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Showing Protein Protein XRP2 (HMDBP08623)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 3 metabolites
Identification
HMDB Protein ID HMDBP08623
Secondary Accession Numbers
  • 14338
Name Protein XRP2
Synonyms Not Available
Gene Name RP2
Protein Type Unknown
Biological Properties
General Function Involved in cell morphogenesis
Specific Function Stimulates the GTPase activity of tubulin, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor for ARL3
Pathways Not Available
Reactions Not Available
GO Classification
Function
nucleoside diphosphate kinase activity
binding
catalytic activity
phosphotransferase activity, phosphate group as acceptor
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
Process
ctp biosynthetic process
pyrimidine nucleoside triphosphate biosynthetic process
pyrimidine ribonucleoside triphosphate biosynthetic process
utp biosynthetic process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
gtp biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
pyrimidine nucleotide metabolic process
pyrimidine nucleotide biosynthetic process
Cellular Location
  1. Cell membrane
  2. Lipid-anchor
  3. Cytoplasmic side
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs RP2
Gene Sequence 
>1053 bp
ATGGGCTGCTTCTTCTCCAAGAGACGGAAGGCTGACAAGGAGTCGCGGCCCGAGAACGAG
GAGGAGCGGCCAAAGCAGTACAGCTGGGATCAGCGCGAGAAGGTTGATCCAAAAGACTAC
ATGTTCAGTGGACTGAAGGATGAAACAGTAGGTCGCTTACCTGGGACGGTAGCAGGACAA
CAGTTTCTCATTCAAGACTGTGAGAACTGTAACATCTATATTTTTGATCACTCTGCTACA
GTTACCATTGATGACTGTACTAACTGCATAATTTTTCTGGGACCCGTGAAAGGCAGCGTG
TTTTTCCGGAATTGCAGAGATTGCAAGTGCACATTAGCCTGCCAACAATTTCGTGTGCGA
GATTGTAGAAAGCTGGAAGTCTTTTTGTGTTGTGCCACTCAACCCATCATTGAGTCTTCC
TCAAATATCAAATTTGGATGTTTTCAATGGTACTATCCTGAATTAGCTTTCCAGTTCAAA
GATGCAGGGCTAAGTATCTTCGACAATACATGGAGTAACATTCATGACTTTACACCTGTG
TCAGGAGAACTCAACTGGAGCCTTCTTCCAGAAGATGCTGTGGTTCAGGACTATGTTCCT
ATACCTACTACCGAAGAGCTCAAAGCTGTTCGTGTTTCCACAGAAGCCAATAGAAGCATT
GTTCCAATATCCCGGGGTCAGAGACAGAAGAGCAGCGATGAATCATGCTTAGTGGTATTA
TTTGCTGGTGATTACACTATTGCAAATGCCAGAAAACTAATTGATGAGATGGTTGGTAAA
GGCTTTTTCCTAGTTCAGACAAAGGAAGTGTCCATGAAAGCTGAGGATGCTCAAAGGGTT
TTTCGGGAAAAAGCACCTGACTTCCTTCCTCTTCTGAACAAAGGTCCTGTTATTGCCTTG
GAGTTTAATGGGGATGGTGCTGTAGAAGTATGTCAACTTATTGTAAACGAGATATTCAAT
GGGACCAAGATGTTTGTATCTGAAAGCAAGGAGACGGCATCTGGAGATGTAGACAGCTTC
TACAACTTTGCTGATATACAGATGGGAATATGA
Protein Properties
Number of Residues 350
Molecular Weight 39640.7
Theoretical pI 4.73
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Protein XRP2
MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQ
QFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVR
DCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPV
SGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVL
FAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIAL
EFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
GenBank ID Protein 3550283
UniProtKB/Swiss-Prot ID O75695
UniProtKB/Swiss-Prot Entry Name XRP2_HUMAN
PDB IDs Not Available
GenBank Gene ID AJ007590
GeneCard ID RP2
GenAtlas ID RP2
HGNC ID HGNC:10274
References
General References
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  2. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
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  4. Sharon D, Bruns GA, McGee TL, Sandberg MA, Berson EL, Dryja TP: X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function. Invest Ophthalmol Vis Sci. 2000 Aug;41(9):2712-21. [PubMed:10937588 ]
  5. Breuer DK, Yashar BM, Filippova E, Hiriyanna S, Lyons RH, Mears AJ, Asaye B, Acar C, Vervoort R, Wright AF, Musarella MA, Wheeler P, MacDonald I, Iannaccone A, Birch D, Hoffman DR, Fishman GA, Heckenlively JR, Jacobson SG, Sieving PA, Swaroop A: A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa. Am J Hum Genet. 2002 Jun;70(6):1545-54. Epub 2002 Apr 30. [PubMed:11992260 ]
  6. Sharon D, Sandberg MA, Rabe VW, Stillberger M, Dryja TP, Berson EL: RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa. Am J Hum Genet. 2003 Nov;73(5):1131-46. Epub 2003 Oct 16. [PubMed:14564670 ]
  7. Bader I, Brandau O, Achatz H, Apfelstedt-Sylla E, Hergersberg M, Lorenz B, Wissinger B, Wittwer B, Rudolph G, Meindl A, Meitinger T: X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15. Invest Ophthalmol Vis Sci. 2003 Apr;44(4):1458-63. [PubMed:12657579 ]
  8. Schwahn U, Lenzner S, Dong J, Feil S, Hinzmann B, van Duijnhoven G, Kirschner R, Hemberger M, Bergen AA, Rosenberg T, Pinckers AJ, Fundele R, Rosenthal A, Cremers FP, Ropers HH, Berger W: Positional cloning of the gene for X-linked retinitis pigmentosa 2. Nat Genet. 1998 Aug;19(4):327-32. [PubMed:9697692 ]
  9. Chapple JP, Hardcastle AJ, Grayson C, Spackman LA, Willison KR, Cheetham ME: Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane. Hum Mol Genet. 2000 Aug 12;9(13):1919-26. [PubMed:10942419 ]
  10. Bartolini F, Bhamidipati A, Thomas S, Schwahn U, Lewis SA, Cowan NJ: Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C. J Biol Chem. 2002 Apr 26;277(17):14629-34. Epub 2002 Feb 14. [PubMed:11847227 ]
  11. Kuhnel K, Veltel S, Schlichting I, Wittinghofer A: Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Structure. 2006 Feb;14(2):367-78. [PubMed:16472755 ]
  12. Hardcastle AJ, Thiselton DL, Van Maldergem L, Saha BK, Jay M, Plant C, Taylor R, Bird AC, Bhattacharya S: Mutations in the RP2 gene cause disease in 10% of families with familial X-linked retinitis pigmentosa assessed in this study. Am J Hum Genet. 1999 Apr;64(4):1210-5. [PubMed:10090907 ]
  13. Rosenberg T, Schwahn U, Feil S, Berger W: Genotype-phenotype correlation in X-linked retinitis pigmentosa 2 (RP2). Ophthalmic Genet. 1999 Sep;20(3):161-72. [PubMed:10520237 ]
  14. Thiselton DL, Zito I, Plant C, Jay M, Hodgson SV, Bird AC, Bhattacharya SS, Hardcastle AJ: Novel frameshift mutations in the RP2 gene and polymorphic variants. Hum Mutat. 2000 Jun;15(6):580. [PubMed:10862093 ]
  15. Wada Y, Nakazawa M, Abe T, Tamai M: A new Leu253Arg mutation in the RP2 gene in a Japanese family with X-linked retinitis pigmentosa. Invest Ophthalmol Vis Sci. 2000 Jan;41(1):290-3. [PubMed:10634633 ]
  16. Miano MG, Testa F, Filippini F, Trujillo M, Conte I, Lanzara C, Millan JM, De Bernardo C, Grammatico B, Mangino M, Torrente I, Carrozzo R, Simonelli F, Rinaldi E, Ventruto V, D'Urso M, Ayuso C, Ciccodicola A: Identification of novel RP2 mutations in a subset of X-linked retinitis pigmentosa families and prediction of new domains. Hum Mutat. 2001 Aug;18(2):109-19. [PubMed:11462235 ]