Q12931 (TRAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRAP1
Synonyms:	HSP75

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	704 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence caution	The sequence AAA87704.1 differs from that shown. Reason: Frameshift at position 656.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oxidative stress Inferred from direct assay PubMed 16551573. Source: BHF-UCL protein folding Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tumor necrosis factor receptor binding Non-traceable author statement Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 59	59	Mitochondrion By similarity
	Chain	60 – 704	645	Heat shock protein 75 kDa, mitochondrial		PRO_0000013604
Sites
	Binding site	119	1	ATP By similarity
	Binding site	158	1	ATP By similarity
	Binding site	171	1	ATP By similarity
	Binding site	205	1	ATP; via amide nitrogen By similarity
	Binding site	402	1	ATP By similarity
Amino acid modifications
	Modified residue	87	1	N6-acetyllysine By similarity
	Modified residue	332	1	N6-acetyllysine Ref.10
	Modified residue	401	1	Phosphoserine Ref.9
	Modified residue	424	1	N6-acetyllysine Ref.10
	Modified residue	466	1	N6-acetyllysine Ref.10
	Modified residue	494	1	Phosphothreonine Ref.8
Natural variations
	Natural variant	307	1	R → G. Ref.1 Ref.5 Corresponds to variant rs13926 [ dbSNP | Ensembl ].		VAR_016108
	Natural variant	395	1	D → E. Ref.6 Corresponds to variant rs1136948 [ dbSNP | Ensembl ].		VAR_049625
	Natural variant	572	1	E → K. Corresponds to variant rs55766649 [ dbSNP | Ensembl ].		VAR_061272
	Natural variant	692	1	R → H. Corresponds to variant rs2791 [ dbSNP | Ensembl ].		VAR_049626
Experimental info
	Sequence conflict	17 – 19	3	PLL → ALR in AAA87704. Ref.5
	Sequence conflict	53	1	L → M in AAC02679. Ref.6
	Sequence conflict	475 – 476	2	Missing in AAC02679. Ref.6
	Sequence conflict	488 – 491	4	SRMR → AHW in AAC02679. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q12931 [UniParc]. Last modified June 7, 2005. Version 3. Checksum: 4B16DE3D2B9E0285	FASTA	704	80,110
	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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-307.
[2]	"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].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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, MASS SPECTROMETRY.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF154108 mRNA. Translation: AAF15314.1. AC005203 Genomic DNA. Translation: AAC24722.1. 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.
IPI	IPI00030275.
RefSeq	NP_057376.2. NM_016292.2.
UniGene	Hs.30345.
3D structure databases
ProteinModelPortal	Q12931.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6250N.
IntAct	Q12931. 22 interactions.
MINT	MINT-1510364.
STRING	9606.ENSP00000246957.
PTM databases
PhosphoSite	Q12931.
Polymorphism databases
DMDM	67477458.
2D gel databases
REPRODUCTION-2DPAGE	IPI00030275.
Proteomic databases
PaxDb	Q12931.
PeptideAtlas	Q12931.
PRIDE	Q12931.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000246957; ENSP00000246957; ENSG00000126602.
GeneID	10131.
KEGG	hsa:10131.
UCSC	uc002cvs.3. human.
Organism-specific databases
CTD	10131.
GeneCards	GC16M003710.
H-InvDB	HIX0012776.
HGNC	HGNC:16264. TRAP1.
HPA	HPA041082. HPA044227.
MIM	606219. gene.
neXtProt	NX_Q12931.
PharmGKB	PA36781.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0326.
HOGENOM	HOG000031987.
HOVERGEN	HBG103147.
InParanoid	Q12931.
KO	K09488.
OMA	TEVLFCY.
OrthoDB	EOG4XKV6D.
PhylomeDB	Q12931.
Gene expression databases
ArrayExpress	Q12931.
Bgee	Q12931.
CleanEx	HS_TRAP1.
Genevestigator	Q12931.
GermOnline	ENSG00000126602. Homo sapiens.
Family and domain databases
Gene3D	3.30.565.10. 1 hit.
InterPro	IPR003594. HATPase_ATP-bd. IPR001404. Hsp90. IPR020575. Hsp90_N. IPR020568. Ribosomal_S5_D2-typ_fold. [Graphical view]
PANTHER	PTHR11528. PTHR11528. 1 hit.
Pfam	PF02518. HATPase_c. 1 hit. PF00183. HSP90. 1 hit. [Graphical view]
PIRSF	PIRSF002583. Hsp90. 1 hit.
PRINTS	PR00775. HEATSHOCK90.
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
PROSITE	PS00298. HSP90. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q12931.
ChEMBL	CHEMBL1075132.
ChiTaRS	TRAP1. human.
GenomeRNAi	10131.
NextBio	38323.
SOURCE	Search...

Entry information

Entry name

TRAP1_HUMAN

Accession

Primary (citable) accession number: Q12931
Secondary accession number(s): D3DUC8 , O43642, O75235, Q9UHL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.