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Q92608

- DOCK2_HUMAN

UniProt

Q92608 - DOCK2_HUMAN

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Protein

Dedicator of cytokinesis protein 2

Gene

DOCK2

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

Functioni

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 RAC2.1 Publication

GO - Molecular functioni

  1. Rac GTPase activator activity Source: Ensembl
  2. Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  3. T cell receptor binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. alpha-beta T cell proliferation Source: Ensembl
  3. chemotaxis Source: Ensembl
  4. establishment of T cell polarity Source: Ensembl
  5. immunological synapse formation Source: Ensembl
  6. macropinocytosis Source: UniProtKB
  7. membrane raft polarization Source: Ensembl
  8. myeloid dendritic cell activation involved in immune response Source: UniProtKB
  9. negative thymic T cell selection Source: Ensembl
  10. positive regulation of phagocytosis Source: UniProtKB
  11. positive thymic T cell selection Source: Ensembl
  12. regulation of defense response to virus by virus Source: Reactome
  13. small GTPase mediated signal transduction Source: InterPro
  14. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_11068. Nef and signal transduction.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Dedicator of cytokinesis protein 2
Gene namesi
Name:DOCK2
Synonyms:KIAA0209
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:2988. DOCK2.

Subcellular locationi

Endomembrane system 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: Colocalizes with F-actin.

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27454.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18301830Dedicator of cytokinesis protein 2PRO_0000189986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041N6-acetyllysine1 Publication
Modified residuei588 – 5881Phosphoserine1 Publication
Modified residuei593 – 5931Phosphoserine1 Publication
Modified residuei738 – 7381N6-acetyllysine1 Publication
Modified residuei1685 – 16851Phosphoserine3 Publications
Modified residuei1731 – 17311Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92608.
PaxDbiQ92608.
PeptideAtlasiQ92608.
PRIDEiQ92608.

PTM databases

PhosphoSiteiQ92608.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ92608.
CleanExiHS_DOCK2.
ExpressionAtlasiQ92608. baseline and differential.
GenevestigatoriQ92608.

Organism-specific databases

HPAiHPA036468.
HPA036469.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with RAC1 and RAC2. Interacts with CRKL and VAV. Interacts with CD3Z.4 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
RAC1P630003EBI-448771,EBI-413628

Protein-protein interaction databases

BioGridi108129. 9 interactions.
DIPiDIP-31791N.
IntActiQ92608. 4 interactions.
MINTiMINT-2813049.
STRINGi9606.ENSP00000256935.

Structurei

Secondary structure

1
1830
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176Combined sources
Beta strandi34 – 418Combined sources
Beta strandi44 – 496Combined sources
Beta strandi52 – 609Combined sources
Helixi61 – 633Combined sources
Beta strandi64 – 674Combined sources
Helixi84 – 10724Combined sources
Helixi111 – 13323Combined sources
Helixi138 – 15821Combined sources
Helixi1197 – 121418Combined sources
Helixi1217 – 123317Combined sources
Helixi1237 – 124812Combined sources
Turni1265 – 12673Combined sources
Helixi1273 – 129119Combined sources
Helixi1294 – 131017Combined sources
Helixi1315 – 133420Combined sources
Beta strandi1342 – 13498Combined sources
Turni1354 – 13585Combined sources
Beta strandi1359 – 13646Combined sources
Helixi1371 – 138111Combined sources
Beta strandi1385 – 13873Combined sources
Helixi1396 – 14005Combined sources
Beta strandi1405 – 141410Combined sources
Helixi1419 – 14213Combined sources
Beta strandi1422 – 14243Combined sources
Helixi1428 – 14369Combined sources
Beta strandi1437 – 144913Combined sources
Helixi1458 – 14614Combined sources
Beta strandi1462 – 149231Combined sources
Helixi1494 – 151825Combined sources
Beta strandi1520 – 15223Combined sources
Helixi1525 – 153511Combined sources
Beta strandi1538 – 15403Combined sources
Helixi1544 – 15507Combined sources
Helixi1553 – 15586Combined sources
Helixi1560 – 15623Combined sources
Helixi1563 – 158927Combined sources
Helixi1593 – 15953Combined sources
Helixi1596 – 161722Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQRNMR-A8-70[»]
2YINX-ray2.70A/B1192-1622[»]
3A98X-ray2.10A/C1-177[»]
3B13X-ray3.01A/C1196-1622[»]
ProteinModelPortaliQ92608.
SMRiQ92608. Positions 1-167, 423-609, 1196-1622.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 6962SH3PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 607185DHR-1Add
BLAST
Domaini1211 – 1622412DHR-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni939 – 1476538Interaction with CRKLAdd
BLAST

Domaini

The DHR-2 domain may mediate the GEF activity.By similarity

Sequence similaritiesi

Belongs to the DOCK family.Curated
Contains 1 DHR-1 domain.Curated
Contains 1 DHR-2 domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG289808.
GeneTreeiENSGT00610000085806.
HOGENOMiHOG000006631.
HOVERGENiHBG051389.
InParanoidiQ92608.
KOiK12367.
OMAiGDWMAMS.
OrthoDBiEOG7QNVK8.
PhylomeDBiQ92608.
TreeFamiTF300423.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR026799. DOCK_2.
IPR010703. DOCK_C.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 1 hit.
PTHR23317:SF73. PTHR23317:SF73. 1 hit.
PfamiPF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92608-1) [UniParc]FASTAAdd to Basket

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
MAPWRKADKE RHGVAIYNFQ GSGAPQLSLQ IGDVVRIQET CGDWYRGYLI
60 70 80 90 100
KHKMLQGIFP KSFIHIKEVT VEKRRNTENI IPAEIPLAQE VTTTLWEWGS
110 120 130 140 150
IWKQLYVASK KERFLQVQSM MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS
160 170 180 190 200
KIDYGNKILE LDLIVRDEDG NILDPDNTSV ISLFHAHEEA TDKITERIKE
210 220 230 240 250
EMSKDQPDYA MYSRISSSPT HSLYVFVRNF VCRIGEDAEL FMSLYDPNKQ
260 270 280 290 300
TVISENYLVR WGSRGFPKEI EMLNNLKVVF TDLGNKDLNR DKIYLICQIV
310 320 330 340 350
RVGKMDLKDT GAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF
360 370 380 390 400
HPVTAENDFL HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL
410 420 430 440 450
VDRTTVVARK LGFPEIIMPG DVRNDIYITL LQGDFDKYNK TTQRNVEVIM
460 470 480 490 500
CVCAEDGKTL PNAICVGAGD KPMNEYRSVV YYQVKQPRWM ETVKVAVPIE
510 520 530 540 550
DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT TLHDGFHDLV
560 570 580 590 600
VLKGDSKKME DASAYLTLPS YRHHVENKGA TLSRSSSSVG GLSVSSRDVF
610 620 630 640 650
SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ
660 670 680 690 700
DTLDALFNIM MEHSQSDEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI
710 720 730 740 750
QQHFSATLAY KKLMTVLKTY LDTSSRGEQC EPILRTLKAL EYVFKFIVRS
760 770 780 790 800
RTLFSQLYEG KEQMEFEESM RRLFESINNL MKSQYKTTIL LQVAALKYIP
810 820 830 840 850
SVLHDVEMVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN EIVQSNLFKK
860 870 880 890 900
QECRDILLPV ITKELKELLE QKDDMQHQVL ERKYCVELLN SILEVLSYQD
910 920 930 940 950
AAFTYHHIQE IMVQLLRTVN RTVITMGRDH ILISHFVACM TAILNQMGDQ
960 970 980 990 1000
HYSFYIETFQ TSSELVDFLM ETFIMFKDLI GKNVYPGDWM AMSMVQNRVF
1010 1020 1030 1040 1050
LRAINKFAET MNQKFLEHTN FEFQLWNNYF HLAVAFITQD SLQLEQFSHA
1060 1070 1080 1090 1100
KYNKILNKYG DMRRLIGFSI RDMWYKLGQN KICFIPGMVG PILEMTLIPE
1110 1120 1130 1140 1150
AELRKATIPI FFDMMLCEYQ RSGDFKKFEN EIILKLDHEV EGGRGDEQYM
1160 1170 1180 1190 1200
QLLESILMEC AAEHPTIAKS VENFVNLVKG LLEKLLDYRG VMTDESKDNR
1210 1220 1230 1240 1250
MSCTVNLLNF YKDNNREEMY IRYLYKLRDL HLDCDNYTEA AYTLLLHTWL
1260 1270 1280 1290 1300
LKWSDEQCAS QVMQTGQQHP QTHRQLKETL YETIIGYFDK GKMWEEAISL
1310 1320 1330 1340 1350
CKELAEQYEM EIFDYELLSQ NLIQQAKFYE SIMKILRPKP DYFAVGYYGQ
1360 1370 1380 1390 1400
GFPSFLRNKV FIYRGKEYER REDFQMQLMT QFPNAEKMNT TSAPGDDVKN
1410 1420 1430 1440 1450
APGQYIQCFT VQPVLDEHPR FKNKPVPDQI INFYKSNYVQ RFHYSRPVRR
1460 1470 1480 1490 1500
GTVDPENEFA SMWIERTSFV TAYKLPGILR WFEVVHMSQT TISPLENAIE
1510 1520 1530 1540 1550
TMSTANEKIL MMINQYQSDE TLPINPLSML LNGIVDPAVM GGFAKYEKAF
1560 1570 1580 1590 1600
FTEEYVRDHP EDQDKLTHLK DLIAWQIPFL GAGIKIHEKR VSDNLRPFHD
1610 1620 1630 1640 1650
RMEECFKNLK MKVEKEYGVR EMPDFDDRRV GRPRSMLRSY RQMSIISLAS
1660 1670 1680 1690 1700
MNSDCSTPSK PTSESFDLEL ASPKTPRVEQ EEPISPGSTL PEVKLRRSKK
1710 1720 1730 1740 1750
RTKRSSVVFA DEKAAAESDL KRLSRKHEFM SDTNLSEHAA IPLKASVLSQ
1760 1770 1780 1790 1800
MSFASQSMPT IPALALSVAG IPGLDEANTS PRLSQTFLQL SDGDKKTLTR
1810 1820 1830
KKVNQFFKTM LASKSAEEGK QIPDSLSTDL
Length:1,830
Mass (Da):211,948
Last modified:July 3, 2003 - v2
Checksum:i18568D3322DAA92A
GO
Isoform 2 (identifier: Q92608-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:336
Mass (Da):38,461
Checksum:iC5D6CAAB1C3A3490
GO

Sequence cautioni

The sequence BAA13200.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1558 – 15581D → A.
Corresponds to variant rs13179480 [ dbSNP | Ensembl ].
VAR_053064
Natural varianti1746 – 17461S → T.
Corresponds to variant rs2270898 [ dbSNP | Ensembl ].
VAR_015822
Natural varianti1779 – 17791T → S.
Corresponds to variant rs2270898 [ dbSNP | Ensembl ].
VAR_022137

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 449449Missing in isoform 2. 1 PublicationVSP_007696Add
BLAST
Alternative sequencei462 – 49433Missing in isoform 2. 1 PublicationVSP_007697Add
BLAST
Alternative sequencei630 – 766137Missing in isoform 2. 1 PublicationVSP_007698Add
BLAST
Alternative sequencei934 – 95522SHFVA…HYSFY → GACCNCGFPSSTPHSLIQWL WG in isoform 2. 1 PublicationVSP_007699Add
BLAST
Alternative sequencei956 – 1830875Missing in isoform 2. 1 PublicationVSP_007700Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86964 mRNA. Translation: BAA13200.1. Different initiation.
BC016996 mRNA. Translation: AAH16996.1.
BC104900 mRNA. Translation: AAI04901.1.
BC113457 mRNA. Translation: AAI13458.1.
CCDSiCCDS4371.1. [Q92608-1]
RefSeqiNP_004937.1. NM_004946.2. [Q92608-1]
UniGeneiHs.586174.

Genome annotation databases

EnsembliENST00000256935; ENSP00000256935; ENSG00000134516. [Q92608-1]
GeneIDi1794.
KEGGihsa:1794.
UCSCiuc003maf.3. human. [Q92608-1]

Polymorphism databases

DMDMi32469765.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86964 mRNA. Translation: BAA13200.1 . Different initiation.
BC016996 mRNA. Translation: AAH16996.1 .
BC104900 mRNA. Translation: AAI04901.1 .
BC113457 mRNA. Translation: AAI13458.1 .
CCDSi CCDS4371.1. [Q92608-1 ]
RefSeqi NP_004937.1. NM_004946.2. [Q92608-1 ]
UniGenei Hs.586174.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q92608.
SMRi Q92608. Positions 1-167, 423-609, 1196-1622.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108129. 9 interactions.
DIPi DIP-31791N.
IntActi Q92608. 4 interactions.
MINTi MINT-2813049.
STRINGi 9606.ENSP00000256935.

PTM databases

PhosphoSitei Q92608.

Polymorphism databases

DMDMi 32469765.

Proteomic databases

MaxQBi Q92608.
PaxDbi Q92608.
PeptideAtlasi Q92608.
PRIDEi Q92608.

Protocols and materials databases

DNASUi 1794.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256935 ; ENSP00000256935 ; ENSG00000134516 . [Q92608-1 ]
GeneIDi 1794.
KEGGi hsa:1794.
UCSCi uc003maf.3. human. [Q92608-1 ]

Organism-specific databases

CTDi 1794.
GeneCardsi GC05P169064.
HGNCi HGNC:2988. DOCK2.
HPAi HPA036468.
HPA036469.
MIMi 603122. gene.
neXtProti NX_Q92608.
PharmGKBi PA27454.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289808.
GeneTreei ENSGT00610000085806.
HOGENOMi HOG000006631.
HOVERGENi HBG051389.
InParanoidi Q92608.
KOi K12367.
OMAi GDWMAMS.
OrthoDBi EOG7QNVK8.
PhylomeDBi Q92608.
TreeFami TF300423.

Enzyme and pathway databases

Reactomei REACT_11068. Nef and signal transduction.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi DOCK2. human.
GeneWikii Dock2.
GenomeRNAii 1794.
NextBioi 7309.
PROi Q92608.
SOURCEi Search...

Gene expression databases

Bgeei Q92608.
CleanExi HS_DOCK2.
ExpressionAtlasi Q92608. baseline and differential.
Genevestigatori Q92608.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR026799. DOCK_2.
IPR010703. DOCK_C.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR23317. PTHR23317. 1 hit.
PTHR23317:SF73. PTHR23317:SF73. 1 hit.
Pfami PF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
SSF50044. SSF50044. 1 hit.
PROSITEi PS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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.

Entry informationi

Entry nameiDOCK2_HUMAN
AccessioniPrimary (citable) accession number: Q92608
Secondary accession number(s): Q2M3I0, Q96AK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: July 3, 2003
Last modified: November 26, 2014
This is version 137 of the entry and version 2 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3