Q92608 (DOCK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dedicator of cytokinesis protein 2

Gene names

Name:	DOCK2
Synonyms:	KIAA0209

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1830 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2. Ref.14
Subunit structure	Homodimer Probable. Interacts with RAC1 and RAC2. Interacts with CRKL and VAV. Interacts with CD3Z. Ref.3 Ref.4 Ref.5 Ref.14
Subcellular location	Endomembrane system; Peripheral membrane protein. Cytoplasm › cytoskeleton. Note: Colocalizes with F-actin. Ref.4
Tissue specificity	Specifically expressed in hematopoietic cells. Highly expressed in peripheral blood leukocytes, and expressed at intermediate level in thymus and spleen. Expressed at very low level in the small intestine and colon. Ref.3
Domain	The DHR-2 domain may mediate the GEF activity By similarity.
Sequence similarities	Belongs to the DOCK family. Contains 1 DHR-1 domain. Contains 1 DHR-2 domain. Contains 1 SH3 domain.
Sequence caution	The sequence BAA13200.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH3 domain
Molecular function	Guanine-nucleotide releasing factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Traceable author statement Ref.5. Source: UniProtKB alpha-beta T cell proliferation Inferred from electronic annotation. Source: Compara chemotaxis Inferred from electronic annotation. Source: Compara establishment of T cell polarity Inferred from electronic annotation. Source: Compara immunological synapse formation Inferred from electronic annotation. Source: Compara macropinocytosis Inferred from sequence or structural similarity. Source: UniProtKB membrane raft polarization Inferred from electronic annotation. Source: Compara myeloid dendritic cell activation involved in immune response Inferred from sequence or structural similarity. Source: UniProtKB negative thymic T cell selection Inferred from electronic annotation. Source: Compara positive regulation of phagocytosis Inferred from sequence or structural similarity. Source: UniProtKB positive thymic T cell selection Inferred from electronic annotation. Source: Compara regulation of defense response to virus by virus Traceable author statement. Source: Reactome small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	Rac GTPase activator activity Inferred from electronic annotation. Source: Compara Rac guanyl-nucleotide exchange factor activity Inferred from direct assay Ref.3. Source: UniProtKB T cell receptor binding Inferred from direct assay Ref.5. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92608-1)

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 2 (identifier: Q92608-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-449: Missing.
     462-494: Missing.
     630-766: Missing.
     934-955: SHFVACMTAILNQMGDQHYSFY → GACCNCGFPSSTPHSLIQWLWG
     956-1830: Missing.

Note: Splicing donor and acceptor sites between exon 6 and exon 7 are not canonical. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1830

1830

Dedicator of cytokinesis protein 2

PRO_0000189986

Regions

Domain

8 – 69

62

SH3

Domain

423 – 607

185

DHR-1

Domain

1211 – 1622

412

DHR-2

Region

939 – 1476

538

Interaction with CRKL

Amino acid modifications

Modified residue

304

1

N6-acetyllysine Ref.11

Modified residue

588

1

Phosphoserine Ref.10

Modified residue

593

1

Phosphoserine Ref.10

Modified residue

738

1

N6-acetyllysine Ref.11

Modified residue

1685

1

Phosphoserine Ref.8 Ref.9 Ref.10

Modified residue

1706

1

Phosphoserine By similarity

Modified residue

1731

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

1 – 449

449

Missing in isoform 2.

VSP_007696

Alternative sequence

462 – 494

33

Missing in isoform 2.

VSP_007697

Alternative sequence

630 – 766

137

Missing in isoform 2.

VSP_007698

Alternative sequence

934 – 955

22

SHFVA…HYSFY → GACCNCGFPSSTPHSLIQWL WG in isoform 2.

VSP_007699

Alternative sequence

956 – 1830

875

Missing in isoform 2.

VSP_007700

Natural variant

1558

1

D → A.
Corresponds to variant rs13179480 [ dbSNP | Ensembl ].

VAR_053064

Natural variant

1746

1

S → T.
Corresponds to variant rs2270898 [ dbSNP | Ensembl ].

VAR_015822

Natural variant

1779

1

T → S.
Corresponds to variant rs2270898 [ dbSNP | Ensembl ].

VAR_022137

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1830

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Beta strand

34 – 41

8

Beta strand

44 – 49

6

Beta strand

52 – 60

9

Helix

61 – 63

3

Beta strand

64 – 67

4

Helix

84 – 107

24

Helix

111 – 133

23

Helix

138 – 158

21

Helix

1197 – 1214

18

Helix

1217 – 1233

17

Helix

1237 – 1248

12

Turn

1265 – 1267

3

Helix

1273 – 1291

19

Helix

1294 – 1310

17

Helix

1315 – 1334

20

Beta strand

1342 – 1349

8

Turn

1354 – 1358

5

Beta strand

1359 – 1364

6

Helix

1371 – 1381

11

Beta strand

1385 – 1387

3

Helix

1396 – 1400

5

Beta strand

1405 – 1414

10

Helix

1419 – 1421

3

Beta strand

1422 – 1424

3

Helix

1428 – 1436

9

Beta strand

1437 – 1449

13

Helix

1458 – 1461

4

Beta strand

1462 – 1492

31

Helix

1494 – 1518

25

Beta strand

1520 – 1522

3

Helix

1525 – 1535

11

Beta strand

1538 – 1540

3

Helix

1544 – 1550

7

Helix

1553 – 1558

6

Helix

1560 – 1562

3

Helix

1563 – 1589

27

Helix

1593 – 1595

3

Helix

1596 – 1617

22

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 3, 2003. Version 2. Checksum: 18568D3322DAA92A	FASTA	1,830	211,948
	10 20 30 40 50 60 MAPWRKADKE RHGVAIYNFQ GSGAPQLSLQ IGDVVRIQET CGDWYRGYLI KHKMLQGIFP 70 80 90 100 110 120 KSFIHIKEVT VEKRRNTENI IPAEIPLAQE VTTTLWEWGS IWKQLYVASK KERFLQVQSM 130 140 150 160 170 180 MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS KIDYGNKILE LDLIVRDEDG NILDPDNTSV 190 200 210 220 230 240 ISLFHAHEEA TDKITERIKE EMSKDQPDYA MYSRISSSPT HSLYVFVRNF VCRIGEDAEL 250 260 270 280 290 300 FMSLYDPNKQ TVISENYLVR WGSRGFPKEI EMLNNLKVVF TDLGNKDLNR DKIYLICQIV 310 320 330 340 350 360 RVGKMDLKDT GAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF HPVTAENDFL 370 380 390 400 410 420 HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL VDRTTVVARK LGFPEIIMPG 430 440 450 460 470 480 DVRNDIYITL LQGDFDKYNK TTQRNVEVIM CVCAEDGKTL PNAICVGAGD KPMNEYRSVV 490 500 510 520 530 540 YYQVKQPRWM ETVKVAVPIE DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT 550 560 570 580 590 600 TLHDGFHDLV VLKGDSKKME DASAYLTLPS YRHHVENKGA TLSRSSSSVG GLSVSSRDVF 610 620 630 640 650 660 SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ DTLDALFNIM 670 680 690 700 710 720 MEHSQSDEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI QQHFSATLAY KKLMTVLKTY 730 740 750 760 770 780 LDTSSRGEQC EPILRTLKAL EYVFKFIVRS RTLFSQLYEG KEQMEFEESM RRLFESINNL 790 800 810 820 830 840 MKSQYKTTIL LQVAALKYIP SVLHDVEMVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN 850 860 870 880 890 900 EIVQSNLFKK QECRDILLPV ITKELKELLE QKDDMQHQVL ERKYCVELLN SILEVLSYQD 910 920 930 940 950 960 AAFTYHHIQE IMVQLLRTVN RTVITMGRDH ILISHFVACM TAILNQMGDQ HYSFYIETFQ 970 980 990 1000 1010 1020 TSSELVDFLM ETFIMFKDLI GKNVYPGDWM AMSMVQNRVF LRAINKFAET MNQKFLEHTN 1030 1040 1050 1060 1070 1080 FEFQLWNNYF HLAVAFITQD SLQLEQFSHA KYNKILNKYG DMRRLIGFSI RDMWYKLGQN 1090 1100 1110 1120 1130 1140 KICFIPGMVG PILEMTLIPE AELRKATIPI FFDMMLCEYQ RSGDFKKFEN EIILKLDHEV 1150 1160 1170 1180 1190 1200 EGGRGDEQYM QLLESILMEC AAEHPTIAKS VENFVNLVKG LLEKLLDYRG VMTDESKDNR 1210 1220 1230 1240 1250 1260 MSCTVNLLNF YKDNNREEMY IRYLYKLRDL HLDCDNYTEA AYTLLLHTWL LKWSDEQCAS 1270 1280 1290 1300 1310 1320 QVMQTGQQHP QTHRQLKETL YETIIGYFDK GKMWEEAISL CKELAEQYEM EIFDYELLSQ 1330 1340 1350 1360 1370 1380 NLIQQAKFYE SIMKILRPKP DYFAVGYYGQ GFPSFLRNKV FIYRGKEYER REDFQMQLMT 1390 1400 1410 1420 1430 1440 QFPNAEKMNT TSAPGDDVKN APGQYIQCFT VQPVLDEHPR FKNKPVPDQI INFYKSNYVQ 1450 1460 1470 1480 1490 1500 RFHYSRPVRR GTVDPENEFA SMWIERTSFV TAYKLPGILR WFEVVHMSQT TISPLENAIE 1510 1520 1530 1540 1550 1560 TMSTANEKIL MMINQYQSDE TLPINPLSML LNGIVDPAVM GGFAKYEKAF FTEEYVRDHP 1570 1580 1590 1600 1610 1620 EDQDKLTHLK DLIAWQIPFL GAGIKIHEKR VSDNLRPFHD RMEECFKNLK MKVEKEYGVR 1630 1640 1650 1660 1670 1680 EMPDFDDRRV GRPRSMLRSY RQMSIISLAS MNSDCSTPSK PTSESFDLEL ASPKTPRVEQ 1690 1700 1710 1720 1730 1740 EEPISPGSTL PEVKLRRSKK RTKRSSVVFA DEKAAAESDL KRLSRKHEFM SDTNLSEHAA 1750 1760 1770 1780 1790 1800 IPLKASVLSQ MSFASQSMPT IPALALSVAG IPGLDEANTS PRLSQTFLQL SDGDKKTLTR 1810 1820 1830 KKVNQFFKTM LASKSAEEGK QIPDSLSTDL
	Isoform 2 [UniParc]. Checksum: C5D6CAAB1C3A3490	FASTA	336	38,461
	10 20 30 40 50 60 MCVCAEDGKT LPVAVPIEDM QRIHLRFMFR HRSSLESKDK GEKNFAMSYV KLMKEDGTTL 70 80 90 100 110 120 HDGFHDLVVL KGDSKKMEDA SAYLTLPSYR HHVENKGATL SRSSSSVGGL SVSSRDVFSI 130 140 150 160 170 180 STLVCSTKLT QNVGLLGLLK WRMKPQLEES MRRLFESINN LMKSQYKTTI LLQVAALKYI 190 200 210 220 230 240 PSVLHDVEMV FDAKLLSQLL YEFYTCIPPV KLQKQKVQSM NEIVQSNLFK KQECRDILLP 250 260 270 280 290 300 VITKELKELL EQKDDMQHQV LERKYCVELL NSILEVLSYQ DAAFTYHHIQ EIMVQLLRTV 310 320 330 NRTVITMGRD HILIGACCNC GFPSSTPHSL IQWLWG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[2]	"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] (ISOFORMS 1 AND 2). Tissue: Colon and Liver.
[3]	"Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins." Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N., Kurata T., Nagashima K., Matsuda M. Biochim. Biophys. Acta 1452:179-187(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, RAC1 ACTIVATION, INTERACTION WITH RAC1 AND RAC2.
[4]	"DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines." Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S. Blood 100:3968-3974(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CRKL AND VAV.
[5]	"DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription." Nishihara H., Maeda M., Tsuda M., Makino Y., Sawa H., Nagashima K., Tanaka S. Biochem. Biophys. Res. Commun. 296:716-720(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CD3Z.
[6]	"Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity." Cote J.-F., Vuori K. J. Cell Sci. 115:4901-4913(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[7]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[8]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1685, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1685, MASS SPECTROMETRY.
[10]	"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-588; SER-593; SER-1685 AND SER-1731, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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-304 AND LYS-738, MASS SPECTROMETRY.
[12]	"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].
[13]	"The solution structure of human DOCK2 SH3 domain - ELMO1 peptide chimera complex." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2010) to the PDB data bank Cited for: STRUCTURE BY NMR OF 8-70.
[14]	"Multiple factors confer specific Cdc42 and Rac protein activation by dedicator of cytokinesis (DOCK) nucleotide exchange factors." Kulkarni K., Yang J., Zhang Z., Barford D. J. Biol. Chem. 286:25341-25351(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1192-1622 IN COMPLEX WITH RAC1, INTERACTION WITH RAC1, SUBUNIT, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86964 mRNA. Translation: BAA13200.1. Different initiation.
BC016996 mRNA. Translation: AAH16996.1.
BC104900 mRNA. Translation: AAI04901.1.
BC113457 mRNA. Translation: AAI13458.1.

IPI

IPI00022449.
IPI00099332.

RefSeq

NP_004937.1. NM_004946.2.

UniGene

Hs.586174.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RQR	NMR	-	A	8-70	[»]
2YIN	X-ray	2.70	A/B	1192-1622	[»]
3A98	X-ray	2.10	A/C	1-177	[»]
3B13	X-ray	3.01	A/C	1196-1622	[»]

ProteinModelPortal

Q92608.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31791N.

IntAct

Q92608. 2 interactions.

STRING

9606.ENSP00000256935.

PTM databases

PhosphoSite

Q92608.

Polymorphism databases

DMDM

32469765.

Proteomic databases

PaxDb

Q92608.

PeptideAtlas

Q92608.

PRIDE

Q92608.

Protocols and materials databases

DNASU

1794.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256935; ENSP00000256935; ENSG00000134516.

GeneID

1794.

KEGG

hsa:1794.

UCSC

uc003maf.3. human.

Organism-specific databases

CTD

1794.

GeneCards

GC05P169064.

HGNC

HGNC:2988. DOCK2.

HPA

HPA036468.

MIM

603122. gene.

neXtProt

NX_Q92608.

PharmGKB

PA27454.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG289808.

HOGENOM

HOG000006631.

HOVERGEN

HBG051389.

InParanoid

Q92608.

KO

K12367.

OMA

RRNTENI.

OrthoDB

EOG4MW855.

PhylomeDB

Q92608.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q92608.

Bgee

Q92608.

CleanEx

HS_DOCK2.

Genevestigator

Q92608.

GermOnline

ENSG00000134516. Homo sapiens.

Family and domain databases

InterPro

IPR009056. Cyt_c_dom.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR026799. DOCK_A.
IPR010703. DOCK_C.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

PANTHER

PTHR23317. PTHR23317. 1 hit.
PTHR23317:SF29. PTHR23317:SF29. 1 hit.

Pfam

PF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF46626. Cytochrome_c. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DOCK2. human.

GenomeRNAi

1794.

NextBio

7309.

SOURCE

Search...

Entry information

Entry name

DOCK2_HUMAN

Accession

Primary (citable) accession number: Q92608
Secondary accession number(s): Q2M3I0, Q96AK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 3, 2003
Last sequence update:	July 3, 2003
Last modified:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.