CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018754
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
44SVISFGSKNRTIGVAubiquitination[1, 2, 3]
53RTIGVAAKNQQITHAubiquitination[2, 4, 5]
68NNTVSNFKRFHGRAFubiquitination[1, 2, 5]
84DPFIQKEKENLSYDLubiquitination[2]
95SYDLVPLKNGGVGIKubiquitination[1, 2, 4, 5]
102KNGGVGIKVMYMGEEubiquitination[2]
185ALNYGIYKQDLPSLDubiquitination[2]
194DLPSLDEKPRIVVFVubiquitination[2]
221AFNKGKLKVLGTAFDubiquitination[1, 2, 5]
234FDPFLGGKNFDEKLVubiquitination[2, 5]
239GGKNFDEKLVEHFCAubiquitination[2]
249EHFCAEFKTKYKLDAubiquitination[2]
272RLYQECEKLKKLMSSubiquitination[2]
274YQECEKLKKLMSSNSubiquitination[2]
275QECEKLKKLMSSNSTubiquitination[2]
295IECFMNDKDVSGKMNubiquitination[2]
300NDKDVSGKMNRSQFEubiquitination[2]
351ATRIPAVKERIAKFFubiquitination[2]
356AVKERIAKFFGKDISubiquitination[2]
360RIAKFFGKDISTTLNubiquitination[1, 2]
388AILSPAFKVREFSVTubiquitination[1, 6]
430NHAAPFSKVLTFLRRacetylation[7]
430NHAAPFSKVLTFLRRubiquitination[2, 4, 5]
458GVPYPEAKIGRFVVQubiquitination[1, 2, 5]
471VQNVSAQKDGEKSRVubiquitination[2, 5]
648YVYEFRDKLCGPYEKubiquitination[2]
655KLCGPYEKFICEQDHubiquitination[2]
691AKQAYVDKLEELMKIubiquitination[4]
697DKLEELMKIGTPVKVubiquitination[2]
703MKIGTPVKVRFQEAEubiquitination[2]
749HIDESEMKKVEKSVNubiquitination[2]
753SEMKKVEKSVNEVMEubiquitination[2]
790QEIKTKIKELNNTCEubiquitination[4]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
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 PPENPDTDKN VQQDNSEAGT 540
QPQVQTDAQQ TSQSPPSPEL TSEENKIPDA DKANEKKVDQ PPEAKKPKIK VVNVELPIEA 600
NLVWQLGKDL LNMYIETEGK MIMQDKLEKE RNDAKNAVEE YVYEFRDKLC GPYEKFICEQ 660
DHQNFLRLLT ETEDWLYEEG EDQAKQAYVD KLEELMKIGT PVKVRFQEAE ERPKMFEELG 720
QRLQHYAKIA ADFRNKDEKY NHIDESEMKK VEKSVNEVME WMNNVMNAQA KKSLDQDPVV 780
RAQEIKTKIK ELNNTCEPVV TQPKPKIESP KLERTPNGPN IDKKEEDLED KNNFGAEPPH 840
QNGECYPNEK NSVNMDLD 858 
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.