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Protein

Heat shock protein 75 kDa, mitochondrial

Gene

Trap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211ATPBy similarity
Binding sitei160 – 1601ATPBy similarity
Binding sitei173 – 1731ATPBy similarity
Binding sitei207 – 2071ATP; via amide nitrogenBy similarity
Binding sitei404 – 4041ATPBy similarity

GO - Molecular functioni

GO - Biological processi

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1915265. Trap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060MitochondrionBy similarityAdd
BLAST
Chaini61 – 706646Heat shock protein 75 kDa, mitochondrialPRO_0000013605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei176 – 1761PhosphothreonineBy similarity
Modified residuei264 – 2641N6-acetyllysine1 Publication
Modified residuei326 – 3261N6-acetyllysine1 Publication
Modified residuei334 – 3341N6-acetyllysineBy similarity
Modified residuei426 – 4261N6-acetyllysine1 Publication
Modified residuei433 – 4331N6-acetyllysine1 Publication
Modified residuei468 – 4681N6-acetyllysineBy similarity
Modified residuei496 – 4961PhosphothreonineBy similarity
Modified residuei570 – 5701PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CQN1.
PaxDbiQ9CQN1.
PRIDEiQ9CQN1.

2D gel databases

REPRODUCTION-2DPAGEQ9CQN1.

PTM databases

PhosphoSiteiQ9CQN1.

Expressioni

Gene expression databases

BgeeiQ9CQN1.
CleanExiMM_TRAP1.
ExpressionAtlasiQ9CQN1. baseline and differential.
GenevisibleiQ9CQN1. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi212597. 1 interaction.
IntActiQ9CQN1. 4 interactions.
MINTiMINT-1861067.
STRINGi10090.ENSMUSP00000006137.

Structurei

3D structure databases

ProteinModelPortaliQ9CQN1.
SMRiQ9CQN1. Positions 72-704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0326.
GeneTreeiENSGT00790000122989.
HOGENOMiHOG000031987.
HOVERGENiHBG103147.
InParanoidiQ9CQN1.
KOiK09488.
OMAiAHDKPRY.
OrthoDBiEOG7C8GGM.
PhylomeDBiQ9CQN1.
TreeFamiTF315234.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF00183. 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.

Sequencei

Sequence statusi: Complete.

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

Q9CQN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACELRAVLL WGRGLQTVLR APALAGVRRG KPVLHLQKTT VQFRGPTQSL
60 70 80 90 100
ASGISAGQLY STQAAEDKEE ESLHSIISNT EAVRGSVSKH EFQAETKKLL
110 120 130 140 150
DIVARSLYSE KEVFIRELIS NASDALEKLR HKLVCEGQVL PEMEIHLQTD
160 170 180 190 200
AKKGTITIQD TGIGMTQEEL VSNLGTIARS GSKAFLEALQ NQAETSSKII
210 220 230 240 250
GQFGVGFYSA FMVADKVEVY SRSAAPESPG YQWLSDGSGV FEIAEASGVR
260 270 280 290 300
PGTKIIIHLK SDCKDFASES RVQDVVTKYS NFVSFPLYLN GKRINTLQAI
310 320 330 340 350
WMMDPKDISE FQHEEFYRYI AQAYDKPRFT LHYKTDAPLN IRSIFYVPEM
360 370 380 390 400
KPSMFDVSRE LGSSVALYSR KVLIQTKAAD ILPKWLRFIR GVVDSEDIPL
410 420 430 440 450
NLSRELLQES ALIRKLRDVL QQRLIKFFID QSKKDAEKYA KFFEDYGLFM
460 470 480 490 500
REGIVTTAEQ DIKEDIAKLL RYESSALPAG QLTSLPDYAS RMQAGTRNIY
510 520 530 540 550
YLCAPNRHLA EHSPYYEAMK QKHTEVLFCY EQFDELTLLH LREFDKKKLI
560 570 580 590 600
SVETDIVVDH YKEEKFEDTS PADERLSEKE TEDLMAWMRN ALGSRVTNVK
610 620 630 640 650
VTFRLDTHPA MVTVLEMGAA RHFLRMQQLA KTQEERAQLL QPTLEINPRH
660 670 680 690 700
TLIKKLCQLR ESEPELAQLL VDQIYENAMI AAGLVDDPRA MVGRLNDLLV

KVLEKH
Length:706
Mass (Da):80,209
Last modified:June 1, 2001 - v1
Checksum:i7183CE538CB36464
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002409 mRNA. Translation: BAB22078.1.
AK010341 mRNA. Translation: BAB26865.1.
AK088471 mRNA. Translation: BAC40374.1.
BC022912 mRNA. Translation: AAH22912.1.
CCDSiCCDS27914.1.
RefSeqiNP_080784.1. NM_026508.2.
UniGeneiMm.123366.

Genome annotation databases

EnsembliENSMUST00000006137; ENSMUSP00000006137; ENSMUSG00000005981.
GeneIDi68015.
KEGGimmu:68015.
UCSCiuc007xzk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002409 mRNA. Translation: BAB22078.1.
AK010341 mRNA. Translation: BAB26865.1.
AK088471 mRNA. Translation: BAC40374.1.
BC022912 mRNA. Translation: AAH22912.1.
CCDSiCCDS27914.1.
RefSeqiNP_080784.1. NM_026508.2.
UniGeneiMm.123366.

3D structure databases

ProteinModelPortaliQ9CQN1.
SMRiQ9CQN1. Positions 72-704.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212597. 1 interaction.
IntActiQ9CQN1. 4 interactions.
MINTiMINT-1861067.
STRINGi10090.ENSMUSP00000006137.

PTM databases

PhosphoSiteiQ9CQN1.

2D gel databases

REPRODUCTION-2DPAGEQ9CQN1.

Proteomic databases

MaxQBiQ9CQN1.
PaxDbiQ9CQN1.
PRIDEiQ9CQN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006137; ENSMUSP00000006137; ENSMUSG00000005981.
GeneIDi68015.
KEGGimmu:68015.
UCSCiuc007xzk.1. mouse.

Organism-specific databases

CTDi10131.
MGIiMGI:1915265. Trap1.

Phylogenomic databases

eggNOGiCOG0326.
GeneTreeiENSGT00790000122989.
HOGENOMiHOG000031987.
HOVERGENiHBG103147.
InParanoidiQ9CQN1.
KOiK09488.
OMAiAHDKPRY.
OrthoDBiEOG7C8GGM.
PhylomeDBiQ9CQN1.
TreeFamiTF315234.

Miscellaneous databases

NextBioi326204.
PROiQ9CQN1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQN1.
CleanExiMM_TRAP1.
ExpressionAtlasiQ9CQN1. baseline and differential.
GenevisibleiQ9CQN1. MM.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF00183. 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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryonic stem cell, Kidney and Thymus.
  2. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 391-404, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264; LYS-326; LYS-426 AND LYS-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTRAP1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQN1
Secondary accession number(s): Q542I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.