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P51636 (CAV2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caveolin-2
Gene names
Name:CAV2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression By similarity. Ref.10 Ref.11

Subunit structure

Monomer or homodimer. Interacts with CAV1; the interaction forms a stable heterooligomeric complex that is required for targeting to lipid rafts and for caveolae formation. Tyrosine phosphorylated forms do not form heterooligomers with the Tyr-19-phosphorylated form existing as a monomer or dimer, and the Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-phosphorylated form) is increased on insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with STAT3; the interaction is increased on insulin-induced tyrosine phosphorylation leading to STAT activation By similarity. Ref.2 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membranecaveola; Peripheral membrane protein. Note: Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin By similarity. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11

Tissue specificity

Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts. Ref.2

Post-translational modification

Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells By similarity. Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin By similarity. Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the caveolin family.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcaveola assembly

Inferred from mutant phenotype PubMed 12633858. Source: BHF-UCL

endoplasmic reticulum organization

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of dopamine receptor signaling pathway

Inferred from mutant phenotype PubMed 15569306. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of mitosis

Inferred from expression pattern Ref.11. Source: BHF-UCL

skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission

Inferred from electronic annotation. Source: Ensembl

vesicle docking

Inferred from direct assay PubMed 12743374. Source: BHF-UCL

vesicle fusion

Inferred from direct assay PubMed 12743374. Source: BHF-UCL

vesicle organization

Inferred from direct assay PubMed 12743374. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: BHF-UCL

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

acrosomal membrane

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from direct assay PubMed 15703204Ref.11. Source: BHF-UCL

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from direct assay PubMed 22792322. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 15569306. Source: BHF-UCL

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: MGI

intracellular

Inferred from direct assay PubMed 15703204. Source: BHF-UCL

lipid particle

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 15569306PubMed 15569306PubMed 15569306. Source: BHF-UCL

membrane raft

Inferred from direct assay PubMed 11294831. Source: HGNC

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay Ref.11. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 15569306. Source: BHF-UCL

protein complex

Inferred from electronic annotation. Source: Ensembl

transport vesicle

Inferred from direct assay. Source: LIFEdb

   Molecular_functionD1 dopamine receptor binding

Inferred from physical interaction PubMed 15569306. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19931615. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]
Isoform Alpha (identifier: P51636-1)

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.
Isoform Beta (identifier: P51636-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.
Note: Produced by alternative initiation.
Isoform C (identifier: P51636-3)

The sequence of this isoform differs from the canonical sequence as follows:
     51-112: LGFEDVIAEP...LFATLSCLHI → DFNAFCKDLP...WTPGLEIGIL
     113-162: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Caveolin-2
PRO_0000004772

Regions

Topological domain1 – 8686Cytoplasmic Potential
Intramembrane87 – 10721Helical; Potential
Topological domain108 – 16255Cytoplasmic Potential

Amino acid modifications

Modified residue191Phosphotyrosine; by SRC Ref.9 Ref.10
Modified residue231Phosphoserine Ref.11
Modified residue271Phosphotyrosine; by SRC Ref.10
Modified residue361Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 1313Missing in isoform Beta.
VSP_018696
Alternative sequence51 – 11262LGFED…SCLHI → DFNAFCKDLPNGSAFSADNM EECDRCYHCSIVYERRTMLL FCQPATEPGLNTWTPGLEIG IL in isoform C.
VSP_038114
Alternative sequence113 – 16250Missing in isoform C.
VSP_038115
Natural variant1301Q → E.
Corresponds to variant rs8940 [ dbSNP | Ensembl ].
VAR_012071

Experimental info

Mutagenesis191Y → A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated tyrosine phosphorylation and binding to RASA1, SRC and NCK1; when associated with A-27. Ref.10
Mutagenesis231S → A: Abolishes phosphorylation. Ref.11
Mutagenesis271Y → A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated phosphorylation and binding of RASA1, SRC and NCK1; when associated with A-19. Ref.10
Mutagenesis361S → A: Abolishes phosphorylation. Ref.11

Sequences

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

Last modified July 15, 1999. Version 2.
Checksum: 89FDEDA861330B87

FASTA16218,291
        10         20         30         40         50         60 
MGLETEKADV QLFMDDDSYS HHSGLEYADP EKFADSDQDR DPHRLNSHLK LGFEDVIAEP 

        70         80         90        100        110        120 
VTTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK 

       130        140        150        160 
TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR CFSSVSLQLS QD 

« Hide

Isoform Beta [UniParc].

Checksum: 0706B574F5E1AAD8
Show »

FASTA14916,829
Isoform C [UniParc].

Checksum: 7C60DC5ABD6B0105
Show »

FASTA11212,780

References

« Hide 'large scale' references
[1]"Identification, sequence, and expression of caveolin-2 defines a caveolin gene family."
Scherer P.E., Okamoto T., Chun M., Nishimoto I., Lodish H.F., Lisanti M.P.
Proc. Natl. Acad. Sci. U.S.A. 93:131-135(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[2]"Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo."
Scherer P.E., Lewis R.Y., Volonte D., Engelman J.A., Galbiati F., Couet J., Kohtz D.S., van Donselaar E., Peters P., Lisanti M.P.
J. Biol. Chem. 272:29337-29346(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines."
Engelman J.A., Zhang X.L., Lisanti M.P.
FEBS Lett. 448:221-230(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
Tissue: Hepatoma.
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 ALPHA).
Tissue: Kidney.
[8]"Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes."
Li S., Galbiati F., Volonte D., Sargiacomo M., Engelman J.A., Das K., Scherer P.E., Lisanti M.P.
FEBS Lett. 434:127-134(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAV1, ALTERNATIVE PRODUCTS, SUBCELLULAR LOCATION.
[9]"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-19, SUBCELLULAR LOCATION, INTERACTION WITH CAV1; SRC; RASA1 AND NCK1.
[10]"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-19 AND TYR-27, SUBCELLULAR LOCATION, INTERACTION WITH CAV1; NCK1; RASA1 AND SRC, FUNCTION, MUTAGENESIS OF TYR-19 AND TYR-27.
[11]"Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated by targeting to lipid raft/caveolae and in mitotic endothelial cells."
Sowa G., Xie L., Xu L., Sessa W.C.
Biochemistry 47:101-111(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-23 AND SER-36, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-23 AND SER-36.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Wikipedia

Caveolin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035752 mRNA. Translation: AAB88492.1.
AJ133269 Genomic DNA. Translation: CAB63653.1.
BT007051 mRNA. Translation: AAP35700.1.
BC005256 mRNA. Translation: AAH05256.1.
AJ242718 Genomic DNA. Translation: CAB65090.1.
AK310786 mRNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24361.1.
CCDSCCDS5765.1. [P51636-3]
CCDS5766.1. [P51636-1]
RefSeqNP_001193676.1. NM_001206747.1. [P51636-2]
NP_001193677.1. NM_001206748.1.
NP_001224.1. NM_001233.4. [P51636-1]
NP_937855.1. NM_198212.2. [P51636-3]
UniGeneHs.212332.
Hs.603096.

3D structure databases

ProteinModelPortalP51636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107306. 12 interactions.
DIPDIP-34929N.
IntActP51636. 6 interactions.
MINTMINT-1403441.
STRING9606.ENSP00000222693.

PTM databases

PhosphoSiteP51636.

Proteomic databases

MaxQBP51636.
PaxDbP51636.
PRIDEP51636.

Protocols and materials databases

DNASU858.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222693; ENSP00000222693; ENSG00000105971. [P51636-1]
ENST00000343213; ENSP00000345679; ENSG00000105971. [P51636-3]
GeneID858.
KEGGhsa:858.
UCSCuc003vid.3. human. [P51636-1]
uc003vie.3. human. [P51636-3]
uc022akj.1. human. [P51636-2]

Organism-specific databases

CTD858.
GeneCardsGC07P115926.
HGNCHGNC:1528. CAV2.
HPACAB013488.
HPA044810.
MIM601048. gene.
neXtProtNX_P51636.
PharmGKBPA26108.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG74268.
HOGENOMHOG000036550.
HOVERGENHBG003422.
InParanoidP51636.
KOK12958.
OMASTHSFDK.
OrthoDBEOG7V1FSD.
PhylomeDBP51636.
TreeFamTF315736.

Enzyme and pathway databases

SignaLinkP51636.

Gene expression databases

ArrayExpressP51636.
BgeeP51636.
CleanExHS_CAV2.
GenevestigatorP51636.

Family and domain databases

InterProIPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERPTHR10844. PTHR10844. 1 hit.
PfamPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAV2. human.
GeneWikiCaveolin_2.
GenomeRNAi858.
NextBio3560.
PROP51636.
SOURCESearch...

Entry information

Entry nameCAV2_HUMAN
AccessionPrimary (citable) accession number: P51636
Secondary accession number(s): A4D0U2, Q9UGM7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 141 of the entry and version 2 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 7

Human chromosome 7: entries, gene names and cross-references to MIM