CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014694
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 105 kDa 
Protein Synonyms/Alias
 Heat shock 110 kDa protein 
Gene Name
 Hsph1 
Gene Synonyms/Alias
 Hsp105; Hsp110 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
95SYDLVPMKNGGVGIKubiquitination[1]
194DLPNADEKPRVVVFVacetylation[2]
430NHAAPFSKVLTFLRRacetylation[2]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] 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
 Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity). 
Sequence Annotation
 MOD_RES 509 509 Phosphoserine (By similarity).
 MOD_RES 558 558 Phosphoserine (By similarity).
 MOD_RES 810 810 Phosphoserine (By similarity).
 MOD_RES 816 816 Phosphothreonine (By similarity).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 858 AA 
Protein Sequence
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGPKNRTIGV AAKNQQITHA 60
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEDH LFSVEQITAM 120
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN 180
YGIYKQDLPN ADEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL 240
VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSAK 300
MNRSQFEELC AELLQKIEVP LHLLMEQTHL KTEEVSAIEI VGGATRIPAV KERIARFFGK 360
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF 420
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ AVPYPEAKIG RFVVQNVSAQ KDGEKSKVKV 480
KVRVNTHGIF TISTASMVEK VPTEEEDGSS VEADMECPNQ KPAESSDVDK NIQQDNSEAG 540
TQPQVQTDGQ QTSQSPPSPE LTSEENKIPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE 600
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE 660
QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPRVLEEL 720
GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLHQDPV 780
VRTHEISAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NMDKKEDLEG KSNLGADAPH 840
QNGECHPNEK GSVSMDLD 858 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Compara.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.