CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019748
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily C member 7 
Protein Synonyms/Alias
 Tetratricopeptide repeat protein 2; TPR repeat protein 2 
Gene Name
 DNAJC7 
Gene Synonyms/Alias
 TPR2; TTC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41QGNAYYAKKDYNEAYubiquitination[1, 2]
42GNAYYAKKDYNEAYNubiquitination[2]
60KAIDMCPKNASYYGNubiquitination[2, 3]
128RALELDHKNAQAQQEubiquitination[1, 2, 4]
137AQAQQEFKNANAVMEubiquitination[1, 2, 4]
155IAETDFEKRDFRKVVubiquitination[1, 2]
182CHRFKILKAECLAMLubiquitination[2, 5, 6]
245RMAPDHEKACIACRNubiquitination[2]
273AFKEGNYKLAYELYTubiquitination[1, 2, 4]
291GIDPNNIKTNAKLYCubiquitination[2]
295NNIKTNAKLYCNRGTubiquitination[2]
322EDCTNAVKLDDTYIKubiquitination[2]
329KLDDTYIKAYLRRAQubiquitination[1, 3, 5, 6]
359EKVYQTEKTKEHKQLacetylation[7]
368KEHKQLLKNAQLELKubiquitination[5, 6]
375KNAQLELKKSKRKDYacetylation[7]
376NAQLELKKSKRKDYYubiquitination[2]
384SKRKDYYKILGVDKNubiquitination[1, 2, 3, 5, 6, 8]
390YKILGVDKNASEDEIubiquitination[1, 2, 3, 7, 8]
398NASEDEIKKAYRKRAubiquitination[1]
399ASEDEIKKAYRKRALubiquitination[2]
422GASAEVQKEEEKKFKubiquitination[1, 7]
429KEEEKKFKEVGEAFTubiquitination[2]
442FTILSDPKKKTRYDSubiquitination[1, 2]
443TILSDPKKKTRYDSGubiquitination[2]
444ILSDPKKKTRYDSGQubiquitination[2]
Reference
 [1] 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]
 [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] 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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity). 
Sequence Annotation
 REPEAT 28 61 TPR 1.
 REPEAT 62 95 TPR 2.
 REPEAT 96 129 TPR 3.
 REPEAT 142 175 TPR 4.
 REPEAT 177 209 TPR 5.
 REPEAT 210 243 TPR 6.
 REPEAT 256 289 TPR 7.
 REPEAT 294 327 TPR 8.
 REPEAT 328 361 TPR 9.
 DOMAIN 381 451 J.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleus; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 494 AA 
Protein Sequence
MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY YTKAIDMCPK 60
NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL REGKCHLSLG NAMAACRSFQ 120
RALELDHKNA QAQQEFKNAN AVMEYEKIAE TDFEKRDFRK VVFCMDRALE FAPACHRFKI 180
LKAECLAMLG RYPEAQSVAS DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA 240
PDHEKACIAC RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR 300
GTVNSKLRKL DDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQYEEAVRD YEKVYQTEKT 360
KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV 420
QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGMNM GDFDPNNIFK AFFGGPGGFS 480
FEASGPGNFF FQFG 494 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB. 
Interpro
 IPR001623; DnaJ_domain.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF00226; DnaJ
 PF00515; TPR_1 
SMART
 SM00271; DnaJ
 SM00028; TPR 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS
 PR00625; JDOMAIN.