CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031412
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock 105kDa/110kDa protein 1, isoform CRA_b 
Protein Synonyms/Alias
 Heat shock protein 105 kDa; cDNA FLJ52364, highly similar to Heat-shock protein 105 kDa 
Gene Name
 HSPH1 
Gene Synonyms/Alias
 hCG_32198 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55RTIGVAAKNQQITHAubiquitination[1, 2, 3, 4]
70NNTVSNFKRFHGRAFubiquitination[2, 3, 5, 6, 7, 8]
84FNDPFIQKEKENLSYubiquitination[7]
86DPFIQKEKENLSYDLubiquitination[3, 8]
97SYDLVPLKNGGVGIKubiquitination[1, 2, 3, 4, 6, 7, 8, 9]
104KNGGVGIKVMYMGEEubiquitination[3]
187ALNYGIYKQDLPSLDubiquitination[3]
196DLPSLDEKPRIVVFVacetylation[8]
196DLPSLDEKPRIVVFVubiquitination[3, 8, 10]
223AFNKGKLKVLGTAFDubiquitination[2, 3, 6, 8, 9]
236FDPFLGGKNFDEKLVubiquitination[2, 9]
390AILSPAFKVREFSVTubiquitination[4, 9]
432NHAAPFSKVLTFLRRubiquitination[4, 9]
657KLCGPYEKFICEQDHubiquitination[9]
693AKQAYVDKLEELMKIubiquitination[4]
699DKLEELMKIGTPVKVubiquitination[9]
792QEIKTKIKELNNTCEubiquitination[4, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [10] 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
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 860 AA 
Protein Sequence
MATAAVLRGP AAHWVESFQK AREEGSGSGT WRGRWRRRSV ISFGSKNRTI GVAAKNQQIT 60
HANNTVSNFK RFHGRAFNDP FIQKEKENLS YDLVPLKNGG VGIKVMYMGE EHLFSVEQIT 120
AMLLTKLKET AENSLKKPVT DCVISVPSFF TDAERRSVLD AAQIVGLNCL RLMNDMTAVA 180
LNYGIYKQDL PSLDEKPRIV VFVDMGHSAF QVSACAFNKG KLKVLGTAFD PFLGGKNFDE 240
KLVEHFCAEF KTKYKLDAKS KIRALLRLYQ ECEKLKKLMS SNSTDLPLNI ECFMNDKDVS 300
GKMNRSQFEE LCAELLQKIE VPLYSLLEQT HLKVEDVSAV EIVGGATRIP AVKERIAKFF 360
GKDISTTLNA DEAVARGCAL QCAILSPAFK VREFSVTDAV PFPISLIWNH DSEDTEGVHE 420
VFSRNHAAPF SKVLTFLRRG PFELEAFYSD PQGVPYPEAK IGRFVVQNVS AQKDGEKSRV 480
KVKVRVNTHG IFTISTASMV EKVPTEENEM SSEADMECLN QRPPENPDTD KNVQQDNSEA 540
GTQPQVQTDA QQTSQSPPSP ELTSEENKIP DADKANEKKV DQPPEAKKPK IKVVNVELPI 600
EANLVWQLGK DLLNMYIETE GKMIMQDKLE KERNDAKNAV EEYVYEFRDK LCGPYEKFIC 660
EQDHQNFLRL LTETEDWLYE EGEDQAKQAY VDKLEELMKI GTPVKVRFQE AEERPKMFEE 720
LGQRLQHYAK IAADFRNKDE KYNHIDESEM KKVEKSVNEV MEWMNNVMNA QAKKSLDQDP 780
VVRAQEIKTK IKELNNTCEP VVTQPKPKIE SPKLERTPNG PNIDKKEEDL EDKNNFGAEP 840
PHQNGECYPN EKNSVNMDLD 860 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 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.