CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038317
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Heat shock protein 105 kDa 
Protein Synonyms/Alias
  
Gene Name
 Hsph1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
95SYDLVPMKNGGVGIKubiquitination[1]
193FDPFLGGKNFDEKLVubiquitination[1]
417GVPYPEAKIGRFVVQubiquitination[1]
430VQNVSAQKDGEKSRVacetylation[2]
430VQNVSAQKDGEKSRVubiquitination[1]
615KLCGPYEKFICEQEHacetylation[3]
624ICEQEHEKFLRLLTEacetylation[3]
624ICEQEHEKFLRLLTEubiquitination[1]
709HIDESEMKKVEKSVNubiquitination[1]
750HEIRAKVKELNNVCEubiquitination[1]
771KPKIESPKLERTPNGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 817 AA 
Protein Sequence
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA 60
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVPSFFTDA ERRSVLDAAQ 120
IVGLNCLRLM NDMTAVALNY GIYKQDLPNA EEKPRVVVFV DMGHSSFQVS ACAFNKGKLK 180
VLGTAFDPFL GGKNFDEKLV EHFCAEFKTK YKLDAKSKIR ALLRLHQECE KLKKLMSSNS 240
TDLPLNIECF MNDKDVSGKM NRSQFEELCA ELLQKIEVPL HSLMAQTQLK AEDVSAIEIV 300
GGATRIPAVK ERIAKFFGKD VSTTLNADEA VARGCALQCA ILSPAFKVRE FSVTDAVPFP 360
ISLVWNHDSE ETEGVHEVFS RNHAAPFSKV LTFLRRGPFE LEAFYSDPQG VPYPEAKIGR 420
FVVQNVSAQK DGEKSRVKVK VRVNTHGIFT ISTASMVEKV PTEEEDGSSL EADMECPNQR 480
PTESSDVDKN IQQDNSEAGT QPQVQTDGQQ TSQSPPSPEL TSEESKTPDA DKANEKKVDQ 540
PPEAKKPKIK VVNVELPVEA NLVWQLGRDL LNMYIETEGK MIMQDKLEKE RNDAKNAVEE 600
CVYEFRDKLC GPYEKFICEQ EHEKFLRLLT ETEDWLYEEG EDQAKQAYID KLEELMKMGT 660
PVKVRFQEAE ERPKVLEELG QRLQHYAKIA ADFRGKDEKY NHIDESEMKK VEKSVNEVME 720
WMNNVMNAQA KRSLDQDPVV RTHEIRAKVK ELNNVCEPVV TQPKPKIESP KLERTPNGPN 780
IDKKEDLEGK NNLGAEAPHQ NGECHPNEKG SVNMDLD 817 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:MGI. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.