CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004239
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endoplasmin 
Protein Synonyms/Alias
 94 kDa glucose-regulated protein; GRP-94; Heat shock protein 90 kDa beta member 1; Tumor rejection antigen 1; gp96 homolog 
Gene Name
 HSP90B1 
Gene Synonyms/Alias
 GRP94; TRA1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
75ELREKSEKFAFQAEVubiquitination[1, 2, 3, 4]
95LIINSLYKNKEIFLRubiquitination[1, 2, 4, 5]
97INSLYKNKEIFLRELubiquitination[2, 5, 6]
114NASDALDKIRLISLTubiquitination[1, 2, 3]
142KIKCDKEKNLLHVTDubiquitination[1, 4]
161MTREELVKNLGTIAKacetylation[7]
161MTREELVKNLGTIAKubiquitination[1, 3, 4]
168KNLGTIAKSGTSEFLubiquitination[1, 2, 3, 4, 5, 6]
252TTITLVLKEEASDYLubiquitination[2]
265YLELDTIKNLVKKYSubiquitination[1, 2, 4, 5]
270TIKNLVKKYSQFINFubiquitination[1, 2, 4, 6]
360DEYKAFYKSFSKESDubiquitination[1, 2, 3, 4]
405FDEYGSKKSDYIKLYubiquitination[2]
410SKKSDYIKLYVRRVFubiquitination[8]
434PKYLNFVKGVVDSDDubiquitination[2, 5, 6, 8]
455RETLQQHKLLKVIRKubiquitination[2, 3, 6, 9]
458LQQHKLLKVIRKKLVacetylation[10]
458LQQHKLLKVIRKKLVubiquitination[6]
467IRKKLVRKTLDMIKKubiquitination[2, 6]
473RKTLDMIKKIADDKYubiquitination[2]
479IKKIADDKYNDTFWKacetylation[7]
479IKKIADDKYNDTFWKubiquitination[3, 6]
486KYNDTFWKEFGTNIKubiquitination[1, 3, 4]
586ALPEFDGKRFQNVAKubiquitination[2]
593KRFQNVAKEGVKFDEubiquitination[2, 3]
633ALKDKIEKAVVSQRLubiquitination[1, 4]
663GNMERIMKAQAYQTGubiquitination[1, 2, 4, 6]
671AQAYQTGKDISTNYYubiquitination[1, 2, 3, 4, 5, 6]
682TNYYASQKKTFEINPubiquitination[2]
683NYYASQKKTFEINPRubiquitination[6]
733GYLLPDTKAYGDRIEubiquitination[2, 5, 6]
800AKESTAEKDEL****ubiquitination[2]
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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 
Functional Description
 Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. 
Sequence Annotation
 MOTIF 800 803 Prevents secretion from ER.
 BINDING 107 107 ATP (By similarity).
 BINDING 149 149 ATP (By similarity).
 BINDING 162 162 ATP (By similarity).
 BINDING 168 168 ATP (By similarity).
 BINDING 199 199 ATP; via amide nitrogen (By similarity).
 BINDING 448 448 ATP (By similarity).
 MOD_RES 306 306 Phosphoserine.
 CARBOHYD 62 62 N-linked (GlcNAc...).
 CARBOHYD 107 107 N-linked (GlcNAc...).
 CARBOHYD 217 217 N-linked (GlcNAc...).
 CARBOHYD 445 445 N-linked (GlcNAc...).
 CARBOHYD 481 481 N-linked (GlcNAc...) (Potential).
 CARBOHYD 502 502 N-linked (GlcNAc...) (Potential).
 DISULFID 138 138 Interchain (By similarity).  
Keyword
 ATP-binding; Calcium; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding; Phosphoprotein; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 803 AA 
Protein Sequence
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG 60
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL 120
TDENALSGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE 180
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT 240
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK 300
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK 360
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD 420
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADDKY 480
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF 540
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 600
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER 660
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV LDLAVVLFET 720
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETAEDT TEDTEQDEDE 780
EMDVGTDEEE ETAKESTAEK DEL 803 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005509; F:calcium ion binding; TAS:UniProtKB.
 GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
 GO:0019903; F:protein phosphatase binding; IDA:MGI.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0046790; F:virion binding; IPI:UniProtKB.
 GO:0031247; P:actin rod assembly; IDA:MGI.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0071318; P:cellular response to ATP; IDA:MGI.
 GO:0030433; P:ER-associated protein catabolic process; IMP:UniProtKB.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0015031; P:protein transport; NAS:UniProtKB.
 GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
 GO:0001666; P:response to hypoxia; IDA:UniProtKB.
 GO:0051208; P:sequestering of calcium ion; NAS:UniProtKB.
 GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR019805; Heat_shock_protein_90_CS.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF00183; HSP90 
SMART
 SM00387; HATPase_c 
PROSITE
 PS00014; ER_TARGET
 PS00298; HSP90 
PRINTS
 PR00775; HEATSHOCK90.