TIM13_HUMAN - dbPTM
TIM13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIM13_HUMAN
UniProt AC Q9Y5L4
Protein Name Mitochondrial import inner membrane translocase subunit Tim13
Gene Name TIMM13
Organism Homo sapiens (Human).
Sequence Length 95
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..
Protein Sequence MEGGFGSDFGGSGSGKLDPGLIMEQVKVQIAVANAQELLQRMTDKCFRKCIGKPGGSLDNSEQKCIAMCMDRYMDAWNTVSRAYNSRLQRERANM
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
1Sulfoxidation-------MEGGFGSD
-------CCCCCCCC		11.0228465586
1Acetylation-------MEGGFGSD
-------CCCCCCCC		11.0225944712
7Phosphorylation-MEGGFGSDFGGSGS
-CCCCCCCCCCCCCC		27.7525159151
12PhosphorylationFGSDFGGSGSGKLDP
CCCCCCCCCCCCCCC		30.1120068231
14PhosphorylationSDFGGSGSGKLDPGL
CCCCCCCCCCCCCCC		34.1620068231
16UbiquitinationFGGSGSGKLDPGLIM
CCCCCCCCCCCCCCH		51.9521906983
23SulfoxidationKLDPGLIMEQVKVQI
CCCCCCCHHHHHHHH		3.3721406390
27UbiquitinationGLIMEQVKVQIAVAN
CCCHHHHHHHHHHHC		28.2822817900
45AcetylationLLQRMTDKCFRKCIG
HHHHHHHHHHHHHHC		26.5525953088
49UbiquitinationMTDKCFRKCIGKPGG
HHHHHHHHHHCCCCC		15.2222817900
50GlutathionylationTDKCFRKCIGKPGGS
HHHHHHHHHCCCCCC		4.2922555962
53SuccinylationCFRKCIGKPGGSLDN
HHHHHHCCCCCCCCC		22.15-
53UbiquitinationCFRKCIGKPGGSLDN
HHHHHHCCCCCCCCC		22.1522817900
53SuccinylationCFRKCIGKPGGSLDN
HHHHHHCCCCCCCCC		22.1521890473
57PhosphorylationCIGKPGGSLDNSEQK
HHCCCCCCCCCHHHH		38.1625159151
61PhosphorylationPGGSLDNSEQKCIAM
CCCCCCCHHHHHHHH		40.8627135362
64AcetylationSLDNSEQKCIAMCMD
CCCCHHHHHHHHHHH		24.4526051181
64UbiquitinationSLDNSEQKCIAMCMD
CCCCHHHHHHHHHHH		24.4525015289
72MethylationCIAMCMDRYMDAWNT
HHHHHHHHHHHHHHH		11.20115918497
73PhosphorylationIAMCMDRYMDAWNTV
HHHHHHHHHHHHHHH		8.6224114839
74SulfoxidationAMCMDRYMDAWNTVS
HHHHHHHHHHHHHHH		2.7028183972
79PhosphorylationRYMDAWNTVSRAYNS
HHHHHHHHHHHHHHH		14.7924114839
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 TIM13_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIM13_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 TIM13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAB39_HUMANCAB39physical
17353931
TIM8B_HUMANTIMM8Bphysical
17353931
PHOCN_HUMANMOB4physical
17353931
RFA3_HUMANRPA3physical
17353931
TIM8A_HUMANTIMM8Aphysical
17353931
TIM50_HUMANTIMM50physical
22939629
WIPI2_HUMANWIPI2physical
22939629
IST1_HUMANIST1physical
22863883
MIF_HUMANMIFphysical
26344197
NDRG1_HUMANNDRG1physical
26344197
TIM10_HUMANTIMM10physical
26344197
TIM8A_HUMANTIMM8Aphysical
26344197
TIM8B_HUMANTIMM8Bphysical
26344197
ALBU_HUMANALBphysical
26496610
BPTF_HUMANBPTFphysical
26496610
BCL7C_HUMANBCL7Cphysical
26496610
DCAF1_HUMANVPRBPphysical
26496610
PSMD6_HUMANPSMD6physical
26496610
SF3B2_HUMANSF3B2physical
26496610
S23IP_HUMANSEC23IPphysical
26496610
RM03_HUMANMRPL3physical
26496610
RASF8_HUMANRASSF8physical
26496610
DICER_HUMANDICER1physical
26496610
NEPRO_HUMANC3orf17physical
26496610
PALMD_HUMANPALMDphysical
26496610
TUT7_HUMANZCCHC6physical
26496610
OARD1_HUMANOARD1physical
26496610
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 TIM13_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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