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P16452 (EPB42_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Erythrocyte membrane protein band 4.2

Short name=Erythrocyte protein 4.2
Short name=P4.2
Gene names
Name:EPB42
Synonyms:E42P
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.

Subunit structure

Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton. Note: Cytoplasmic surface of erythrocyte membranes.

Post-translational modification

Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42.

Involvement in disease

Spherocytosis 5 (SPH5) [MIM:612690]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Absence of band 4.2 associated with spur or target erythrocytes has also been reported.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Miscellaneous

The substitution of an Ala for a Cys in the active site may be responsible for the lack of transglutaminase activity of band 4.2.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence caution

The sequence AAA36401.1 differs from that shown. Reason: Frameshift at positions 335 and 340.

The sequence AAA36402.1 differs from that shown. Reason: Frameshift at positions 335 and 340.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SPINK7P580623EBI-1182496,EBI-1182445

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Short (identifier: P16452-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform.
Isoform Long (identifier: P16452-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3-3: Q → QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 691690Erythrocyte membrane protein band 4.2
PRO_0000213720

Regions

Region31 – 399Band 3 binding By similarity

Amino acid modifications

Modified residue2481Phosphoserine; by PKA Probable
Lipidation21N-myristoyl glycine Ref.7

Natural variations

Alternative sequence31Q → QGEPSQRSTGLAGLYAAPAA SPVFIKGSGMD in isoform Long.
VSP_006416
Natural variant1121A → T in SPH5; Nippon/Fukuoka. Ref.9 Ref.10 Ref.12 Ref.14
Corresponds to variant rs28933988 [ dbSNP | Ensembl ].
VAR_007482
Natural variant1451D → Y in SPH5; Komatsu. Ref.13
VAR_058099
Natural variant2801R → Q in SPH5; Tozeur. Ref.11
VAR_012268
Natural variant2871R → C in SPH5; Shiga. Ref.12
VAR_058100

Experimental info

Sequence conflict3501H → D in AAA74589. Ref.1
Sequence conflict3501H → D in AAA52385. Ref.1
Sequence conflict3501H → D in AAA35798. Ref.2
Sequence conflict3761L → V in AAA74589. Ref.1
Sequence conflict3761L → V in AAA52385. Ref.1
Sequence conflict3761L → V in AAA35798. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Short [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 38225C311E478580

FASTA69177,009
        10         20         30         40         50         60 
MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR AFLPALKKVA 

        70         80         90        100        110        120 
LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ SWTISVTTPA DAVIGHYSLL 

       130        140        150        160        170        180 
LQVSGRKQLL LGQFTLLFNP WNREDAVFLK NEAQRMEYLL NQNGLIYLGT ADCIQAESWD 

       190        200        210        220        230        240 
FGQFEGDVID LSLRLLSKDK QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA 

       250        260        270        280        290        300 
LLNKRRGSVP ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG 

       310        320        330        340        350        360 
RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH PSAPNGGGVL 

       370        380        390        400        410        420 
GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE DGTLELTDSN TKYVGNNIST 

       430        440        450        460        470        480 
KGVGSDRCED ITQNYKYPEG SLQEKEVLER VEKEKMEREK DNGIRPPSLE TASPLYLLLK 

       490        500        510        520        530        540 
APSSLPLRGD AQISVTLVNH SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE 

       550        560        570        580        590        600 
KIITIGLFFS NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ 

       610        620        630        640        650        660 
YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA KFQFTPTHVG 

       670        680        690 
LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A 

« Hide

Isoform Long [UniParc].

Checksum: A1C85B41298A93C0
Show »

FASTA72179,927

References

« Hide 'large scale' references
[1]"Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII."
Korsgren C., Cohen C.M.
Proc. Natl. Acad. Sci. U.S.A. 88:4840-4844(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Reticulocyte.
[2]"Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2."
Korsgren C., Lawler J., Lambert S., Speicher D., Cohen C.M.
Proc. Natl. Acad. Sci. U.S.A. 87:613-617(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE (ISOFORM SHORT).
Tissue: Reticulocyte.
[3]"Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane."
Sung L.A., Chien S., Chang L.-S., Lambert K., Bliss S.A., Bouhassira E.E., Nagel R.L., Schwartz R.S., Rybicki A.C.
Proc. Natl. Acad. Sci. U.S.A. 87:955-959(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Reticulocyte.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
[7]"Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated."
Risinger M.A., Dotimas E.M., Cohen C.M.
J. Biol. Chem. 267:5680-5685(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[8]"Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2)."
Dotimas E., Speicher D.W., Guptaroy B., Cohen C.M.
Biochim. Biophys. Acta 1148:19-29(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-248.
[9]"An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2 Nippon)."
Bouhassira E.E., Schwartz R.S., Yawata Y., Ata K., Kanzaki A., Qiu J.J.-H., Nagel R.L., Rybicki A.C.
Blood 79:1846-1854(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPH5 THR-112.
[10]"A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka)."
Takaoka Y., Ideguchi H., Matsuda M., Sakamoto N., Takeuchi T., Fukumaki Y.
Br. J. Haematol. 88:527-533(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPH5 THR-112.
[11]"A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia."
Hayette S., Morle L., Bozon M., Ghanem A., Risinger M., Korsgren C., Tanner M.J.A., Fattoum S., Cohen C.M., Delaunay J.
Br. J. Haematol. 89:762-770(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPH5 GLN-280.
[12]"Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT results in band 4.2 deficiency and microspherocytosis."
Kanzaki A., Yasunaga M., Okamoto N., Inoue T., Yawata A., Wada H., Andoh A., Hodohara K., Fujiyama Y., Bamba T., Harano T., Harano K., Yawata Y.
Br. J. Haematol. 91:333-340(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPH5 THR-112 AND CYS-287.
[13]"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."
Kanzaki A., Yawata Y., Yawata A., Inoue T., Okamoto N., Wada H., Harano T., Harano K., Wilmotte R., Hayette S., Nakamura Y., Niki T., Kawamura Y., Nakamura S., Matsuda T.
Int. J. Hematol. 61:165-178(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPH5 TYR-145.
[14]"4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis."
Perrotta S., Iolascon A., Polito R., d'Urzo G., Conte M.L., Miraglia del Giudice E.
Haematologica 84:660-662(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPH5 THR-112.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60298 mRNA. Translation: AAA74589.1.
L06519 expand/collapse EMBL AC list , L06447, L06448, L06449, L06450, L06511, L06512, L06513, L06515, L06516, L06517, L06518 Genomic DNA. Translation: AAA52385.1.
M29399 mRNA. Translation: AAA35798.1.
M30647 mRNA. Translation: AAA36401.1. Frameshift.
M30646 mRNA. Translation: AAA36402.1. Frameshift.
AC068724 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92591.1.
BC096093 mRNA. Translation: AAH96093.1.
BC096094 mRNA. Translation: AAH96094.1.
PIRA39707.
RefSeqNP_000110.2. NM_000119.2.
NP_001107606.1. NM_001114134.1.
UniGeneHs.368642.

3D structure databases

ProteinModelPortalP16452.
SMRP16452. Positions 5-689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108352. 6 interactions.
IntActP16452. 3 interactions.
STRING9606.ENSP00000300215.

PTM databases

PhosphoSiteP16452.

Polymorphism databases

DMDM215274164.

Proteomic databases

PaxDbP16452.
PRIDEP16452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300215; ENSP00000300215; ENSG00000166947. [P16452-2]
ENST00000441366; ENSP00000396616; ENSG00000166947. [P16452-1]
GeneID2038.
KEGGhsa:2038.
UCSCuc001zqz.4. human. [P16452-1]
uc001zrb.4. human. [P16452-2]

Organism-specific databases

CTD2038.
GeneCardsGC15M043398.
HGNCHGNC:3381. EPB42.
HPAHPA040261.
MIM177070. gene.
612690. phenotype.
neXtProtNX_P16452.
Orphanet822. Hereditary spherocytosis.
PharmGKBPA27814.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87163.
HOGENOMHOG000231695.
HOVERGENHBG106048.
InParanoidP16452.
OMASCFAQED.
OrthoDBEOG7Z0JVS.
PhylomeDBP16452.
TreeFamTF324278.

Gene expression databases

ArrayExpressP16452.
BgeeP16452.
CleanExHS_EPB42.
GenevestigatorP16452.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiProtein_4.2.
GenomeRNAi2038.
NextBio8277.
PROP16452.
SOURCESearch...

Entry information

Entry nameEPB42_HUMAN
AccessionPrimary (citable) accession number: P16452
Secondary accession number(s): Q4VB97
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM