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Protein Page:
DOCK1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DOCK1 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. 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. Highly expressed in placenta, lung, kidney, pancreas and ovary. Expressed at intermediate level in thymus, testes and colon. Belongs to the DOCK family. Note: This description may include information from UniProtKB.
Protein type: GEFs, Rac/Rho; Adaptor/scaffold; Motility/polarity/chemotaxis; GEFs; Cytoskeletal protein
Cellular Component: membrane; cytoplasm; nucleolus; cytosol; nucleus
Molecular Function: protein binding; guanyl-nucleotide exchange factor activity; SH3 domain binding; GTPase activator activity
Biological Process: integrin-mediated signaling pathway; axon guidance; cell migration; apoptosis; small GTPase mediated signal transduction; innate immune response; signal transduction; phagocytosis, engulfment; blood coagulation; positive regulation of GTPase activity
Reference #:  Q14185 (UniProtKB)
Alt. Names/Synonyms: 180 kDa protein downstream of CRK; ced5; dedicator of cyto-kinesis 1; dedicator of cytokinesis 1; Dedicator of cytokinesis protein 1; DOCK1; DOCK180; DOwnstream of CrK
Gene Symbols: DOCK1
Molecular weight: 215,346 Da
Basal Isoelectric point: 7.29  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DOCK1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S100-p TTTLREWstIWRQLy
0 1 T101-p TTLREWstIWRQLyV
0 1 Y107-p stIWRQLyVQDNREM
0 1 S204-p ERLQEEKsQKQNIDI
0 1 S265-p NYLVRWSsSGLPKDI
0 1 K288 VFTDLGSKDLKREKI
0 1 K291 DLGSKDLKREKISFV
0 1 T314-p MELRDNNtRKLTsGL
0 1 S319-p NNtRKLTsGLRRPFG
0 1 Y478-p GDEAISEyKSVIyYQ
0 1 Y483-p SEyKSVIyYQVKQPR
0 1 T542 KLMRYDGTTLRDGEH
0 1 S583-p ELEEKGHsATGKSMQ
0 1 S591-p ATGKSMQsLGSCTIS
0 1 S601 SCTISKDSFQISTLV
0 2 S784-p RSINDMMsSMSDQTV
0 2 K799-ub RVKGAALkyLPtIVN
0 1 Y800-p VKGAALkyLPtIVND
0 2 T803-p AALkyLPtIVNDVKL
0 1 S818-p VFDPKELsKMFTEFI
0 8 K1054-ub KRAKILNkYGDMRRQ
1 0 S1250-p HAKLLKWsEDVCVAH
0 1 K1320 QLSELLKKQAQFYEN
0 2 Y1439 NEVQRFEYSRPIRKG
0 1 K1602-ac ERMEACFkQLkEKVE
0 1 K1605-ac EACFkQLkEKVEKEY
0 1 S1654 VASVSSLSSDSTPSR
0 1 S1655 ASVSSLSSDSTPSRP
0 1 S1657 VSSLSSDSTPSRPGS
0 2 S1681-p PKKMHSRsQDKLDKD
0 1 K1699 KEKKDKKKEKRNSKH
0 1 K1701 KKDKKKEKRNSKHQE
0 6 S1743-p LRPQRPKsQVMNVIG
0 2 S1751-p QVMNVIGsERRFsVs
0 6 S1756-p IGsERRFsVsPSSPs
0 4 S1758-p sERRFsVsPSSPsSQ
0 1 S1761 RFsVsPSSPsSQQtP
0 1 S1763-p sVsPSSPsSQQtPPP
0 1 S1764 VsPSSPsSQQtPPPV
0 3 T1767-p SSPsSQQtPPPVtPR
1 7 T1772-p QQtPPPVtPRAKLSF
0 1 S1807-p PPLPLKGsVADyGNL
0 142 Y1811-p LKGsVADyGNLMENQ
0 1 S1823-p ENQDLLGsPtPPPPP
0 1 T1825-p QDLLGsPtPPPPPPH
0 1 P1826 DLLGsPtPPPPPPHQ
0 2 S1842-p HLPPPLPsKtPPPPP
0 2 T1844-p PPPLPsKtPPPPPPK
0 2 A1857 PKTTRKQAsVDSGIV
0 11 S1858-p KTTRKQAsVDSGIVQ
0 2 S1861 RKQAsVDSGIVQ___
  DOCK1 iso1  
S100 TTTLREWSTIWRQLY
T101 TTLREWSTIWRQLYV
Y107 STIWRQLYVQDNREM
S204 ERLQEEKSQKQNIDI
S265 NYLVRWSSSGLPKDI
K288 VFTDLGSKDLKREKI
K291 DLGSKDLKREKISFV
T314 MELRDNNTRKLTSGL
S319 NNTRKLTSGLRRPFG
Y478 GDEAISEYKSVIYYQ
Y483 SEYKSVIYYQVKQPR
T542 KLMRYDGTTLRDGEH
S583 ELEEKGHSATGKSMQ
S591 ATGKSMQSLGSCTIS
S601 SCTISKDSFQISTLV
S784 RSINDMMSSMSDQTV
K799 RVKGAALKYLPTIVN
Y800 VKGAALKYLPTIVND
T803 AALKYLPTIVNDVKL
S818 VFDPKELSKMFTEFI
K1054 KRAKILNKYGDMRRQ
S1250 HAKLLKWSEDVCVAH
K1320 QLSELLKKQAQFYEN
Y1439 NEVQRFEYSRPIRKG
K1602 ERMEACFKQLKEKVE
K1605 EACFKQLKEKVEKEY
S1654 VASVSSLSSDSTPSR
S1655 ASVSSLSSDSTPSRP
S1657 VSSLSSDSTPSRPGS
S1681 PKKMHSRSQDKLDKD
K1699 KEKKDKKKEKRNSKH
K1701 KKDKKKEKRNSKHQE
S1743 LRPQRPKSQVMNVIG
S1751 QVMNVIGSERRFSVS
S1756 IGSERRFSVSPSSPS
S1758 SERRFSVSPSSPSSQ
S1761 RFSVSPSSPSSQQTP
S1763 SVSPSSPSSQQTPPP
S1764 VSPSSPSSQQTPPPV
T1767 SSPSSQQTPPPVTPR
T1772 QQTPPPVTPRAKLSF
S1807 PPLPLKGSVADYGNL
Y1811 LKGSVADYGNLMENQ
S1823 ENQDLLGSPTPPPPP
T1825 QDLLGSPTPPPPPPH
P1826 DLLGSPTPPPPPPHQ
S1842 HLPPPLPSKTPPPPP
T1844 PPPLPSKTPPPPPPK
T1857-p PKTTRKQtsVDsGIV
S1858-p KTTRKQtsVDsGIVQ
S1861-p RKQtsVDsGIVQ___
  mouse

 
S100 TTTLREWSTIWRQLY
T101 TTLREWSTIWRQLYV
Y107 STIWRQLYVQDNREM
S204 ERLQEEKSQKQNMDI
S265 NYLVRWSSSGLPKDI
K288-ac VFTDLGSkDLkREKI
K291-ac DLGSkDLkREKISFV
T314 MELRDSNTRKLTSGL
S319 SNTRKLTSGLRRPFG
Y478 GDEAISEYKSVIYYQ
Y483 SEYKSVIYYQVKQPR
T542-p KLMRYDGtTLRDGEH
S583 ELEEKGHSATGKGMQ
S591 ATGKGMQSLGSCTIS
S601-p SCTISKDsFQISTLV
S784 RSINDMMSSLSELTV
K799-ub RVKGAALkYLPTIVN
Y800 VKGAALkYLPTIVND
T803 AALkYLPTIVNDVKL
S818 VFDPKELSKMFTEFI
K1054 KRAKILNKYGDMRRQ
S1250 HAKLLKWSEDVCAAH
K1320-ub QLSELLKkQAQFYEN
Y1439 NEVQRFEYSRPIRKG
K1602 ERMEACFKQLKEKVE
K1605 EACFKQLKEKVEKQY
S1654-p VASVSSFssDsTPSR
S1655-p ASVSSFssDsTPSRP
S1657-p VSSFssDsTPSRPGS
S1681-p PKKMHSRsQDKLDKD
K1699-ac KEKKDKKkEkRNSKH
K1701-ac KKDKKkEkRNSKHQE
S1743-p LRPQRPKsQVINVIG
N1751 QVINVIGNERRFsVs
S1756-p IGNERRFsVsPAsPS
S1758-p NERRFsVsPAsPSsQ
S1761-p RFsVsPAsPSsQQtP
S1763 sVsPAsPSsQQtPPP
S1764-p VsPAsPSsQQtPPPV
T1767-p AsPSsQQtPPPVtPR
T1772-p QQtPPPVtPRAKLSF
N1807 PPLPLKGNMADyGNL
Y1811-p LKGNMADyGNLMENQ
S1823 ENQDMMVSPTsPPPP
T1825 QDMMVSPTsPPPPPP
S1826-p DMMVSPTsPPPPPPQ
S1842 QQPPPLPSKtPPPPP
T1844-p PPPLPSKtPPPPPPK
T1857-p PKTTRKQtsVDsGIV
S1858-p KTTRKQtsVDsGIVQ
S1861-p RKQtsVDsGIVQ___
  rat

 
S100 TTTLREWSTIWRQLY
T101 TTLREWSTIWRQLYV
Y107 STIWRQLYVQDNREM
S204 ERLQEEKSQKQNMDI
S265 NYLVRWSSSGLPKDI
K288 VFTDLGSKDLKREKI
K291 DLGSKDLKREKISFV
T314 MELRDSNTRKLTSGL
S319 SNTRKLTSGLRRPFG
Y478 GDEAISEYKSVIYYQ
Y483 SEYKSVIYYQVKQPR
T542 KLMRYDGTTLRDGEH
S583 ELEEKGHSATGKGMQ
S591 ATGKGMQSLGSCTIS
S601 SCTISKDSFQISTLV
S784 RSINDMMSSMSELTV
K799 RVKGAALKYLPTIVN
Y800 VKGAALKYLPTIVND
T803 AALKYLPTIVNDVKL
S818 VFDPKELSKMFTEFI
K1054 KRAKILNKYGDMRRQ
S1250 HAKLLKWSEDACAAH
K1320 QLSELLKKQAQFYEN
Y1439-p NEVQRFEySRPIRKG
K1602 ERMEACFKQLKEKVE
K1605 EACFKQLKEKVEKQY
S1654 VASVSSFSSDSTPSR
S1655 ASVSSFSSDSTPSRP
S1657 VSSFSSDSTPSRPGS
S1681 PKKMHSRSQDKLDKD
K1699 KEKKDKKKEKRNSKH
K1701 KKDKKKEKRNSKHQE
S1743 LRPQRPKSQVINVIG
S1751 QVINVIGSERRFSVS
S1756 IGSERRFSVSPASPC
S1758 SERRFSVSPASPCSQ
S1761 RFSVSPASPCSQPTP
C1763 SVSPASPCSQPTPPP
S1764 VSPASPCSQPTPPPV
T1767 ASPCSQPTPPPVTPR
T1772 QPTPPPVTPRAKLSF
N1807 PPLPLKGNMADYGNL
Y1811 LKGNMADYGNLMENQ
S1823 ENQDLMGSPTSPPPP
T1825 QDLMGSPTSPPPPPQ
S1826 DLMGSPTSPPPPPQR
S1841 QQPPPLPSKTPPPPP
T1843 PPPLPSKTPPPPPPK
T1856 PKTTRKQTsVDSGIV
S1857-p KTTRKQTsVDSGIVQ
S1860 RKQTsVDSGIVQ___
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