CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014152
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 75 kDa, mitochondrial 
Protein Synonyms/Alias
 HSP 75; TNFR-associated protein 1; Tumor necrosis factor type 1 receptor-associated protein; TRAP-1 
Gene Name
 Trap1 
Gene Synonyms/Alias
 Hsp75 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
128NASDALEKLRHKRVCacetylation[1]
326YIAQAYDKPRFILHYacetylation[1]
334PRFILHYKTDAPLNIacetylation[1]
351IFYVPEMKPSMFDVSacetylation[1]
384KATDILPKWLRFVRGacetylation[1]
426VLQQRLIKFFIDQSKacetylation[1]
433KFFIDQSKKDAEKYAacetylation[1]
434FFIDQSKKDAEKYAKacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Chaperone that expresses an ATPase activity (By similarity). 
Sequence Annotation
 BINDING 121 121 ATP (By similarity).
 BINDING 160 160 ATP (By similarity).
 BINDING 173 173 ATP (By similarity).
 BINDING 207 207 ATP; via amide nitrogen (By similarity).
 BINDING 404 404 ATP (By similarity).
 MOD_RES 89 89 N6-acetyllysine (By similarity).
 MOD_RES 172 172 Phosphoserine.
 MOD_RES 176 176 Phosphothreonine.
 MOD_RES 334 334 N6-acetyllysine (By similarity).
 MOD_RES 403 403 Phosphoserine (By similarity).
 MOD_RES 426 426 N6-acetyllysine (By similarity).
 MOD_RES 468 468 N6-acetyllysine (By similarity).
 MOD_RES 496 496 Phosphothreonine (By similarity).  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 706 AA 
Protein Sequence
MARELRALLL WGRGLQSALR APALAGVRRG KPVLHLQKTT VHFRDPTQSL ASGISAGQLY 60
STQAAEDKKE EALHSIISNT EAVQGSVSKH EFQAETKKLL DIVARSLYSE KEVFIRELIS 120
NASDALEKLR HKRVCEGQVL PEMEIHLQTD AEKGTITIQD TGIGMTKEEL VSNLGTIARS 180
GSKAFLEALQ HQAETSSRII GQFGVGFYSA FMVADKVEVY SRPAAPESPG YQWLSDGSGV 240
FEIAEASGVR PGTKIIIHLK SDCKDFANES RVQDVVTKYS NFVSFPLYLN GRRINTLQAI 300
WMMDPKDISE FQHEEFYRYI AQAYDKPRFI LHYKTDAPLN IRSIFYVPEM KPSMFDVSRE 360
LGSSVALYSR KVLIQTKATD ILPKWLRFVR GVVDSEDIPL NLSRELLQES ALIRKLRDVL 420
QQRLIKFFID QSKKDAEKYA KFFEDYGLFM REGIVTTAEQ DIKEDIAKLL RYESSALPAG 480
QLTSLSDYAS RMQAGTRNIY YLCAPNRHLA EHSPYYEAMK QKQTEVLFCY EQFDELTLLH 540
LREFDKKKLI SVETDIVVDH YKEEKFEDTS PAGERLSEKE TEELMAWMRN ALGSRVTNVK 600
VTFRLDTHPA MVTVLEMGAA RHFLRMQQLA KTQEERAQLL QPTLEINPRH TLIKKLNQLR 660
EREPELAQLL VDQIYENAMI AAGLVDDPRA MVGRLNDLLV KALERH 706 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0034599; P:cellular response to oxidative stress; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF00183; HSP90 
SMART
 SM00387; HATPase_c 
PROSITE
  
PRINTS
 PR00775; HEATSHOCK90.