SH3B4_HUMAN - dbPTM
SH3B4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH3B4_HUMAN
UniProt AC Q9P0V3
Protein Name SH3 domain-binding protein 4
Gene Name SH3BP4
Organism Homo sapiens (Human).
Sequence Length 963
Subcellular Localization Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus . Specifically associated with transferrin receptor-containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus.
Protein Description May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy..
Protein Sequence MAAQRIRAANSNGLPRCKSEGTLIDLSEGFSETSFNDIKVPSPSALLVDNPTPFGNAKEVIAIKDYCPTNFTTLKFSKGDHLYVLDTSGGEWWYAHNTTEMGYIPSSYVQPLNYRNSTLSDSGMIDNLPDSPDEVAKELELLGGWTDDKKVPGRMYSNNPFWNGVQTNPFLNGNVPVMPSLDELNPKSTVDLLLFDAGTSSFTESSSATTNSTGNIFDELPVTNGLHAEPPVRRDNPFFRSKRSYSLSELSVLQAKSDAPTSSSFFTGLKSPAPEQFQSREDFRTAWLNHRKLARSCHDLDLLGQSPGWGQTQAVETNIVCKLDSSGGAVQLPDTSISIHVPEGHVAPGETQQISMKALLDPPLELNSDRSCSISPVLEVKLSNLEVKTSIILEMKVSAEIKNDLFSKSTVGLQCLRSDSKEGPYVSVPLNCSCGDTVQAQLHNLEPCMYVAVVAHGPSILYPSTVWDFINKKVTVGLYGPKHIHPSFKTVVTIFGHDCAPKTLLVSEVTRQAPNPAPVALQLWGKHQFVLSRPQDLKVCMFSNMTNYEVKASEQAKVVRGFQLKLGKVSRLIFPITSQNPNELSDFTLRVQVKDDQEAILTQFCVQTPQPPPKSAIKPSGQRRFLKKNEVGKIILSPFATTTKYPTFQDRPVSSLKFGKLLKTVVRQNKNHYLLEYKKGDGIALLSEERVRLRGQLWTKEWYIGYYQGRVGLVHTKNVLVVGRARPSLCSGPELSTSVLLEQILRPCKFLTYIYASVRTLLMENISSWRSFADALGYVNLPLTFFCRAELDSEPERVASVLEKLKEDCNNTENKERKSFQKELVMALLKMDCQGLVVRLIQDFVLLTTAVEVAQRWRELAEKLAKVSKQQMDAYESPHRDRNGVVDSEAMWKPAYDFLLTWSHQIGDSYRDVIQELHLGLDKMKNPITKRWKHLTGTLILVNSLDVLRAAAFSPADQDDFVI
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
11PhosphorylationQRIRAANSNGLPRCK
HHHHHHHCCCCCCCC		27.7828102081
19PhosphorylationNGLPRCKSEGTLIDL
CCCCCCCCCCEEEEC		44.9022912867
22PhosphorylationPRCKSEGTLIDLSEG
CCCCCCCEEEECCCC		19.2524173317
42PhosphorylationFNDIKVPSPSALLVD
CCCCCCCCCCEEEEC		34.1825159151
44PhosphorylationDIKVPSPSALLVDNP
CCCCCCCCEEEECCC		35.5725159151
64UbiquitinationAKEVIAIKDYCPTNF
CCEEEEEEECCCCCC		33.3529967540
66PhosphorylationEVIAIKDYCPTNFTT
EEEEEEECCCCCCEE		8.7028674419
73PhosphorylationYCPTNFTTLKFSKGD
CCCCCCEEEEECCCC		24.6628555341
117PhosphorylationQPLNYRNSTLSDSGM
CCCCCCCCCCCCCCC		23.0223403867
118PhosphorylationPLNYRNSTLSDSGMI
CCCCCCCCCCCCCCC		33.5529255136
120PhosphorylationNYRNSTLSDSGMIDN
CCCCCCCCCCCCCCC		29.8029255136
122PhosphorylationRNSTLSDSGMIDNLP
CCCCCCCCCCCCCCC		27.2129255136
131PhosphorylationMIDNLPDSPDEVAKE
CCCCCCCCHHHHHHH		32.1030266825
146PhosphorylationLELLGGWTDDKKVPG
HHHCCCCCCCCCCCC		37.2822199227
149UbiquitinationLGGWTDDKKVPGRMY
CCCCCCCCCCCCCCC		59.4829967540
241PhosphorylationRDNPFFRSKRSYSLS
CCCHHHCCCCCCCHH		27.5426462736
244PhosphorylationPFFRSKRSYSLSELS
HHHCCCCCCCHHHHH		23.8622167270
245PhosphorylationFFRSKRSYSLSELSV
HHCCCCCCCHHHHHH		20.0522167270
246PhosphorylationFRSKRSYSLSELSVL
HCCCCCCCHHHHHHE		27.0222167270
248PhosphorylationSKRSYSLSELSVLQA
CCCCCCHHHHHHEEE		30.4730266825
251PhosphorylationSYSLSELSVLQAKSD
CCCHHHHHHEEECCC		19.4123927012
257PhosphorylationLSVLQAKSDAPTSSS
HHHEEECCCCCCCCH		41.8624732914
261PhosphorylationQAKSDAPTSSSFFTG
EECCCCCCCCHHHCC		42.8524732914
262PhosphorylationAKSDAPTSSSFFTGL
ECCCCCCCCHHHCCC		23.9524732914
263PhosphorylationKSDAPTSSSFFTGLK
CCCCCCCCHHHCCCC		33.3724732914
264PhosphorylationSDAPTSSSFFTGLKS
CCCCCCCHHHCCCCC		24.9324732914
267PhosphorylationPTSSSFFTGLKSPAP
CCCCHHHCCCCCCCC		39.3224732914
270 (in isoform 2)Ubiquitination-56.5921906983
270 (in isoform 1)Ubiquitination-56.5921890473
270UbiquitinationSSFFTGLKSPAPEQF
CHHHCCCCCCCCHHH		56.5921906983
270MethylationSSFFTGLKSPAPEQF
CHHHCCCCCCCCHHH		56.5942369285
271PhosphorylationSFFTGLKSPAPEQFQ
HHHCCCCCCCCHHHH		31.1925159151
279PhosphorylationPAPEQFQSREDFRTA
CCCHHHHCCHHHHHH		38.6423401153
296PhosphorylationNHRKLARSCHDLDLL
HHHHHHHHCCCCHHC		15.3623401153
306PhosphorylationDLDLLGQSPGWGQTQ
CCHHCCCCCCCCCCC		24.4723663014
312PhosphorylationQSPGWGQTQAVETNI
CCCCCCCCCEEEEEE		17.9823927012
317PhosphorylationGQTQAVETNIVCKLD
CCCCEEEEEEEEEEC		24.5223090842
381UbiquitinationISPVLEVKLSNLEVK
CCCEEEEEECCCEEE		36.5029967540
407PhosphorylationEIKNDLFSKSTVGLQ
HHCCCCCCCCCEEEE		32.7524719451
473UbiquitinationVWDFINKKVTVGLYG
HHHHHCCCCEEEEEC		38.3529967540
479PhosphorylationKKVTVGLYGPKHIHP
CCCEEEEECCCCCCC		26.00-
503PhosphorylationGHDCAPKTLLVSEVT
CCCCCCCEEEEEEHH		25.0222210691
507PhosphorylationAPKTLLVSEVTRQAP
CCCEEEEEEHHHCCC		26.7322210691
557UbiquitinationVKASEQAKVVRGFQL
ECHHHHHHEECEEEE		40.7429967540
588PhosphorylationPNELSDFTLRVQVKD
CCCCCCEEEEEEECC		20.7424719451
615PhosphorylationTPQPPPKSAIKPSGQ
CCCCCCCCCCCCCCC		40.7921712546
633UbiquitinationLKKNEVGKIILSPFA
ECCCCCCCEEECCCC		31.5829967540
637PhosphorylationEVGKIILSPFATTTK
CCCCEEECCCCCCCC		13.9416964243
641PhosphorylationIILSPFATTTKYPTF
EEECCCCCCCCCCCC		35.0629396449
642PhosphorylationILSPFATTTKYPTFQ
EECCCCCCCCCCCCC		20.1929396449
643PhosphorylationLSPFATTTKYPTFQD
ECCCCCCCCCCCCCC		24.9929396449
644UbiquitinationSPFATTTKYPTFQDR
CCCCCCCCCCCCCCC		47.3329967540
645PhosphorylationPFATTTKYPTFQDRP
CCCCCCCCCCCCCCC		12.8623403867
647PhosphorylationATTTKYPTFQDRPVS
CCCCCCCCCCCCCCH		30.7328387310
654PhosphorylationTFQDRPVSSLKFGKL
CCCCCCCHHHHHHHH		32.4123403867
655PhosphorylationFQDRPVSSLKFGKLL
CCCCCCHHHHHHHHH		35.49-
657UbiquitinationDRPVSSLKFGKLLKT
CCCCHHHHHHHHHHH		54.7623000965
657 (in isoform 1)Ubiquitination-54.7621890473
660UbiquitinationVSSLKFGKLLKTVVR
CHHHHHHHHHHHHHH		54.5023000965
663UbiquitinationLKFGKLLKTVVRQNK
HHHHHHHHHHHHCCC		50.1123000965
678UbiquitinationNHYLLEYKKGDGIAL
CEEEEEEECCCCEEE		40.6923000965
678 (in isoform 1)Ubiquitination-40.6921890473
679UbiquitinationHYLLEYKKGDGIALL
EEEEEEECCCCEEEE		62.4223000965
728PhosphorylationVVGRARPSLCSGPEL
EEECCCHHHCCCCCC		36.1327050516
736PhosphorylationLCSGPELSTSVLLEQ
HCCCCCCCHHHHHHH		19.5827050516
806UbiquitinationASVLEKLKEDCNNTE
HHHHHHHHHHHCCCC		63.6833845483
815UbiquitinationDCNNTENKERKSFQK
HHCCCCCHHHHHHHH		53.3033845483
869UbiquitinationEKLAKVSKQQMDAYE
HHHHHHCHHHHHHHH		47.7633845483
875PhosphorylationSKQQMDAYESPHRDR
CHHHHHHHHCCCCCC		16.8117081983
877PhosphorylationQQMDAYESPHRDRNG
HHHHHHHCCCCCCCC		17.2117081983
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 SH3B4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH3B4_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 SH3B4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CIZ1_HUMANCIZ1physical
18654987
PSA1_HUMANPSMA1physical
18654987
MRGBP_HUMANMRGBPphysical
18654987
MPP8_HUMANMPHOSPH8physical
18654987
GRP78_HUMANHSPA5physical
18654987
GKAP1_HUMANGKAP1physical
18654987
NFU1_HUMANNFU1physical
18654987
TXNL1_HUMANTXNL1physical
18654987
TTC1_HUMANTTC1physical
18654987
ZBT37_HUMANZBTB37physical
18654987
CEP78_HUMANCEP78physical
18654987
PKHA1_HUMANPLEKHA1physical
18654987
DNJA4_HUMANDNAJA4physical
18654987
TCPA_HUMANTCP1physical
18654987
TCPG_HUMANCCT3physical
18654987
FKBP4_HUMANFKBP4physical
18654987
PRR14_HUMANPRR14physical
18654987
G3PT_HUMANGAPDHSphysical
18654987
CB073_HUMANC2orf73physical
18654987
EPS15_HUMANEPS15physical
16325581
AP2A_HUMANTFAP2Aphysical
16325581
SH3B4_HUMANSH3BP4physical
16325581
DYN1_HUMANDNM1physical
16325581
TFR1_HUMANTFRCphysical
16325581
F110A_HUMANFAM110Aphysical
27173435
F110B_HUMANFAM110Bphysical
27173435
SYDE1_HUMANSYDE1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
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 SH3B4_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-246, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND MASSSPECTROMETRY.

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