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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAGNFDSEE ------CCCCCCHHH | 22.95 | - | |
40 | Phosphorylation | GVFLVRDSSTSPGDY EEEEEEECCCCCCCE | 25.58 | 25521595 | |
41 | Phosphorylation | VFLVRDSSTSPGDYV EEEEEECCCCCCCEE | 36.87 | 25521595 | |
42 | Phosphorylation | FLVRDSSTSPGDYVL EEEEECCCCCCCEEE | 42.78 | 24925903 | |
43 | Phosphorylation | LVRDSSTSPGDYVLS EEEECCCCCCCEEEE | 28.91 | 24925903 | |
47 | Phosphorylation | SSTSPGDYVLSVSEN CCCCCCCEEEEEECC | 14.81 | 25619855 | |
50 | Phosphorylation | SPGDYVLSVSENSRV CCCCEEEEEECCCEE | 17.35 | 25619855 | |
52 | Phosphorylation | GDYVLSVSENSRVSH CCEEEEEECCCEEEE | 27.90 | 25619855 | |
55 | Phosphorylation | VLSVSENSRVSHYII EEEEECCCEEEEEEE | 29.97 | 25619855 | |
58 | Phosphorylation | VSENSRVSHYIINSS EECCCEEEEEEECCC | 14.95 | 18846507 | |
60 | Phosphorylation | ENSRVSHYIINSSGP CCCEEEEEEECCCCC | 8.94 | 18846507 | |
64 | Phosphorylation | VSHYIINSSGPRPPV EEEEEECCCCCCCCC | 26.68 | 18846507 | |
65 | Phosphorylation | SHYIINSSGPRPPVP EEEEECCCCCCCCCC | 48.61 | 18846507 | |
74 | Phosphorylation | PRPPVPPSPAQPPPG CCCCCCCCCCCCCCC | 27.14 | 29514104 | |
83 | Phosphorylation | AQPPPGVSPSRLRIG CCCCCCCCHHHCEEC | 24.07 | 26643407 | |
85 | Phosphorylation | PPPGVSPSRLRIGDQ CCCCCCHHHCEECCC | 36.12 | 25521595 | |
108 | Phosphorylation | LEFYKIHYLDTTTLI HHHHEEEEEECCCEE | 15.11 | 23023260 | |
121 | Phosphorylation | LIEPVARSRQGSGVI EEEEHHHCCCCCEEE | 21.15 | 25338131 | |
125 | Phosphorylation | VARSRQGSGVILRQE HHHCCCCCEEEECHH | 22.88 | 26824392 | |
136 | Phosphorylation | LRQEEAEYVRALFDF ECHHHHHHHHHHHCC | 11.41 | 25521595 | |
186 | Phosphorylation | RGMIPVPYVEKYRPA CCCEECCCHHCCCCC | 22.83 | 29514104 | |
190 | Phosphorylation | PVPYVEKYRPASASV ECCCHHCCCCCCCEE | 14.34 | 25367039 | |
194 | Phosphorylation | VEKYRPASASVSALI HHCCCCCCCEEEHHC | 24.61 | 19060867 | |
196 | Phosphorylation | KYRPASASVSALIGG CCCCCCCEEEHHCCC | 17.70 | 25367039 | |
198 | Phosphorylation | RPASASVSALIGGNQ CCCCCEEEHHCCCCC | 18.18 | 25367039 | |
208 | Phosphorylation | IGGNQEGSHPQPLGG CCCCCCCCCCCCCCC | 31.10 | 25367039 | |
221 | Phosphorylation | GGPEPGPYAQPSVNT CCCCCCCCCCCCCCC | 24.63 | 8194526 | |
225 | Phosphorylation | PGPYAQPSVNTPLPN CCCCCCCCCCCCCCC | 18.87 | 25367039 | |
228 | Phosphorylation | YAQPSVNTPLPNLQN CCCCCCCCCCCCCCC | 24.85 | 24453211 | |
239 | Phosphorylation | NLQNGPIYARVIQKR CCCCCCEEEEEHHHH | 7.47 | 22817900 | |
251 | Phosphorylation | QKRVPNAYDKTALAL HHHCCCCCCCHHHEE | 25.31 | 29899451 | |
253 | Acetylation | RVPNAYDKTALALEV HCCCCCCCHHHEEEC | 24.03 | 22826441 | |
304 | Phosphorylation | QNPDEDFS------- CCCCCCCC------- | 52.19 | 25619855 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
221 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
221 | Y | Phosphorylation | Kinase | ABL1 | P00520 | Uniprot |
221 | Y | Phosphorylation | Kinase | IGF1R | Q60751 | PSP |
221 | Y | Phosphorylation | Kinase | ABL-FAMILY | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CRK_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DVL2_MOUSE | Dvl2 | physical | 19920076 | |
CBL_MOUSE | Cbl | physical | 9013636 | |
CBL_MOUSE | Cbl | physical | 11997497 | |
CBL_MOUSE | Cbl | physical | 9447983 | |
P85B_MOUSE | Pik3r2 | physical | 20697350 | |
PK3CB_MOUSE | Pik3cb | physical | 20697350 | |
ABL1_MOUSE | Abl1 | physical | 20697350 | |
PRAG1_MOUSE | D8Ertd82e | physical | 20697350 | |
P85A_MOUSE | Pik3r1 | physical | 20697350 | |
BCR_MOUSE | Bcr | physical | 20697350 | |
CBL_MOUSE | Cbl | physical | 20697350 | |
1433E_MOUSE | Ywhae | physical | 20697350 | |
1433Z_MOUSE | Ywhaz | physical | 20697350 | |
1433F_MOUSE | Ywhah | physical | 20697350 | |
AVIL_MOUSE | Avil | physical | 20697350 | |
PLEC_MOUSE | Plec | physical | 20697350 | |
1433T_MOUSE | Ywhaq | physical | 20697350 | |
1433B_MOUSE | Ywhab | physical | 20697350 | |
1433G_MOUSE | Ywhag | physical | 20697350 | |
RHG33_MOUSE | Arhgap33 | physical | 12773384 | |
CBL_MOUSE | Cbl | physical | 8635998 | |
CBL_MOUSE | Cbl | physical | 11069064 | |
IRS1_MOUSE | Irs1 | physical | 9729467 | |
BCAR1_MOUSE | Bcar1 | physical | 9729467 | |
CBL_MOUSE | Cbl | physical | 9210408 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |