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Identification
HMDB Protein ID HMDBP08126
Secondary Accession Numbers
  • 13837
Name Erythrocyte membrane protein band 4.2
Synonyms
  1. Erythrocyte protein 4.2
  2. P4.2
Gene Name EPB42
Protein Type Unknown
Biological Properties
General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Specific Function Probably plays an important role in the regulation of erythrocyte shape and mechanical properties
Pathways Not Available
Reactions Not Available
GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring amino-acyl groups
protein-glutamine gamma-glutamyltransferase activity
Process
metabolic process
macromolecule metabolic process
post-translational protein modification
peptide cross-linking
macromolecule modification
protein modification process
Cellular Location
  1. Cell membrane
  2. Lipid-anchor
  3. Cytoplasm
  4. Cytoplasmic side
  5. cytoskeleton
Gene Properties
Chromosome Location Chromosome:1
Locus 15q15-q21
SNPs EPB42
Gene Sequence
>2076 bp
ATGGGACAGGCCCTGGGTATCAAGAGCTGTGACTTTCAGGCAGCAAGAAACAATGAGGAG
CACCACACCAAGGCCCTCAGCTCCCGGCGCCTCTTTGTGAGGAGGGGGCAGCCCTTCACC
ATCATCCTGTACTTCCGCGCTCCAGTCCGTGCATTTCTGCCTGCCCTGAAGAAGGTGGCC
CTCACTGCACAAACTGGAGAGCAGCCTTCCAAGATCAACAGGACCCAAGCCACATTCCCA
ATTTCCAGTCTGGGGGACCGAAAGTGGTGGAGTGCAGTGGTGGAGGAGAGAGATGCCCAG
TCCTGGACCATCTCTGTGACCACACCTGCGGACGCTGTCATTGGCCACTACTCGCTTCTG
CTGCAGGTCTCAGGCAGGAAGCAACTCCTCTTGGGTCAGTTCACACTGCTTTTTAACCCC
TGGAATAGAGAGGATGCTGTGTTCCTGAAGAATGAGGCTCAGCGCATGGAGTACTTGTTG
AACCAGAATGGTCTCATCTACCTGGGTACAGCTGACTGCATCCAGGCAGAGTCCTGGGAC
TTTGGCCAGTTCGAGGGGGATGTCATTGACCTCAGCCTGCGCTTGCTGAGCAAGGACAAG
CAGGTAGAGAAGTGGAGCCAGCCGGTGCACGTGGCCCGTGTGTTGGGTGCCTTGCTGCAT
TTTCTCAAGGAGCAGAGGGTCCTGCCCACCCCGCAGACCCAGGCCACCCAGGAAGGGGCC
TTGCTGAACAAGCGCCGGGGCAGCGTGCCCATCCTGCGGCAGTGGCTCACCGGCCGAGGC
CGACCTGTGTATGATGGCCAGGCCTGGGTGTTGGCTGCTGTTGCTTGCACAGTGCTGCGA
TGCCTGGGAATCCCTGCCCGCGTGGTGACCACGTTTGCCTCAGCACAGGGCACCGGTGGG
CGTCTTCTCATAGATGAATACTATAATGAGGAGGGACTTCAGAACGGAGAAGGCCAGAGA
GGCAGAATCTGGATCTTCCAGACTTCCACAGAGTGCTGGATGACGCGGCCTGCCTTGCCC
CAGGGTTATGATGGATGGCAGATTCTGCACCCAAGTGCTCCTAATGGAGGTGGAGTCCTG
GGGTCCTGTGATCTGGTGCCGGTCAGAGCAGTCAAGGAGGGGACGCTGGGGCTGACCCCA
GCAGTGTCAGACCTTTTTGCTGCCATAAATGCCTCATGTGTGGTCTGGAAGTGCTGTGAG
GATGGGACACTGGAGTTGACTGACTCCAACACAAAGTATGTTGGCAACAACATCAGCACC
AAGGGTGTGGGCAGTGACCGCTGCGAGGACATCACTCAGAACTACAAGTATCCTGAAGGG
TCTCTTCAGGAAAAAGAGGTGCTGGAGAGAGTCGAGAAAGAGAAAATGGAACGTGAGAAA
GACAACGGCATCCGTCCTCCCAGTCTCGAGACTGCCAGTCCTCTGTACCTGCTCTTGAAA
GCACCCAGCTCCCTACCCCTGAGAGGGGATGCCCAGATCTCAGTGACGCTGGTTAATCAC
AGTGAGCAGGAGAAGGCAGTGCAGCTGGCAATTGGGGTCCAGGCTGTACACTACAACGGT
GTCCTTGCTGCCAAGCTCTGGAGGAAGAAGCTGCACCTCACGCTCAGTGCCAACCTGGAA
AAGATAATAACCATCGGCCTGTTCTTCTCCAATTTTGAGCGAAACCCACCCGAGAACACC
TTCCTTAGACTCACCGCCATGGCAACACACTCTGAATCCAACCTTAGCTGCTTTGCTCAG
GAAGACATTGCCATTTGTAGACCACACCTTGCCATCAAGATGCCAGAGAAAGCAGAGCAG
TATCAACCCCTCACAGCCTCAGTCAGCCTCCAGAACTCCCTAGATGCCCCCATGGAGGAC
TGTGTGATCTCCATCCTGGGAAGGGGGCTCATTCACAGAGAGAGGAGCTACAGATTCCGT
TCAGTGTGGCCTGAAAACACCATGTGTGCCAAGTTCCAGTTCACGCCAACACATGTGGGG
CTCCAGAGACTCACTGTGGAAGTGGACTGCAACATGTTCCAGAACCTAACCAACTATAAA
AGCGTCACCGTGGTAGCCCCTGAACTATCAGCTTAA
Protein Properties
Number of Residues 691
Molecular Weight 77008.5
Theoretical pI 8.17
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Erythrocyte membrane protein band 4.2
MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVA
LTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLL
LQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWD
FGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGA
LLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGG
RLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVL
GSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNIST
KGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLK
APSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLE
KIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQ
YQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVG
LQRLTVEVDCNMFQNLTNYKSVTVVAPELSA
GenBank ID Protein 166362737
UniProtKB/Swiss-Prot ID P16452
UniProtKB/Swiss-Prot Entry Name EPB42_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001114134.1
GeneCard ID EPB42
GenAtlas ID EPB42
HGNC ID HGNC:3381
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed:16572171 ]
  3. Korsgren C, Cohen CM: Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4840-4. [PubMed:2052563 ]
  4. Korsgren C, Lawler J, Lambert S, Speicher D, Cohen CM: Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. Proc Natl Acad Sci U S A. 1990 Jan;87(2):613-7. [PubMed:2300550 ]
  5. Sung LA, Chien S, Chang LS, Lambert K, Bliss SA, Bouhassira EE, Nagel RL, Schwartz RS, Rybicki AC: Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. Proc Natl Acad Sci U S A. 1990 Feb;87(3):955-9. [PubMed:1689063 ]
  6. Risinger MA, Dotimas EM, Cohen CM: Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem. 1992 Mar 15;267(8):5680-5. [PubMed:1544941 ]
  7. Dotimas E, Speicher DW, GuptaRoy B, Cohen CM: Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2). Biochim Biophys Acta. 1993 May 14;1148(1):19-29. [PubMed:8499466 ]
  8. Bouhassira EE, Schwartz RS, Yawata Y, Ata K, Kanzaki A, Qiu JJ, Nagel RL, Rybicki AC: An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON). Blood. 1992 Apr 1;79(7):1846-54. [PubMed:1558976 ]
  9. Takaoka Y, Ideguchi H, Matsuda M, Sakamoto N, Takeuchi T, Fukumaki Y: A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka). Br J Haematol. 1994 Nov;88(3):527-33. [PubMed:7819064 ]
  10. Hayette S, Morle L, Bozon M, Ghanem A, Risinger M, Korsgren C, Tanner MJ, Fattoum S, Cohen CM, Delaunay J: A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. Br J Haematol. 1995 Apr;89(4):762-70. [PubMed:7772513 ]
  11. Kanzaki A, Yasunaga M, Okamoto N, Inoue T, Yawata A, Wada H, Andoh A, Hodohara K, Fujiyama Y, Bamba T, et al.: Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT results in band 4.2 deficiency and microspherocytosis. Br J Haematol. 1995 Oct;91(2):333-40. [PubMed:8547071 ]
  12. Kanzaki A, Yawata Y, Yawata A, Inoue T, Okamoto N, Wada H, Harano T, Harano K, Wilmotte R, Hayette S, et al.: Band 4.2 Komatsu: 523 GAT-->TAT (175 Asp-->Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network. Int J Hematol. 1995 Jun;61(4):165-78. [PubMed:8547605 ]
  13. Perrotta S, Iolascon A, Polito R, d'Urzo G, Conte ML, Miraglia del Giudice E: 4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis. Haematologica. 1999 Jul;84(7):660-2. [PubMed:10406914 ]