TIM8A_HUMAN - dbPTM
TIM8A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIM8A_HUMAN
UniProt AC O60220
Protein Name Mitochondrial import inner membrane translocase subunit Tim8 A
Gene Name TIMM8A
Organism Homo sapiens (Human).
Sequence Length 97
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Intermembrane side .
Protein Description Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development..
Protein Sequence MDSSSSSSAAGLGAVDPQLQHFIEVETQKQRFQQLVHQMTELCWEKCMDKPGPKLDSRAEACFVNCVERFIDTSQFILNRLEQTQKSKPVFSESLSD
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-------MDSSSSSS
-------CCCCCCCC
11.56-
3Phosphorylation-----MDSSSSSSAA
-----CCCCCCCCCC
30.7130108239
4Phosphorylation----MDSSSSSSAAG
----CCCCCCCCCCC
29.9430108239
5Phosphorylation---MDSSSSSSAAGL
---CCCCCCCCCCCC
37.8930108239
6Phosphorylation--MDSSSSSSAAGLG
--CCCCCCCCCCCCC
30.2030108239
7Phosphorylation-MDSSSSSSAAGLGA
-CCCCCCCCCCCCCC
26.4130108239
8PhosphorylationMDSSSSSSAAGLGAV
CCCCCCCCCCCCCCC
24.8830108239
57PhosphorylationKPGPKLDSRAEACFV
CCCCCCCHHHHHHHH
43.7720833797
86UbiquitinationNRLEQTQKSKPVFSE
HHHHHHHHCCCCCCC
64.9321890473
87PhosphorylationRLEQTQKSKPVFSES
HHHHHHHCCCCCCCC
32.1630576142
88AcetylationLEQTQKSKPVFSESL
HHHHHHCCCCCCCCC
52.847668055
88UbiquitinationLEQTQKSKPVFSESL
HHHHHHCCCCCCCCC
52.8421890473
92PhosphorylationQKSKPVFSESLSD--
HHCCCCCCCCCCC--
26.8921955146
94PhosphorylationSKPVFSESLSD----
CCCCCCCCCCC----
31.7928355574
96PhosphorylationPVFSESLSD------
CCCCCCCCC------
51.0225159151

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 TIM8A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIM8A_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 TIM8A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAM1_HUMANSTAMphysical
12745081
TIM13_HUMANTIMM13physical
11875042
K1C15_HUMANKRT15physical
25416956
STAM2_HUMANSTAM2physical
25416956
TIM10_HUMANTIMM10physical
26344197

Drug and Disease Associations
Kegg Disease
OMIM Disease
304700Mohr-Tranebjaerg syndrome (MTS)
311150Jensen syndrome (JENSS)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIM8A_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.
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 SER-94, AND MASSSPECTROMETRY.

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