SH3G1_MOUSE - dbPTM
SH3G1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH3G1_MOUSE
UniProt AC Q62419
Protein Name Endophilin-A2
Gene Name Sh3gl1
Organism Mus musculus (Mouse).
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 MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKDMEKKVDVTSKAVAEVLVRTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMVRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILEELADKLKRRVREASSRPKREFKPRPREPFELGELEQPNGGFPCAPAPKITASSSFRSSDKPIRMPSKSMPPLDQPSCKALYDFEPENDGELGFREGDLITLTNQIDENWYEGMLHGQSGFFPLSYVQVLVPLPQ
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
22.2222006019
12AcetylationGLKKQFYKASQLVSE
HHHHHHHHHHHHHHH
42.7322826441
14PhosphorylationKKQFYKASQLVSEKV
HHHHHHHHHHHHHHH
21.6429514104
20AcetylationASQLVSEKVGGAEGT
HHHHHHHHHCCCCCC
38.3822826441
27O-linked_GlycosylationKVGGAEGTKLDDDFK
HHCCCCCCCCCHHHH
21.6830059200
73PhosphorylationAKLTMLNTVSKIRGQ
HHHEHHHHHHHHHCC
23.3829514104
75PhosphorylationLTMLNTVSKIRGQVK
HEHHHHHHHHHCCCC
21.9629514104
76AcetylationTMLNTVSKIRGQVKN
EHHHHHHHHHCCCCC
31.8922826441
76UbiquitinationTMLNTVSKIRGQVKN
EHHHHHHHHHCCCCC
31.89-
102AcetylationECMVRHGKELGGESN
HHHHHCCHHCCCCCC
43.577711841
102UbiquitinationECMVRHGKELGGESN
HHHHHCCHHCCCCCC
43.57-
108PhosphorylationGKELGGESNFGDALL
CHHCCCCCCHHHHHH
40.5122817900
122AcetylationLDAGESMKRLAEVKD
HHHHHHHHHHHHHHH
54.247711851
170PhosphorylationGRRLDFDYKKKRQGK
CCCCCCCHHHHHCCC
25.3829514104
239UbiquitinationILEELADKLKRRVRE
HHHHHHHHHHHHHHH
50.75-
284PhosphorylationCAPAPKITASSSFRS
CCCCCCCCCCCCCCC
26.9826745281
284O-linked_GlycosylationCAPAPKITASSSFRS
CCCCCCCCCCCCCCC
26.9830059200
286PhosphorylationPAPKITASSSFRSSD
CCCCCCCCCCCCCCC
20.1923684622
287PhosphorylationAPKITASSSFRSSDK
CCCCCCCCCCCCCCC
30.9127087446
288PhosphorylationPKITASSSFRSSDKP
CCCCCCCCCCCCCCC
23.3726824392
291PhosphorylationTASSSFRSSDKPIRM
CCCCCCCCCCCCCCC
40.6626239621
292PhosphorylationASSSFRSSDKPIRMP
CCCCCCCCCCCCCCC
45.4526239621
300PhosphorylationDKPIRMPSKSMPPLD
CCCCCCCCCCCCCCC
28.1925266776
302PhosphorylationPIRMPSKSMPPLDQP
CCCCCCCCCCCCCCC
40.6424719451
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
315YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH3G1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SH3G1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SH3G1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.

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