Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Crk (human)

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: Motility/polarity/chemotaxis; Adaptor/scaffold
Cellular Component: cytoplasm; plasma membrane; cytosol; nucleus
Molecular Function: protein phosphorylated amino acid binding; protein binding; SH3/SH2 adaptor activity; ephrin receptor binding; 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; activation of MAPKK activity; nerve growth factor receptor signaling pathway; regulation of actin cytoskeleton organization and biogenesis; insulin receptor signaling pathway; ephrin 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
CST Pathways:  Actin Dynamics  |  ErbB/HER Signaling  |  Growth And Differentiation Control by MAPKs  |  Insulin Receptor Signaling  |  SAPK/JNK Signaling Cascades
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Crk

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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

► Hide Isoforms
 
0 13 S40-p GVFLVRDsstsPGDY
1 27 S41-p VFLVRDsstsPGDYV
0 8 T42-p FLVRDsstsPGDYVL
0 2 S43-p LVRDsstsPGDYVLS
0 16 S74-p PRPPVPPsPAQPPPG
0 5 S83-p AQPPPGVsPsRLRIG
0 4 S85-p PPPGVsPsRLRIGDQ
0 76 Y108-p LEFYKIHyLDTtTLI
0 3 T112-p KIHyLDTtTLIEPVS
0 7 S125-p VSRSRQGsGVILRQE
0 64 Y136-p LRQEEAEyVRALFDF
0 6 Y190-p PVPYVEKyRPAsAsV
0 10 S194-p VEKyRPAsAsVsALI
0 6 S196-p KyRPAsAsVsALIGG
0 4 S198-p RPAsAsVsALIGGNQ
0 8 S208-p IGGNQEGsHPQPLGG
20 1149 Y221-p GGPEPGPyAQPsVNt
0 419 S225-p PGPyAQPsVNtPLPN
0 46 T228-p yAQPsVNtPLPNLQN
1 257 Y239-p NLQNGPIyARVIQKR
1 302 Y251-p QKRVPNAyDKtALAL
0 2 T254-p VPNAyDKtALALEVG
3491 : Phospho-CrkII (Tyr221) Antibody
  Crk iso2  
S40 GVFLVRDSSTSPGDY
S41 VFLVRDSSTSPGDYV
T42 FLVRDSSTSPGDYVL
S43 LVRDSSTSPGDYVLS
S74 PRPPVPPSPAQPPPG
S83 AQPPPGVSPSRLRIG
S85 PPPGVSPSRLRIGDQ
Y108 LEFYKIHYLDTTTLI
T112 KIHYLDTTTLIEPVS
S125 VSRSRQGSGVILRQE
Y136 LRQEEAEYVRALFDF
Y190 PVPYVEKYRPAsAsV
S194-p VEKYRPAsAsVSALI
S196-p KYRPAsAsVSALIGG
S198 RPAsAsVSALIGGR_
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

► Hide Isoforms
 
S40-p GVFLVRDsstsPGDY
S41-p VFLVRDsstsPGDYV
T42-p FLVRDsstsPGDYVL
S43-p LVRDsstsPGDYVLS
S74-p PRPPVPPsPAQPPPG
S83-p AQPPPGVsPsRLRIG
S85-p PPPGVsPsRLRIGDQ
Y108-p LEFYKIHyLDTTTLI
T112 KIHyLDTTTLIEPVA
S125-p VARSRQGsGVILRQE
Y136-p LRQEEAEyVRALFDF
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
T254 VPNAyDKTALALEVG
3491 : Phospho-CrkII (Tyr221) Antibody
  Crk iso3  
S40 GVFLVRDSSTSPGDY
S41 VFLVRDSSTSPGDYV
T42 FLVRDSSTSPGDYVL
S43 LVRDSSTSPGDYVLS
S74 PRPPVPPSPAQPPPG
S83 AQPPPGVSPSRLRIG
S85 PPPGVSPSRLRIGDQ
Y108 LEFYKIHYLDTTTLI
T112 KIHYLDTTTLIEPVA
S125 VARSRQGSGVILRQE
Y136 LRQEEAEYVRALFDF
Y190 PVPYVEKYRPAsASV
S194-p VEKYRPAsASVSALI
S196 KYRPAsASVSALIGG
S198 RPAsASVSALIGGR_
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  rat

 
S40 GVFLVRDSSTSPGDY
S41 VFLVRDSSTSPGDYV
T42 FLVRDSSTSPGDYVL
S43 LVRDSSTSPGDYVLS
S74 PRPPVPPSPAQPPPG
S83 AQPPPGVSPSRLRIG
S85 PPPGVSPSRLRIGDQ
Y108 LEFYKIHYLDTTTLI
T112 KIHYLDTTTLIEPVS
S125-p VSRSRQGsGVILRQE
Y136 LRQEEAEYVRALFDF
Y190 PVPYVEKYRPASASV
S194 VEKYRPASASVSALI
S196 KYRPASASVSALIGG
S198 RPASASVSALIGGNQ
S208 IGGNQEGSHPQPLGG
Y221-p GGPEPGPyAQPSVNT
S225 PGPyAQPSVNTPLPN
T228 yAQPSVNTPLPNLQN
Y239 NLQNGPIYARVIQKR
Y251-p QKRVPNAyDKTALAL
T254 VPNAyDKTALALEVG
3491 : Phospho-CrkII (Tyr221) Antibody
  chicken

 
S40 GTFLVRDSGSIPGDF
G41 TFLVRDSGSIPGDFV
S42 FLVRDSGSIPGDFVL
I43 LVRDSGSIPGDFVLS
G74 PAGGRRAGGEGPGAP
N84 GPGAPGLNPTRFRIG
T86 GAPGLNPTRFRIGDQ
Y109 LEFYKIHYLDTTTLI
T113 KIHYLDTTTLIEPVS
S126 VSRSRQNSGVILRQE
Y137 LRQEEVEYVRALFDF
C191 PVPYVEKCRPSSASV
S195 VEKCRPSSASVSTLT
S197 KCRPSSASVSTLTGG
S199 RPSSASVSTLTGGNQ
S209 TGGNQDSSHPQPLGG
Y222-p GGPEPGPyAQPSINT
S226 PGPyAQPSINTPLPN
T229 yAQPSINTPLPNLQN
Y240-p NLQNGPFyARVIQKR
Y252 QKRVPNAYDKTALAL
T255 VPNAYDKTALALEVG
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.