SH3G3_HUMAN - dbPTM
SH3G3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH3G3_HUMAN
UniProt AC Q99963
Protein Name Endophilin-A3
Gene Name SH3GL3
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Cytoplasm . Early endosome membrane
Peripheral membrane protein . Associated with postsynaptic endosomes in hippocampal neurons. Associated with presynaptic endosomes in olfactory neurons.
Protein Description Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity)..
Protein Sequence MSVAGLKKQFHKASQLFSEKISGAEGTKLDDEFLDMERKIDVTNKVVAEILSKTTEYLQPNPAYRAKLGMLNTVSKIRGQVKTTGYPQTEGLLGDCMLKYGKELGEDSTFGNALIEVGESMKLMAEVKDSLDINVKQTFIDPLQLLQDKDLKEIGHHLKKLEGRRLDYDYKKKRVGKIPDEEVRQAVEKFEESKELAERSMFNFLENDVEQVSQLAVFIEAALDYHRQSTEILQELQSKLQMRISAASSVPRREYKPRPVKRSSSELNGVSTTSVVKTTGSNIPMDQPCCRGLYDFEPENQGELGFKEGDIITLTNQIDENWYEGMIHGESGFFPINYVEVIVPLPQ
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
14PhosphorylationKKQFHKASQLFSEKI
HHHHHHHHHHHHHHH		32.0226074081
18PhosphorylationHKASQLFSEKISGAE
HHHHHHHHHHHCCCC		46.7226074081
22PhosphorylationQLFSEKISGAEGTKL
HHHHHHHCCCCCCCC		42.9126074081
55O-linked_GlycosylationAEILSKTTEYLQPNP
HHHHHHCCHHHCCCH		26.7728657654
83PhosphorylationKIRGQVKTTGYPQTE
HHCCCCCCCCCCCCC		26.96-
86PhosphorylationGQVKTTGYPQTEGLL
CCCCCCCCCCCCCHH		7.06-
168PhosphorylationLEGRRLDYDYKKKRV
HCCCCCCCCCCCCCC		26.2626074081
170PhosphorylationGRRLDYDYKKKRVGK
CCCCCCCCCCCCCCC		20.6226074081
245PhosphorylationSKLQMRISAASSVPR
HHHHHHHHHHHCCCC		13.8623312004
248PhosphorylationQMRISAASSVPRREY
HHHHHHHHCCCCCCC		31.4223312004
249PhosphorylationMRISAASSVPRREYK
HHHHHHHCCCCCCCC		31.2623312004
255PhosphorylationSSVPRREYKPRPVKR
HCCCCCCCCCCCCCC		25.20-
261AcetylationEYKPRPVKRSSSELN
CCCCCCCCCCCHHCC		49.6012431723
263PhosphorylationKPRPVKRSSSELNGV
CCCCCCCCCHHCCCC		32.2822617229
264PhosphorylationPRPVKRSSSELNGVS
CCCCCCCCHHCCCCC		31.6822617229
265PhosphorylationRPVKRSSSELNGVST
CCCCCCCHHCCCCCC		47.5522617229
271PhosphorylationSSELNGVSTTSVVKT
CHHCCCCCCCEEEEE		27.6321406692
272PhosphorylationSELNGVSTTSVVKTT
HHCCCCCCCEEEEEC		22.2321406692
273PhosphorylationELNGVSTTSVVKTTG
HCCCCCCCEEEEECC		16.4221406692
274PhosphorylationLNGVSTTSVVKTTGS
CCCCCCCEEEEECCC		25.6321406692
277AcetylationVSTTSVVKTTGSNIP
CCCCEEEEECCCCCC		37.9112431731
279PhosphorylationTTSVVKTTGSNIPMD
CCEEEEECCCCCCCC		32.6625690035
281PhosphorylationSVVKTTGSNIPMDQP
EEEEECCCCCCCCCC		29.5125690035
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
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:20064468
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH3G3_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 SH3G3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3K1_HUMANSH3KBP1physical
11894096
SH3G3_HUMANSH3GL3physical
21900206
ATX2_HUMANATXN2physical
18602463
DYN3_HUMANDNM3physical
18602463
VIME_HUMANVIMphysical
15383276
PIAS4_HUMANPIAS4physical
15383276
ATX2_HUMANATXN2physical
16115810
SH3G3_HUMANSH3GL3physical
16115810
SH3G2_HUMANSH3GL2physical
16115810
SH3G1_HUMANSH3GL1physical
16115810
SH3G1_HUMANSH3GL1physical
26186194
SH3G1_HUMANSH3GL1physical
28514442
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 SH3G3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-265, AND MASSSPECTROMETRY.

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