Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14185

- DOCK1_HUMAN

UniProt

Q14185 - DOCK1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dedicator of cytokinesis protein 1

Gene

DOCK1

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

Functioni

Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1.1 Publication

GO - Molecular functioni

  1. GTPase activator activity Source: ProtInc
  2. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. axon guidance Source: Reactome
  3. blood coagulation Source: Reactome
  4. cell migration Source: Ensembl
  5. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  6. hematopoietic progenitor cell differentiation Source: Ensembl
  7. innate immune response Source: Reactome
  8. integrin-mediated signaling pathway Source: ProtInc
  9. phagocytosis, engulfment Source: ProtInc
  10. positive regulation of GTPase activity Source: GOC
  11. signal transduction Source: ProtInc
  12. small GTPase mediated signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Apoptosis, Phagocytosis

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_22351. DCC mediated attractive signaling.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Dedicator of cytokinesis protein 1
Alternative name(s):
180 kDa protein downstream of CRK
Short name:
DOCK180
Gene namesi
Name:DOCK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:2987. DOCK1.

Subcellular locationi

Cytoplasm Curated. Membrane Curated
Note: Recruited to membranes via its interaction with phosphatidylinositol 3,4,5-trisphosphate.Curated

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB-KW
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1401 – 14022YI → AA: Abolishes Rac GEF activity. 1 Publication
Mutagenesisi1487 – 14893ISP → AAA: Abolishes Rac GEF activity. 1 Publication

Organism-specific databases

PharmGKBiPA27453.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18651865Dedicator of cytokinesis protein 1PRO_0000189984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1751 – 17511Phosphoserine1 Publication
Modified residuei1756 – 17561PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14185.
PaxDbiQ14185.
PRIDEiQ14185.

PTM databases

PhosphoSiteiQ14185.

Expressioni

Tissue specificityi

Highly expressed in placenta, lung, kidney, pancreas and ovary. Expressed at intermediate level in thymus, testes and colon.

Gene expression databases

BgeeiQ14185.
CleanExiHS_DOCK1.
GenevestigatoriQ14185.

Organism-specific databases

HPAiCAB004378.
HPA048692.
HPA053277.

Interactioni

Subunit structurei

Interacts with the SH3 domains of CRK and NCK2 via multiple sites. Interacts with nucleotide-free RAC1 via its DHR-2 domain. Interacts with ELMO1, ELMO2 and probably ELMO3 via its SH3 domain. Interacts with RAC1 and BAI1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANKRD28O150844EBI-446740,EBI-359567
ELMO1Q9255616EBI-446740,EBI-346417
GRB2P629932EBI-446740,EBI-401755
RAC1P6300010EBI-446740,EBI-413628

Protein-protein interaction databases

BioGridi108128. 13 interactions.
DIPiDIP-29391N.
IntActiQ14185. 13 interactions.
MINTiMINT-190985.
STRINGi9606.ENSP00000381107.

Structurei

Secondary structure

1
1865
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi426 – 43611
Beta strandi440 – 4445
Beta strandi448 – 4569
Beta strandi493 – 4997
Beta strandi507 – 5159
Beta strandi528 – 53710
Beta strandi546 – 55510
Helixi558 – 5614
Helixi564 – 5674
Helixi574 – 5785
Beta strandi595 – 60814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4CX-ray2.37A/B422-619[»]
ProteinModelPortaliQ14185.
SMRiQ14185. Positions 1-168, 425-611, 1192-1617.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14185.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 7062SH3PROSITE-ProRule annotationAdd
BLAST
Domaini425 – 609185DHR-1Add
BLAST
Domaini1207 – 1617411DHR-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1687 – 16959Phosphoinositide-bindingSequence Analysis
Regioni1793 – 181927Interaction with NCK2 second and third SH3 domain (minor)Add
BLAST
Regioni1820 – 183617Interaction with NCK2 third SH3 domain (major)Add
BLAST
Regioni1837 – 185216Interaction with NCK2 (minor)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1799 – 18057SH3-binding; interaction with CRKSequence Analysis
Motifi1838 – 18436SH3-binding; interaction with CRKSequence Analysis

Domaini

The DHR-2 domain is necessary and sufficient for the GEF activity.

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, SH3-binding

Phylogenomic databases

eggNOGiNOG289808.
GeneTreeiENSGT00610000085806.
HOGENOMiHOG000006631.
HOVERGENiHBG051389.
InParanoidiQ14185.
KOiK13708.
OMAiNYVVKWS.
OrthoDBiEOG7QNVK8.
PhylomeDBiQ14185.
TreeFamiTF300423.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 1 hit.
PfamiPF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14185 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT
60 70 80 90 100
LRKKSKKGIF PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWS
110 120 130 140 150
TIWRQLYVQD NREMFRSVRH MIYDLIEWRS QILSGTLPQD ELKELKKKVT
160 170 180 190 200
AKIDYGNRIL DLDLVVRDED GNILDPELTS TISLFRAHEI ASKQVEERLQ
210 220 230 240 250
EEKSQKQNID INRQAKFAAT PSLALFVNLK NVVCKIGEDA EVLMSLYDPV
260 270 280 290 300
ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ
310 320 330 340 350
IVRVGRMELR DNNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP
360 370 380 390 400
FQPVAGENDF LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DIHQIRKEFP
410 420 430 440 450
HLVDRTTAVA RKTGFPEIIM PGDVRNDIYV TLVQGDFDKG SKTTAKNVEV
460 470 480 490 500
TVSVYDEDGK RLEHVIFPGA GDEAISEYKS VIYYQVKQPR WFETVKVAIP
510 520 530 540 550
IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD GTTLRDGEHD
560 570 580 590 600
LIVYKAEAKK LEDAATYLSL PSTKAELEEK GHSATGKSMQ SLGSCTISKD
610 620 630 640 650
SFQISTLVCS TKLTQNVDLL GLLKWRSNTS LLQQNLRQLM KVDGGEVVKF
660 670 680 690 700
LQDTLDALFN IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET
710 720 730 740 750
YIKKHFSATL AYTKLTKVLK NYVDGAEKPG VNEQLYKAMK ALESIFKFIV
760 770 780 790 800
RSRILFNQLY ENKGEADFVE SLLQLFRSIN DMMSSMSDQT VRVKGAALKY
810 820 830 840 850
LPTIVNDVKL VFDPKELSKM FTEFILNVPM GLLTIQKLYC LIEIVHSDLF
860 870 880 890 900
TQHDCREILL PMMTDQLKYH LERQEDLEAC CQLLSHILEV LYRKDVGPTQ
910 920 930 940 950
RHVQIIMEKL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL
960 970 980 990 1000
IKTFGKMRTD VVDFLMETFI MFKNLIGKNV YPFDWVIMNM VQNKVFLRAI
1010 1020 1030 1040 1050
NQYADMLNKK FLDQANFELQ LWNNYFHLAV AFLTQESLQL ENFSSAKRAK
1060 1070 1080 1090 1100
ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF IPEMVGPILE MTLIPETELR
1110 1120 1130 1140 1150
KATIPIFFDM MQCEFHSTRS FQMFENEIIT KLDHEVEGGR GDEQYKVLFD
1160 1170 1180 1190 1200
KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMHD ENKENRMSCT
1210 1220 1230 1240 1250
VNVLNFYKEI EREEMYIRYL YKLCDLHKEC DNYTEAAYTL LLHAKLLKWS
1260 1270 1280 1290 1300
EDVCVAHLTQ RDGYQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL
1310 1320 1330 1340 1350
AEQYENEMFD YEQLSELLKK QAQFYENIVK VIRPKPDYFA VGYYGQGFPT
1360 1370 1380 1390 1400
FLRGKVFIYR GKEYERREDF EARLLTQFPN AEKMKTTSPP GDDIKNSPGQ
1410 1420 1430 1440 1450
YIQCFTVKPK LDLPPKFHRP VSEQIVSFYR VNEVQRFEYS RPIRKGEKNP
1460 1470 1480 1490 1500
DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT
1510 1520 1530 1540 1550
NDKINSMVQQ HLDDPSLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTDRY
1560 1570 1580 1590 1600
LQEHPEAHEK IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC
1610 1620 1630 1640 1650
FKQLKEKVEK EYGVRIMPSS LDDRRGSRPR SMVRSFTMPS SSRPLSVASV
1660 1670 1680 1690 1700
SSLSSDSTPS RPGSDGFALE PLLPKKMHSR SQDKLDKDDL EKEKKDKKKE
1710 1720 1730 1740 1750
KRNSKHQEIF EKEFKPTDIS LQQSEAVILS ETISPLRPQR PKSQVMNVIG
1760 1770 1780 1790 1800
SERRFSVSPS SPSSQQTPPP VTPRAKLSFS MQSSLELNGM TGADVADVPP
1810 1820 1830 1840 1850
PLPLKGSVAD YGNLMENQDL LGSPTPPPPP PHQRHLPPPL PSKTPPPPPP
1860
KTTRKQASVD SGIVQ
Length:1,865
Mass (Da):215,346
Last modified:October 14, 2008 - v2
Checksum:i940C5AFD047EBEDE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1857 – 18571A → T in BAA09454. (PubMed:8657152)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1793 – 17931A → T.
Corresponds to variant rs869801 [ dbSNP | Ensembl ].
VAR_059971

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50857 mRNA. Translation: BAA09454.1.
AL157711
, AL355316, AL359094, AL390920, AL607029, BX470155, BX470201 Genomic DNA. Translation: CAH71463.2.
AL359094
, AL157711, AL355316, AL390920, AL607029, BX470155, BX470201 Genomic DNA. Translation: CAH71477.2.
BX470201
, AL157711, AL355316, AL359094, AL390920, AL607029, BX470155 Genomic DNA. Translation: CAH72560.2.
AL390920
, AL157711, AL355316, AL359094, AL607029, BX470155, BX470201 Genomic DNA. Translation: CAH73231.2.
AL607029
, AL157711, AL355316, AL359094, AL390920, BX470155, BX470201 Genomic DNA. Translation: CAI15329.2.
AL355316
, AL157711, AL359094, AL390920, AL607029, BX470155, BX470201 Genomic DNA. Translation: CAI16871.2.
BX470155
, AL157711, AL355316, AL359094, AL390920, AL607029, BX470201 Genomic DNA. Translation: CAI22477.2.
CCDSiCCDS73222.1.
RefSeqiNP_001371.1. NM_001380.4.
UniGeneiHs.159195.

Genome annotation databases

EnsembliENST00000280333; ENSP00000280333; ENSG00000150760.
GeneIDi1793.
KEGGihsa:1793.
UCSCiuc001ljt.3. human.

Polymorphism databases

DMDMi209572608.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50857 mRNA. Translation: BAA09454.1 .
AL157711
, AL355316 , AL359094 , AL390920 , AL607029 , BX470155 , BX470201 Genomic DNA. Translation: CAH71463.2 .
AL359094
, AL157711 , AL355316 , AL390920 , AL607029 , BX470155 , BX470201 Genomic DNA. Translation: CAH71477.2 .
BX470201
, AL157711 , AL355316 , AL359094 , AL390920 , AL607029 , BX470155 Genomic DNA. Translation: CAH72560.2 .
AL390920
, AL157711 , AL355316 , AL359094 , AL607029 , BX470155 , BX470201 Genomic DNA. Translation: CAH73231.2 .
AL607029
, AL157711 , AL355316 , AL359094 , AL390920 , BX470155 , BX470201 Genomic DNA. Translation: CAI15329.2 .
AL355316
, AL157711 , AL359094 , AL390920 , AL607029 , BX470155 , BX470201 Genomic DNA. Translation: CAI16871.2 .
BX470155
, AL157711 , AL355316 , AL359094 , AL390920 , AL607029 , BX470201 Genomic DNA. Translation: CAI22477.2 .
CCDSi CCDS73222.1.
RefSeqi NP_001371.1. NM_001380.4.
UniGenei Hs.159195.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L4C X-ray 2.37 A/B 422-619 [» ]
ProteinModelPortali Q14185.
SMRi Q14185. Positions 1-168, 425-611, 1192-1617.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108128. 13 interactions.
DIPi DIP-29391N.
IntActi Q14185. 13 interactions.
MINTi MINT-190985.
STRINGi 9606.ENSP00000381107.

PTM databases

PhosphoSitei Q14185.

Polymorphism databases

DMDMi 209572608.

Proteomic databases

MaxQBi Q14185.
PaxDbi Q14185.
PRIDEi Q14185.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000280333 ; ENSP00000280333 ; ENSG00000150760 .
GeneIDi 1793.
KEGGi hsa:1793.
UCSCi uc001ljt.3. human.

Organism-specific databases

CTDi 1793.
GeneCardsi GC10P128584.
HGNCi HGNC:2987. DOCK1.
HPAi CAB004378.
HPA048692.
HPA053277.
MIMi 601403. gene.
neXtProti NX_Q14185.
PharmGKBi PA27453.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289808.
GeneTreei ENSGT00610000085806.
HOGENOMi HOG000006631.
HOVERGENi HBG051389.
InParanoidi Q14185.
KOi K13708.
OMAi NYVVKWS.
OrthoDBi EOG7QNVK8.
PhylomeDBi Q14185.
TreeFami TF300423.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_22351. DCC mediated attractive signaling.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi DOCK1. human.
EvolutionaryTracei Q14185.
GeneWikii Dock180.
GenomeRNAii 1793.
NextBioi 7305.
PROi Q14185.
SOURCEi Search...

Gene expression databases

Bgeei Q14185.
CleanExi HS_DOCK1.
Genevestigatori Q14185.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR23317. PTHR23317. 1 hit.
Pfami PF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 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. "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane."
    Hasegawa H., Kiyokawa E., Tanaka S., Nagashima K., Gotoh N., Shibuya M., Kurata T., Matsuda M.
    Mol. Cell. Biol. 16:1770-1776(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CRK.
    Tissue: Placenta.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins."
    Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T., Nagashima K., Kurata T.
    J. Biol. Chem. 271:14468-14472(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRK.
  4. Cited for: GEF ACTIVITY, INTERACTION WITH RAC1.
  5. "Identification and kinetic analysis of the interaction between Nck-2 and DOCK180."
    Tu Y., Kucik D.F., Wu C.
    FEBS Lett. 491:193-199(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCK2.
  6. "Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3."
    Kobayashi S., Shirai T., Kiyokawa E., Mochizuki N., Matsuda M., Fukui Y.
    Biochem. J. 354:73-78(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTDINS(3,4,5)P3.
  7. Cited for: GEF ACTIVITY, INTERACTION WITH RAC1; ELMO1 AND ELMO2, SUBUNIT OF A COMPLEX CONTAINING ELMO1 AND DOCK1, MUTAGENESIS OF 1401-TYR-ILE-1402 AND 1487-ILE--PRO-1489.
  8. "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, GEF ACTIVITY.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDOCK1_HUMAN
AccessioniPrimary (citable) accession number: Q14185
Secondary accession number(s): A9Z1Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 133 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 10
    Human chromosome 10: 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