Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Mitochondrial import inner membrane translocase subunit TIM14  

UniProtKB / Swiss-Prot ID :  TIM14_HUMAN

Gene Name (Synonyms) : 
DNAJC19, TIM14, TIMM14  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion inner membrane; Single-pass membrane protein (Probable). 

Protein Function :  Probable 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. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity). 

Transmembrane Topology (topPTM) : TIM14_HUMAN 

Protein Sequence MASTVVAVGLTIAAAGFAGRYVLQAMKHMEPQVKQVFQSLPKSAFSGGYYRGGFEPKMTKREAALILGVS...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCHHHHHHHCCCC...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASTVV
---CHHHHH
17.57UniProtKB
Link-
34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EPQVKQVFQ
HHHHHHHHH
35.18Phosphositeplus
Link-
42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QSLPKSAFS
HHCCCCCCC
60.76Phosphositeplus
Link-
70PhosphoserineILGVSPTAN
HCCCCCCCC
18.09HPRD
Link-
70PhosphoserineILGVSPTAN
HCCCCCCCC
18.09Phosphositeplus
Link-
93N6-acetyllysineNHPDKGGSP
HCCCCCCCH
70.40HPRD
Link-
93N6-acetyllysineNHPDKGGSP
HCCCCCCCH
70.40Phosphositeplus
Link-
93N6-acetyllysine.NHPDKGGSP
HCCCCCCCH
70.40UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Kegg disease
H00754 3-Methylglutaconic aciduria (MGCA)
OMIM disease
6101983-methylglutaconic aciduria 5 (MGA5)
Drug Reference
There are no disease associations of PTM sites.
- top -
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.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures