TIM44_HUMAN - dbPTM
TIM44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIM44_HUMAN
UniProt AC O43615
Protein Name Mitochondrial import inner membrane translocase subunit TIM44
Gene Name TIMM44
Organism Homo sapiens (Human).
Sequence Length 452
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side . Mitochondrion matrix .
Protein Description Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source..
Protein Sequence MAAAALRSGWCRCPRRCLGSGIQFLSSHNLPHGSTYQMRRPGGELPLSKSYSSGNRKGFLSGLLDNVKQELAKNKEMKESIKKFRDEARRLEESDVLQEARRKYKTIESETVRTSEVLRKKLGELTGTVKESLHEVSKSDLGRKIKEGVEEAAKTAKQSAESVSKGGEKLGRTAAFRALSQGVESVKKEIDDSVLGQTGPYRRPQRLRKRTEFAGDKFKEEKVFEPNEEALGVVLHKDSKWYQQWKDFKENNVVFNRFFEMKMKYDESDNAFIRASRALTDKVTDLLGGLFSKTEMSEVLTEILRVDPAFDKDRFLKQCENDIIPNVLEAMISGELDILKDWCYEATYSQLAHPIQQAKALGLQFHSRILDIDNVDLAMGKMMEQGPVLIITFQAQLVMVVRNPKGEVVEGDPDKVLRMLYVWALCRDQDELNPYAAWRLLDISASSTEQIL
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
61PhosphorylationGNRKGFLSGLLDNVK
CCCCHHHHHHHHHHH		25.7422777824
80PhosphorylationKNKEMKESIKKFRDE
HCHHHHHHHHHHHHH		33.9026074081
105UbiquitinationQEARRKYKTIESETV
HHHHHHHHCHHHHHH		46.1724816145
105AcetylationQEARRKYKTIESETV
HHHHHHHHCHHHHHH		46.1727452117
106PhosphorylationEARRKYKTIESETVR
HHHHHHHCHHHHHHC		27.2120068231
109PhosphorylationRKYKTIESETVRTSE
HHHHCHHHHHHCCHH		34.4226074081
111PhosphorylationYKTIESETVRTSEVL
HHCHHHHHHCCHHHH		25.2726074081
114PhosphorylationIESETVRTSEVLRKK
HHHHHHCCHHHHHHH		25.5426074081
115PhosphorylationESETVRTSEVLRKKL
HHHHHCCHHHHHHHH		18.3626074081
128PhosphorylationKLGELTGTVKESLHE
HHHHHHHHHHHHHHH		24.1428060719
137PhosphorylationKESLHEVSKSDLGRK
HHHHHHHCHHHHHHH		24.3726471730
138AcetylationESLHEVSKSDLGRKI
HHHHHHCHHHHHHHH		53.8427452117
139PhosphorylationSLHEVSKSDLGRKIK
HHHHHCHHHHHHHHH		30.4826471730
146UbiquitinationSDLGRKIKEGVEEAA
HHHHHHHHHHHHHHH		51.99-
159PhosphorylationAAKTAKQSAESVSKG
HHHHHHHHHHHHHCH		33.04-
165UbiquitinationQSAESVSKGGEKLGR
HHHHHHHCHHHHHHH		69.6324816145
180PhosphorylationTAAFRALSQGVESVK
HHHHHHHHHHHHHHH		24.7325159151
185PhosphorylationALSQGVESVKKEIDD
HHHHHHHHHHHHCCC		36.5123186163
187AcetylationSQGVESVKKEIDDSV
HHHHHHHHHHCCCCC		54.7018585067
187UbiquitinationSQGVESVKKEIDDSV
HHHHHHHHHHCCCCC		54.7024816145
1872-HydroxyisobutyrylationSQGVESVKKEIDDSV
HHHHHHHHHHCCCCC		54.70-
188AcetylationQGVESVKKEIDDSVL
HHHHHHHHHCCCCCC		58.7218585077
193PhosphorylationVKKEIDDSVLGQTGP
HHHHCCCCCCCCCCC		18.5928857561
201NitrationVLGQTGPYRRPQRLR
CCCCCCCCCCCHHHH		22.16-
201PhosphorylationVLGQTGPYRRPQRLR
CCCCCCCCCCCHHHH		22.16-
217SuccinylationRTEFAGDKFKEEKVF
HCCCCCCCCCCCCCC		58.37-
217SuccinylationRTEFAGDKFKEEKVF
HCCCCCCCCCCCCCC		58.3721890473
217UbiquitinationRTEFAGDKFKEEKVF
HCCCCCCCCCCCCCC		58.3721890473
2172-HydroxyisobutyrylationRTEFAGDKFKEEKVF
HCCCCCCCCCCCCCC		58.37-
219UbiquitinationEFAGDKFKEEKVFEP
CCCCCCCCCCCCCCC		71.3722817900
222UbiquitinationGDKFKEEKVFEPNEE
CCCCCCCCCCCCCHH		54.0021890473
237UbiquitinationALGVVLHKDSKWYQQ
HHEEEEECCCHHHHH		60.5822817900
2372-HydroxyisobutyrylationALGVVLHKDSKWYQQ
HHEEEEECCCHHHHH		60.58-
240UbiquitinationVVLHKDSKWYQQWKD
EEEECCCHHHHHHHH		61.1221890473
246UbiquitinationSKWYQQWKDFKENNV
CHHHHHHHHHHHCCE		49.2821890473
249UbiquitinationYQQWKDFKENNVVFN
HHHHHHHHHCCEEEH		70.4422817900
2492-HydroxyisobutyrylationYQQWKDFKENNVVFN
HHHHHHHHHCCEEEH		70.44-
262UbiquitinationFNRFFEMKMKYDESD
EHHHHEEECCCCCCC		25.6622817900
264AcetylationRFFEMKMKYDESDNA
HHHEEECCCCCCCCH		43.9927452117
264UbiquitinationRFFEMKMKYDESDNA
HHHEEECCCCCCCCH		43.9922817900
2642-HydroxyisobutyrylationRFFEMKMKYDESDNA
HHHEEECCCCCCCCH		43.99-
268PhosphorylationMKMKYDESDNAFIRA
EECCCCCCCCHHHHH		33.01-
280PhosphorylationIRASRALTDKVTDLL
HHHHHHHHHHHHHHH		32.56-
292PhosphorylationDLLGGLFSKTEMSEV
HHHHHHCCHHHHHHH		43.6520068231
296SulfoxidationGLFSKTEMSEVLTEI
HHCCHHHHHHHHHHH		5.1121406390
312UbiquitinationRVDPAFDKDRFLKQC
CCCCCCCHHHHHHHH		44.3324816145
3122-HydroxyisobutyrylationRVDPAFDKDRFLKQC
CCCCCCCHHHHHHHH		44.33-
379SulfoxidationIDNVDLAMGKMMEQG
CCCCHHHHHHHHCCC		7.4321406390
405UbiquitinationVMVVRNPKGEVVEGD
EEEECCCCCCEECCC		71.8524816145
435PhosphorylationDQDELNPYAAWRLLD
CCHHCCHHHHHHHHH		14.1025147952
448PhosphorylationLDISASSTEQIL---
HHCCCCCCHHHC---		29.4324719451
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 TIM44_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIM44_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 TIM44_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CKLF5_HUMANCMTM5physical
25416956
GRP75_HUMANHSPA9physical
12677068
TPM2_HUMANTPM2physical
28514442
CO1A1_HUMANCOL1A1physical
28514442
CO1A2_HUMANCOL1A2physical
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 TIM44_HUMAN

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Related Literatures of Post-Translational Modification

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