Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Adapter molecule crk  

UniProtKB / Swiss-Prot ID :  CRK_MOUSE

Gene Name (Synonyms) : 
Crk, Crko  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocated to the plasma membrane upon cell adhesion (By similarity). 

Protein Function :  The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk- II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. 

Protein Sequence MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPP...
Predicted Secondary Structure CCCCCCCHHCCCCCCCCCCHHHHHHHHCCCCCCCEEEECCCCCCCCEEEEEEECCCEEEEEEEECCCCCE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
40PhosphoserineLVRDSSTSP
EEECCCCCC
25.58Phosphositeplus
Link-
41PhosphoserineVRDSSTSPG
EECCCCCCC
36.87PhosphoELM
Link-
41PhosphoserineVRDSSTSPG
EECCCCCCC
36.87Phosphositeplus
Link-
41PhosphoserineVRDSSTSPG
EECCCCCCC
36.87SysPTM
Link-
41Phosphoserine.VRDSSTSPG
EECCCCCCC
36.87UniProtKB
Link-
42PhosphothreonineRDSSTSPGD
ECCCCCCCC
42.78PhosphoELM
Link-
42PhosphothreonineRDSSTSPGD
ECCCCCCCC
42.78Phosphositeplus
Link-
42PhosphothreonineRDSSTSPGD
ECCCCCCCC
42.78SysPTM
Link-
42Phosphothreonine.RDSSTSPGD
ECCCCCCCC
42.78UniProtKB
Link-
125PhosphoserineSRQGSGVIL
CCCCCCCCC
22.88Phosphositeplus
Link-
125PhosphoserineSRQGSGVIL
CCCCCCCCC
22.88SysPTM
Link-
136PhosphotyrosineEEAEYVRAL
HCCEEEEEE
11.41Phosphositeplus
Link
221PhosphotyrosineEPGPYAQPS
CCCCCCCCC
24.63Phosphositeplus
Link-
221PhosphotyrosineEPGPYAQPS
CCCCCCCCC
24.63SysPTM
Link-
221Phosphotyrosine (Abl;Abl;IGF1R)EPGPYAQPS
CCCCCCCCC
24.63PhosphoELM
Link-
221Phosphotyrosine; by ABL1.EPGPYAQPS
CCCCCCCCC
24.63UniProtKB
Link-
239PhosphotyrosineNGPIYARVI
CCCEEEEEE
7.47Phosphositeplus
Link-
239PhosphotyrosineNGPIYARVI
CCCEEEEEE
7.47SysPTM
Link-
251PhosphotyrosineVPNAYDKTA
CCCCCCCCC
25.31Phosphositeplus
Link-
251PhosphotyrosineVPNAYDKTA
CCCCCCCCC
25.31SysPTM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, AND MASSSPECTROMETRY.
"c-Abl kinase regulates the protein binding activity of c-Crk.";
Feller S.M., Knudsen B., Hanafusa H.;
EMBO J. 13:2341-2351(1994).
Cited for: PHOSPHORYLATION AT TYR-221, AND INTERACTION WITH ABL1.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures