3BP2_HUMAN - dbPTM
3BP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 3BP2_HUMAN
UniProt AC P78314
Protein Name SH3 domain-binding protein 2
Gene Name SH3BP2
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization
Protein Description Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism..
Protein Sequence MAAEEMHWPVPMKAIGAQNLLTMPGGVAKAGYLHKKGGTQLQLLKWPLRFVIIHKRCVYYFKSSTSASPQGAFSLSGYNRVMRAAEETTSNNVFPFKIIHISKKHRTWFFSASSEEERKSWMALLRREIGHFHEKKDLPLDTSDSSSDTDSFYGAVERPVDISLSPYPTDNEDYEHDDEDDSYLEPDSPEPGRLEDALMHPPAYPPPPVPTPRKPAFSDMPRAHSFTSKGPGPLLPPPPPKHGLPDVGLAAEDSKRDPLCPRRAEPCPRVPATPRRMSDPPLSTMPTAPGLRKPPCFRESASPSPEPWTPGHGACSTSSAAIMATATSRNCDKLKSFHLSPRGPPTSEPPPVPANKPKFLKIAEEDPPREAAMPGLFVPPVAPRPPALKLPVPEAMARPAVLPRPEKPQLPHLQRSPPDGQSFRSFSFEKPRQPSQADTGGDDSDEDYEKVPLPNSVFVNTTESCEVERLFKATSPRGEPQDGLYCIRNSSTKSGKVLVVWDETSNKVRNYRIFEKDSKFYLEGEVLFVSVGSMVEHYHTHVLPSHQSLLLRHPYGYTGPR
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
3 (in isoform 3)Phosphorylation-16.4026270265
4 (in isoform 4)Phosphorylation-46.4422210691
10 (in isoform 4)Phosphorylation-6.4522210691
24 (in isoform 3)Phosphorylation-31.0226434776
25 (in isoform 3)Phosphorylation-32.1726434776
27 (in isoform 3)Phosphorylation-6.4726434776
28 (in isoform 4)Methylation-10.15-
29UbiquitinationTMPGGVAKAGYLHKK
CCCCCCHHHCEEECC		39.68-
34 (in isoform 4)Methylation-22.69-
39PhosphorylationYLHKKGGTQLQLLKW
EEECCCCCCEEECCC		34.47-
86UbiquitinationNRVMRAAEETTSNNV
HHHHHHHHHHCCCCE		55.69-
174PhosphorylationYPTDNEDYEHDDEDD
CCCCCCCCCCCCCCC		14.6912709437
183PhosphorylationHDDEDDSYLEPDSPE
CCCCCCCCCCCCCCC		23.2911390470
218PhosphorylationTPRKPAFSDMPRAHS
CCCCCCCCCCCCCCC		34.8024719451
225PhosphorylationSDMPRAHSFTSKGPG
CCCCCCCCCCCCCCC		29.2726699800
227PhosphorylationMPRAHSFTSKGPGPL
CCCCCCCCCCCCCCC		32.3226699800
228PhosphorylationPRAHSFTSKGPGPLL
CCCCCCCCCCCCCCC		33.3424719451
273PhosphorylationPCPRVPATPRRMSDP
CCCCCCCCCCCCCCC		15.9727794612
275 (in isoform 4)Phosphorylation-42.4524719451
278PhosphorylationPATPRRMSDPPLSTM
CCCCCCCCCCCCCCC		45.1923927012
282 (in isoform 4)Phosphorylation-8.9524719451
283PhosphorylationRMSDPPLSTMPTAPG
CCCCCCCCCCCCCCC		28.5628450419
284 (in isoform 4)Phosphorylation-34.5524719451
284PhosphorylationMSDPPLSTMPTAPGL
CCCCCCCCCCCCCCC		34.5528450419
285 (in isoform 4)Phosphorylation-2.2024719451
287PhosphorylationPPLSTMPTAPGLRKP
CCCCCCCCCCCCCCC		34.3622210691
302PhosphorylationPCFRESASPSPEPWT
CCCCCCCCCCCCCCC		34.8822210691
304PhosphorylationFRESASPSPEPWTPG
CCCCCCCCCCCCCCC		39.1222210691
328PhosphorylationAIMATATSRNCDKLK
HHHHHHHHCCHHHCC		21.0222210691
335 (in isoform 4)Phosphorylation-57.7427251275
336PhosphorylationRNCDKLKSFHLSPRG
CCHHHCCCCCCCCCC		28.4729396449
340PhosphorylationKLKSFHLSPRGPPTS
HCCCCCCCCCCCCCC		12.1829396449
346PhosphorylationLSPRGPPTSEPPPVP
CCCCCCCCCCCCCCC		49.1824114839
347PhosphorylationSPRGPPTSEPPPVPA
CCCCCCCCCCCCCCC		54.6124114839
361UbiquitinationANKPKFLKIAEEDPP
CCCCCCEECCCCCCC		42.90-
393 (in isoform 4)Phosphorylation-22.9927251275
397 (in isoform 4)Phosphorylation-22.7324719451
416PhosphorylationQLPHLQRSPPDGQSF
CCCCCCCCCCCCCCC		28.0230266825
422PhosphorylationRSPPDGQSFRSFSFE
CCCCCCCCCCCEECC		28.3223186163
425PhosphorylationPDGQSFRSFSFEKPR
CCCCCCCCEECCCCC		24.1923312004
427PhosphorylationGQSFRSFSFEKPRQP
CCCCCCEECCCCCCC		33.4723401153
430UbiquitinationFRSFSFEKPRQPSQA
CCCEECCCCCCCCCC		43.41-
435PhosphorylationFEKPRQPSQADTGGD
CCCCCCCCCCCCCCC		29.6623927012
439PhosphorylationRQPSQADTGGDDSDE
CCCCCCCCCCCCCCC		46.1926657352
444PhosphorylationADTGGDDSDEDYEKV
CCCCCCCCCCCHHCC		47.8728355574
448PhosphorylationGDDSDEDYEKVPLPN
CCCCCCCHHCCCCCC		18.6623927012
473 (in isoform 4)Phosphorylation-13.1324719451
484 (in isoform 4)Phosphorylation-4.1924719451
487UbiquitinationPQDGLYCIRNSSTKS
CCCCEEEEECCCCCC		2.70-
501 (in isoform 4)Phosphorylation-7.1127251275
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
174YPhosphorylationKinaseSYKP43405
Uniprot
183YPhosphorylationKinaseSYKP43405
Uniprot
225SPhosphorylationKinaseKPCAP17252
PhosphoELM
225SPhosphorylationKinasePRKCAP05696
GPS
278SPhosphorylationKinasePRKCAP05696
GPS
448YPhosphorylationKinaseSYKP43405
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 3BP2_HUMAN !!
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 3BP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZAP70_HUMANZAP70physical
9846481
GRB2_HUMANGRB2physical
9846481
CBL_HUMANCBLphysical
9846481
PLCG1_HUMANPLCG1physical
9846481
LAT_HUMANLATphysical
9846481
VAV_HUMANVAV1physical
11390470
LAT_HUMANLATphysical
11390470
DBNL_HUMANDBNLphysical
17306257
SH3K1_HUMANSH3KBP1physical
17306257
VAV_HUMANVAV1physical
17306257
SRC_HUMANSRCphysical
20439986
KSYK_HUMANSYKphysical
20439986
VAV_HUMANVAV1physical
20439986
CBL_HUMANCBLphysical
20439986
TNKS1_HUMANTNKSphysical
22153076
TNKS2_HUMANTNKS2physical
22153076
RN146_HUMANRNF146physical
22153076
IKZF1_HUMANIKZF1physical
26002965
RHG10_HUMANARHGAP10physical
25814554
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
118400Cherubism (CRBM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 3BP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-278, AND MASSSPECTROMETRY.

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