TRIA1_HUMAN - dbPTM
TRIA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIA1_HUMAN
UniProt AC O43715
Protein Name TP53-regulated inhibitor of apoptosis 1
Gene Name TRIAP1
Organism Homo sapiens (Human).
Sequence Length 76
Subcellular Localization Cytoplasm, perinuclear region . Mitochondrion . Mitochondrion intermembrane space .
Protein Description Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. [PubMed: 23931759 Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo)]
Protein Sequence MNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCTDLFKRYQQCVQKAIKEKEIPIEGLEFMGHGKEKPENSS
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
1Acetylation-------MNSVGEAC
-------CCCHHHHH
8.3322814378
9PhosphorylationNSVGEACTDMKREYD
CCHHHHHHHHHHHHH
46.2924043423
12AcetylationGEACTDMKREYDQCF
HHHHHHHHHHHHHHH
44.9127452117
21MethylationEYDQCFNRWFAEKFL
HHHHHHHHHHHHHHH
15.05115918945
26UbiquitinationFNRWFAEKFLKGDSS
HHHHHHHHHHCCCCC
53.2022817900
29UbiquitinationWFAEKFLKGDSSGDP
HHHHHHHCCCCCCCC
64.9022817900
32PhosphorylationEKFLKGDSSGDPCTD
HHHHCCCCCCCCHHH
44.9125627689
42UbiquitinationDPCTDLFKRYQQCVQ
CCHHHHHHHHHHHHH
58.4529967540
42AcetylationDPCTDLFKRYQQCVQ
CCHHHHHHHHHHHHH
58.4526822725
50UbiquitinationRYQQCVQKAIKEKEI
HHHHHHHHHHHHCCC
31.5129967540
50AcetylationRYQQCVQKAIKEKEI
HHHHHHHHHHHHCCC
31.5126051181
55UbiquitinationVQKAIKEKEIPIEGL
HHHHHHHCCCCCCCC
56.8129967540
55AcetylationVQKAIKEKEIPIEGL
HHHHHHHCCCCCCCC
56.8125953088

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 TRIA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIA1_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 TRIA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP74_HUMANHSPA4physical
15735003
APAF_HUMANAPAF1physical
15735003
PRLD1_HUMANPRELID1physical
28514442
PLD3B_HUMANSLMO2physical
28514442
PLD3A_HUMANSLMO1physical
28514442
IGJ_HUMANIGJphysical
28514442

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 TRIA1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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