T53I2_HUMAN - dbPTM
T53I2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T53I2_HUMAN
UniProt AC Q8IXH6
Protein Name Tumor protein p53-inducible nuclear protein 2
Gene Name TP53INP2
Organism Homo sapiens (Human).
Sequence Length 220
Subcellular Localization Cytoplasm, cytosol. Nucleus. Nucleus, PML body. Cytoplasmic vesicle, autophagosome. Shuttles between the nucleus and the cytoplasm, depending on cellular stress conditions, and re-localizes to autophagosomes on autophagy activation.
Protein Description Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA..
Protein Sequence MFQRLSSLFFSTPSPPEDPDCPRAFVSEEDEVDGWLIIDLPDSYAAPPSPGAAPAPAGRPPPAPSLMDESWFVTPPACFTAEGPGLGPARLQSSPLEDLLIEHPSMSVYVTGSTIVLEPGSPSPLPDAALPDGDLSEGELTPARREPRAARHAAPLPARAALLEKAGQVRRLQRARQRAERHALSAKAVQRQNRARESRPRRSKNQSSFIYQPCQRQFNY
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
6Phosphorylation--MFQRLSSLFFSTP
--CCHHHHHHHCCCC
27.4727174698
7Phosphorylation-MFQRLSSLFFSTPS
-CCHHHHHHHCCCCC
33.5127174698
11PhosphorylationRLSSLFFSTPSPPED
HHHHHHCCCCCCCCC
31.8822199227
12PhosphorylationLSSLFFSTPSPPEDP
HHHHHCCCCCCCCCC
23.7222199227
14PhosphorylationSLFFSTPSPPEDPDC
HHHCCCCCCCCCCCC
53.8522617229
49PhosphorylationDSYAAPPSPGAAPAP
CCCCCCCCCCCCCCC
34.6026074081
65PhosphorylationGRPPPAPSLMDESWF
CCCCCCCCCCCCCCE
38.1326074081
70PhosphorylationAPSLMDESWFVTPPA
CCCCCCCCCEECCCC
22.8826074081
136PhosphorylationALPDGDLSEGELTPA
CCCCCCCCCCCCCCC
48.5824275569
165UbiquitinationARAALLEKAGQVRRL
HHHHHHHHHHHHHHH
58.7632142685

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 T53I2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T53I2_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 T53I2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLP3A_HUMANMAP1LC3Aphysical
20010805
GBRL2_HUMANGABARAPL2physical
20010805

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 T53I2_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 THR-12 AND SER-14, AND MASSSPECTROMETRY.

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