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Protein Page:
Dok1 (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
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: Adaptor/scaffold; Motility/polarity/chemotaxis
Cellular Component: perinuclear region of cytoplasm; cytoplasm; nucleus; cytosol
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 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

 
0 1 Y30-p RKTWAVLyPAsPHGV
0 11 S33-p WAVLyPAsPHGVARL
0 3 S48-p EFFDHKGsSSGGGRG
0 1 K63 SSRRLDCKVIRLAEC
0 1 T93-p ATAFRLDtAQRSHLL
0 1 S123-p RNAFPKGsWtLAPTD
0 1 T125-p AFPKGsWtLAPTDNP
0 1 S136 TDNPPKLSALEMLEN
2 3 Y146-p EMLENSLySPTWEGS
0 1 S217-p GRDKVMFsFEAGRRC
0 1 A267 QGHDVLRADsHEGEV
0 21 S269-p HDVLRADsHEGEVAE
0 2 A275 DsHEGEVAEGKLPsP
0 3 S281-p VAEGKLPsPPGPQEL
0 6 S291-p GPQELLDsPPALyAE
2 176 Y296-p LDsPPALyAEPLDSL
0 8 S310-p LRIAPCPsQDsLysD
0 9 S313-p APCPsQDsLysDPLD
1 349 Y315-p CPsQDsLysDPLDST
0 3 S316-p PsQDsLysDPLDSTS
1 350 Y337-p VQRKKPLyWDLyEHA
0 320 Y341-p KPLyWDLyEHAQQQL
0 19 T354-p QLLKAKLtDPKEDPI
0 2 P356 LKAKLtDPKEDPIyD
7 513 Y362-p DPKEDPIyDEPEGLA
1 361 Y377-p PVPPQGLyDLPREPK
4 546 Y398-p ARVKEEGyELPyNPA
0 158 Y402-p EEGyELPyNPAtDDy
0 55 T406-p ELPyNPAtDDyAVPP
2 773 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 22 S446-p sGIKsHNsALysQVQ
2 1033 Y449-p KsHNsALysQVQKSG
1 2 S450-p sHNsALysQVQKSGA
0 1 S460-p QKSGASGsWDCGLSR
0 4 T470-p CGLSRVGtDKTGVKS
  mouse

 
Y30 RKTWAVLYPASPHGV
S33 WAVLYPASPHGVARL
S48-p EFFDHKGsSSRGGRG
K63-ac GSRRLDCkMIRLAEC
T93 AVAFRLDTAQRSHLL
G123 RTAFPKGGWALAQTE
A125 AFPKGGWALAQTENQ
S136-p TENQPKFsALEMLEN
Y146-p EMLENSLySPTWEGS
S217 GRDKVMFSFEAGRRC
T267-p QAQDILRtDsHDGEt
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
K63 GSRRLDCKMIRLAEC
T93 ASAFRLDTAQRSHLL
G123 RTAFPKGGWALAQTE
A125 AFPKGGWALAQTENP
S136 TENPPKFSALEMLEN
Y146 EMLENSLYSPTWEGS
S217 GRDKVMFSFEAGRRC
T267 QGQDITRTDSHDGET
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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