Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q12931 (TRAP1_HUMAN)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Heat shock protein 75 kDa, mitochondrial
      Short name=HSP 75
Alternative name(s):
    Tumor necrosis factor type 1 receptor-associated protein
      Short name=TRAP-1
    TNFR-associated protein 1
Gene names
Name: TRAP1
Synonyms: HSP75
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length704 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.

Subunit structure

Binds to the intracellular domain of tumor necrosis factor type 1 receptor. Binds to RB1.

Subcellular location

Mitochondrion.

Tissue specificity

Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tumor necrosis factor receptor binding Ref.3

Non-traceable author statement. Source: UniProtKB

unfolded protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Mitochondrion By similarity
Chain60 – 704645Heat shock protein 75 kDa, mitochondrial
PRO_0000013604

Sites

Binding site1191ATP By similarity
Binding site1581ATP By similarity
Binding site1711ATP By similarity
Binding site2051ATP; via amide nitrogen By similarity

Amino acid modifications

Modified residue871N6-acetyllysine By similarity
Modified residue3661Phosphotyrosine Ref.7
Modified residue4941Phosphothreonine Ref.8

Natural variations

Natural variant3071R → G: dbSNP rs13926. Ref.1 Ref.3
VAR_016108
Natural variant3951D → E: dbSNP rs1136948. Ref.5
VAR_049625
Natural variant6921R → H: dbSNP rs2791.
VAR_049626

Experimental info

Sequence conflict17 – 193PLL → ALR in AAA87704. Ref.3
Sequence conflict531L → M in AAC02679. Ref.5
Sequence conflict475 – 4762Missing in AAC02679. Ref.5
Sequence conflict488 – 4914SRMR → AHW in AAC02679. Ref.5
Sequence conflict656 – 70449QLRAS…ALERH → HCAQASLAWLSCWWIRYTRT P Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q12931-1 [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: 4B16DE3D2B9E0285

FASTA70480,110
        10         20         30         40         50         60 
MARELRALLL WGRRLRPLLR APALAAVPGG KPILCPRRTT AQLGPRRNPA WSLQAGRLFS 

        70         80         90        100        110        120 
TQTAEDKEEP LHSIISSTES VQGSTSKHEF QAETKKLLDI VARSLYSEKE VFIRELISNA 

       130        140        150        160        170        180 
SDALEKLRHK LVSDGQALPE MEIHLQTNAE KGTITIQDTG IGMTQEELVS NLGTIARSGS 

       190        200        210        220        230        240 
KAFLDALQNQ AEASSKIIGQ FGVGFYSAFM VADRVEVYSR SAAPGSLGYQ WLSDGSGVFE 

       250        260        270        280        290        300 
IAEASGVRTG TKIIIHLKSD CKEFSSEARV RDVVTKYSNF VSFPLYLNGR RMNTLQAIWM 

       310        320        330        340        350        360 
MDPKDVREWQ HEEFYRYVAQ AHDKPRYTLH YKTDAPLNIR SIFYVPDMKP SMFDVSRELG 

       370        380        390        400        410        420 
SSVALYSRKV LIQTKATDIL PKWLRFIRGV VDSEDIPLNL SRELLQESAL IRKLRDVLQQ 

       430        440        450        460        470        480 
RLIKFFIDQS KKDAEKYAKF FEDYGLFMRE GIVTATEQEV KEDIAKLLRY ESSALPSGQL 

       490        500        510        520        530        540 
TSLSEYASRM RAGTRNIYYL CAPNRHLAEH SPYYEAMKKK DTEVLFCFEQ FDELTLLHLR 

       550        560        570        580        590        600 
EFDKKKLISV ETDIVVDHYK EEKFEDRSPA AECLSEKETE ELMAWMRNVL GSRVTNVKVT 

       610        620        630        640        650        660 
LRLDTHPAMV TVLEMGAARH FLRMQQLAKT QEERAQLLQP TLEINPRHAL IKKLNQLRAS 

       670        680        690        700 
EPGLAQLLVD QIYENAMIAA GLVDDPRAMV GRLNELLVKA LERH 

« Hide

References

« Hide 'large scale' references
[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: 10545594] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-307.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Eye.
[3]"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: 7876093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-704, VARIANT GLY-307.
[4]Ricke D.O., Bruce D., Mundt M., Doggett N., Munk C., Saunders E., Robinson D., Jones M., Buckingham J., Chasteen L., Thompson S., Goodwin L., Bryant J., Tesmer J., Meincke L., Longmire J., White S., Ueng S. expand/collapse author list , Tatum O., Campbell C., Fawcett J., Maltbie M., Misra M., Deaven L.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 32-677.
[5]"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: 8756626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-704, VARIANT GLU-395.
[6]"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: 10652318] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-366, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, MASS SPECTROMETRY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF154108 mRNA. Translation: AAF15314.1.
BC018950 mRNA. Translation: AAH18950.1.
BC023585 mRNA. Translation: AAH23585.1.
U12595 mRNA. Translation: AAA87704.1.
AC005203 Genomic DNA. Translation: AAC24722.1.
AF043254 mRNA. Translation: AAC02679.1.
IPIIPI00030275.
RefSeqNP_057376.2.
UniGeneHs.30345

3D structure databases

HSSPHSSP built from PDB template 1AMW based on UniProtKB P02829.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6250N.
IntActQ12931. 2 interactions.

PTM databases

PhosphoSiteQ12931.

2-D gel databases

REPRODUCTION-2DPAGEIPI00030275.

Proteomic databases

PeptideAtlasQ12931.
PRIDEQ12931.

Genome annotation databases

EnsemblENSG00000126602. Homo sapiens. [Contig view]
GeneID10131.
KEGGhsa:10131.
NMPDRfig|9606.3.peg.11646.

Organism-specific databases

GeneCardsGC16M003648.
H-InvDBHIX0012774.
HIX0012776.
HGNCHGNC:16264. TRAP1.
HPACAB004281.
MIM606219. gene.
PharmGKBPA36781.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ12931.
HOVERGENQ12931.
OMAQ12931. TEVLFCY.

Gene expression databases

BgeeQ12931.
CleanExHS_TRAP1.
GermOnlineENSG00000126602. Homo sapiens.

Family and domain databases

InterProIPR003594. ATP_bd_ATPase.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90.
[Graphical view]
PANTHERPTHR11528. Hsp90. 1 hit.
PfamPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 4 hits.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
PROSITEPS00298. HSP90. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio38323.
SOURCESearch...

Entry information

Entry nameTRAP1_HUMAN
AccessionPrimary (citable) accession number: Q12931
Secondary accession number(s): O43642, O75235, Q9UHL5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 7, 2005
Last modified: June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents