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O43615

- TIM44_HUMAN

UniProt

O43615 - TIM44_HUMAN

Protein

Mitochondrial import inner membrane translocase subunit TIM44

Gene

TIMM44

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (08 Nov 2002)
      Previous versions | rss
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    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. P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. protein targeting to mitochondrion Source: Reactome

    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

    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

    ArrayExpressiO43615.
    BgeeiO43615.
    CleanExiHS_TIMM44.
    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. 24 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 – 28616
    Helixi292 – 30615
    Helixi312 – 32110
    Helixi323 – 33311
    Helixi336 – 3427
    Helixi345 – 36016
    Beta strandi368 – 38316
    Beta strandi386 – 39813
    Beta strandi400 – 4023
    Beta strandi408 – 4114
    Beta strandi417 – 42711
    Helixi434 – 4363
    Beta strandi438 – 44710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000013004.
    HOVERGENiHBG055113.
    InParanoidiO43615.
    KOiK17804.
    OMAiKQCENDI.
    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

    MAAAALRSGW CRCPRRCLGS GIQFLSSHNL PHGSTYQMRR PGGELPLSKS    50
    YSSGNRKGFL SGLLDNVKQE LAKNKEMKES IKKFRDEARR LEESDVLQEA 100
    RRKYKTIESE TVRTSEVLRK KLGELTGTVK ESLHEVSKSD LGRKIKEGVE 150
    EAAKTAKQSA ESVSKGGEKL GRTAAFRALS QGVESVKKEI DDSVLGQTGP 200
    YRRPQRLRKR TEFAGDKFKE EKVFEPNEEA LGVVLHKDSK WYQQWKDFKE 250
    NNVVFNRFFE MKMKYDESDN AFIRASRALT DKVTDLLGGL FSKTEMSEVL 300
    TEILRVDPAF DKDRFLKQCE NDIIPNVLEA MISGELDILK DWCYEATYSQ 350
    LAHPIQQAKA LGLQFHSRIL DIDNVDLAMG KMMEQGPVLI ITFQAQLVMV 400
    VRNPKGEVVE GDPDKVLRML YVWALCRDQD ELNPYAAWRL LDISASSTEQ 450
    IL 452
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12192.1.
    RefSeqi NP_006342.2. NM_006351.3.
    UniGenei Hs.465784.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CW9 X-ray 1.90 A 266-452 [» ]
    ProteinModelPortali O43615.
    SMRi O43615. Positions 270-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115732. 24 interactions.
    IntActi O43615. 4 interactions.
    MINTi MINT-2999483.
    STRINGi 9606.ENSP00000270538.

    PTM databases

    PhosphoSitei O43615.

    Proteomic databases

    MaxQBi O43615.
    PaxDbi O43615.
    PeptideAtlasi O43615.
    PRIDEi O43615.

    Protocols and materials databases

    DNASUi 10469.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270538 ; ENSP00000270538 ; ENSG00000104980 .
    GeneIDi 10469.
    KEGGi hsa:10469.
    UCSCi uc002miz.3. human.

    Organism-specific databases

    CTDi 10469.
    GeneCardsi GC19M007991.
    HGNCi HGNC:17316. TIMM44.
    HPAi HPA043052.
    MIMi 605058. gene.
    neXtProti NX_O43615.
    PharmGKBi PA38229.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240138.
    HOGENOMi HOG000013004.
    HOVERGENi HBG055113.
    InParanoidi O43615.
    KOi K17804.
    OMAi KQCENDI.
    PhylomeDBi O43615.
    TreeFami TF106197.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei O43615.
    GeneWikii TIMM44.
    GenomeRNAii 10469.
    NextBioi 39705.
    PROi O43615.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43615.
    Bgeei O43615.
    CleanExi HS_TIMM44.
    Genevestigatori O43615.

    Family and domain databases

    InterProi IPR017303. Tim44.
    IPR007379. Tim44-like_dom.
    [Graphical view ]
    Pfami PF04280. Tim44. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037871. TIM44. 1 hit.
    SMARTi SM00978. Tim44. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00984. 3a0801s03tim44. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 132 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