SH3G1_HUMAN - dbPTM
SH3G1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH3G1_HUMAN
UniProt AC Q99961
Protein Name Endophilin-A2
Gene Name SH3GL1
Organism Homo sapiens (Human).
Sequence Length 368
Subcellular Localization Cytoplasm. Early endosome membrane
Peripheral membrane protein. Cell projection, podosome . Associated with postsynaptic endosomes in hippocampal neurons..
Protein Description Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity)..
Protein Sequence MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ
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
2Phosphorylation------MSVAGLKKQ
------CCHHHHHHH		22.2229514088
7Ubiquitination-MSVAGLKKQFYKAS
-CCHHHHHHHHHHHH		43.54-
7Acetylation-MSVAGLKKQFYKAS
-CCHHHHHHHHHHHH		43.5425953088
8UbiquitinationMSVAGLKKQFYKASQ
CCHHHHHHHHHHHHH		51.16-
12UbiquitinationGLKKQFYKASQLVSE
HHHHHHHHHHHHHHH		42.73-
12MethylationGLKKQFYKASQLVSE
HHHHHHHHHHHHHHH		42.73-
14PhosphorylationKKQFYKASQLVSEKV
HHHHHHHHHHHHHHH		21.6428857561
18PhosphorylationYKASQLVSEKVGGAE
HHHHHHHHHHHCCCC		40.0528857561
20AcetylationASQLVSEKVGGAEGT
HHHHHHHHHCCCCCC		38.3823954790
20UbiquitinationASQLVSEKVGGAEGT
HHHHHHHHHCCCCCC		38.38-
54PhosphorylationVTEVLARTIEYLQPN
HHHHHHHHHHHHCCC		16.7428152594
57PhosphorylationVLARTIEYLQPNPAS
HHHHHHHHHCCCHHH		13.5428152594
64PhosphorylationYLQPNPASRAKLTML
HHCCCHHHHHHHHHH		33.7528152594
69PhosphorylationPASRAKLTMLNTVSK
HHHHHHHHHHHHHHH		20.9321406692
70SulfoxidationASRAKLTMLNTVSKI
HHHHHHHHHHHHHHH		3.8321406390
73PhosphorylationAKLTMLNTVSKIRGQ
HHHHHHHHHHHHHCC		23.3821406692
75PhosphorylationLTMLNTVSKIRGQVK
HHHHHHHHHHHCCCC		21.9620068231
76UbiquitinationTMLNTVSKIRGQVKN
HHHHHHHHHHCCCCC		31.89-
82UbiquitinationSKIRGQVKNPGYPQS
HHHHCCCCCCCCCCC		49.92-
96GlutathionylationSEGLLGECMIRHGKE
CCCCHHHHHHHCCHH		2.3222555962
102UbiquitinationECMIRHGKELGGESN
HHHHHCCHHCCCCCC		43.57-
121SulfoxidationLLDAGESMKRLAEVK
HHHHHHHHHHHHHHH		2.2630846556
122AcetylationLDAGESMKRLAEVKD
HHHHHHHHHHHHHHH		54.247711855
122UbiquitinationLDAGESMKRLAEVKD
HHHHHHHHHHHHHHH		54.24-
147S-nitrosocysteineIDPLQNLCEKDLKEI
CHHHHHHHHHHHHHH		8.84-
147S-nitrosylationIDPLQNLCEKDLKEI
CHHHHHHHHHHHHHH		8.8419483679
147GlutathionylationIDPLQNLCEKDLKEI
CHHHHHHHHHHHHHH		8.8422555962
149UbiquitinationPLQNLCEKDLKEIQH
HHHHHHHHHHHHHHH		68.32-
152MalonylationNLCEKDLKEIQHHLK
HHHHHHHHHHHHHHH		64.0126320211
159UbiquitinationKEIQHHLKKLEGRRL
HHHHHHHHHHCCCCC		51.46-
177UbiquitinationYKKKRQGKIPDEELR
HHHHHCCCCCHHHHH		42.60-
177MalonylationYKKKRQGKIPDEELR
HHHHHCCCCCHHHHH		42.6026320211
177AcetylationYKKKRQGKIPDEELR
HHHHHCCCCCHHHHH		42.6025953088
184MethylationKIPDEELRQALEKFE
CCCHHHHHHHHHHHH		24.01-
189UbiquitinationELRQALEKFEESKEV
HHHHHHHHHHHHHHH		59.95-
239UbiquitinationILDELAEKLKRRMRE
HHHHHHHHHHHHHHH		54.4221139048
271PhosphorylationDLGEPEQSNGGFPCT
CCCCCCCCCCCCCCC		35.4626074081
278PhosphorylationSNGGFPCTTAPKIAA
CCCCCCCCCCCHHHC		26.6526074081
279PhosphorylationNGGFPCTTAPKIAAS
CCCCCCCCCCHHHCC		47.9126074081
286PhosphorylationTAPKIAASSSFRSSD
CCCHHHCCCCCCCCC		19.9325463755
286O-linked_GlycosylationTAPKIAASSSFRSSD
CCCHHHCCCCCCCCC		19.9323301498
287PhosphorylationAPKIAASSSFRSSDK
CCHHHCCCCCCCCCC		28.8629255136
288PhosphorylationPKIAASSSFRSSDKP
CHHHCCCCCCCCCCC		23.3729255136
291PhosphorylationAASSSFRSSDKPIRT
HCCCCCCCCCCCCCC		40.6625159151
292PhosphorylationASSSFRSSDKPIRTP
CCCCCCCCCCCCCCC		45.4525159151
298PhosphorylationSSDKPIRTPSRSMPP
CCCCCCCCCCCCCCC		26.7425159151
300PhosphorylationDKPIRTPSRSMPPLD
CCCCCCCCCCCCCCC		36.0523403867
302PhosphorylationPIRTPSRSMPPLDQP
CCCCCCCCCCCCCCC		39.7228985074
311S-nitrosylationPPLDQPSCKALYDFE
CCCCCCCCCCCCCCC		3.682212679
315PhosphorylationQPSCKALYDFEPEND
CCCCCCCCCCCCCCC		24.3622817900
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
315YPhosphorylationKinasePTK2Q05397
GPS
315YPhosphorylationKinaseSRCP12931
PSP
315YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH3G1_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 SH3G1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3G1_HUMANSH3GL1physical
16189514
SH24A_HUMANSH2D4Aphysical
16189514
DPPA4_HUMANDPPA4physical
16169070
SH3G3_HUMANSH3GL3physical
16169070
DYN1_HUMANDNM1physical
10764144
ANM1_HUMANPRMT1physical
17891136
KHDR1_HUMANKHDRBS1physical
17891136
CBP_HUMANCREBBPphysical
17891136
1433Z_HUMANYWHAZphysical
21900206
DPPA4_HUMANDPPA4physical
21900206
SH3G3_HUMANSH3GL3physical
21900206
DPYL4_HUMANDPYSL4physical
21900206
SH3G1_HUMANSH3GL1physical
21900206
SH3G1_HUMANSH3GL1physical
22167186
SH3G3_HUMANSH3GL3physical
16115810
SH3G2_HUMANSH3GL2physical
16115810
SH3G1_HUMANSH3GL1physical
16115810
AASD1_HUMANAARSD1physical
22863883
ARP3_HUMANACTR3physical
22863883
ARPC2_HUMANARPC2physical
22863883
FUBP1_HUMANFUBP1physical
22863883
RFA1_HUMANRPA1physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
SH3G1_HUMANSH3GL1physical
25416956
SH3G2_HUMANSH3GL2physical
25416956
MTA1_HUMANMTA1physical
25416956
GPKOW_HUMANGPKOWphysical
25416956
VP37C_HUMANVPS37Cphysical
25416956
DPPA4_HUMANDPPA4physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
MAL2_HUMANMAL2physical
25416956
F102A_HUMANFAM102Aphysical
25416956
FBX32_HUMANFBXO32physical
27720640
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 SH3G1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, 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-287 AND SER-288, ANDMASS SPECTROMETRY.
"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-288, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.

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