CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024043
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MORC family CW-type zinc finger protein 2 
Protein Synonyms/Alias
 Zinc finger CW-type coiled-coil domain protein 1 
Gene Name
 MORC2 
Gene Synonyms/Alias
 KIAA0852; ZCWCC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
105GQYGNGLKSGSMRIGubiquitination[1, 2]
113SGSMRIGKDFILFTKubiquitination[3]
234ETSPEGTKPERRSFRubiquitination[1]
767KRGRFVVKEEKKDSNacetylation[4, 5]
827HVVRWKVKFDYVPTDubiquitination[6, 7]
932PSFPISKKQLSAMNSubiquitination[6, 7, 8]
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] 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]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] 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]
 [6] 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]
 [7] 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]
 [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
Functional Description
 May act as a transcriptional repressor. Down-regulates CA9 expression. 
Sequence Annotation
 ZN_FING 490 544 CW-type.
 MOD_RES 615 615 Phosphoserine.
 MOD_RES 696 696 Phosphoserine.
 MOD_RES 705 705 Phosphoserine.
 MOD_RES 725 725 Phosphoserine.
 MOD_RES 730 730 Phosphoserine.
 MOD_RES 733 733 Phosphothreonine.
 MOD_RES 739 739 Phosphoserine.
 MOD_RES 743 743 Phosphoserine.
 MOD_RES 777 777 Phosphoserine.
 MOD_RES 779 779 Phosphoserine.
 MOD_RES 856 856 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1032 AA 
Protein Sequence
MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI YAERREDLRG 60
GFMLCFLDDG AGMDPSDAAS VIQFGKSAKR TPESTQIGQY GNGLKSGSMR IGKDFILFTK 120
KEDTMTCLFL SRTFHEEEGI DEVIVPLPTW NARTREPVTD NVEKFAIETE LIYKYSPFRT 180
EEEVMTQFMK IPGDSGTLVI IFNLKLMDNG EPELDIISNP RDIQMAETSP EGTKPERRSF 240
RAYAAVLYID PRMRIFIHGH KVQTKRLSCC LYKPRMYKYT SSRFKTRAEQ EVKKAEHVAR 300
IAEEKAREAE SKARTLEVRL GGDLTRDSRV MLRQVQNRAI TLRREADVKK RIKEAKQRAL 360
KEPKELNFVF GVNIEHRDLD GMFIYNCSRL IKMYEKVGPQ LEGGMACGGV VGVVDVPYLV 420
LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY WKDIAIAQRG IIKFWDEFGY LSANWNQPPS 480
SELRYKRRRA MEIPTTIQCD LCLKWRTLPF QLSSVEKDYP DTWVCSMNPD PEQDRCEASE 540
QKQKVPLGTF RKDMKTQEEK QKQLTEKIRQ QQEKLEALQK TTPIRSQADL KKLPLEVTTR 600
PSTEEPVRRP QRPRSPPLPA VIRNAPSRPP SLPTPRPASQ PRKAPVISST PKLPALAARE 660
EASTSRLLQP PEAPRKPANT LVKTASRPAP LVQQLSPSLL PNSKSPREVP SPKVIKTPVV 720
KKTESPIKLS PATPSRKRSV AVSDEEEVEE EAERRKERCK RGRFVVKEEK KDSNELSDSA 780
GEEDSADLKR AQKDKGLHVE VRVNREWYTG RVTAVEVGKH VVRWKVKFDY VPTDTTPRDR 840
WVEKGSEDVR LMKPPSPEHQ SLDTQQEGGE EEVGPVAQQA IAVAEPSTSE CLRIEPDTTA 900
LSTNHETIDL LVQILRNCLR YFLPPSFPIS KKQLSAMNSD ELISFPLKEY FKQYEVGLQN 960
LCNSYQSRAD SRAKASEESL RTSERKLRET EEKLQKLRTN IVALLQKVQE DIDINTDDEL 1020
DAYIEDLITK GD 1032 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR011124; Znf_CW. 
Pfam
 PF07496; zf-CW 
SMART
 SM00387; HATPase_c 
PROSITE
 PS51050; ZF_CW 
PRINTS