CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018755
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 105 kDa 
Protein Synonyms/Alias
 Antigen NY-CO-25; Heat shock 110 kDa protein 
Gene Name
 HSPH1 
Gene Synonyms/Alias
 HSP105; HSP110; KIAA0201 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
68NNTVSNFKRFHGRAFubiquitination[1]
82FNDPFIQKEKENLSYubiquitination[1]
95SYDLVPLKNGGVGIKubiquitination[1]
194DLPSLDEKPRIVVFVubiquitination[2]
234FDPFLGGKNFDEKLVubiquitination[1]
388AILSPAFKVREFSVTubiquitination[2]
430NHAAPFSKVLTFLRRubiquitination[2]
458GVPYPEAKIGRFVVQubiquitination[1, 2]
471VQNVSAQKDGEKSRVubiquitination[1]
611KLCGPYEKFICEQDHubiquitination[2]
659MKIGTPVKVRFQEAEubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
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 557 557 Phosphoserine.
 MOD_RES 809 809 Phosphoserine.
 MOD_RES 815 815 Phosphothreonine.  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 858 AA 
Protein Sequence
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA 60
NNTVSNFKRF HGRAFNDPFI QKEKENLSYD LVPLKNGGVG IKVMYMGEEH LFSVEQITAM 120
LLTKLKETAE NSLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN 180
YGIYKQDLPS LDEKPRIVVF VDMGHSAFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL 240
VEHFCAEFKT KYKLDAKSKI RALLRLYQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK 300
MNRSQFEELC AELLQKIEVP LYSLLEQTHL KVEDVSAVEI VGGATRIPAV KERIAKFFGK 360
DISTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLIWNHDS EDTEGVHEVF 420
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV 480
KVRVNTHGIF TISTASMVEK VPTEENEMSS EADMECLNQR PPENPDTDAN EKKVDQPPEA 540
KKPKIKVVNV ELPIEANLVW QLGKDLLNMY IETEGKMIMQ DKLEKERNDA KNAVEEYVYE 600
FRDKLCGPYE KFICEQDHQN FLRLLTETED WLYEEGEDQA KQAYVDKLEE LMKIGTPVKV 660
RFQEAEERPK MFEELGQRLQ HYAKIAADFR NKDEKYNHID ESEMKKVEKS VNEVMEWMNN 720
VMNAQAKKSL DQDPVVRAQE IKTKIKELNN TCEPVVTQPK PKIESPKLER TPNGPNIDKK 780
EEDLEDKNNF GAEPPHQNGE CYPNEKNSVN MDLD 814 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:BHF-UCL.
 GO:0005576; C:extracellular region; TAS:BHF-UCL.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Compara.
 GO:0045345; P:positive regulation of MHC class I biosynthetic process; TAS:BHF-UCL.
 GO:0051135; P:positive regulation of NK T cell activation; TAS:BHF-UCL.
 GO:0006986; P:response to unfolded protein; TAS:ProtInc. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.