CRK_MOUSE - dbPTM
CRK_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRK_MOUSE
UniProt AC Q64010
Protein Name Adapter molecule crk
Gene Name Crk
Organism Mus musculus (Mouse).
Sequence Length 304
Subcellular Localization Cytoplasm. Cell membrane. Translocated to the plasma membrane upon cell adhesion..
Protein Description Isoform Crk-II: Regulates cell adhesion, spreading and migration. 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 MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVARSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAGNFDSEE
------CCCCCCHHH		22.95-
40PhosphorylationGVFLVRDSSTSPGDY
EEEEEEECCCCCCCE		25.5825521595
41PhosphorylationVFLVRDSSTSPGDYV
EEEEEECCCCCCCEE		36.8725521595
42PhosphorylationFLVRDSSTSPGDYVL
EEEEECCCCCCCEEE		42.7824925903
43PhosphorylationLVRDSSTSPGDYVLS
EEEECCCCCCCEEEE		28.9124925903
47PhosphorylationSSTSPGDYVLSVSEN
CCCCCCCEEEEEECC		14.8125619855
50PhosphorylationSPGDYVLSVSENSRV
CCCCEEEEEECCCEE		17.3525619855
52PhosphorylationGDYVLSVSENSRVSH
CCEEEEEECCCEEEE		27.9025619855
55PhosphorylationVLSVSENSRVSHYII
EEEEECCCEEEEEEE		29.9725619855
58PhosphorylationVSENSRVSHYIINSS
EECCCEEEEEEECCC		14.9518846507
60PhosphorylationENSRVSHYIINSSGP
CCCEEEEEEECCCCC		8.9418846507
64PhosphorylationVSHYIINSSGPRPPV
EEEEEECCCCCCCCC		26.6818846507
65PhosphorylationSHYIINSSGPRPPVP
EEEEECCCCCCCCCC		48.6118846507
74PhosphorylationPRPPVPPSPAQPPPG
CCCCCCCCCCCCCCC		27.1429514104
83PhosphorylationAQPPPGVSPSRLRIG
CCCCCCCCHHHCEEC		24.0726643407
85PhosphorylationPPPGVSPSRLRIGDQ
CCCCCCHHHCEECCC		36.1225521595
108PhosphorylationLEFYKIHYLDTTTLI
HHHHEEEEEECCCEE		15.1123023260
121PhosphorylationLIEPVARSRQGSGVI
EEEEHHHCCCCCEEE		21.1525338131
125PhosphorylationVARSRQGSGVILRQE
HHHCCCCCEEEECHH		22.8826824392
136PhosphorylationLRQEEAEYVRALFDF
ECHHHHHHHHHHHCC		11.4125521595
186PhosphorylationRGMIPVPYVEKYRPA
CCCEECCCHHCCCCC		22.8329514104
190PhosphorylationPVPYVEKYRPASASV
ECCCHHCCCCCCCEE		14.3425367039
194PhosphorylationVEKYRPASASVSALI
HHCCCCCCCEEEHHC		24.6119060867
196PhosphorylationKYRPASASVSALIGG
CCCCCCCEEEHHCCC		17.7025367039
198PhosphorylationRPASASVSALIGGNQ
CCCCCEEEHHCCCCC		18.1825367039
208PhosphorylationIGGNQEGSHPQPLGG
CCCCCCCCCCCCCCC		31.1025367039
221PhosphorylationGGPEPGPYAQPSVNT
CCCCCCCCCCCCCCC		24.638194526
225PhosphorylationPGPYAQPSVNTPLPN
CCCCCCCCCCCCCCC		18.8725367039
228PhosphorylationYAQPSVNTPLPNLQN
CCCCCCCCCCCCCCC		24.8524453211
239PhosphorylationNLQNGPIYARVIQKR
CCCCCCEEEEEHHHH		7.4722817900
251PhosphorylationQKRVPNAYDKTALAL
HHHCCCCCCCHHHEE		25.3129899451
253AcetylationRVPNAYDKTALALEV
HCCCCCCCHHHEEEC		24.0322826441
304PhosphorylationQNPDEDFS-------
CCCCCCCC-------		52.1925619855
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
221YPhosphorylationKinaseABL1P00519
GPS
221YPhosphorylationKinaseABL1P00520
Uniprot
221YPhosphorylationKinaseIGF1RQ60751
PSP
221YPhosphorylationKinaseABL-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRK_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CRK_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DVL2_MOUSEDvl2physical
19920076
CBL_MOUSECblphysical
9013636
CBL_MOUSECblphysical
11997497
CBL_MOUSECblphysical
9447983
P85B_MOUSEPik3r2physical
20697350
PK3CB_MOUSEPik3cbphysical
20697350
ABL1_MOUSEAbl1physical
20697350
PRAG1_MOUSED8Ertd82ephysical
20697350
P85A_MOUSEPik3r1physical
20697350
BCR_MOUSEBcrphysical
20697350
CBL_MOUSECblphysical
20697350
1433E_MOUSEYwhaephysical
20697350
1433Z_MOUSEYwhazphysical
20697350
1433F_MOUSEYwhahphysical
20697350
AVIL_MOUSEAvilphysical
20697350
PLEC_MOUSEPlecphysical
20697350
1433T_MOUSEYwhaqphysical
20697350
1433B_MOUSEYwhabphysical
20697350
1433G_MOUSEYwhagphysical
20697350
RHG33_MOUSEArhgap33physical
12773384
CBL_MOUSECblphysical
8635998
CBL_MOUSECblphysical
11069064
IRS1_MOUSEIrs1physical
9729467
BCAR1_MOUSEBcar1physical
9729467
CBL_MOUSECblphysical
9210408
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRK_MOUSE

loading...

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 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.
"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.
"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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory