UniProt ID | SH3K1_HUMAN | |
---|---|---|
UniProt AC | Q96B97 | |
Protein Name | SH3 domain-containing kinase-binding protein 1 | |
Gene Name | SH3KBP1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 665 | |
Subcellular Localization |
Cytoplasm . Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane Peripheral membrane protein. Cell junction, synapse, synaptosome. Cell junction, focal adhesion. Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1 |
|
Protein Description | Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration.. | |
Protein Sequence | MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQINGRRGLFPDNFVREIKKEMKKDPLTNKAPEKPLHEVPSGNSLLSSETILRTNKRGERRRRRCQVAFSYLPQNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQLSKSSLRETTGSESDGGDSSSTKSEGANGTVATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTIGKKLPATTATPDSSKTEMDSRTKSKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCIDVGWWEGELNGRRGVFPDNFVKLLPPDFEKEGNRPKKPPPPSAPVIKQGAGTTERKHEIKKIPPERPEMLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLSRPGALPPRRPERPVGPLTHTRGDSPKIDLAGSSLSGILDKDLSDRSNDIDLEGFDSVVSSTEKLSHPTTSRPKATGRRPPSQSLTSSSLSSPDIFDSPSPEEDKEEHISLAHRGVDASKKTSKTVTISQVSDNKASLPPKPGTMAAGGGGPAPLSSAAPSPLSSSLGTAGHRANSPSLFGTEGKPKMEPAASSQAAVEELRTQVRELRSIIETMKDQQKREIKQLLSELDEEKKIRLRLQMEVNDIKKALQSK | |
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 |
---|---|---|---|---|---|
10 (in isoform 2) | Phosphorylation | - | 15.86 | 26657352 | |
10 | Phosphorylation | EAIVEFDYQAQHDDE EEEEEECEECCCCCE | 15.86 | 24043423 | |
19 | Phosphorylation | AQHDDELTISVGEII CCCCCEEEEEHHHHH | 14.79 | 24043423 | |
21 | Phosphorylation | HDDELTISVGEIITN CCCEEEEEHHHHHHE | 20.87 | 24043423 | |
27 | Phosphorylation | ISVGEIITNIRKEDG EEHHHHHHEEEHHHC | 30.19 | 24043423 | |
42 (in isoform 2) | Phosphorylation | - | 29.99 | - | |
45 (in isoform 2) | Phosphorylation | - | 47.79 | - | |
57 | Acetylation | DNFVREIKKEMKKDP HHHHHHHHHHHHCCC | 37.62 | 7370243 | |
58 | Acetylation | NFVREIKKEMKKDPL HHHHHHHHHHHCCCC | 69.56 | 7373309 | |
61 | Acetylation | REIKKEMKKDPLTNK HHHHHHHHCCCCCCC | 55.93 | 7373321 | |
62 | Acetylation | EIKKEMKKDPLTNKA HHHHHHHCCCCCCCC | 64.37 | 7370255 | |
66 | Phosphorylation | EMKKDPLTNKAPEKP HHHCCCCCCCCCCCC | 39.81 | 26074081 | |
72 | Ubiquitination | LTNKAPEKPLHEVPS CCCCCCCCCCCCCCC | 52.39 | - | |
72 | Acetylation | LTNKAPEKPLHEVPS CCCCCCCCCCCCCCC | 52.39 | 25953088 | |
79 | Phosphorylation | KPLHEVPSGNSLLSS CCCCCCCCCCCCCCH | 56.64 | 23401153 | |
82 | Phosphorylation | HEVPSGNSLLSSETI CCCCCCCCCCCHHHH | 33.92 | 25159151 | |
85 | Phosphorylation | PSGNSLLSSETILRT CCCCCCCCHHHHHHC | 31.27 | 28450419 | |
86 | Phosphorylation | SGNSLLSSETILRTN CCCCCCCHHHHHHCC | 38.43 | 28450419 | |
88 | Phosphorylation | NSLLSSETILRTNKR CCCCCHHHHHHCCCC | 27.53 | 28450419 | |
108 | Phosphorylation | RRCQVAFSYLPQNDD HHHEEEEEECCCCCC | 18.93 | 22617229 | |
109 | Phosphorylation | RCQVAFSYLPQNDDE HHEEEEEECCCCCCC | 18.89 | 30183078 | |
156 | Phosphorylation | SNFIKELSGESDELG HHHHHHHCCCCCCCC | 41.42 | 20164059 | |
159 | Phosphorylation | IKELSGESDELGISQ HHHHCCCCCCCCCCH | 39.65 | 28450419 | |
165 | Phosphorylation | ESDELGISQDEQLSK CCCCCCCCHHHHHCH | 29.76 | 20164059 | |
171 | Phosphorylation | ISQDEQLSKSSLRET CCHHHHHCHHHHHHC | 30.13 | 30108239 | |
172 | Ubiquitination | SQDEQLSKSSLRETT CHHHHHCHHHHHHCC | 53.29 | - | |
173 | Phosphorylation | QDEQLSKSSLRETTG HHHHHCHHHHHHCCC | 31.09 | 23401153 | |
174 | Phosphorylation | DEQLSKSSLRETTGS HHHHCHHHHHHCCCC | 34.87 | 23403867 | |
178 | Phosphorylation | SKSSLRETTGSESDG CHHHHHHCCCCCCCC | 29.98 | 29255136 | |
179 | Phosphorylation | KSSLRETTGSESDGG HHHHHHCCCCCCCCC | 33.68 | 29255136 | |
181 | Phosphorylation | SLRETTGSESDGGDS HHHHCCCCCCCCCCC | 31.66 | 29255136 | |
183 | Phosphorylation | RETTGSESDGGDSSS HHCCCCCCCCCCCCC | 43.16 | 23401153 | |
188 | Phosphorylation | SESDGGDSSSTKSEG CCCCCCCCCCCCCCC | 29.48 | 28176443 | |
189 | Phosphorylation | ESDGGDSSSTKSEGA CCCCCCCCCCCCCCC | 46.93 | 23403867 | |
190 | Phosphorylation | SDGGDSSSTKSEGAN CCCCCCCCCCCCCCC | 43.75 | 23403867 | |
191 | Phosphorylation | DGGDSSSTKSEGANG CCCCCCCCCCCCCCC | 40.30 | 23403867 | |
193 | Phosphorylation | GDSSSTKSEGANGTV CCCCCCCCCCCCCCE | 41.15 | 19664994 | |
193 (in isoform 2) | Phosphorylation | - | 41.15 | - | |
199 | Phosphorylation | KSEGANGTVATAAIQ CCCCCCCCEEEEEEC | 13.53 | 29255136 | |
202 | Phosphorylation | GANGTVATAAIQPKK CCCCCEEEEEECCCE | 16.58 | 26074081 | |
217 (in isoform 2) | Phosphorylation | - | 40.67 | - | |
230 | Phosphorylation | PIKLRPRSIEVENDF CCEECCCEEEEECCC | 26.28 | 19664994 | |
242 | Ubiquitination | NDFLPVEKTIGKKLP CCCCCCCCCCCCCCC | 45.75 | - | |
243 | Phosphorylation | DFLPVEKTIGKKLPA CCCCCCCCCCCCCCC | 22.81 | 26074081 | |
251 | Phosphorylation | IGKKLPATTATPDSS CCCCCCCCCCCCCCC | 18.28 | 28450419 | |
252 | Phosphorylation | GKKLPATTATPDSSK CCCCCCCCCCCCCCC | 30.55 | 28450419 | |
254 | Phosphorylation | KLPATTATPDSSKTE CCCCCCCCCCCCCCC | 26.07 | 29255136 | |
257 | Phosphorylation | ATTATPDSSKTEMDS CCCCCCCCCCCCCCC | 34.63 | 28450419 | |
258 | Phosphorylation | TTATPDSSKTEMDSR CCCCCCCCCCCCCCC | 51.48 | 28450419 | |
260 | Phosphorylation | ATPDSSKTEMDSRTK CCCCCCCCCCCCCCC | 38.19 | 23186163 | |
262 | Sulfoxidation | PDSSKTEMDSRTKSK CCCCCCCCCCCCCCC | 7.39 | 21406390 | |
344 | Phosphorylation | PKKPPPPSAPVIKQG CCCCCCCCCCCCCCC | 51.48 | 21712546 | |
349 | Methylation | PPSAPVIKQGAGTTE CCCCCCCCCCCCCCC | 42.80 | 115981273 | |
354 | Phosphorylation | VIKQGAGTTERKHEI CCCCCCCCCCCHHHH | 25.58 | 21712546 | |
355 | Phosphorylation | IKQGAGTTERKHEIK CCCCCCCCCCHHHHC | 32.64 | 21712546 | |
399 (in isoform 2) | Phosphorylation | - | 36.44 | - | |
401 | Acetylation | SVPAIPPKKPRPPKT CCCCCCCCCCCCCCC | 70.79 | 30587677 | |
408 | Phosphorylation | KKPRPPKTNSLSRPG CCCCCCCCCCCCCCC | 35.49 | 29978859 | |
410 | Phosphorylation | PRPPKTNSLSRPGAL CCCCCCCCCCCCCCC | 32.71 | 24260401 | |
410 (in isoform 2) | Phosphorylation | - | 32.71 | - | |
412 | Phosphorylation | PPKTNSLSRPGALPP CCCCCCCCCCCCCCC | 35.93 | 29978859 | |
435 (in isoform 2) | Phosphorylation | - | 59.48 | - | |
436 | Phosphorylation | LTHTRGDSPKIDLAG CCCCCCCCCCCCCCC | 30.80 | 22617229 | |
436 (in isoform 2) | Phosphorylation | - | 30.80 | - | |
438 | Ubiquitination | HTRGDSPKIDLAGSS CCCCCCCCCCCCCCC | 53.45 | - | |
444 | Phosphorylation | PKIDLAGSSLSGILD CCCCCCCCCHHHHHC | 23.62 | 24732914 | |
445 | Phosphorylation | KIDLAGSSLSGILDK CCCCCCCCHHHHHCC | 26.15 | 24732914 | |
447 | Phosphorylation | DLAGSSLSGILDKDL CCCCCCHHHHHCCCC | 26.24 | 22617229 | |
452 | Ubiquitination | SLSGILDKDLSDRSN CHHHHHCCCCCCCCC | 58.06 | - | |
455 | Phosphorylation | GILDKDLSDRSNDID HHHCCCCCCCCCCCC | 40.90 | 29083192 | |
468 | Phosphorylation | IDLEGFDSVVSSTEK CCCCCHHHHHCCCCC | 23.35 | 22210691 | |
471 | Phosphorylation | EGFDSVVSSTEKLSH CCHHHHHCCCCCCCC | 29.41 | 22199227 | |
471 | O-linked_Glycosylation | EGFDSVVSSTEKLSH CCHHHHHCCCCCCCC | 29.41 | 30379171 | |
472 | Phosphorylation | GFDSVVSSTEKLSHP CHHHHHCCCCCCCCC | 29.04 | 21815630 | |
472 (in isoform 2) | Phosphorylation | - | 29.04 | - | |
472 | O-linked_Glycosylation | GFDSVVSSTEKLSHP CHHHHHCCCCCCCCC | 29.04 | 30379171 | |
473 | Phosphorylation | FDSVVSSTEKLSHPT HHHHHCCCCCCCCCC | 29.63 | 22199227 | |
474 (in isoform 2) | Phosphorylation | - | 54.68 | - | |
475 | Ubiquitination | SVVSSTEKLSHPTTS HHHCCCCCCCCCCCC | 56.21 | - | |
482 | Phosphorylation | KLSHPTTSRPKATGR CCCCCCCCCCCCCCC | 49.41 | 22210691 | |
484 (in isoform 2) | Phosphorylation | - | 30.33 | - | |
493 | Phosphorylation | ATGRRPPSQSLTSSS CCCCCCCCCCCCCCC | 34.77 | 25159151 | |
495 | Phosphorylation | GRRPPSQSLTSSSLS CCCCCCCCCCCCCCC | 37.64 | 25159151 | |
497 | Phosphorylation | RPPSQSLTSSSLSSP CCCCCCCCCCCCCCC | 31.63 | 30206219 | |
498 | Phosphorylation | PPSQSLTSSSLSSPD CCCCCCCCCCCCCCC | 24.19 | 23927012 | |
499 (in isoform 2) | Phosphorylation | - | 30.02 | - | |
499 | Phosphorylation | PSQSLTSSSLSSPDI CCCCCCCCCCCCCCC | 30.02 | 23927012 | |
500 | Phosphorylation | SQSLTSSSLSSPDIF CCCCCCCCCCCCCCC | 31.85 | 23927012 | |
501 (in isoform 2) | Phosphorylation | - | 6.76 | - | |
502 | Phosphorylation | SLTSSSLSSPDIFDS CCCCCCCCCCCCCCC | 41.60 | 25159151 | |
503 | Phosphorylation | LTSSSLSSPDIFDSP CCCCCCCCCCCCCCC | 31.70 | 23927012 | |
503 (in isoform 2) | Phosphorylation | - | 31.70 | - | |
509 | Phosphorylation | SSPDIFDSPSPEEDK CCCCCCCCCCCHHHH | 19.27 | 29255136 | |
511 | Phosphorylation | PDIFDSPSPEEDKEE CCCCCCCCCHHHHHH | 49.23 | 29255136 | |
521 | Phosphorylation | EDKEEHISLAHRGVD HHHHHHHHHHHHCCC | 22.78 | 23927012 | |
535 | Acetylation | DASKKTSKTVTISQV CCCCCCCCEEEEEEE | 52.85 | 15609851 | |
536 | Phosphorylation | ASKKTSKTVTISQVS CCCCCCCEEEEEEEC | 23.73 | 18077418 | |
536 | O-linked_Glycosylation | ASKKTSKTVTISQVS CCCCCCCEEEEEEEC | 23.73 | 30379171 | |
538 | Phosphorylation | KKTSKTVTISQVSDN CCCCCEEEEEEECCC | 21.83 | 27470641 | |
540 | Phosphorylation | TSKTVTISQVSDNKA CCCEEEEEEECCCCC | 18.37 | 18077418 | |
546 | Acetylation | ISQVSDNKASLPPKP EEEECCCCCCCCCCC | 44.32 | 19818093 | |
548 | Phosphorylation | QVSDNKASLPPKPGT EECCCCCCCCCCCCC | 42.91 | 25002506 | |
550 (in isoform 2) | Phosphorylation | - | 32.16 | - | |
552 (in isoform 2) | Phosphorylation | - | 54.89 | - | |
555 | O-linked_Glycosylation | SLPPKPGTMAAGGGG CCCCCCCCCCCCCCC | 16.50 | 30379171 | |
555 | Phosphorylation | SLPPKPGTMAAGGGG CCCCCCCCCCCCCCC | 16.50 | 25002506 | |
567 | O-linked_Glycosylation | GGGPAPLSSAAPSPL CCCCCCCCCCCCCCC | 19.51 | 30379171 | |
567 | Phosphorylation | GGGPAPLSSAAPSPL CCCCCCCCCCCCCCC | 19.51 | 25002506 | |
568 | Phosphorylation | GGPAPLSSAAPSPLS CCCCCCCCCCCCCCC | 35.81 | 25002506 | |
572 | Phosphorylation | PLSSAAPSPLSSSLG CCCCCCCCCCCCCCC | 33.47 | 27050516 | |
575 | Phosphorylation | SAAPSPLSSSLGTAG CCCCCCCCCCCCCCC | 22.67 | 25002506 | |
576 | Phosphorylation | AAPSPLSSSLGTAGH CCCCCCCCCCCCCCH | 36.95 | 25002506 | |
577 | Phosphorylation | APSPLSSSLGTAGHR CCCCCCCCCCCCCHH | 27.69 | 25002506 | |
580 | Phosphorylation | PLSSSLGTAGHRANS CCCCCCCCCCHHCCC | 34.46 | 25002506 | |
587 | Phosphorylation | TAGHRANSPSLFGTE CCCHHCCCCHHCCCC | 18.19 | 19664994 | |
589 | Phosphorylation | GHRANSPSLFGTEGK CHHCCCCHHCCCCCC | 35.83 | 26329039 | |
593 | Phosphorylation | NSPSLFGTEGKPKME CCCHHCCCCCCCCCC | 33.94 | 25159151 | |
596 | Malonylation | SLFGTEGKPKMEPAA HHCCCCCCCCCCCCH | 34.92 | 26320211 | |
598 | Sumoylation | FGTEGKPKMEPAASS CCCCCCCCCCCCHHC | 60.42 | - | |
598 | Sumoylation | FGTEGKPKMEPAASS CCCCCCCCCCCCHHC | 60.42 | - | |
604 | Phosphorylation | PKMEPAASSQAAVEE CCCCCCHHCHHHHHH | 25.70 | 26074081 | |
605 | Phosphorylation | KMEPAASSQAAVEEL CCCCCHHCHHHHHHH | 21.07 | 26074081 | |
614 | Phosphorylation | AAVEELRTQVRELRS HHHHHHHHHHHHHHH | 44.00 | 26074081 | |
621 | Phosphorylation | TQVRELRSIIETMKD HHHHHHHHHHHHHHH | 40.31 | 23403867 | |
625 | Phosphorylation | ELRSIIETMKDQQKR HHHHHHHHHHHHHHH | 21.07 | 23403867 | |
627 | Acetylation | RSIIETMKDQQKREI HHHHHHHHHHHHHHH | 60.86 | 25953088 | |
639 | Phosphorylation | REIKQLLSELDEEKK HHHHHHHHHCCHHHH | 44.71 | - | |
653 | Sulfoxidation | KIRLRLQMEVNDIKK HHHHHHHHHHHHHHH | 8.01 | 21406390 | |
659 | 2-Hydroxyisobutyrylation | QMEVNDIKKALQSK- HHHHHHHHHHHHCC- | 34.55 | - | |
664 | Phosphorylation | DIKKALQSK------ HHHHHHHCC------ | 40.98 | 29978859 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
- | K | Ubiquitination | E3 ubiquitin ligase | CBL | P22681 | PMID:12177062 |
- | K | Ubiquitination | E3 ubiquitin ligase | CBLB | Q13191 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:22199232 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SH3K1_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 SH3K1_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. |
loading...
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-230; THR-254; SER-436;SER-509; SER-511; SER-521 AND SER-587, AND MASS SPECTROMETRY. | |
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY. | |
"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 SER-230; SER-509 ANDSER-511, AND MASS SPECTROMETRY. | |
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASSSPECTROMETRY. |