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Q12931

- TRAP1_HUMAN

UniProt

Q12931 - TRAP1_HUMAN

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Protein

Heat shock protein 75 kDa, mitochondrial

Gene
TRAP1, HSP75
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1191ATP By similarity
Binding sitei158 – 1581ATP By similarity
Binding sitei171 – 1711ATP By similarity
Binding sitei205 – 2051ATP; via amide nitrogen By similarity
Binding sitei402 – 4021ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: InterPro
  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: UniProtKB-KW
Complete GO annotation...

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. Mitochondrion inner membrane. Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrion Source: HPA
  5. nucleus Source: HPA
Complete GO annotation...

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 – 5959Mitochondrion By similarityAdd
BLAST
Chaini60 – 704645Heat shock protein 75 kDa, mitochondrialUniRule annotationPRO_0000013604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphoserine By similarity
Modified residuei174 – 1741Phosphothreonine By similarity
Modified residuei262 – 2621N6-acetyllysine By similarity
Modified residuei324 – 3241N6-acetyllysine By similarity
Modified residuei332 – 3321N6-acetyllysine1 Publication
Modified residuei424 – 4241N6-acetyllysine1 Publication
Modified residuei431 – 4311N6-acetyllysine By 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.

Family & Domainsi

Sequence similaritiesi

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.

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. VSP_055061Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 193PLL → ALR in AAA87704. 1 Publication
Sequence conflicti53 – 531L → M in AAC02679. 1 Publication
Sequence conflicti360 – 3601G → D in BAG61180. 1 Publication
Sequence conflicti475 – 4762Missing in AAC02679. 1 Publication
Sequence conflicti488 – 4914SRMR → AHW in AAC02679. 1 Publication

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]
RefSeqiNP_001258978.1. NM_001272049.1.
NP_057376.2. NM_016292.2.
UniGeneiHs.30345.

Genome annotation databases

EnsembliENST00000246957; ENSP00000246957; ENSG00000126602.
ENST00000538171; ENSP00000442070; ENSG00000126602.
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 ]
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 .
ENST00000538171 ; ENSP00000442070 ; ENSG00000126602 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 148 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

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