CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012258
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MORC family CW-type zinc finger protein 3 
Protein Synonyms/Alias
 Zinc finger CW-type coiled-coil domain protein 3 
Gene Name
 MORC3 
Gene Synonyms/Alias
 KIAA0136; ZCWCC3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79MTSDKLHKMLSFGFSubiquitination[1]
105GLYGNGFKSGSMRLGubiquitination[1]
152VPIVAFNKHRQMINLubiquitination[1]
192LDAIIGKKGTRIIIWubiquitination[1]
214ATEFDFEKDKYDIRIubiquitination[1]
216EFDFEKDKYDIRIPEubiquitination[1]
231DLDEITGKKGYKKQEubiquitination[1, 2]
232LDEITGKKGYKKQERubiquitination[1, 2]
261YCSILYLKPRMQIILubiquitination[1]
274ILRGQKVKTQLVSKSubiquitination[1]
280VKTQLVSKSLAYIERubiquitination[1, 3, 4]
293ERDVYRPKFLSKTVRubiquitination[1, 3]
297YRPKFLSKTVRITFGubiquitination[1, 4]
310FGFNCRNKDHYGIMMubiquitination[1]
325YHRNRLIKAYEKVGCubiquitination[1]
329RLIKAYEKVGCQLRAubiquitination[1]
353IIECNFLKPTHNKQDubiquitination[1]
358FLKPTHNKQDFDYTNubiquitination[1]
377TITALGEKLNDYWNEubiquitination[1, 2]
386NDYWNEMKVKKNTEYubiquitination[1]
388YWNEMKVKKNTEYPLubiquitination[1]
389WNEMKVKKNTEYPLNubiquitination[1, 2, 4]
404LPVEDIQKRPDQTWVubiquitination[1]
432GMDQLPEKWYCSNNPubiquitination[1, 5]
464LVHPTYEKTYKKTNKubiquitination[1]
468TYEKTYKKTNKEKFRubiquitination[1]
687ETQETTDKSADDAGCubiquitination[2]
710LLLVTEEKENYKRQCubiquitination[3]
762LLESINGKSESPDHMubiquitination[6]
806QCSNNESKSEMDEMAubiquitination[2]
825DVFRQLDKCSIERDQubiquitination[1, 2, 3, 7, 8]
834SIERDQYKSEVELLEubiquitination[2]
844VELLEMEKSQIRSQCubiquitination[1, 2, 9]
862KTEVEQLKSTNQQTAubiquitination[2, 9]
891HMDGESLKLRSLRVNubiquitination[1, 2, 3, 8, 9, 10]
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] 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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] 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]
 [9] 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]
 [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
 ZN_FING 404 454 CW-type.
 MOD_RES 503 503 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 939 AA 
Protein Sequence
MAAQPPRGIR LSALCPKFLH TNSTSHTWPF SAVAELIDNA YDPDVNAKQI WIDKTVINDH 60
ICLTFTDNGN GMTSDKLHKM LSFGFSDKVT MNGHVPVGLY GNGFKSGSMR LGKDAIVFTK 120
NGESMSVGLL SQTYLEVIKA EHVVVPIVAF NKHRQMINLA ESKASLAAIL EHSLFSTEQK 180
LLAELDAIIG KKGTRIIIWN LRSYKNATEF DFEKDKYDIR IPEDLDEITG KKGYKKQERM 240
DQIAPESDYS LRAYCSILYL KPRMQIILRG QKVKTQLVSK SLAYIERDVY RPKFLSKTVR 300
ITFGFNCRNK DHYGIMMYHR NRLIKAYEKV GCQLRANNMG VGVVGIIECN FLKPTHNKQD 360
FDYTNEYRLT ITALGEKLND YWNEMKVKKN TEYPLNLPVE DIQKRPDQTW VQCDACLKWR 420
KLPDGMDQLP EKWYCSNNPD PQFRNCEVPE EPEDEDLVHP TYEKTYKKTN KEKFRIRQPE 480
MIPRINAELL FRPTALSTPS FSSPKESVPR RHLSEGTNSY ATRLLNNHQV PPQSEPESNS 540
LKRRLSTRSS ILNAKNRRLS SQFENSVYKG DDDDEDVIIL EENSTPKPAV DHDIDMKSEQ 600
SHVEQGGVQV EFVGDSEPCG QTGSTSTSSS RCDQGNTAAT QTEVPSLVVK KEETVEDEID 660
VRNDAVILPS CVEAEAKIHE TQETTDKSAD DAGCQLQELR NQLLLVTEEK ENYKRQCHMF 720
TDQIKVLQQR ILEMNDKYVK KETCHQSTET DAVFLLESIN GKSESPDHMV SQYQQALEEI 780
ERLKKQCSAL QHVKAECSQC SNNESKSEMD EMAVQLDDVF RQLDKCSIER DQYKSEVELL 840
EMEKSQIRSQ CEELKTEVEQ LKSTNQQTAT DVSTSSNIEE SVNHMDGESL KLRSLRVNVG 900
QLLAMIVPDL DLQQVNYDVD VVDEILGQVV EQMSEISST 939 
Gene Ontology
 GO:0016235; C:aggresome; IDA:HPA.
 GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
 GO:0016605; C:PML body; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007569; P:cell aging; IDA:MGI.
 GO:0051457; P:maintenance of protein location in nucleus; IDA:MGI.
 GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0050821; P:protein stabilization; IDA:MGI. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR011124; Znf_CW. 
Pfam
 PF07496; zf-CW 
SMART
  
PROSITE
 PS51050; ZF_CW 
PRINTS