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Protein Page:
CRK (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
CRK an adaptor protein with an SH2-SH3-SH3 domain structure. Recruits cytoplasmic proteins through SH2-phospho-tyrosine interaction. Phosphorylated by Abl, IGF-IR and EGFR. Phosphorylation induces a change in intramolecular folding and SH2 interactions, causing its rapid dissociation from the tyrosine kinase complex. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis
Cellular Component: cytoplasm; plasma membrane; nucleus; cytosol
Molecular Function: protein phosphorylated amino acid binding; protein binding; ephrin receptor binding; SH3/SH2 adaptor activity; SH2 domain binding
Biological Process: regulation of transcription from RNA polymerase II promoter; regulation of Rac protein signal transduction; platelet activation; regulation of Rho GTPase activity; nerve growth factor receptor signaling pathway; positive regulation of signal transduction; activation of MAPKK activity; regulation of actin cytoskeleton organization and biogenesis; ephrin receptor signaling pathway; insulin receptor signaling pathway; innate immune response; blood coagulation
Reference #:  P46108 (UniProtKB)
Alt. Names/Synonyms: Adapter molecule crk; avian sarcoma virus CT10 (v-crk) oncogene homolog; CRK; CRKII; Proto-oncogene c-Crk; v-crk avian sarcoma virus CT10 oncogene homolog; v-crk sarcoma virus CT10 oncogene homolog (avian)
Gene Symbols: CRK
Molecular weight: 33,831 Da
Basal Isoelectric point: 5.38  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CRK

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: Y221‑p
enzymatic activity, induced: Y251‑p
molecular association, regulation: Y221‑p, Y251‑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

► Hide Isoforms
 
0 14 S40-p GVFLVRDsstsPGDy
1 27 S41-p VFLVRDsstsPGDyV
0 8 T42-p FLVRDsstsPGDyVL
0 2 S43-p LVRDsstsPGDyVLS
0 2 Y47-p sstsPGDyVLSVSEN
0 17 S74-p PRPPVPPsPAQPPPG
0 6 S83-p AQPPPGVsPsRLRIG
0 4 S85-p PPPGVsPsRLRIGDQ
0 1 S96-p IGDQEFDsLPALLEF
0 82 Y108-p LEFYKIHyLDtttLI
0 1 T111-p YKIHyLDtttLIEPV
0 4 T112-p KIHyLDtttLIEPVS
0 1 T113-p IHyLDtttLIEPVSR
0 1 S121-p LIEPVSRsRQGsGVI
0 10 S125-p VSRsRQGsGVILRQE
0 76 Y136-p LRQEEAEyVRALFDF
0 1 K154-ac DEEDLPFkKGDILRI
0 7 Y190-p PVPYVEKyRPAsAsV
0 11 S194-p VEKyRPAsAsVsALI
0 6 S196-p KyRPAsAsVsALIGG
0 4 S198-p RPAsAsVsALIGGNQ
0 8 S208-p IGGNQEGsHPQPLGG
21 1164 Y221-p GGPEPGPyAQPsVNt
0 423 S225-p PGPyAQPsVNtPLPN
0 49 T228-p yAQPsVNtPLPNLQN
1 263 Y239-p NLQNGPIyARVIQKR
1 295 Y251-p QKRVPNAyDktALAL
0 1 K253-ac RVPNAyDktALALEV
0 2 T254-p VPNAyDktALALEVG
3491 : Phospho-CrkII (Tyr221) Antibody
  CRK iso2  
S40 GVFLVRDSSTSPGDY
S41 VFLVRDSSTSPGDYV
T42 FLVRDSSTSPGDYVL
S43 LVRDSSTSPGDYVLS
Y47 SSTSPGDYVLSVSEN
S74 PRPPVPPSPAQPPPG
S83 AQPPPGVSPSRLRIG
S85 PPPGVSPSRLRIGDQ
S96 IGDQEFDSLPALLEF
Y108 LEFYKIHYLDTTTLI
T111 YKIHYLDTTTLIEPV
T112 KIHYLDTTTLIEPVS
T113 IHYLDTTTLIEPVSR
S121 LIEPVSRSRQGSGVI
S125 VSRSRQGSGVILRQE
Y136 LRQEEAEYVRALFDF
K154 DEEDLPFKKGDILRI
Y190 PVPYVEKYRPAsAsV
S194-p VEKYRPAsAsVSALI
S196-p KYRPAsAsVSALIGG
S198 RPAsAsVSALIGGR_
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

► Hide Isoforms
 
S40-p GVFLVRDsstsPGDY
S41-p VFLVRDsstsPGDYV
T42-p FLVRDsstsPGDYVL
S43-p LVRDsstsPGDYVLS
Y47 sstsPGDYVLSVSEN
S74-p PRPPVPPsPAQPPPG
S83-p AQPPPGVsPsRLRIG
S85-p PPPGVsPsRLRIGDQ
S96 IGDQEFDSLPALLEF
Y108-p LEFYKIHyLDTTTLI
T111 YKIHyLDTTTLIEPV
T112 KIHyLDTTTLIEPVA
T113 IHyLDTTTLIEPVAR
S121 LIEPVARSRQGsGVI
S125-p VARSRQGsGVILRQE
Y136-p LRQEEAEyVRALFDF
K154 DEEDLPFKKGDILRI
Y190-p PVPYVEKyRPAsASV
S194-p VEKyRPAsASVsALI
S196 KyRPAsASVsALIGG
S198-p RPAsASVsALIGGNQ
S208-p IGGNQEGsHPQPLGG
Y221-p GGPEPGPyAQPsVNt
S225-p PGPyAQPsVNtPLPN
T228-p yAQPsVNtPLPNLQN
Y239-p NLQNGPIyARVIQKR
Y251-p QKRVPNAyDKTALAL
K253 RVPNAyDKTALALEV
T254 VPNAyDKTALALEVG
3491 : Phospho-CrkII (Tyr221) Antibody
  CRK iso3  
S40 GVFLVRDSSTSPGDY
S41 VFLVRDSSTSPGDYV
T42 FLVRDSSTSPGDYVL
S43 LVRDSSTSPGDYVLS
Y47 SSTSPGDYVLSVSEN
S74 PRPPVPPSPAQPPPG
S83 AQPPPGVSPSRLRIG
S85 PPPGVSPSRLRIGDQ
S96 IGDQEFDSLPALLEF
Y108 LEFYKIHYLDTTTLI
T111 YKIHYLDTTTLIEPV
T112 KIHYLDTTTLIEPVA
T113 IHYLDTTTLIEPVAR
S121 LIEPVARSRQGSGVI
S125 VARSRQGSGVILRQE
Y136 LRQEEAEYVRALFDF
K154 DEEDLPFKKGDILRI
Y190 PVPYVEKYRPAsASV
S194-p VEKYRPAsASVSALI
S196 KYRPAsASVSALIGG
S198 RPAsASVSALIGGR_
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  rat

 
S40 GVFLVRDSSTSPGDY
S41 VFLVRDSSTSPGDYV
T42 FLVRDSSTSPGDYVL
S43 LVRDSSTSPGDYVLS
Y47 SSTSPGDYVLSVSEN
S74 PRPPVPPSPAQPPPG
S83 AQPPPGVSPSRLRIG
S85 PPPGVSPSRLRIGDQ
S96 IGDQEFDSLPALLEF
Y108 LEFYKIHYLDTTTLI
T111 YKIHYLDTTTLIEPV
T112 KIHYLDTTTLIEPVS
T113 IHYLDTTTLIEPVSR
S121-p LIEPVSRsRQGsGVI
S125-p VSRsRQGsGVILRQE
Y136 LRQEEAEYVRALFDF
K154 DEEDLPFKKGDILRI
Y190 PVPYVEKYRPASASV
S194 VEKYRPASASVSALI
S196 KYRPASASVSALIGG
S198 RPASASVSALIGGNQ
S208 IGGNQEGSHPQPLGG
Y221-p GGPEPGPyAQPsVNt
S225-p PGPyAQPsVNtPLPN
T228-p yAQPsVNtPLPNLQN
Y239 NLQNGPIYARVIQKR
Y251-p QKRVPNAyDKTALAL
K253 RVPNAyDKTALALEV
T254 VPNAyDKTALALEVG
3491 : Phospho-CrkII (Tyr221) Antibody
  chicken

 
S40 GTFLVRDSGSIPGDF
G41 TFLVRDSGSIPGDFV
S42 FLVRDSGSIPGDFVL
I43 LVRDSGSIPGDFVLS
F47 SGSIPGDFVLSVSES
G74 PAGGRRAGGEGPGAP
N84 GPGAPGLNPTRFRIG
T86 GAPGLNPTRFRIGDQ
S97 IGDQEFDSLPSLLEF
Y109 LEFYKIHYLDTTTLI
T112 YKIHYLDTTTLIEPV
T113 KIHYLDTTTLIEPVS
T114 IHYLDTTTLIEPVSR
S122 LIEPVSRSRQNSGVI
S126 VSRSRQNSGVILRQE
Y137 LRQEEVEYVRALFDF
K155 DDEDLPFKKGDILKI
C191 PVPYVEKCRPSSASV
S195 VEKCRPSSASVSTLT
S197 KCRPSSASVSTLTGG
S199 RPSSASVSTLTGGNQ
S209 TGGNQDSSHPQPLGG
Y222-p GGPEPGPyAQPSINT
S226 PGPyAQPSINTPLPN
T229 yAQPSINTPLPNLQN
Y240-p NLQNGPFyARVIQKR
Y252 QKRVPNAYDKTALAL
K254 RVPNAYDKTALALEV
T255 VPNAYDKTALALEVG
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