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Q99704

- DOK1_HUMAN

UniProt

Q99704 - DOK1_HUMAN

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Protein

Docking protein 1

Gene

DOK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3.1 Publication

GO - Molecular functioni

  1. receptor signaling protein activity Source: Ensembl

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. insulin receptor signaling pathway Source: Reactome
  3. Ras protein signal transduction Source: Ensembl
  4. signal transduction Source: ProtInc
  5. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_508. Signal attenuation.
REACT_570. IRS activation.
REACT_976. PI3K Cascade.
SignaLinkiQ99704.

Names & Taxonomyi

Protein namesi
Recommended name:
Docking protein 1
Alternative name(s):
Downstream of tyrosine kinase 1
p62(dok)
pp62
Gene namesi
Name:DOK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2990. DOK1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi362 – 3621Y → F: No association with NCK. No association with GAP; when associated with F-398. 1 Publication
Mutagenesisi398 – 3981Y → F: No association with GAP; when associated with F-362. 1 Publication

Organism-specific databases

PharmGKBiPA27456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481Docking protein 1PRO_0000187268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei269 – 2691Phosphoserine2 Publications
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei296 – 2961PhosphotyrosineBy similarity
Modified residuei337 – 3371PhosphotyrosineBy similarity
Modified residuei341 – 3411Phosphotyrosine1 Publication
Modified residuei362 – 3621Phosphotyrosine; by INSR3 Publications
Modified residuei377 – 3771Phosphotyrosine1 Publication
Modified residuei398 – 3981Phosphotyrosine; by INSR2 Publications
Modified residuei409 – 4091Phosphotyrosine1 Publication
Modified residuei449 – 4491PhosphotyrosineBy similarity

Post-translational modificationi

Constitutively tyrosine-phosphorylated. Phosphorylated by TEC (By similarity). Phosphorylated by LYN (By similarity). Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway. Phosphorylated on tyrosine residues by SRMS.By similarity7 Publications
Isoform 3 contains a N-acetylmethionine at position 1.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99704.
PaxDbiQ99704.
PRIDEiQ99704.

PTM databases

PhosphoSiteiQ99704.

Expressioni

Tissue specificityi

Expressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells. Expressed in breast cancer.1 Publication

Gene expression databases

BgeeiQ99704.
CleanExiHS_DOK1.
ExpressionAtlasiQ99704. baseline and differential.
GenevestigatoriQ99704.

Organism-specific databases

HPAiCAB004224.
HPA048561.

Interactioni

Subunit structurei

Interacts with ABL1 (By similarity). Interacts with RasGAP and INPP5D/SHIP1. Interacts directly with phosphorylated ITGB3. Interacts with SRMS (via the SH2 and SH3 domains).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cbll1Q9JIY22EBI-1384360,EBI-7644904From a different organism.
ERBB2P046262EBI-1384360,EBI-641062
ORFQ9Q2G42EBI-1384360,EBI-6248094From a different organism.
SRMSQ9H3Y67EBI-1384360,EBI-8541270

Protein-protein interaction databases

BioGridi108131. 35 interactions.
IntActiQ99704. 11 interactions.
MINTiMINT-1494101.
STRINGi9606.ENSP00000233668.

Structurei

Secondary structure

1
481
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi153 – 1597
Helixi163 – 1675
Beta strandi172 – 1787
Beta strandi180 – 1889
Beta strandi195 – 2028
Helixi203 – 2053
Beta strandi206 – 2116
Beta strandi213 – 2208
Beta strandi228 – 2347
Helixi238 – 25114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V76X-ray1.60A/B/C/D152-256[»]
ProteinModelPortaliQ99704.
SMRiQ99704. Positions 4-119, 153-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99704.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 119116PHAdd
BLAST
Domaini151 – 259109IRS-type PTBPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi280 – 31839Pro-richAdd
BLAST
Compositional biasi356 – 43378Pro-richAdd
BLAST

Domaini

The PTB domain mediates receptor interaction.

Sequence similaritiesi

Belongs to the DOK family. Type A subfamily.Curated
Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation
Contains 1 PH domain.Curated

Phylogenomic databases

eggNOGiNOG243145.
GeneTreeiENSGT00730000110348.
HOGENOMiHOG000112245.
HOVERGENiHBG018962.
InParanoidiQ99704.
KOiK14752.
OMAiWPYTLLR.
OrthoDBiEOG77WWC5.
PhylomeDBiQ99704.
TreeFamiTF324994.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR002404. Insln_rcpt_S1.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF02174. IRS. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
PROSITEiPS51064. IRS_PTB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: Q99704-1) [UniParc]FASTAAdd to Basket

Also known as: p62Dok1

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.

« Hide

        10         20         30         40         50
MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS
60 70 80 90 100
GGGRGSSRRL DCKVIRLAEC VSVAPVTVET PPEPGATAFR LDTAQRSHLL
110 120 130 140 150
AADAPSSAAW VQTLCRNAFP KGSWTLAPTD NPPKLSALEM LENSLYSPTW
160 170 180 190 200
EGSQFWVTVQ RTEAAERCGL HGSYVLRVEA ERLTLLTVGA QSQILEPLLS
210 220 230 240 250
WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND IFQAVETAIH
260 270 280 290 300
RQKAQGKAGQ GHDVLRADSH EGEVAEGKLP SPPGPQELLD SPPALYAEPL
310 320 330 340 350
DSLRIAPCPS QDSLYSDPLD STSAQAGEGV QRKKPLYWDL YEHAQQQLLK
360 370 380 390 400
AKLTDPKEDP IYDEPEGLAP VPPQGLYDLP REPKDAWWCQ ARVKEEGYEL
410 420 430 440 450
PYNPATDDYA VPPPRSTKPL LAPKPQGPAF PEPGTATGSG IKSHNSALYS
460 470 480
QVQKSGASGS WDCGLSRVGT DKTGVKSEGS T
Length:481
Mass (Da):52,392
Last modified:May 1, 1997 - v1
Checksum:iE9D947831244BA6C
GO
Isoform 2 (identifier: Q99704-2) [UniParc]FASTAAdd to Basket

Also known as: p22Dokdel

The sequence of this isoform differs from the canonical sequence as follows:
     153-177: SQFWVTVQRTEAAERCGLHGSYVLR → HVLFRGRPPLPLRPWNLHLPDGTGK
     178-481: Missing.

Show »
Length:177
Mass (Da):19,370
Checksum:i91A504A89EB6ED15
GO
Isoform 3 (identifier: Q99704-3) [UniParc]FASTAAdd to Basket

Also known as: p44Dok

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Note: Produced by alternative initiation at Met-140 of isoform 1. Contains a N-acetylmethionine at position 1.

Show »
Length:342
Mass (Da):37,405
Checksum:iDEF8E9DF694C38C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2020MDGAV…RFGTK → RLPAQASATREREPRWSPFQ in AAB88182. 1 PublicationCuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 139139Missing in isoform 3. CuratedVSP_038224Add
BLAST
Alternative sequencei153 – 17725SQFWV…SYVLR → HVLFRGRPPLPLRPWNLHLP DGTGK in isoform 2. 1 PublicationVSP_003852Add
BLAST
Alternative sequencei178 – 481304Missing in isoform 2. 1 PublicationVSP_003853Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70987 mRNA. Translation: AAC51127.1.
AF180527 mRNA. Translation: AAF19167.1.
AF035299 mRNA. Translation: AAB88182.1.
AC005033 Genomic DNA. Translation: AAX93224.1.
BC114440 mRNA. Translation: AAI14441.1.
CCDSiCCDS1954.1. [Q99704-1]
CCDS56125.1. [Q99704-3]
RefSeqiNP_001184189.1. NM_001197260.1. [Q99704-3]
NP_001372.1. NM_001381.3. [Q99704-1]
XP_005264237.1. XM_005264180.1. [Q99704-2]
XP_006712022.1. XM_006711959.1. [Q99704-3]
UniGeneiHs.103854.

Genome annotation databases

EnsembliENST00000233668; ENSP00000233668; ENSG00000115325. [Q99704-1]
ENST00000340004; ENSP00000344330; ENSG00000115325. [Q99704-2]
ENST00000409429; ENSP00000387016; ENSG00000115325. [Q99704-3]
GeneIDi1796.
KEGGihsa:1796.
UCSCiuc002smr.3. human. [Q99704-1]

Polymorphism databases

DMDMi17366642.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70987 mRNA. Translation: AAC51127.1 .
AF180527 mRNA. Translation: AAF19167.1 .
AF035299 mRNA. Translation: AAB88182.1 .
AC005033 Genomic DNA. Translation: AAX93224.1 .
BC114440 mRNA. Translation: AAI14441.1 .
CCDSi CCDS1954.1. [Q99704-1 ]
CCDS56125.1. [Q99704-3 ]
RefSeqi NP_001184189.1. NM_001197260.1. [Q99704-3 ]
NP_001372.1. NM_001381.3. [Q99704-1 ]
XP_005264237.1. XM_005264180.1. [Q99704-2 ]
XP_006712022.1. XM_006711959.1. [Q99704-3 ]
UniGenei Hs.103854.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V76 X-ray 1.60 A/B/C/D 152-256 [» ]
ProteinModelPortali Q99704.
SMRi Q99704. Positions 4-119, 153-283.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108131. 35 interactions.
IntActi Q99704. 11 interactions.
MINTi MINT-1494101.
STRINGi 9606.ENSP00000233668.

PTM databases

PhosphoSitei Q99704.

Polymorphism databases

DMDMi 17366642.

Proteomic databases

MaxQBi Q99704.
PaxDbi Q99704.
PRIDEi Q99704.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233668 ; ENSP00000233668 ; ENSG00000115325 . [Q99704-1 ]
ENST00000340004 ; ENSP00000344330 ; ENSG00000115325 . [Q99704-2 ]
ENST00000409429 ; ENSP00000387016 ; ENSG00000115325 . [Q99704-3 ]
GeneIDi 1796.
KEGGi hsa:1796.
UCSCi uc002smr.3. human. [Q99704-1 ]

Organism-specific databases

CTDi 1796.
GeneCardsi GC02P074776.
HGNCi HGNC:2990. DOK1.
HPAi CAB004224.
HPA048561.
MIMi 602919. gene.
neXtProti NX_Q99704.
PharmGKBi PA27456.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243145.
GeneTreei ENSGT00730000110348.
HOGENOMi HOG000112245.
HOVERGENi HBG018962.
InParanoidi Q99704.
KOi K14752.
OMAi WPYTLLR.
OrthoDBi EOG77WWC5.
PhylomeDBi Q99704.
TreeFami TF324994.

Enzyme and pathway databases

Reactomei REACT_508. Signal attenuation.
REACT_570. IRS activation.
REACT_976. PI3K Cascade.
SignaLinki Q99704.

Miscellaneous databases

EvolutionaryTracei Q99704.
GeneWikii DOK1.
GenomeRNAii 1796.
NextBioi 7317.
PROi Q99704.
SOURCEi Search...

Gene expression databases

Bgeei Q99704.
CleanExi HS_DOK1.
ExpressionAtlasi Q99704. baseline and differential.
Genevestigatori Q99704.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR002404. Insln_rcpt_S1.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF02174. IRS. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view ]
PROSITEi PS51064. IRS_PTB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells."
    Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R., Stillman B., Clarkson B.
    Cell 88:197-204(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT TYROSINE RESIDUES.
  2. "Molecular cloning of a truncated p62Dok1 isoform, p22Dokdel."
    Hubert P., Ferreira V., Debre P., Bismuth G.
    Eur. J. Immunogenet. 27:145-148(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. Yu W., Sarginson J., Gibbs R.A.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
  6. "Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt."
    Wick M.J., Dong L.Q., Hu D., Langlais P., Liu F.
    J. Biol. Chem. 276:42843-42850(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-362 AND TYR-398, MUTAGENESIS OF TYR-362 AND TYR-398.
  7. "DOK4 and DOK5: new Dok-related genes expressed in human T cells."
    Favre C., Gerard A., Clauzier E., Pontarotti P., Olive D., Nunes J.A.
    Genes Immun. 4:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-362; TYR-377; TYR-398 AND TYR-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Targeted mass spectrometric analysis of N-terminally truncated isoforms generated via alternative translation initiation."
    Kobayashi R., Patenia R., Ashizawa S., Vykoukal J.
    FEBS Lett. 583:2441-2445(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 3), ACETYLATION AT MET-1 (ISOFORM 3).
  12. "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-269; TYR-341 AND TYR-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The unique N-terminal region of SRMS regulates enzymatic activity and phosphorylation of its novel substrate Dok1."
    Goel R.K., Miah S., Black K., Kalra N., Dai C., Lukong K.E.
    FEBS J. 280:4539-4559(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SRMS.
  15. "An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding."
    Oxley C.L., Anthis N.J., Lowe E.D., Vakonakis I., Campbell I.D., Wegener K.L.
    J. Biol. Chem. 283:5420-5426(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 152-256, FUNCTION, INTERACTION WITH ITGB3.

Entry informationi

Entry nameiDOK1_HUMAN
AccessioniPrimary (citable) accession number: Q99704
Secondary accession number(s): O43204, Q53TY2, Q9UHG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3