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Protein Page:
Dok1 (human)

Overview
Dok1 a docking protein that interacts with receptor tyrosine kinases. It is constitutively tyrosine phosphorylated in hematopoietic progenitors isolated from chronic myelogenous leukemia (CML) patients in the chronic phase. It may be a critical substrate for p210(bcr/abl), a chimeric protein whose presence is associated with CML. Docking protein 1 contains a putative pleckstrin homology domain at the amino terminus and ten PXXP SH3 recognition motifs. Docking protein 2 binds p120 (RasGAP) from CML cells. It has been postulated to play a role in mitogenic signaling. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Adaptor/scaffold
Cellular Component: perinuclear region of cytoplasm; cytoplasm; cytosol; nucleus
Molecular Function: protein binding; receptor signaling protein activity; insulin receptor binding
Biological Process: cell surface receptor linked signal transduction; Ras protein signal transduction; insulin receptor signaling pathway; signal transduction; transmembrane receptor protein tyrosine kinase signaling pathway
Reference #:  Q99704 (UniProtKB)
Alt. Names/Synonyms: Docking protein 1; docking protein 1 (downstream of tyrosine kinase 1); docking protein 1, 62kDa (downstream of tyrosine kinase 1); DOK1; Downstream of tyrosine kinase 1; MGC117395; MGC138860; p62(dok); P62DOK; pp62
Gene Symbols: DOK1
Molecular weight: 52,392 Da
Basal Isoelectric point: 6.05  Predict pI for various phosphorylation states
CST Pathways:  B Cell Receptor Signaling  |  ErbB/HER Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Dok1

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: S439‑p, S443‑p, S446‑p, S450‑p
cell motility, altered: S439‑p, S443‑p, S446‑p, S450‑p
intracellular localization: Y296‑p
molecular association, regulation: Y146‑p, Y296‑p, Y315‑p, Y362‑p, Y398‑p, Y449‑p
phosphorylation: Y362‑p, Y398‑p, S439‑p, S443‑p, S446‑p, S450‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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

 
0 1 Y30-p RKTWAVLyPAsPHGV
0 10 S33-p WAVLyPAsPHGVARL
0 2 S48-p EFFDHKGsSSGGGRG
0 1 S136 TDNPPKLSALEMLEN
2 4 Y146-p EMLENSLySPTWEGS
0 19 S269-p HDVLRADsHEGEVAE
0 1 A275 DsHEGEVAEGKLPsP
0 2 S281-p VAEGKLPsPPGPQEL
0 5 S291-p GPQELLDsPPALyAE
2 174 Y296-p LDsPPALyAEPLDSL
0 8 S310-p LRIAPCPsQDsLysD
0 10 S313-p APCPsQDsLysDPLD
1 381 Y315-p CPsQDsLysDPLDST
0 3 S316-p PsQDsLysDPLDSTS
1 366 Y337-p VQRKKPLyWDLyEHA
0 336 Y341-p KPLyWDLyEHAQQQL
0 19 T354-p QLLKAKLtDPKEDPI
0 2 P356 LKAKLtDPKEDPIyD
7 531 Y362-p DPKEDPIyDEPEGLA
1 380 Y377-p PVPPQGLyDLPREPK
4 578 Y398-p ARVKEEGyELPyNPA
0 162 Y402-p EEGyELPyNPAtDDy
0 54 T406-p ELPyNPAtDDyAVPP
2 814 Y409-p yNPAtDDyAVPPPRS
0 13 S416 yAVPPPRSTKPLLAP
0 1 P433 QGPAFPEPGtATGsG
0 2 T435-p PAFPEPGtATGsGIK
0 1 A436 AFPEPGtATGsGIKs
1 1 S439-p EPGtATGsGIKsHNs
1 0 S443-p ATGsGIKsHNsALys
1 20 S446-p sGIKsHNsALysQVQ
2 1088 Y449-p KsHNsALysQVQKSG
1 1 S450-p sHNsALysQVQKSGA
0 1 S460-p QKSGASGsWDCGLSR
0 4 T470-p CGLSRVGtDKTGVKS
  mouse

 
Y30 RKTWAVLYPASPHGV
S33 WAVLYPASPHGVARL
S48-p EFFDHKGsSSRGGRG
S136-p TENQPKFsALEMLEN
Y146-p EMLENSLySPTWEGS
S269-p QDILRTDsHDGEtEG
T274-p TDsHDGEtEGKTVPP
P280 EtEGKTVPPPVPQDP
S290-p VPQDPLGsPPALyAE
Y295-p LGsPPALyAEPLDSL
S309 LRIPPGPSQDSVysD
S312 PPGPSQDSVysDPLG
Y314-p GPSQDSVysDPLGST
S315-p PSQDSVysDPLGSTP
Y336-p VHSKKPLyWDLyGHV
Y340-p KPLyWDLyGHVQQQL
T353-p QLLKTKLtDsKEDPI
S355-p LKTKLtDsKEDPIyD
Y361-p DsKEDPIyDEPEGLA
Y376-p PAPPRGLyDLPQEPR
Y397-p ARLKEEGyELPyNPA
Y401-p EEGyELPyNPAtDDy
T405-p ELPyNPAtDDyAVPP
Y408-p yNPAtDDyAVPPPRs
S415-p yAVPPPRsPKPAPAP
S432-p QGLILPEsGttRGsG
T434-p LILPEsGttRGsGSK
T435-p ILPEsGttRGsGSKG
S438-p EsGttRGsGSKGFSS
S444 GsGSKGFSSDTALyS
T447 SKGFSSDTALySQVQ
Y450-p FSSDTALySQVQKSG
S451 SSDTALySQVQKSGT
A461 QKSGTSGAWDCGLSK
N471 CGLSKVGNDRAGVKS
  rat

 
Y30 KKTWAVLYPASPHGV
S33 WAVLYPASPHGVARL
S48 EFFDHKGSSSGGGRG
S136 TENPPKFSALEMLEN
Y146 EMLENSLYSPTWEGS
S269 QDITRTDSHDGETEG
T274 TDSHDGETEGKMAPT
P280 ETEGKMAPTPVPQEP
S290-p VPQEPLGsPPALYAE
Y295 LGsPPALYAEPLDSL
S309 LRIPPGPSQDSLYSD
S312 PPGPSQDSLYSDPLG
Y314 GPSQDSLYSDPLGST
S315 PSQDSLYSDPLGSTP
Y336 VQRKKPLYWDLYGHV
Y340 KPLYWDLYGHVQQQL
I353 QLLKTKLIDSKEDPI
S355 LKTKLIDSKEDPIyD
Y361-p DSKEDPIyDEPEGLA
Y376 PAPLRGLYDLPQEPK
Y397 ARLKEEGYELPYNPA
Y401 EEGYELPYNPATDDY
T405 ELPYNPATDDYAVPP
Y408 YNPATDDYAVPPPRS
S415 YAVPPPRSSKPTPAP
S432 QGLILPESGTTAGSG
T434 LILPESGTTAGSGSK
T435 ILPESGTTAGSGSKG
S438 ESGTTAGSGSKGSDT
- gap
T445 SGSKGSDTALYSQVQ
Y448 KGSDTALYSQVQKSG
S449 GSDTALYSQVQKSGT
R459 QKSGTPGRWDCGLSR
N469 CGLSRVGNDRVGVKS
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