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Q12931

- TRAP1_HUMAN

UniProt

Q12931 - TRAP1_HUMAN

Protein

Heat shock protein 75 kDa, mitochondrial

Gene

TRAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191ATPBy similarity
    Binding sitei158 – 1581ATPBy similarity
    Binding sitei171 – 1711ATPBy similarity
    Binding sitei205 – 2051ATP; via amide nitrogenBy similarity
    Binding sitei402 – 4021ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. tumor necrosis factor receptor binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of cellular respiration Source: UniProtKB
    2. protein folding Source: InterPro
    3. response to stress Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein 75 kDa, mitochondrial
    Short name:
    HSP 75
    Alternative name(s):
    TNFR-associated protein 1
    Tumor necrosis factor type 1 receptor-associated protein
    Short name:
    TRAP-1
    Gene namesi
    Name:TRAP1
    Synonyms:HSP75
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16264. TRAP1.

    Subcellular locationi

    Mitochondrion 1 Publication. Mitochondrion inner membrane 1 Publication. Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB
    3. mitochondrial inner membrane Source: UniProtKB
    4. mitochondrial matrix Source: UniProtKB
    5. mitochondrion Source: ParkinsonsUK-UCL
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36781.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5959MitochondrionBy similarityAdd
    BLAST
    Chaini60 – 704645Heat shock protein 75 kDa, mitochondrialPRO_0000013604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei170 – 1701PhosphoserineBy similarity
    Modified residuei174 – 1741PhosphothreonineBy similarity
    Modified residuei262 – 2621N6-acetyllysineBy similarity
    Modified residuei324 – 3241N6-acetyllysineBy similarity
    Modified residuei332 – 3321N6-acetyllysine1 Publication
    Modified residuei424 – 4241N6-acetyllysine1 Publication
    Modified residuei431 – 4311N6-acetyllysineBy similarity
    Modified residuei466 – 4661N6-acetyllysine1 Publication
    Modified residuei494 – 4941Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ12931.
    PaxDbiQ12931.
    PeptideAtlasiQ12931.
    PRIDEiQ12931.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00030275.

    PTM databases

    PhosphoSiteiQ12931.

    Expressioni

    Tissue specificityi

    Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung, placenta and bladder. Expression is higly reduced in bladder cancer and renal cell carcinoma specimens compared to healthy tissues, but it is increased in other type of tumors.1 Publication

    Gene expression databases

    ArrayExpressiQ12931.
    BgeeiQ12931.
    CleanExiHS_TRAP1.
    GenevestigatoriQ12931.

    Organism-specific databases

    HPAiHPA041082.
    HPA044227.

    Interactioni

    Subunit structurei

    Binds to the intracellular domain of tumor necrosis factor type 1 receptor. Binds to RB1. Interacts with SRC. Interacts with SDHA.2 Publications

    Protein-protein interaction databases

    BioGridi115435. 43 interactions.
    DIPiDIP-6250N.
    IntActiQ12931. 27 interactions.
    MINTiMINT-1510364.
    STRINGi9606.ENSP00000246957.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12931.
    SMRiQ12931. Positions 71-702.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031987.
    HOVERGENiHBG103147.
    InParanoidiQ12931.
    KOiK09488.
    OMAiAHDKPRY.
    OrthoDBiEOG7C8GGM.
    PhylomeDBiQ12931.
    TreeFamiTF315234.

    Family and domain databases

    Gene3Di3.30.565.10. 1 hit.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12931-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MARELRALLL WGRRLRPLLR APALAAVPGG KPILCPRRTT AQLGPRRNPA    50
    WSLQAGRLFS TQTAEDKEEP LHSIISSTES VQGSTSKHEF QAETKKLLDI 100
    VARSLYSEKE VFIRELISNA SDALEKLRHK LVSDGQALPE MEIHLQTNAE 150
    KGTITIQDTG IGMTQEELVS NLGTIARSGS KAFLDALQNQ AEASSKIIGQ 200
    FGVGFYSAFM VADRVEVYSR SAAPGSLGYQ WLSDGSGVFE IAEASGVRTG 250
    TKIIIHLKSD CKEFSSEARV RDVVTKYSNF VSFPLYLNGR RMNTLQAIWM 300
    MDPKDVREWQ HEEFYRYVAQ AHDKPRYTLH YKTDAPLNIR SIFYVPDMKP 350
    SMFDVSRELG SSVALYSRKV LIQTKATDIL PKWLRFIRGV VDSEDIPLNL 400
    SRELLQESAL IRKLRDVLQQ RLIKFFIDQS KKDAEKYAKF FEDYGLFMRE 450
    GIVTATEQEV KEDIAKLLRY ESSALPSGQL TSLSEYASRM RAGTRNIYYL 500
    CAPNRHLAEH SPYYEAMKKK DTEVLFCFEQ FDELTLLHLR EFDKKKLISV 550
    ETDIVVDHYK EEKFEDRSPA AECLSEKETE ELMAWMRNVL GSRVTNVKVT 600
    LRLDTHPAMV TVLEMGAARH FLRMQQLAKT QEERAQLLQP TLEINPRHAL 650
    IKKLNQLRAS EPGLAQLLVD QIYENAMIAA GLVDDPRAMV GRLNELLVKA 700
    LERH 704
    Length:704
    Mass (Da):80,110
    Last modified:June 7, 2005 - v3
    Checksum:i4B16DE3D2B9E0285
    GO
    Isoform 2 (identifier: Q12931-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         30-82: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:651
    Mass (Da):74,267
    Checksum:iA0B8927FC74C41F2
    GO

    Sequence cautioni

    The sequence AAA87704.1 differs from that shown. Reason: Frameshift at position 656.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 193PLL → ALR in AAA87704. (PubMed:7876093)Curated
    Sequence conflicti53 – 531L → M in AAC02679. (PubMed:8756626)Curated
    Sequence conflicti360 – 3601G → D in BAG61180. (PubMed:14702039)Curated
    Sequence conflicti475 – 4762Missing in AAC02679. (PubMed:8756626)Curated
    Sequence conflicti488 – 4914SRMR → AHW in AAC02679. (PubMed:8756626)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti307 – 3071R → G.2 Publications
    Corresponds to variant rs13926 [ dbSNP | Ensembl ].
    VAR_016108
    Natural varianti395 – 3951D → E.1 Publication
    Corresponds to variant rs1136948 [ dbSNP | Ensembl ].
    VAR_049625
    Natural varianti572 – 5721E → K.
    Corresponds to variant rs55766649 [ dbSNP | Ensembl ].
    VAR_061272
    Natural varianti692 – 6921R → H.
    Corresponds to variant rs2791 [ dbSNP | Ensembl ].
    VAR_049626

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei30 – 8253Missing in isoform 2. 1 PublicationVSP_055061Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154108 mRNA. Translation: AAF15314.1.
    AK299127 mRNA. Translation: BAG61180.1.
    AC005203 Genomic DNA. Translation: AAC24722.1.
    AC006111 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85338.1.
    CH471112 Genomic DNA. Translation: EAW85340.1.
    BC018950 mRNA. Translation: AAH18950.1.
    BC023585 mRNA. Translation: AAH23585.1.
    U12595 mRNA. Translation: AAA87704.1. Frameshift.
    AF043254 mRNA. Translation: AAC02679.1.
    CCDSiCCDS10508.1. [Q12931-1]
    CCDS61824.1. [Q12931-2]
    RefSeqiNP_001258978.1. NM_001272049.1.
    NP_057376.2. NM_016292.2.
    UniGeneiHs.30345.

    Genome annotation databases

    EnsembliENST00000246957; ENSP00000246957; ENSG00000126602. [Q12931-1]
    ENST00000538171; ENSP00000442070; ENSG00000126602. [Q12931-2]
    GeneIDi10131.
    KEGGihsa:10131.
    UCSCiuc002cvs.3. human. [Q12931-1]

    Polymorphism databases

    DMDMi67477458.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154108 mRNA. Translation: AAF15314.1 .
    AK299127 mRNA. Translation: BAG61180.1 .
    AC005203 Genomic DNA. Translation: AAC24722.1 .
    AC006111 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85338.1 .
    CH471112 Genomic DNA. Translation: EAW85340.1 .
    BC018950 mRNA. Translation: AAH18950.1 .
    BC023585 mRNA. Translation: AAH23585.1 .
    U12595 mRNA. Translation: AAA87704.1 . Frameshift.
    AF043254 mRNA. Translation: AAC02679.1 .
    CCDSi CCDS10508.1. [Q12931-1 ]
    CCDS61824.1. [Q12931-2 ]
    RefSeqi NP_001258978.1. NM_001272049.1.
    NP_057376.2. NM_016292.2.
    UniGenei Hs.30345.

    3D structure databases

    ProteinModelPortali Q12931.
    SMRi Q12931. Positions 71-702.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115435. 43 interactions.
    DIPi DIP-6250N.
    IntActi Q12931. 27 interactions.
    MINTi MINT-1510364.
    STRINGi 9606.ENSP00000246957.

    Chemistry

    BindingDBi Q12931.
    ChEMBLi CHEMBL1075132.

    PTM databases

    PhosphoSitei Q12931.

    Polymorphism databases

    DMDMi 67477458.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00030275.

    Proteomic databases

    MaxQBi Q12931.
    PaxDbi Q12931.
    PeptideAtlasi Q12931.
    PRIDEi Q12931.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246957 ; ENSP00000246957 ; ENSG00000126602 . [Q12931-1 ]
    ENST00000538171 ; ENSP00000442070 ; ENSG00000126602 . [Q12931-2 ]
    GeneIDi 10131.
    KEGGi hsa:10131.
    UCSCi uc002cvs.3. human. [Q12931-1 ]

    Organism-specific databases

    CTDi 10131.
    GeneCardsi GC16M003710.
    H-InvDB HIX0012776.
    HGNCi HGNC:16264. TRAP1.
    HPAi HPA041082.
    HPA044227.
    MIMi 606219. gene.
    neXtProti NX_Q12931.
    PharmGKBi PA36781.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0326.
    HOGENOMi HOG000031987.
    HOVERGENi HBG103147.
    InParanoidi Q12931.
    KOi K09488.
    OMAi AHDKPRY.
    OrthoDBi EOG7C8GGM.
    PhylomeDBi Q12931.
    TreeFami TF315234.

    Miscellaneous databases

    ChiTaRSi TRAP1. human.
    GeneWikii TRAP1.
    GenomeRNAii 10131.
    NextBioi 35474312.
    PROi Q12931.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12931.
    Bgeei Q12931.
    CleanExi HS_TRAP1.
    Genevestigatori Q12931.

    Family and domain databases

    Gene3Di 3.30.565.10. 1 hit.
    HAMAPi MF_00505. HSP90.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    PANTHERi PTHR11528. PTHR11528. 1 hit.
    Pfami PF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002583. Hsp90. 1 hit.
    PRINTSi PR00775. HEATSHOCK90.
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses."
      Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M.
      Hum. Mol. Genet. 8:2155-2164(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-307.
    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] (ISOFORM 2).
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 and Eye.
    6. "Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor."
      Song H.Y., Dunbar J.D., Zhang Y.X., Guo D., Donner D.B.
      J. Biol. Chem. 270:3574-3581(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-704, VARIANT GLY-307.
    7. "A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock."
      Chen C.-F., Chen Y., Dai K., Chen P.-L., Riley D.J., Lee W.-H.
      Mol. Cell. Biol. 16:4691-4699(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-704, VARIANT GLU-395.
    8. "The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties."
      Felts S.J., Owen B.A.L., Nguyen P., Trepel J., Donner D.B., Toft D.O.
      J. Biol. Chem. 275:3305-3312(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-332; LYS-424 AND LYS-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase."
      Sciacovelli M., Guzzo G., Morello V., Frezza C., Zheng L., Nannini N., Calabrese F., Laudiero G., Esposito F., Landriscina M., Defilippi P., Bernardi P., Rasola A.
      Cell Metab. 17:988-999(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS NEGATIVE REGULATOR OF MITOCHONDRIAL RESPIRATION, INTERACTION WITH SDHA.
    13. Cited for: FUNCTION.
    14. Cited for: FUNCTION AS NEGATIVE REGULATOR OF MITOCHONDRIAL RESPIRATION, INTERACTION WITH SRC, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiTRAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q12931
    Secondary accession number(s): B4DR68
    , D3DUC8, F5H897, O43642, O75235, Q9UHL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3