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Q9CQN1 (TRAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Trap1
Synonyms:Hsp75
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length706 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chaperone that expresses an ATPase activity By similarity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I By similarity. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis By similarity. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA By similarity. HAMAP-Rule MF_00505

Subunit structure

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

Subcellular location

Mitochondrion By similarity. Mitochondrion inner membrane By similarity. Mitochondrion matrix By similarity HAMAP-Rule MF_00505.

Sequence similarities

Belongs to the heat shock protein 90 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6060Mitochondrion By similarity
Chain61 – 706646Heat shock protein 75 kDa, mitochondrial HAMAP-Rule MF_00505
PRO_0000013605

Sites

Binding site1211ATP By similarity
Binding site1601ATP By similarity
Binding site1731ATP By similarity
Binding site2071ATP; via amide nitrogen By similarity
Binding site4041ATP By similarity

Amino acid modifications

Modified residue1721Phosphoserine By similarity
Modified residue1761Phosphothreonine By similarity
Modified residue2641N6-acetyllysine Ref.4
Modified residue3261N6-acetyllysine Ref.4
Modified residue3341N6-acetyllysine By similarity
Modified residue4261N6-acetyllysine Ref.4
Modified residue4331N6-acetyllysine Ref.4
Modified residue4681N6-acetyllysine By similarity
Modified residue4961Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CQN1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7183CE538CB36464

FASTA70680,209
        10         20         30         40         50         60 
MACELRAVLL WGRGLQTVLR APALAGVRRG KPVLHLQKTT VQFRGPTQSL ASGISAGQLY 

        70         80         90        100        110        120 
STQAAEDKEE ESLHSIISNT EAVRGSVSKH EFQAETKKLL DIVARSLYSE KEVFIRELIS 

       130        140        150        160        170        180 
NASDALEKLR HKLVCEGQVL PEMEIHLQTD AKKGTITIQD TGIGMTQEEL VSNLGTIARS 

       190        200        210        220        230        240 
GSKAFLEALQ NQAETSSKII GQFGVGFYSA FMVADKVEVY SRSAAPESPG YQWLSDGSGV 

       250        260        270        280        290        300 
FEIAEASGVR PGTKIIIHLK SDCKDFASES RVQDVVTKYS NFVSFPLYLN GKRINTLQAI 

       310        320        330        340        350        360 
WMMDPKDISE FQHEEFYRYI AQAYDKPRFT LHYKTDAPLN IRSIFYVPEM KPSMFDVSRE 

       370        380        390        400        410        420 
LGSSVALYSR KVLIQTKAAD ILPKWLRFIR GVVDSEDIPL NLSRELLQES ALIRKLRDVL 

       430        440        450        460        470        480 
QQRLIKFFID QSKKDAEKYA KFFEDYGLFM REGIVTTAEQ DIKEDIAKLL RYESSALPAG 

       490        500        510        520        530        540 
QLTSLPDYAS RMQAGTRNIY YLCAPNRHLA EHSPYYEAMK QKHTEVLFCY EQFDELTLLH 

       550        560        570        580        590        600 
LREFDKKKLI SVETDIVVDH YKEEKFEDTS PADERLSEKE TEDLMAWMRN ALGSRVTNVK 

       610        620        630        640        650        660 
VTFRLDTHPA MVTVLEMGAA RHFLRMQQLA KTQEERAQLL QPTLEINPRH TLIKKLCQLR 

       670        680        690        700 
ESEPELAQLL VDQIYENAMI AAGLVDDPRA MVGRLNDLLV KVLEKH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002409 mRNA. Translation: BAB22078.1.
AK010341 mRNA. Translation: BAB26865.1.
AK088471 mRNA. Translation: BAC40374.1.
BC022912 mRNA. Translation: AAH22912.1.
RefSeqNP_080784.1. NM_026508.2.
UniGeneMm.123366.

3D structure databases

ProteinModelPortalQ9CQN1.
SMRQ9CQN1. Positions 92-700.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212597. 1 interaction.
IntActQ9CQN1. 4 interactions.
MINTMINT-1861067.
STRING10090.ENSMUSP00000006137.

PTM databases

PhosphoSiteQ9CQN1.

2D gel databases

REPRODUCTION-2DPAGEQ9CQN1.

Proteomic databases

PaxDbQ9CQN1.
PRIDEQ9CQN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006137; ENSMUSP00000006137; ENSMUSG00000005981.
GeneID68015.
KEGGmmu:68015.
UCSCuc007xzk.1. mouse.

Organism-specific databases

CTD10131.
MGIMGI:1915265. Trap1.

Phylogenomic databases

eggNOGCOG0326.
GeneTreeENSGT00750000117672.
HOGENOMHOG000031987.
HOVERGENHBG103147.
InParanoidQ9CQN1.
KOK09488.
OMAAHDKPRY.
OrthoDBEOG7C8GGM.
PhylomeDBQ9CQN1.
TreeFamTF315234.

Gene expression databases

ArrayExpressQ9CQN1.
BgeeQ9CQN1.
CleanExMM_TRAP1.
GenevestigatorQ9CQN1.

Family and domain databases

Gene3D3.30.565.10. 1 hit.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
ProtoNetSearch...

Other

NextBio326204.
PROQ9CQN1.
SOURCESearch...

Entry information

Entry nameTRAP1_MOUSE
AccessionPrimary (citable) accession number: Q9CQN1
Secondary accession number(s): Q542I4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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