3BP1_HUMAN - dbPTM
3BP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 3BP1_HUMAN
UniProt AC Q9Y3L3
Protein Name SH3 domain-binding protein 1 {ECO:0000312|HGNC:HGNC:10824}
Gene Name SH3BP1 {ECO:0000312|HGNC:HGNC:10824}
Organism Homo sapiens (Human).
Sequence Length 701
Subcellular Localization Cell projection . Cell junction, tight junction . Cell junction, adherens junction . Cell projection, phagocytic cup . Nucleus . Cytoplasm, cytosol . Localizes at the leading edge of migrating cells (PubMed:21658605, PubMed:24841563). Accumulation at
Protein Description GTPase activating protein (GAP) which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration. [PubMed: 21658605 Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions]
Protein Sequence MMKRQLHRMRQLAQTGSLGRTPETAEFLGEDLLQVEQRLEPAKRAAHNIHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQATKNSGSSQGLGGSPGSHSHTTMANKVETLKEEEEELKRKVEQCRDEYLADLYHFVTKEDSYANYFIRLLEIQADYHRRSLSSLDTALAELRENHGQADHSPSMTATHFPRVYGVSLATHLQELGREIALPIEACVMMLLSEGMKEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTFDLYDDWMRAASLKEPGARLQALQEVCSRLPPENLSNLRYLMKFLARLAEEQEVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSIQVVGVVEALIQSADTLFPGDINFNVSGLFSAVTLQDTVSDRLASEELPSTAVPTPATTPAPAPAPAPAPAPALASAATKERTESEVPPRPASPKVTRSPPETAAPVEDMARRTKRPAPARPTMPPPQVSGSRSSPPAPPLPPGSGSPGTPQALPRRLVGSSLRAPTVPPPLPPTPPQPARRQSRRSPASPSPASPGPASPSPVSLSNPAQVDLGAATAEGGAPEAISGVPTPPAIPPQPRPRSLASETN
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
3Methylation-----MMKRQLHRMR
-----CHHHHHHHHH		35.3823644510
15PhosphorylationRMRQLAQTGSLGRTP
HHHHHHHHCCCCCCH		24.1129255136
17PhosphorylationRQLAQTGSLGRTPET
HHHHHHCCCCCCHHH		30.9123401153
21PhosphorylationQTGSLGRTPETAEFL
HHCCCCCCHHHHHHH		24.5528450419
21O-linked_GlycosylationQTGSLGRTPETAEFL
HHCCCCCCHHHHHHH		24.5529351928
24PhosphorylationSLGRTPETAEFLGED
CCCCCHHHHHHHCHH		32.4628450419
78PhosphorylationKLPLMALSTTMAESF
HHHHHHHHHHHHHHH		16.58-
79PhosphorylationLPLMALSTTMAESFK
HHHHHHHHHHHHHHH		22.8025599653
92PhosphorylationFKELDPDSSMGKALE
HHHHCCCCHHHHHHH		27.8425599653
93PhosphorylationKELDPDSSMGKALEM
HHHCCCCHHHHHHHH		38.6525599653
140AcetylationEELPAILKHKKSLQK
HHHHHHHHCHHHHHH		47.4625953088
142AcetylationLPAILKHKKSLQKLV
HHHHHHCHHHHHHHH		42.3391191
142MethylationLPAILKHKKSLQKLV
HHHHHHCHHHHHHHH		42.33-
142"N6,N6-dimethyllysine"LPAILKHKKSLQKLV
HHHHHHCHHHHHHHH		42.33-
143"N6,N6-dimethyllysine"PAILKHKKSLQKLVS
HHHHHCHHHHHHHHH		57.00-
143MethylationPAILKHKKSLQKLVS
HHHHHCHHHHHHHHH		57.00-
143AcetylationPAILKHKKSLQKLVS
HHHHHCHHHHHHHHH		57.0091195
147MethylationKHKKSLQKLVSDWNT
HCHHHHHHHHHCHHH		57.03-
147AcetylationKHKKSLQKLVSDWNT
HCHHHHHHHHHCHHH		57.0391199
147"N6,N6-dimethyllysine"KHKKSLQKLVSDWNT
HCHHHHHHHHHCHHH		57.03-
156UbiquitinationVSDWNTLKSRLSQAT
HHCHHHHHHHHHHHH		31.34-
163PhosphorylationKSRLSQATKNSGSSQ
HHHHHHHHHHCCCCC		24.1124719451
166PhosphorylationLSQATKNSGSSQGLG
HHHHHHHCCCCCCCC		41.4223684312
168PhosphorylationQATKNSGSSQGLGGS
HHHHHCCCCCCCCCC		21.2223684312
169PhosphorylationATKNSGSSQGLGGSP
HHHHCCCCCCCCCCC		31.6228450419
175PhosphorylationSSQGLGGSPGSHSHT
CCCCCCCCCCCCCHH		25.0423401153
178PhosphorylationGLGGSPGSHSHTTMA
CCCCCCCCCCHHHHH		25.7923911959
180PhosphorylationGGSPGSHSHTTMANK
CCCCCCCCHHHHHHH		24.9927794612
182PhosphorylationSPGSHSHTTMANKVE
CCCCCCHHHHHHHHH		22.6828450419
183PhosphorylationPGSHSHTTMANKVET
CCCCCHHHHHHHHHH		14.6328450419
190PhosphorylationTMANKVETLKEEEEE
HHHHHHHHHHHHHHH		46.2323186163
209PhosphorylationVEQCRDEYLADLYHF
HHHHHHHHHHHHHHH		16.10-
214PhosphorylationDEYLADLYHFVTKED
HHHHHHHHHHHCCCC		8.1827642862
226PhosphorylationKEDSYANYFIRLLEI
CCCHHHHHHHHHHHH		7.69-
241PhosphorylationQADYHRRSLSSLDTA
HHHHHHHCHHHHHHH		32.3429978859
243PhosphorylationDYHRRSLSSLDTALA
HHHHHCHHHHHHHHH		30.0627080861
244PhosphorylationYHRRSLSSLDTALAE
HHHHCHHHHHHHHHH		35.2429978859
247PhosphorylationRSLSSLDTALAELRE
HCHHHHHHHHHHHHH		28.9429978859
262PhosphorylationNHGQADHSPSMTATH
HCCCCCCCCCCCCCC		21.1523401153
264PhosphorylationGQADHSPSMTATHFP
CCCCCCCCCCCCCCC		31.6030266825
266PhosphorylationADHSPSMTATHFPRV
CCCCCCCCCCCCCHH		32.5130266825
268PhosphorylationHSPSMTATHFPRVYG
CCCCCCCCCCCHHHC		18.1930266825
318PhosphorylationFRLAAGASVLKRLKQ
HHHHHHHHHHHHHHH		27.3727067055
321 (in isoform 2)Ubiquitination-54.2321906983
321UbiquitinationAAGASVLKRLKQTMA
HHHHHHHHHHHHHHC		54.2321906983
321 (in isoform 1)Ubiquitination-54.2321906983
375 (in isoform 2)Ubiquitination-60.4121906983
375 (in isoform 1)Ubiquitination-60.4121906983
375UbiquitinationWMRAASLKEPGARLQ
HHHHHHCCCCCHHHH		60.4121906983
397PhosphorylationRLPPENLSNLRYLMK
CCCHHHHHHHHHHHH		45.4624719451
404 (in isoform 2)Ubiquitination-34.3321906983
404UbiquitinationSNLRYLMKFLARLAE
HHHHHHHHHHHHHHH		34.3321906983
404 (in isoform 1)Ubiquitination-34.3321906983
534PhosphorylationSAATKERTESEVPPR
HHHHHCCCCCCCCCC		44.9828176443
536PhosphorylationATKERTESEVPPRPA
HHHCCCCCCCCCCCC		43.1928176443
544PhosphorylationEVPPRPASPKVTRSP
CCCCCCCCCCCCCCC		28.1229255136
548PhosphorylationRPASPKVTRSPPETA
CCCCCCCCCCCCCCC		31.4023401153
550PhosphorylationASPKVTRSPPETAAP
CCCCCCCCCCCCCCC		35.1319664994
554PhosphorylationVTRSPPETAAPVEDM
CCCCCCCCCCCHHHH		33.6130266825
574PhosphorylationRPAPARPTMPPPQVS
CCCCCCCCCCCCCCC		36.4428464451
581PhosphorylationTMPPPQVSGSRSSPP
CCCCCCCCCCCCCCC		26.2928464451
583PhosphorylationPPPQVSGSRSSPPAP
CCCCCCCCCCCCCCC		22.8328348404
585PhosphorylationPQVSGSRSSPPAPPL
CCCCCCCCCCCCCCC		49.2223401153
586PhosphorylationQVSGSRSSPPAPPLP
CCCCCCCCCCCCCCC		33.5223401153
596PhosphorylationAPPLPPGSGSPGTPQ
CCCCCCCCCCCCCCC		41.7023401153
598PhosphorylationPLPPGSGSPGTPQAL
CCCCCCCCCCCCCCC		23.1230278072
601PhosphorylationPGSGSPGTPQALPRR
CCCCCCCCCCCCCHH		18.6630278072
612PhosphorylationLPRRLVGSSLRAPTV
CCHHHCCCCCCCCCC		20.7923684312
613PhosphorylationPRRLVGSSLRAPTVP
CHHHCCCCCCCCCCC		18.8829970186
618PhosphorylationGSSLRAPTVPPPLPP
CCCCCCCCCCCCCCC		44.6628060719
626PhosphorylationVPPPLPPTPPQPARR
CCCCCCCCCCCCCCC		45.7429255136
638PhosphorylationARRQSRRSPASPSPA
CCCCCCCCCCCCCCC		24.5727251275
641PhosphorylationQSRRSPASPSPASPG
CCCCCCCCCCCCCCC		29.3321552520
643PhosphorylationRRSPASPSPASPGPA
CCCCCCCCCCCCCCC		30.5120058876
646PhosphorylationPASPSPASPGPASPS
CCCCCCCCCCCCCCC		33.5023879269
651PhosphorylationPASPGPASPSPVSLS
CCCCCCCCCCCCCCC		29.1021552520
653PhosphorylationSPGPASPSPVSLSNP
CCCCCCCCCCCCCCC		35.12-
695PhosphorylationPPQPRPRSLASETN-
CCCCCCCCCCCCCC-		30.8525394399
698PhosphorylationPRPRSLASETN----
CCCCCCCCCCC----		50.6928450419
700PhosphorylationPRSLASETN------
CCCCCCCCC------		43.6728102081
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

Oops, there are no upstream regulatory protein records of 3BP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 3BP1_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 3BP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABL1_HUMANABL1physical
1379745
SRC_HUMANSRCphysical
1379745
CRK_HUMANCRKphysical
1379745
NLRP3_HUMANNLRP3physical
26344197
NALP4_HUMANNLRP4physical
26344197
Drug and Disease Associations
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.
Regulatory Network of 3BP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND THR-626, ANDMASS 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-544, AND MASSSPECTROMETRY.

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