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P14317 (HCLS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hematopoietic lineage cell-specific protein
Alternative name(s):
Hematopoietic cell-specific LYN substrate 1
LckBP1
p75
Gene names
Name:HCLS1
Synonyms:HS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression.

Subunit structure

Associates with the SH2 and SH3 domains of LCK. Binding to he LCK SH3 domain occurs constitutively, while binding to the LCK SH2 domain occurs only upon TCR stimulation. A similar binding pattern was observed with LYN, but not with FYN in which the FYN SH2 region associates upon TCR stimulation but the FYN SH3 region does not associate regardless of TCR stimulation. Directly associates with HAX1, through binding to its C-terminal region. Interacts with HS1BP3. Interacts with FES/FPS By similarity. Interacts (via SH2 domain) with FGR. Forms a multiprotein complex with LYN and ANKRD54 By similarity. Ref.7 Ref.10 Ref.11

Subcellular location

Membrane; Peripheral membrane protein. Cytoplasm. Mitochondrion Probable Ref.7.

Tissue specificity

Expressed only in tissues and cells of hematopoietic origin.

Developmental stage

Expressed in early stage of myeloid and erythroid differentiation.

Post-translational modification

Phosphorylated by FES By similarity. Phosphorylated by LYN, FYN and FGR after cross-linking of surface IgM on B-cells. Phosphorylation by LYN, FYN and FGR requires prior phosphorylation by SYK or FES. Ref.7 Ref.9 Ref.11

Sequence similarities

Contains 4 cortactin repeats.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Mitochondrion
   Coding sequence diversityPolymorphism
   DomainRepeat
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament polymerization

Inferred from electronic annotation. Source: InterPro

cellular response to cytokine stimulus

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Traceable author statement PubMed 8978766. Source: ProtInc

negative regulation of leukocyte apoptotic process

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin cytoskeleton reorganization

Inferred by curator PubMed 23001182. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of granulocyte differentiation

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of macrophage differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of transcription factor import into nucleus

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of STAT protein

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: ProtInc

response to hormone

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 23001182. Source: BHF-UCL

   Molecular_functionRNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 23001182. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 21398607. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 23001182. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WIPF1O435162EBI-750369,EBI-346356

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Hematopoietic lineage cell-specific protein
PRO_0000083921

Regions

Repeat79 – 11537Cortactin 1
Repeat116 – 15237Cortactin 2
Repeat153 – 18937Cortactin 3
Repeat190 – 21223Cortactin 4; truncated
Domain428 – 48659SH3
Region27 – 6640Involved in HAX-1 binding

Amino acid modifications

Modified residue411N6-acetyllysine Ref.15
Modified residue1031Phosphotyrosine
Modified residue1231N6-acetyllysine Ref.15
Modified residue1401Phosphotyrosine By similarity
Modified residue1921N6-acetyllysine Ref.15
Modified residue1981Phosphotyrosine Ref.12 Ref.13
Modified residue2221Phosphotyrosine; by FGR Ref.9 Ref.11
Modified residue2411N6-acetyllysine Ref.15
Modified residue2751Phosphoserine Ref.14
Modified residue3081Phosphothreonine Ref.14
Modified residue3781Phosphotyrosine; by SYK and FES By similarity
Modified residue3971Phosphotyrosine; by SYK and FES By similarity

Natural variations

Natural variant2351T → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs2070179 [ dbSNP | Ensembl ].
VAR_055006
Natural variant3611E → K.
Corresponds to variant rs2070180 [ dbSNP | Ensembl ].
VAR_055007
Natural variant4361V → L. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs9869984 [ dbSNP | Ensembl ].
VAR_056910

Experimental info

Sequence conflict241 – 2422KF → FK AA sequence Ref.8
Sequence conflict4861E → D in CAG33075. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P14317 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 20AE72A28DA33DFB

FASTA48654,014
        10         20         30         40         50         60 
MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE HINIHQLRNK 

        70         80         90        100        110        120 
VSEEHDVLRK KEMESGPKAS HGYGGRFGVE RDRMDKSAVG HEYVAEVEKH SSQTDAAKGF 

       130        140        150        160        170        180 
GGKYGVERDR ADKSAVGFDY KGEVEKHTSQ KDYSRGFGGR YGVEKDKWDK AALGYDYKGE 

       190        200        210        220        230        240 
TEKHESQRDY AKGFGGQYGI QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGTRGLKA 

       250        260        270        280        290        300 
KFESMAEEKR KREEEEKAQQ VARRQQERKA VTKRSPEAPQ PVIAMEEPAV PAPLPKKISS 

       310        320        330        340        350        360 
EAWPPVGTPP SSESEPVRTS REHPVPLLPI RQTLPEDNEE PPALPPRTLE GLQVEEEPVY 

       370        380        390        400        410        420 
EAEPEPEPEP EPEPENDYED VEEMDRHEQE DEPEGDYEEV LEPEDSSFSS ALAGSSGCPA 

       430        440        450        460        470        480 
GAGAGAVALG ISAVAVYDYQ GEGSDELSFD PDDVITDIEM VDEGWWRGRC HGHFGLFPAN 


YVKLLE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage."
Kitamura D., Kaneko H., Miyagoe Y., Ariyasu T., Watanabe T.
Nucleic Acids Res. 17:9367-9379(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-235 AND LEU-436.
[2]"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], VARIANTS ALA-235 AND LEU-436.
[3]"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], VARIANTS ALA-235 AND LEU-436.
Tissue: Spleen.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-235 AND LEU-436.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
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], VARIANTS ALA-235 AND LEU-436.
Tissue: Lymph.
[7]"Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling."
Yamanashi Y., Okada M., Semba T., Yamori T., Umemori H., Tsunasawa S., Toyoshima K., Kitamura D., Watanabe T., Yamamoto T.
Proc. Natl. Acad. Sci. U.S.A. 90:3631-3635(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 4-26; 79-95; 134-146; 208-223 AND 274-289, INTERACTION WITH LYN, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Tissue: B-cell lymphoma.
[8]"Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 97-108; 193-201 AND 240-248.
[9]"SH2 domains mediate the sequential phosphorylation of HS1 protein by p72syk and Src-related protein tyrosine kinases."
Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.
Biochemistry 35:5327-5332(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-222 AND TYR-397, PHOSPHORYLATION BY SYK; LYN; FYN AND FGR.
[10]"HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases."
Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U., Watanabe T.
J. Immunol. 158:2736-2744(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAX1.
[11]"Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fgr protein-tyrosine kinase."
Brunati A.M., Donella-Deana A., James P., Quadroni M., Contri A., Marin O., Pinna L.A.
J. Biol. Chem. 274:7557-7564(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-222 AND TYR-397, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FGR.
[12]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-123; LYS-192 AND LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16663 mRNA. Translation: CAA34651.1.
BT006824 mRNA. Translation: AAP35470.1.
AK312750 mRNA. Translation: BAG35617.1.
CR456794 mRNA. Translation: CAG33075.1.
AC133750 Genomic DNA. No translation available.
BC016758 mRNA. Translation: AAH16758.1.
CCDSCCDS3003.1.
PIRS07633.
UniGeneHs.14601.

3D structure databases

ProteinModelPortalP14317.
SMRP14317. Positions 429-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109309. 20 interactions.
IntActP14317. 12 interactions.
MINTMINT-1343660.
STRING9606.ENSP00000320176.

PTM databases

PhosphoSiteP14317.

Polymorphism databases

DMDM317373440.

Proteomic databases

MaxQBP14317.
PaxDbP14317.
PRIDEP14317.

Protocols and materials databases

DNASU3059.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314583; ENSP00000320176; ENSG00000180353.
KEGGhsa:3059.
UCSCuc003eeh.4. human.

Organism-specific databases

CTD3059.
GeneCardsGC03M121350.
HGNCHGNC:4844. HCLS1.
HPAHPA019143.
MIM601306. gene.
neXtProtNX_P14317.
PharmGKBPA29220.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG123488.
HOGENOMHOG000006523.
HOVERGENHBG005994.
InParanoidP14317.
KOK06106.
OMAEMDRHEQ.
OrthoDBEOG7V49ZC.
PhylomeDBP14317.
TreeFamTF318935.

Gene expression databases

ArrayExpressP14317.
BgeeP14317.
CleanExHS_HCLS1.
GenevestigatorP14317.

Family and domain databases

InterProIPR028534. HS1.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10829:SF5. PTHR10829:SF5. 1 hit.
PfamPF02218. HS1_rep. 4 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51090. CORTACTIN. 4 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHCLS1. human.
GeneWikiHCLS1.
GenomeRNAi3059.
NextBio12103.
PMAP-CutDBP14317.
PROP14317.
SOURCESearch...

Entry information

Entry nameHCLS1_HUMAN
AccessionPrimary (citable) accession number: P14317
Secondary accession number(s): Q53Y93, Q6IBK9, Q9UDK0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 157 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 3

Human chromosome 3: entries, gene names and cross-references to MIM