Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitochondrial import inner membrane translocase subunit TIM44

Gene

TIMM44

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi166 – 1738ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chaperone binding Source: GO_Central
  3. P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. protein import into mitochondrial matrix Source: GO_Central
  3. protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit TIM44
Gene namesi
Name:TIMM44
Synonyms:MIMT44, TIM44
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17316. TIMM44.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: BHF-UCL
  2. mitochondrial matrix Source: BHF-UCL
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38229.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 452Mitochondrial import inner membrane translocase subunit TIM44PRO_0000034314
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Phosphoserine1 Publication
Modified residuei217 – 2171N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43615.
PaxDbiO43615.
PeptideAtlasiO43615.
PRIDEiO43615.

PTM databases

PhosphoSiteiO43615.

Expressioni

Gene expression databases

BgeeiO43615.
CleanExiHS_TIMM44.
ExpressionAtlasiO43615. baseline and differential.
GenevestigatoriO43615.

Organism-specific databases

HPAiHPA043052.

Interactioni

Subunit structurei

Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity). The complex interacts with the TIMM23 component of the TIM23 complex.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103983EBI-861737,EBI-365961

Protein-protein interaction databases

BioGridi115732. 27 interactions.
IntActiO43615. 4 interactions.
MINTiMINT-2999483.
STRINGi9606.ENSP00000270538.

Structurei

Secondary structure

1
452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi271 – 28616Combined sources
Helixi292 – 30615Combined sources
Helixi312 – 32110Combined sources
Helixi323 – 33311Combined sources
Helixi336 – 3427Combined sources
Helixi345 – 36016Combined sources
Beta strandi368 – 38316Combined sources
Beta strandi386 – 39813Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi408 – 4114Combined sources
Beta strandi417 – 42711Combined sources
Helixi434 – 4363Combined sources
Beta strandi438 – 44710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CW9X-ray1.90A266-452[»]
ProteinModelPortaliO43615.
SMRiO43615. Positions 270-451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43615.

Family & Domainsi

Sequence similaritiesi

Belongs to the Tim44 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG240138.
GeneTreeiENSGT00390000000051.
HOGENOMiHOG000013004.
HOVERGENiHBG055113.
InParanoidiO43615.
KOiK17804.
OMAiDFRDNNV.
PhylomeDBiO43615.
TreeFamiTF106197.

Family and domain databases

InterProiIPR017303. Tim44.
IPR007379. Tim44-like_dom.
[Graphical view]
PfamiPF04280. Tim44. 1 hit.
[Graphical view]
PIRSFiPIRSF037871. TIM44. 1 hit.
SMARTiSM00978. Tim44. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00984. 3a0801s03tim44. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43615-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAALRSGW CRCPRRCLGS GIQFLSSHNL PHGSTYQMRR PGGELPLSKS
60 70 80 90 100
YSSGNRKGFL SGLLDNVKQE LAKNKEMKES IKKFRDEARR LEESDVLQEA
110 120 130 140 150
RRKYKTIESE TVRTSEVLRK KLGELTGTVK ESLHEVSKSD LGRKIKEGVE
160 170 180 190 200
EAAKTAKQSA ESVSKGGEKL GRTAAFRALS QGVESVKKEI DDSVLGQTGP
210 220 230 240 250
YRRPQRLRKR TEFAGDKFKE EKVFEPNEEA LGVVLHKDSK WYQQWKDFKE
260 270 280 290 300
NNVVFNRFFE MKMKYDESDN AFIRASRALT DKVTDLLGGL FSKTEMSEVL
310 320 330 340 350
TEILRVDPAF DKDRFLKQCE NDIIPNVLEA MISGELDILK DWCYEATYSQ
360 370 380 390 400
LAHPIQQAKA LGLQFHSRIL DIDNVDLAMG KMMEQGPVLI ITFQAQLVMV
410 420 430 440 450
VRNPKGEVVE GDPDKVLRML YVWALCRDQD ELNPYAAWRL LDISASSTEQ

IL
Length:452
Mass (Da):51,356
Last modified:November 8, 2002 - v2
Checksum:i15BECF875611BE96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891E → A in AAB97740. (PubMed:10339406)Curated
Sequence conflicti226 – 2261P → A in AAB97740. (PubMed:10339406)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041254 mRNA. Translation: AAB97740.1.
AK289634 mRNA. Translation: BAF82323.1.
CH471139 Genomic DNA. Translation: EAW68954.1.
CH471139 Genomic DNA. Translation: EAW68955.1.
BC033628 mRNA. Translation: AAH33628.1.
CCDSiCCDS12192.1.
RefSeqiNP_006342.2. NM_006351.3.
UniGeneiHs.465784.

Genome annotation databases

EnsembliENST00000270538; ENSP00000270538; ENSG00000104980.
GeneIDi10469.
KEGGihsa:10469.
UCSCiuc002miz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041254 mRNA. Translation: AAB97740.1.
AK289634 mRNA. Translation: BAF82323.1.
CH471139 Genomic DNA. Translation: EAW68954.1.
CH471139 Genomic DNA. Translation: EAW68955.1.
BC033628 mRNA. Translation: AAH33628.1.
CCDSiCCDS12192.1.
RefSeqiNP_006342.2. NM_006351.3.
UniGeneiHs.465784.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CW9X-ray1.90A266-452[»]
ProteinModelPortaliO43615.
SMRiO43615. Positions 270-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115732. 27 interactions.
IntActiO43615. 4 interactions.
MINTiMINT-2999483.
STRINGi9606.ENSP00000270538.

PTM databases

PhosphoSiteiO43615.

Proteomic databases

MaxQBiO43615.
PaxDbiO43615.
PeptideAtlasiO43615.
PRIDEiO43615.

Protocols and materials databases

DNASUi10469.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270538; ENSP00000270538; ENSG00000104980.
GeneIDi10469.
KEGGihsa:10469.
UCSCiuc002miz.3. human.

Organism-specific databases

CTDi10469.
GeneCardsiGC19M007991.
HGNCiHGNC:17316. TIMM44.
HPAiHPA043052.
MIMi605058. gene.
neXtProtiNX_O43615.
PharmGKBiPA38229.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG240138.
GeneTreeiENSGT00390000000051.
HOGENOMiHOG000013004.
HOVERGENiHBG055113.
InParanoidiO43615.
KOiK17804.
OMAiDFRDNNV.
PhylomeDBiO43615.
TreeFamiTF106197.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiO43615.
GeneWikiiTIMM44.
GenomeRNAii10469.
NextBioi39705.
PROiO43615.
SOURCEiSearch...

Gene expression databases

BgeeiO43615.
CleanExiHS_TIMM44.
ExpressionAtlasiO43615. baseline and differential.
GenevestigatoriO43615.

Family and domain databases

InterProiIPR017303. Tim44.
IPR007379. Tim44-like_dom.
[Graphical view]
PfamiPF04280. Tim44. 1 hit.
[Graphical view]
PIRSFiPIRSF037871. TIM44. 1 hit.
SMARTiSM00978. Tim44. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00984. 3a0801s03tim44. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and structural characterization of the human mitochondrial inner membrane translocase."
    Bauer M.F., Gempel K., Reichert A.S., Rappold G.A., Lichtner P., Gerbitz K.-D., Neupert W., Brunner M., Hofmann S.
    J. Mol. Biol. 289:69-82(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Amygdala.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTIM44_HUMAN
AccessioniPrimary (citable) accession number: O43615
Secondary accession number(s): A8K0R9, D6W664, Q8N193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 8, 2002
Last modified: February 4, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.