UniProt ID | CRK_HUMAN | |
---|---|---|
UniProt AC | P46108 | |
Protein Name | Adapter molecule crk | |
Gene Name | CRK | |
Organism | Homo sapiens (Human). | |
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 | MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | |
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 | 22223895 | |
7 | Phosphorylation | -MAGNFDSEERSSWY -CCCCCCHHHHHHCC | 36.90 | 25690035 | |
11 | Phosphorylation | NFDSEERSSWYWGRL CCCHHHHHHCCCCCC | 28.62 | 27251275 | |
12 | Phosphorylation | FDSEERSSWYWGRLS CCHHHHHHCCCCCCC | 30.33 | 27251275 | |
40 | Phosphorylation | GVFLVRDSSTSPGDY EEEEEEECCCCCCCE | 25.58 | 22167270 | |
41 | Phosphorylation | VFLVRDSSTSPGDYV EEEEEECCCCCCCEE | 36.87 | 22167270 | |
42 | Phosphorylation | FLVRDSSTSPGDYVL EEEEECCCCCCCEEE | 42.78 | 22167270 | |
43 | Phosphorylation | LVRDSSTSPGDYVLS EEEECCCCCCCEEEE | 28.91 | 30266825 | |
47 | Phosphorylation | SSTSPGDYVLSVSEN CCCCCCCEEEEEECC | 14.81 | 23403867 | |
50 | Phosphorylation | SPGDYVLSVSENSRV CCCCEEEEEECCCEE | 17.35 | 23403867 | |
52 | Phosphorylation | GDYVLSVSENSRVSH CCEEEEEECCCEEEE | 27.90 | 23403867 | |
55 | Phosphorylation | VLSVSENSRVSHYII EEEEECCCEEEEEEE | 29.97 | 23403867 | |
58 | Phosphorylation | VSENSRVSHYIINSS EECCCEEEEEEECCC | 14.95 | 23186163 | |
60 | Phosphorylation | ENSRVSHYIINSSGP CCCEEEEEEECCCCC | 8.94 | 26091039 | |
64 | Phosphorylation | VSHYIINSSGPRPPV EEEEEECCCCCCCCC | 26.68 | 26074081 | |
65 | Phosphorylation | SHYIINSSGPRPPVP EEEEECCCCCCCCCC | 48.61 | 26074081 | |
74 | Phosphorylation | PRPPVPPSPAQPPPG CCCCCCCCCCCCCCC | 27.14 | 26055452 | |
83 | Phosphorylation | AQPPPGVSPSRLRIG CCCCCCCCHHHCEEC | 24.07 | 26055452 | |
85 | Phosphorylation | PPPGVSPSRLRIGDQ CCCCCCHHHCEECCC | 36.12 | 22617229 | |
96 | Phosphorylation | IGDQEFDSLPALLEF ECCCCCCCHHHHHHH | 41.39 | 26657352 | |
108 | Phosphorylation | LEFYKIHYLDTTTLI HHHHEEEEEECCEEE | 15.11 | 23917254 | |
111 | Phosphorylation | YKIHYLDTTTLIEPV HEEEEEECCEEEEEC | 21.05 | 27251275 | |
112 | Phosphorylation | KIHYLDTTTLIEPVS EEEEEECCEEEEECC | 21.19 | 27251275 | |
113 | Phosphorylation | IHYLDTTTLIEPVSR EEEEECCEEEEECCC | 28.03 | 27251275 | |
119 | Phosphorylation | TTLIEPVSRSRQGSG CEEEEECCCCCCCCE | 34.94 | 30576142 | |
121 | Phosphorylation | LIEPVSRSRQGSGVI EEEECCCCCCCCEEE | 22.81 | 29507054 | |
122 | Methylation | IEPVSRSRQGSGVIL EEECCCCCCCCEEEE | 43.71 | - | |
125 | Phosphorylation | VSRSRQGSGVILRQE CCCCCCCCEEEECHH | 22.88 | 25159151 | |
136 | Phosphorylation | LRQEEAEYVRALFDF ECHHHHHHHHHHHCC | 11.41 | 25159151 | |
154 | 2-Hydroxyisobutyrylation | DEEDLPFKKGDILRI CCCCCCCCCCCEEEE | 54.64 | - | |
154 | Acetylation | DEEDLPFKKGDILRI CCCCCCCCCCCEEEE | 54.64 | 24179697 | |
175 | Phosphorylation | QWWNAEDSEGKRGMI HCCCCCCCCCCCCCE | 39.49 | - | |
181 | Sulfoxidation | DSEGKRGMIPVPYVE CCCCCCCCEECCCHH | 3.48 | 30846556 | |
190 (in isoform 2) | Phosphorylation | - | 14.34 | 30266825 | |
190 | Phosphorylation | PVPYVEKYRPASASV ECCCHHCCCCCCCEE | 14.34 | 26356563 | |
194 | Phosphorylation | VEKYRPASASVSALI HHCCCCCCCEEEHHC | 24.61 | 20166139 | |
194 (in isoform 2) | Phosphorylation | - | 24.61 | 30266825 | |
196 | Phosphorylation | KYRPASASVSALIGG CCCCCCCEEEHHCCC | 17.70 | 26356563 | |
196 (in isoform 2) | Phosphorylation | - | 17.70 | 30266825 | |
198 (in isoform 2) | Phosphorylation | - | 18.18 | 30266825 | |
198 | Phosphorylation | RPASASVSALIGGNQ CCCCCEEEHHCCCCC | 18.18 | 26356563 | |
208 | Phosphorylation | IGGNQEGSHPQPLGG CCCCCCCCCCCCCCC | 31.10 | 30576142 | |
221 | Phosphorylation | GGPEPGPYAQPSVNT CCCCCCCCCCCCCCC | 24.63 | 8194526 | |
225 | Phosphorylation | PGPYAQPSVNTPLPN CCCCCCCCCCCCCCC | 18.87 | 26356563 | |
228 | Phosphorylation | YAQPSVNTPLPNLQN CCCCCCCCCCCCCCC | 24.85 | 26356563 | |
239 | Phosphorylation | NLQNGPIYARVIQKR CCCCCCEEEEEHHHH | 7.47 | 17081983 | |
251 | Phosphorylation | QKRVPNAYDKTALAL HHHCCCCCCCHHHEE | 25.31 | 21082442 | |
253 | Acetylation | RVPNAYDKTALALEV HCCCCCCCHHHEEEC | 24.03 | 23954790 | |
254 | Phosphorylation | VPNAYDKTALALEVG CCCCCCCHHHEEECC | 24.81 | 28152594 | |
282 | Acetylation | WEGECNGKRGHFPFT EECCCCCCCCCCCCE | 41.01 | 26051181 | |
304 | Phosphorylation | QNPDEDFS------- CCCCCCCC------- | 52.19 | 28985074 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
41 | S | Phosphorylation | Kinase | PAK1 | Q13153 | PSP |
221 | Y | Phosphorylation | Kinase | ABL | P00519 | PSP |
221 | Y | Phosphorylation | Kinase | ABL2 | P42684 | GPS |
221 | Y | Phosphorylation | Kinase | ABL-FAMILY | - | GPS |
239 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
251 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
251 | Y | Phosphorylation | Kinase | ABL-FAMILY | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CRK_HUMAN !! |
* 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_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-83, AND MASSSPECTROMETRY. | |
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-136; TYR-221 ANDTYR-251, AND MASS SPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, AND MASSSPECTROMETRY. | |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASSSPECTROMETRY. |