGGAGGACATGGCTAAGTACAGACGAATGTCGGGAGTTCGGCCC
CAGAGCTTCCGGGACCTGGAGACGCCCCCACACTGGGCAGCCTATGACACTGGCCTGGAG
CTACTGGGGCGCCAGGAGGCAGGACTGGCACTGCCCAGGCTAGAGGAGGCTCTTCAGGGG
AGCCTGGCCCAGATGGAGAGCTGCCGTGCTGACTGTGAGGGGCCTGAGGAGCAGCAGGGG
GCTGAAGAAGAGGAGGATGGGGCTGCGAGCCAGGGGGGCCTCTATGAGGCCATTGCAGGA
CACTGGATTCAGGTCCTGCAGTGCCGGCAACGCTGTGTGGGGGAAACAGCCACACGCCCT
GGTCGCAGCTTCCCTGTCCCAGACTTCCTTCCCAACCAGCTGAGGCGGCTACATGAGGCC
CATGCTCAGGTGGGCAATCTGTCCCAGGCTATAGAAAATGTCCTGAGTGTCCTGCTCTTC
TACCCGGAGGATGAGGCTGCCAAGAGGGCTCTGAACCAGTACCAGGCCCAGCTGGGAGAG
CCGAGACCTGGCCTCGGACCCAGAGAGGACATCCAGCGCTTCATCCTCCGATCCCTGGGG
GAGAAGAGGCAGCTCTACTATGCCATGGAGCACCTGGGGACCAGCTTCAAGGATCCTGAC
CCCTGGACCCCTGCAGCTCTCATCCCTGAGGCACTTAGAGAAAAGCTCAGAGAGGATCAA
GAGAAGAGGCCTTGGGACCATGAGCCCGTGAAGCCAAAGCCCTTGACCTACTGGAAGGAT
GTCCTTCTCCTGGAGGGTGTGACCTTGACCCAGGATTCCAGGCAGCTGAATGGGTCGGAG
CGGGCGGTGTTGGATGGGCTGCTCACCCCAGCCGAGTGTGGGGTGCTGCTGCAGCTGGCT
AAGGATGCAGCTGGGGCTGGAGCCAGGTCTGGCTATCGTGGTCGCCGCTCCCCTCACACC
CCCCATGAACGCTTCGAGGGGCTCACGGTGCTTAAGGCTGCGCAGCTGGCCCGGGCTGGG
ACAGTGGGCAGTCAGGGTGCTAAGCTGCTTCTGGAGGTGAGCGAGCGGGTGCGGACCTTG
ACCCAGGCCTACTTCTCCCCGGAACGGCCCCTGCATCTGTCCTTCACCCACCTGGTGTGC
CGCAGCGCCATAGAAGGAGAGCAAGAGCAGCGCATGGACCTGAGTCACCCAGTGCACGCA
GACAACTGCGTCCTGGACCCTGACACGGGAGAGTGCTGGCGGGAGCCCCCAGCCTACACC
TATCGGGACTACAGCGGACTCCTCTACCTCAACGATGACTTCCAGGGTGGGGACCTGTTC
TTCACGGAGCCCAACGCCCTCACTGTCACGGCTCGGGTGCGTCCTCGCTGTGGGCGCCTT
GTGGCCTTCAGCTCCGGTGTCGAGAATCCCCATGGGGTGTGGGCCGTGACTCGGGGACGG
CGCTGTGCCCTGGCACTGTGGCACACGTGGGCACCTGAGCACAGGGAGCAGGAGTGGATA
GAAGCCAAAGAACTGCTGCAGGAGTCACAGGAGGAGGAGGAAGAGGAAGAGGAAGAAATG
CCCAGCAAAGACCCTTCCCCAGAGCCCCCTAGCCGCAGGCACCAGAGGGTCCAAGACAAG
ACTGGAAGGGCACCTCGGGTTCGGGAGGAGCTGTGA

1. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed ]
2. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed ]

1. 4-PH alpha-3

MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEA
RLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGY
EKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLT
GDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRA
GNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDT
YEGLCQTLGSQPTLYQIPSLYCSYETNSNAYLLLQPIRKEVIHLEPYIALYHDFVSDSEA
QKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTGLDVRP
PYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIY
ANLSVPVVRNAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSS
SPED

• Arginine and Proline Metabolism (map00330 )

• procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219] ALL_REAC R03219
• (other) R01252

• 2OG-FeII_Oxy (PF03171 )
• P4Ha_N (PF08336 )

• None

• None

ATGGGTCCTGGGGCGCGGCTGGCGGCGCTGCTGGCGGTGCTGGCGCTCGGGACAGGAGAC
CCAGAAAGGGCTGCGGCTCGGGGCGACACGTTCTCGGCGCTGACCAGCGTGGCGCGCGCC
CTGGCGCCCGAGCGCCGGCTGCTGGGGCTGCTGAGGCGGTACCTGCGCGGGGAGGAGGCG
CGGCTGCGGGACCTGACTAGATTCTACGACAAGGTACTTTCTTTGCATGAGGATTCAACA
ACCCCTGTGGCTAACCCTCTGCTTGCATTTACTCTCATCAAACGCCTGCAGTCTGACTGG
AGGAATGTGGTACATAGTCTGGAGGCCAGTGAGAACATCCGAGCTCTGAAGGATGGCTAT
GAGAAGGTGGAGCAAGACCTTCCAGCCTTTGAGGACCTTGAGGGAGCAGCAAGGGCCCTG
ATGCGGCTGCAGGACGTGTACATGCTCAATGTGAAAGGCCTGGCCCGAGGTGTCTTTCAG
AGAGTCACTGGCTCTGCCATCACTGACCTGTACAGCCCCAAACGGCTCTTTTCTCTCACA
GGGGATGACTGCTTCCAAGTTGGCAAGGTGGCCTATGACATGGGGGATTATTACCATGCC
ATTCCATGGCTGGAGGAGGCTGTCAGTCTCTTCCGAGGATCTTACGGAGAGTGGAAGACA
GAGGATGAGGCAAGTCTAGAAGATGCCTTGGATCACTTGGCCTTTGCTTATTTCCGGGCA
GGAAATGTTTCGTGTGCCCTCAGCCTCTCTCGGGAGTTTCTTCTCTACAGCCCAGATAAT
AAGAGGATGGCCAGGAATGTCTTGAAATATGAAAGGCTCTTGGCAGAGAGCCCCAACCAC
GTGGTAGCTGAGGCTGTCATCCAGAGGCCCAATATACCCCACCTGCAGACCAGAGACACC
TACGAGGGGCTATGTCAGACCCTGGGTTCCCAGCCCACTCTCTACCAGATCCCTAGCCTC
TACTGTTCCTATGAGACCAATTCCAACGCCTACCTGCTGCTCCAGCCCATCCGGAAGGAG
GTCATCCACCTGGAGCCCTACATTGCTCTCTACCATGACTTCGTCAGTGACTCAGAGGCT
CAGAAAATTAGAGAACTTGCAGAACCATGGCTACAGAGGTCAGTGGTGGCATCAGGGGAG
AAGCAGTTACAAGTGGAGTACCGCATCAGCAAAAGTGCCTGGCTGAAGGACACTGTTGAC
CCAAAACTGGTGACCCTCAACCACCGCATTGCTGCCCTCACAGGCCTTGATGTCCGGCCT
CCCTATGCAGAGTATCTGCAGGTGGTGAACTATGGCATCGGAGGACACTATGAGCCTCAC
TTTGACCATGCTACGTCACCAAGCAGCCCCCTCTACAGAATGAAGTCAGGAAACCGAGTT
GCAACATTTATGATCTATCTGAGCTCGGTGGAAGCTGGAGGAGCCACAGCCTTCATCTAT
GCCAACCTCAGCGTGCCTGTGGTTAGGAATGCAGCACTGTTTTGGTGGAACCTGCACAGG
AGTGGTGAAGGGGACAGTGACACACTTCATGCTGGCTGTCCTGTCCTGGTGGGAGATAAG
TGGGTGGCCAACAAGTGGATACATGAGTATGGACAGGAATTCCGCAGACCCTGCAGCTCC
AGCCCTGAAGACTGA

1. Van Den Diepstraten C, Papay K, Bolender Z, Brown A, Pickering JG: Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque. Circulation. 2003 Aug 5;108(5):508-11. Epub 2003 Jul 21. [PubMed ]
2. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]
3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
4. Kukkola L, Hieta R, Kivirikko KI, Myllyharju J: Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme. J Biol Chem. 2003 Nov 28;278(48):47685-93. Epub 2003 Sep 18. [PubMed ]

1. Hypoxia-inducible factor prolyl hydroxylase 2
2. HIF-prolyl hydroxylase 2
3. HIF-PH2
4. HPH-2
5. Prolyl hydroxylase domain-containing protein 2
6. PHD2
7. SM-20

MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQG
SEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADP
AAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLR
PNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQL
VSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMV
ACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKF
DRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDS
VGKDVF

• 2OG-FeII_Oxy (PF03171 )
• zf-MYND (PF01753 )

• None

• None

ATGGCCAATGACAGCGGCGGGCCCGGCGGGCCGAGCCCGAGCGAGCGAGACCGGCAGTAC
TGCGAGCTGTGCGGGAAGATGGAGAACCTGCTGCGCTGCAGCCGCTGCCGCAGCTCCTTC
TACTGCTGCAAGGAGCACCAGCGTCAGGACTGGAAGAAGCACAAGCTCGTGTGCCAGGGC
AGCGAGGGCGCCCTCGGCCACGGAGTGGGCCCACACCAGCATTCCGGCCCCGCGCCGCCG
GCTGCAGTGCCGCCGCCCAGGGCCGGGGCCCGGGAGCCCAGGAAGGCAGCGGCGCGCCGG
GACAACGCCTCCGGGGACGCGGCCAAGGGAAAAGTAAAGGCCAAGCCCCCGGCCGACCCA
GCGGCGGCCGCGTCGCCGTGTCGTGCGGCCGCCGGCGGCCAGGGCTCGGCGGTGGCTGCC
GAAGCCGAGCCCGGCAAGGAGGAGCCGCCGGCCCGCTCATCGCTGTTCCAGGAGAAGGCG
AACCTGTACCCCCCAAGCAACACGCCCGGGGATGCGCTGAGCCCCGGCGGCGGCCTGCGG
CCCAACGGGCAGACGAAGCCCCTGCCGGCGCTGAAGCTGGCGCTCGAGTACATCGTGCCG
TGCATGAACAAGCACGGCATCTGTGTGGTGGACGACTTCCTCGGCAAGGAGACCGGACAG
CAGATCGGCGACGAGGTGCGCGCCCTGCACGACACCGGGAAGTTCACGGACGGGCAGCTG
GTCAGCCAGAAGAGTGACTCGTCCAAGGACATCCGAGGCGATAAGATCACCTGGATCGAG
GGCAAGGAGCCCGGCTGCGAAACCATTGGGCTGCTCATGAGCAGCATGGACGACCTGATA
CGCCACTGTAACGGGAAGCTGGGCAGCTACAAAATCAATGGCCGGACGAAAGCCATGGTT
GCTTGTTATCCGGGCAATGGAACGGGTTATGTACGTCATGTTGATAATCCAAATGGAGAT
GGAAGATGTGTGACATGTATATATTATCTTAATAAAGACTGGGATGCCAAGGTAAGTGGA
GGTATACTTCGAATTTTTCCAGAAGGCAAAGCCCAGTTTGCTGACATTGAACCCAAATTT
GATAGACTGCTGTTTTTCTGGTCTGACCGTCGCAACCCTCATGAAGTACAACCAGCATAT
GCTACAAGGTACGCAATAACTGTTTGGTATTTTGATGCAGATGAGAGAGCACGAGCTAAA
GTAAAATATCTAACAGGTGAAAAAGGTGTGAGGGTTGAACTCAATAAACCTTCAGATTCG
GTCGGTAAAGACGTCTTCTAG

1. Dupuy D, Aubert I, Duperat VG, Petit J, Taine L, Stef M, Bloch B, Arveiler B: Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2. Genomics. 2000 Nov 1;69(3):348-54. [PubMed ]
2. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed ]
3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed ]
4. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed ]
5. Ivan M, Haberberger T, Gervasi DC, Michelson KS, Gunzler V, Kondo K, Yang H, Sorokina I, Conaway RC, Conaway JW, Kaelin WG Jr: Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13459-64. Epub 2002 Sep 26. [PubMed ]
6. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed ]
7. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed ]

1. Hypoxia-inducible factor prolyl hydroxylase 1
2. HIF-prolyl hydroxylase 1
3. HIF-PH1
4. HPH-3
5. Prolyl hydroxylase domain-containing protein 1
6. PHD1
7. Estrogen-induced tag 6

MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAG
SGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRK
WAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALD
YIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQI
AWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDN
PHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEV
KPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT

• 2OG-FeII_Oxy (PF03171 )

• None

• None

ATGGACAGCCCGTGCCAGCCGCAGCCCCTAAGTCAGGCTCTCCCTCAGTTACCAGGGTCT
TCGTCAGAGCCCTTGGAGCCTGAGCCTGGCCGGGCCAGGATGGGAGTGGAGAGTTACCTG
CCCTGTCCCCTGCTCCCCTCCTACCACTGTCCAGGAGTGCCTAGTGAGGCCTCGGCAGGG
AGTGGGACCCCCAGAGCCACAGCCACCTCTACCACTGCCAGCCCTCTTCGGGACGGTTTT
GGCGGGCAGGATGGTGGTGAGCTGCGGCCGCTGCAGAGTGAAGGCGCTGCAGCGCTGGTC
ACCAAGGGGTGCCAGCGATTGGCAGCCCAGGGCGCACGGCCTGAGGCCCCCAAACGGAAA
TGGGCCGAGGATGGTGGGGATGCCCCTTCACCCAGCAAACGGCCCTGGGCCAGGCAAGAG
AACCAGGAGGCAGAGCGGGAGGGTGGCATGAGCTGCAGCTGCAGCAGTGGCAGTGGTGAG
GCCAGTGCTGGGCTGATGGAGGAGGCGCTGCCCTCTGCGCCCGAGCGCCTGGCCCTGGAC
TATATCGTGCCCTGCATGCGGTACTACGGCATCTGCGTCAAGGACAGCTTCCTGGGGGCA
GCACTGGGCGGTCGCGTGCTGGCCGAGGTGGAGGCCCTCAAACGGGGTGGGCGCCTGCGA
GACGGGCAGCTAGTGAGCCAGAGGGCGATCCCGCCGCGCAGCATCCGTGGGGACCAGATT
GCCTGGGTGGAAGGCCATGAACCAGGCTGTCGAAGCATTGGTGCCCTCATGGCCCATGTG
GACGCCGTCATCCGCCACTGCGCAGGGCGGCTGGGCAGCTATGTCATCAACGGGCGCACC
AAGGCCATGGTGGCGTGTTACCCAGGCAACGGGCTCGGGTACGTAAGGCACGTTGACAAT
CCCCACGGCGATGGGCGCTGCATCACCTGTATCTATTACCTGAATCAGAACTGGGACGTT
AAGGTGCATGGCGGCCTGCTGCAGATCTTCCCTGAGGGCCGGCCCGTGGTAGCCAACATC
GAGCCACTCTTTGACCGGTTGCTCATTTTCTGGTCTGACCGGCGGAACCCCCACGAGGTG
AAGCCAGCCTATGCCACCAGGTACGCCATCACTGTCTGGTATTTTGATGCCAAGGAGCGG
GCAGCAGCCAAAGACAAGTATCAGCTAGCATCAGGACAGAAAGGTGTCCAAGTACCTGTA
TCACAGCCGCCTACGCCCACCTAG

1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed ]
2. Seth P, Krop I, Porter D, Polyak K: Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression). Oncogene. 2002 Jan 24;21(5):836-43. [PubMed ]
3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed ]
4. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed ]
5. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed ]
6. McNeill LA, Hewitson KS, Gleadle JM, Horsfall LE, Oldham NJ, Maxwell PH, Pugh CW, Ratcliffe PJ, Schofield CJ: The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg Med Chem Lett. 2002 Jun 17;12(12):1547-50. [PubMed ]

1. Hypoxia-inducible factor prolyl hydroxylase 3
2. HIF-prolyl hydroxylase 3
3. HIF-PH3
4. HPH-1
5. Prolyl hydroxylase domain-containing protein 3
6. PHD3

MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQ
LAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKA
MVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEP
IFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED

• 2OG-FeII_Oxy (PF03171 )

• None

• None

ATGCCCCTGGGACACATCATGAGGCTGGACCTGGAGAAAATTGCCCTGGAGTACATCGTG
CCCTGTCTGCACGAGGTGGGCTTCTGCTACCTGGACAACTTCCTGGGCGAGGTGGTGGGC
GACTGCGTCCTGGAGCGCGTCAAGCAGCTGCACTGCACCGGGGCCCTGCGGGACGGCCAG
CTGGCGGGGCCGCGCGCCGGCGTCTCCAAGCGACACCTGCGGGGCGACCAGATCACGTGG
ATCGGGGGCAACGAGGAGGGCTGCGAGGCCATCAGCTTCCTCCTGTCCCTCATCGACAGG
CTGGTCCTCTACTGCGGGAGCCGGCTGGGCAAATACTACGTCAAGGAGAGGTCTAAGGCA
ATGGTGGCTTGCTATCCGGGAAATGGAACAGGTTATGTTCGCCACGTGGACAACCCCAAC
GGTGATGGTCGCTGCATCACCTGCATCTACTATCTGAACAAGAATTGGGATGCCAAGCTA
CATGGTGGGATCCTGCGGATATTTCCAGAGGGGAAATCATTCATAGCAGATGTGGAGCCC
ATTTTTGACAGACTCCTGTTCTTCTGGTCAGATCGTAGGAACCCACACGAAGTGCAGCCC
TCTTACGCAACCAGATATGCTATGACTGTCTGGTACTTTGATGCTGAAGAAAGGGCAGAA
GCCAAAAAGAAATTCAGGAATTTAACTAGGAAAACTGAATCTGCCCTCACTGAAGACTGA

1. Taylor MS: Characterization and comparative analysis of the EGLN gene family. Gene. 2001 Sep 5;275(1):125-32. [PubMed ]
2. Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, Ratcliffe PJ: C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell. 2001 Oct 5;107(1):43-54. [PubMed ]
3. Semenza GL: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. Cell. 2001 Oct 5;107(1):1-3. [PubMed ]
4. Bruick RK, McKnight SL: A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 2001 Nov 9;294(5545):1337-40. Epub 2001 Oct 11. [PubMed ]
5. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed ]
6. Cioffi CL, Liu XQ, Kosinski PA, Garay M, Bowen BR: Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem Biophys Res Commun. 2003 Apr 11;303(3):947-53. [PubMed ]

1. Hypoxia-inducible factor prolyl 4-hydroxylase

MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAY
FLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVG
HERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYE
EAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDG
DGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRL
TRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYM
TVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVF
WYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLARE
GGTDSQPEWALDRAYRDARVEL

• 2OG-FeII_Oxy (PF03171 )

• None

• None

ATGGCGGCAGCGGCGGTGACAGGCCAGCGGCCTGAGACCGCGGCGGCCGAGGAGGCCTCG
AGGCCGCAGTGGGCGCCGCCAGACCACTGCCAGGCTCAGGCGGCGGCCGGGCTGGGCGAC
GGCGAGGACGCACCGGTGCGTCCGCTGTGCAAGCCCCGCGGCATCTGCTCGCGCGCCTAC
TTCCTGGTGCTGATGGTGTTCGTGCACCTGTACCTGGGTAACGTGCTGGCGCTGCTGCTC
TTCGTGCACTACAGCAACGGCGACGAAAGCAGCGATCCCGGGCCCCAACACCGTGCCCAG
GGCCCCGGGCCCGAGCCCACCTTAGGTCCCCTCACCCGGCTGGAGGGCATCAAGGTGGGG
CACGAGCGTAAGGTCCAGCTGGTCACCGACAGGGATCACTTCATCCGAACCCTCAGCCTC
AAGCCGCTGCTCTTCGAAATCCCCGGCTTCCTGACTGATGAAGAGTGTCGGCTCATCATC
CATCTGGCGCAGATGAAGGGGTTACAGCGCAGCCAGATCCTGCCTACTGAAGAGTATGAA
GAGGCAATGAGCACTATGCAGGTCAGCCAGCTGGACCTCTTCCGGCTGCTGGACCAGAAC
CGTGATGGGCACCTTCAGCTCCGTGAGGTTCTGGCCCAGACTCGCCTGGGAAATGGATGG
TGGATGACTCCAGAGAGCATTCAGGAGATGTACGCCGCGATCAAGGCTGACCCTGATGCT
GACGGAGTGCTGAGTCTGCAGGAGTTCTCCAACATGGACCTTCGGGACTTCCACAAGTAC
ATGAGGAGCCACAAGGCAGAGTCCAGTGAGCTGGTGCGGAACAGCCACCATACCTGGCTC
TACCAGGGTGAGGGTGCCCACCACATCATGCGTGCCATCCGCCAGAGGGTGCTGCGCCTC
ACTCGCCTGTCGCCTGAGATCGTGGAGCTCAGCGAGCCGCTGCAGGTTGTTCGATATGGT
GAGGGGGGCCACTACCATGCCCACGTGGACAGTGGGCCTGTGTACCCAGAGACCATCTGC
TCCCATACCAAGCTGGTAGCCAACGAGTCTGTACCCTTCGAGACCTCCTGCCGCTACATG
ACAGTGCTGTTTTATTTGAACAACGTCACTGGTGGGGGCGAGACTGTTTTCCCTGTAGCA
GATAACAGAACCTACGATGAAATGAGTCTGATTCAGGATGACGTGGACCTCCGTGACACA
CGGAGGCACTGTGACAAGGGAAACCTGCGTGTCAAGCCCCAACAGGGCACAGCAGTCTTC
TGGTACAACTACCTGCCTGATGGGCAAGGTTGGGTGGGTGACGTAGACGACTACTCGCTG
CACGGGGGCTGCCTGGTCACGCGCGGCACCAAGTGGATTGCCAACAACTGGATTAATGTG
GACCCCAGCCGAGCGCGGCAAGCGCTGTTCCAACAGGAGATGGCCCGCCTTGCCCGAGAA
GGGGGCACCGACTCACAGCCCGAGTGGGCTCTGGACCGGGCCTACCGCGATGCGCGCGTG
GAACTCTGA

1. Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hutter J, Schramm M, Flamme I: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem Biophys Res Commun. 2002 Aug 16;296(2):343-9. [PubMed ]

MEGLLTRCRALPALATCSRQLSGYVPCRFHHCAPRRGRRLLLSRVFQPQNLREDRVLSLQ
DKSDDLTCKSQRLMLQVGLIYPASPGCYHLLPYTVRAMEKLVRVIDQEMQAIGGQKVNMP
SLSPAELWQATNRWDLMGKELLRLRDRHGKEYCLGPTHEEAITALIASQKKLSYKQLPFL
LYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSPEAAQQTYSLVCDAYCSLFNKLGLP
FVKVQADVGTIGGTVSHEFQLPVDIGEDRLAICPRCSFSANMETLDLSQMNCPACQGPLT
KTKGIEVGHTFYLGTKYSSIFNAQFTNVCGKPTLAEMGCYGLGVTRILAAAIEVLSTEDC
VRWPSLLAPYQACLIPPKKGSKEQAASELIGQLYDHITEAVPQLHGEVLLDDRTHLTIGN
RLKDANKFGYPFVIIAGKRALEDPAHFEVWCQNTGEVAFLTKDGVMDLLTPVQTV

• None

• None

ATGGAAGGGCTGCTGACAAGATGCAGAGCATTGCCCGCCCTGGCCACCTGCAGCCGCCAG
CTCTCTGGGTATGTTCCTTGCAGGTTTCACCACTGTGCCCCAAGAAGAGGGCGGCGCCTG
CTGCTGTCTCGTGTGTTCCAGCCACAGAACCTTCGGGAAGACCGGGTGCTCTCCCTGCAG
GACAAATCTGATGACCTGACCTGTAAGAGCCAGCGGCTGATGCTGCAGGTGGGCCTGATC
TACCCAGCAAGCCCCGGCTGTTACCACCTCCTGCCATATACCGTCCGTGCCATGGAGAAG
CTCGTGCGAGTGATAGACCAGGAGATGCAGGCCATCGGGGGCCAGAAAGTCAACATGCCC
AGCCTCAGCCCGGCAGAGCTCTGGCAAGCCACCAACCGGTGGGACTTGATGGGCAAAGAG
CTGCTAAGACTTAGAGACAGGCATGGCAAGGAATACTGCTTAGGACCAACTCACGAGGAA
GCCATTACGGCCTTAATTGCCTCCCAGAAGAAACTGTCCTACAAGCAGCTTCCCTTCCTG
CTGTACCAAGTGACAAGGAAGTTTCGGGATGAGCCCAGGCCCCGCTTTGGTCTTCTCCGT
GGCCGAGAGTTTTACATGAAGGATATGTACACCTTTGACTCCTCCCCAGAGGCTGCCCAG
CAGACCTACAGCCTGGTGTGTGATGCCTACTGCAGCCTGTTCAACAAGCTAGGGCTGCCA
TTTGTCAAGGTCCAGGCCGATGTGGGCACCATCGGGGGCACAGTGTCTCATGAGTTCCAG
CTCCCAGTGGATATTGGAGAGGACCGGCTTGCCATCTGTCCCCGCTGCAGCTTCTCAGCC
AACATGGAGACACTAGACTTGTCACAAATGAACTGCCCTGCTTGCCAGGGCCCATTGACT
AAAACCAAAGGCATTGAGGTGGGGCACACATTTTACCTGGGTACCAAGTACTCATCCATT
TTCAATGCCCAGTTTACCAATGTCTGTGGCAAACCAACCCTGGCTGAAATGGGGTGCTAT
GGCTTGGGTGTGACACGGATCTTGGCTGCTGCCATTGAAGTCCTCTCTACAGAAGACTGT
GTCCGCTGGCCCAGCCTACTGGCCCCTTACCAAGCCTGCCTCATCCCCCCTAAGAAGGGC
AGTAAGGAGCAGGCGGCCTCCGAGCTCATAGGGCAGCTGTACGACCACATCACAGAGGCA
GTGCCTCAGCTTCACGGGGAGGTGCTCCTGGACGACAGGACCCATCTGACCATCGGAAAC
AGACTGAAAGATGCCAACAAGTTTGGCTACCCCTTTGTGATAATCGCTGGCAAGAGGGCC
CTGGAGGACCCTGCACATTTTGAGGTTTGGTGTCAGAACACTGGTGAGGTGGCCTTCCTC
ACCAAAGATGGAGTCATGGATTTACTGACCCCAGTGCAGACTGTCTAA

MESALAVPWLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDH
VRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGL
VPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGK
VMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFL
YGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKS
SATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIIEDDDPLRDGFLLK

• Pro_racemase (PF05544 )

• None

• None

1. PPIase
2. Rotamase
3. Cyclophilin F

MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLG
RVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI
YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDV
VKKIESFGSKSGRTSKKIVITDCGQLS

• Pro_isomerase (PF00160 )

• None

• None

1. Bergsma DJ, Eder C, Gross M, Kersten H, Sylvester D, Appelbaum E, Cusimano D, Livi GP, McLaughlin MM, Kasyan K, et al.: The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms. J Biol Chem. 1991 Dec 5;266(34):23204-14. [PubMed ]

1. PPIase A
2. Rotamase A
3. Cyclophilin A
4. Cyclosporin A-binding protein

MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGF
MCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE

• Pro_isomerase (PF00160 )

• None

• None

1. Haendler B, Hofer-Warbinek R, Hofer E: Complementary DNA for human T-cell cyclophilin. EMBO J. 1987 Apr;6(4):947-50. [PubMed ]
2. Haendler B, Hofer E: Characterization of the human cyclophilin gene and of related processed pseudogenes. Eur J Biochem. 1990 Jul 5;190(3):477-82. [PubMed ]
3. Meier U, Beier-Hellwig K, Klug J, Linder D, Beier HM: Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy. Hum Reprod. 1995 May;10(5):1305-10. [PubMed ]
4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
5. Liu J, Chen CM, Walsh CT: Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry. 1991 Mar 5;30(9):2306-10. [PubMed ]
6. Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell. 1993 Jun 18;73(6):1067-78. [PubMed ]
7. Kallen J, Spitzfaden C, Zurini MG, Wider G, Widmer H, Wuthrich K, Walkinshaw MD: Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature. 1991 Sep 19;353(6341):276-9. [PubMed ]
8. Ke HM, Zydowsky LD, Liu J, Walsh CT: Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9483-7. [PubMed ]
9. Pflugl G, Kallen J, Schirmer T, Jansonius JN, Zurini MG, Walkinshaw MD: X-ray structure of a decameric cyclophilin-cyclosporin crystal complex. Nature. 1993 Jan 7;361(6407):91-4. [PubMed ]
10. Mikol V, Kallen J, Pflugl G, Walkinshaw MD: X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J Mol Biol. 1993 Dec 20;234(4):1119-30. [PubMed ]
11. Zhao Y, Ke H: Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry. 1996 Jun 11;35(23):7356-61. [PubMed ]
12. Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP: Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci. 1997 Nov;6(11):2297-307. [PubMed ]
13. Kallen J, Mikol V, Taylor P, Walkinshaw MD: X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. J Mol Biol. 1998 Oct 23;283(2):435-49. [PubMed ]
14. Theriault Y, Logan TM, Meadows R, Yu L, Olejniczak ET, Holzman TF, Simmer RL, Fesik SW: Solution structure of the cyclosporin A/cyclophilin complex by NMR. Nature. 1993 Jan 7;361(6407):88-91. [PubMed ]
15. Ottiger M, Zerbe O, Guntert P, Wuthrich K: The NMR solution conformation of unligated human cyclophilin A. J Mol Biol. 1997 Sep 12;272(1):64-81. [PubMed ]

1. PPIase
2. Rotamase
3. Cyclophilin B
4. S-cyclophilin
5. SCYLP
6. CYP-S1

MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRV
IFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYG
ERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVR
KVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE

• Pro_isomerase (PF00160 )

• 1-33

• None

1. Spik G, Haendler B, Delmas O, Mariller C, Chamoux M, Maes P, Tartar A, Montreuil J, Stedman K, Kocher HP, et al.: A novel secreted cyclophilin-like protein (SCYLP). J Biol Chem. 1991 Jun 15;266(17):10735-8. [PubMed ]
2. Price ER, Zydowsky LD, Jin MJ, Baker CH, McKeon FD, Walsh CT: Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc Natl Acad Sci U S A. 1991 Mar 1;88(5):1903-7. [PubMed ]
3. Hasel KW, Glass JR, Godbout M, Sutcliffe JG: An endoplasmic reticulum-specific cyclophilin. Mol Cell Biol. 1991 Jul;11(7):3484-91. [PubMed ]
4. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed ]
5. Arber S, Krause KH, Caroni P: s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J Cell Biol. 1992 Jan;116(1):113-25. [PubMed ]
6. Mikol V, Kallen J, Walkinshaw MD: X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain. Proc Natl Acad Sci U S A. 1994 May 24;91(11):5183-6. [PubMed ]

1. Peptidyl-prolyl isomerase G
2. PPIase G
3. Rotamase G
4. Cyclophilin G
5. Clk-associating RS-cyclophilin
6. CARS-cyclophilin
7. CARS-Cyp
8. SR-cyclophilin
9. SR-cyp
10. SRcyp
11. CASP10

MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHY
KSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTN
GSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPK
SKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRK
HKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERK
NRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPP
HWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKN
EKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRN
EEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDR
RAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRR
RGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSES
EKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDDELKSSMLKNKEDEKIRSSVEK
ENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG

• Pro_isomerase (PF00160 )

• None

• None

1. Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK: RS cyclophilins: identification of an NK-TR1-related cyclophilin. Gene. 1996 Nov 21;180(1-2):151-5. [PubMed ]
2. Bourquin JP, Stagljar I, Meier P, Moosmann P, Silke J, Baechi T, Georgiev O, Schaffner W: A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II. Nucleic Acids Res. 1997 Jun 1;25(11):2055-61. [PubMed ]

1. Proline--tRNA ligase
2. ProRS

MEGLLTRCRALPALATCSRQLSGYVPCRFHHCAPRRGRRLLLSRVFQPQNLREDRVLSLQ
DKSDDLTCKSQRLMLQVGLIYPASPGCYHLLPYTVRAMEKLVRVIDQEMQAIGGQKVNMP
SLSPAELWQATNRWDLMGKELLRLRDRHGKEYCLGPTHEEAITALIASQKKLSYKQLPFL
LYQVTRKFRDEPRPRFGLLRGREFYMKDMYTFDSSPEAAQQTYSLVCDAYCSLFNKLGLP
FVKVQADVGTIGGTVSHEFQLPVDIGEDRLAICPRCSFSANMETLDLSQMNCPACQGPLT
KTKGIEVGHTFYLGTKYSSIFNAQFTNVCGKPTLAEMGCYGLGVTRILAAAIEVLSTEDC
VRWPSLLAPYQACLIPPKKGSKEQAASELIGQLYDHITEAVPQLHGEVLLDDRTHLTIGN
RLKDANKFGYPFVIIAGKRALEDPAHFEVWCQNTGEVAFLTKDGVMDLLTPVQTV

• HGTP_anticodon (PF03129 )
• tRNA-synt_2b (PF00587 )

• None

• None

1. PPIase H
2. Rotamase H
3. U-snRNP-associated cyclophilin SnuCyp-20
4. USA-CYP
5. Small nuclear ribonucleoprotein particle-specific cyclophilin H
6. CypH

MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGY
KGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTN
GCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVISQCGEM

• Pro_isomerase (PF00160 )

• None

• None

1. Horowitz DS, Kobayashi R, Krainer AR: A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. RNA. 1997 Dec;3(12):1374-87. [PubMed ]
2. Teigelkamp S, Achsel T, Mundt C, Gothel SF, Cronshagen U, Lane WS, Marahiel M, Luhrmann R: The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins. RNA. 1998 Feb;4(2):127-41. [PubMed ]
3. Horowitz DS, Lee EJ, Mabon SA, Misteli T: A cyclophilin functions in pre-mRNA splicing. EMBO J. 2002 Feb 1;21(3):470-80. [PubMed ]
4. Reidt U, Reuter K, Achsel T, Ingelfinger D, Luhrmann R, Ficner R: Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin. J Biol Chem. 2000 Mar 17;275(11):7439-42. [PubMed ]
5. Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Luhrmann R, Ficner R: Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol. 2003 Aug 1;331(1):45-56. [PubMed ]