TIM9_HUMAN - dbPTM
TIM9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIM9_HUMAN
UniProt AC Q9Y5J7
Protein Name Mitochondrial import inner membrane translocase subunit Tim9
Gene Name TIMM9
Organism Homo sapiens (Human).
Sequence Length 89
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Intermembrane side .
Protein Description Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be 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..
Protein Sequence MAAQIPESDQIKQFKEFLGTYNKLTETCFLDCVKDFTTREVKPEETTCSEHCLQKYLKMTQRISMRFQEYHIQQNEALAAKAGLLGQPR
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
2Acetylation------MAAQIPESD
------CCCCCCCHH
14.2019413330
15SuccinylationSDQIKQFKEFLGTYN
HHHHHHHHHHHHHHH
45.0923954790
34UbiquitinationTCFLDCVKDFTTREV
HHHHHHHCCCCCCCC
54.15-
46PhosphorylationREVKPEETTCSEHCL
CCCCCCCCCCCHHHH
31.29-
55AcetylationCSEHCLQKYLKMTQR
CCHHHHHHHHHHHHH
39.3327452117
58AcetylationHCLQKYLKMTQRISM
HHHHHHHHHHHHHHH
36.4927452117
70PhosphorylationISMRFQEYHIQQNEA
HHHHHHHHHHHHHHH
8.0827642862
81UbiquitinationQNEALAAKAGLLGQP
HHHHHHHHHHHCCCC
37.0621890473
81UbiquitinationQNEALAAKAGLLGQP
HHHHHHHHHHHCCCC
37.0621890473

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 TIM9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIM9_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 TIM9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UCRI_HUMANUQCRFS1physical
22939629
COX5A_HUMANCOX5Aphysical
26344197
NUDC_HUMANNUDCphysical
26344197
TEBP_HUMANPTGES3physical
26344197
TIM10_HUMANTIMM10physical
26344197
TIM13_HUMANTIMM13physical
26344197
TIM8A_HUMANTIMM8Aphysical
26344197
TIM8B_HUMANTIMM8Bphysical
26344197

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 TIM9_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 ALA-2, AND MASS SPECTROMETRY.

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