CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031401
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 105 kDa 
Protein Synonyms/Alias
 cDNA FLJ52360, highly similar to Heat-shock protein 105 kDa 
Gene Name
 HSPH1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
53FDPFLGGKNFDEKLVubiquitination[1, 2, 3]
58GGKNFDEKLVEHFCAubiquitination[1, 3]
68EHFCAEFKTKYKLDAubiquitination[1]
91RLYQECEKLKKLMSSacetylation[3, 4, 5]
91RLYQECEKLKKLMSSubiquitination[1]
93YQECEKLKKLMSSNSubiquitination[1]
94QECEKLKKLMSSNSTubiquitination[1]
114IECFMNDKDVSGKMNubiquitination[1]
119NDKDVSGKMNRSQFEubiquitination[1]
170ATRIPAVKERIAKFFubiquitination[1, 3]
175AVKERIAKFFGKDISubiquitination[1]
179RIAKFFGKDISTTLNubiquitination[1, 6]
207AILSPAFKVREFSVTubiquitination[1, 3, 6, 7, 8, 9, 10]
249NHAAPFSKVLTFLRRacetylation[4]
249NHAAPFSKVLTFLRRubiquitination[1, 7, 8, 9, 10]
277GVPYPEAKIGRFVVQubiquitination[1, 2, 3, 6, 8, 9, 10]
290VQNVSAQKDGEKSRVacetylation[5]
290VQNVSAQKDGEKSRVubiquitination[1, 2, 3, 8]
445GKMIMQDKLEKERNDacetylation[5]
445GKMIMQDKLEKERNDubiquitination[1, 8]
467YVYEFRDKLCGPYEKubiquitination[1]
474KLCGPYEKFICEQDHubiquitination[1, 9, 10]
510AKQAYVDKLEELMKIacetylation[5]
510AKQAYVDKLEELMKIubiquitination[7]
516DKLEELMKIGTPVKVubiquitination[1]
522MKIGTPVKVRFQEAEubiquitination[1, 2]
568HIDESEMKKVEKSVNubiquitination[1]
572SEMKKVEKSVNEVMEubiquitination[1]
609QEIKTKIKELNNTCEubiquitination[3, 7]
630KPKIESPKLERTPNGacetylation[3]
642PNGPNIDKKEEDLEDacetylation[5]
669GECYPNEKNSVNMDLubiquitination[9]
Reference
 [1] 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]
 [2] 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]
 [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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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] 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]
 [8] 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]
 [9] 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]
 [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. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 677 AA 
Protein Sequence
MYMGEEHLFS VEQITAMLLT KLKETAENSL KKPVTDCVIS VLGTAFDPFL GGKNFDEKLV 60
EHFCAEFKTK YKLDAKSKIR ALLRLYQECE KLKKLMSSNS TDLPLNIECF MNDKDVSGKM 120
NRSQFEELCA ELLQKIEVPL YSLLEQTHLK VEDVSAVEIV GGATRIPAVK ERIAKFFGKD 180
ISTTLNADEA VARGCALQCA ILSPAFKVRE FSVTDAVPFP ISLIWNHDSE DTEGVHEVFS 240
RNHAAPFSKV LTFLRRGPFE LEAFYSDPQG VPYPEAKIGR FVVQNVSAQK DGEKSRVKVK 300
VRVNTHGIFT ISTASMVEKV PTEENEMSSE ADMECLNQRP PENPDTDKNV QQDNSEAGTQ 360
PQVQTDAQQT SQSPPSPELT SEENKIPDAD KANEKKVDQP PEAKKPKIKV VNVELPIEAN 420
LVWQLGKDLL NMYIETEGKM IMQDKLEKER NDAKNAVEEY VYEFRDKLCG PYEKFICEQD 480
HQNFLRLLTE TEDWLYEEGE DQAKQAYVDK LEELMKIGTP VKVRFQEAEE RPKMFEELGQ 540
RLQHYAKIAA DFRNKDEKYN HIDESEMKKV EKSVNEVMEW MNNVMNAQAK KSLDQDPVVR 600
AQEIKTKIKE LNNTCEPVVT QPKPKIESPK LERTPNGPNI DKKEEDLEDK NNFGAEPPHQ 660
NGECYPNEKN SVNMDLD 677 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 
Interpro
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 
Pfam
 PF00012; HSP70 
SMART
  
PROSITE
 PS01036; HSP70_3 
PRINTS
 PR00301; HEATSHOCK70.