Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  MORC family CW-type zinc finger protein 2  

UniProtKB / Swiss-Prot ID :  MORC2_HUMAN

Gene Name (Synonyms) : 
MORC2, KIAA0852, ZCWCC1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm, cytosol. Note=Mainly located in the nucleus. 

Protein Function :  May act as a transcriptional repressor. Down-regulates CA9 expression. 

Protein Sequence MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDG...
Predicted Secondary Structure CCCCCCCHHHHHHCCHHHHHCCCCCHHHHHHHHHHHHHCCCCCCCCEEEEEEEECHHHCCCCEEEEEECC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GNGLKSGSM
CCCEEEEEE
54.92Phosphositeplus
Link-
602PhosphoserineTTRPSTEEP
CCCCCCCCC
45.20Phosphositeplus
Link-
603PhosphothreonineTRPSTEEPV
CCCCCCCCC
47.23Phosphositeplus
Link-
615PhosphoserineQRPRSPPLP
CCCCCCCCC
33.29PhosphoELM
Link-
615PhosphoserineQRPRSPPLP
CCCCCCCCC
33.29Phosphositeplus
Link-
615PhosphoserineQRPRSPPLP
CCCCCCCCC
33.29SysPTM
Link-
615Phosphoserine.QRPRSPPLP
CCCCCCCCC
33.29UniProtKB
Link-
663PhosphoserineREEASTSRL
CCCCCCCCC
30.14HPRD
Link-
696PhosphoserineVQQLSPSLL
CCCCCCCCC
14.22PhosphoELM
Link-
696PhosphoserineVQQLSPSLL
CCCCCCCCC
14.22Phosphositeplus
Link-
696PhosphoserineVQQLSPSLL
CCCCCCCCC
14.22SysPTM
Link-
696Phosphoserine.VQQLSPSLL
CCCCCCCCC
14.22UniProtKB
Link-
698PhosphoserineQLSPSLLPN
CCCCCCCCC
38.88Phosphositeplus
Link-
703PhosphoserineLLPNSKSPR
CCCCCCCCC
32.35PhosphoELM
Link-
705PhosphoserinePNSKSPREV
CCCCCCCCC
29.07PhosphoELM
Link-
705PhosphoserinePNSKSPREV
CCCCCCCCC
29.07Phosphositeplus
Link-
705PhosphoserinePNSKSPREV
CCCCCCCCC
29.07SysPTM
Link-
705Phosphoserine.PNSKSPREV
CCCCCCCCC
29.07UniProtKB
Link-
711PhosphoserineREVPSPKVI
CCCCCCCCC
42.39HPRD
Link-
717PhosphothreonineKVIKTPVVK
CCCCCCCCC
15.36PhosphoELM
Link-
717PhosphothreonineKVIKTPVVK
CCCCCCCCC
15.36Phosphositeplus
Link-
717PhosphothreonineKVIKTPVVK
CCCCCCCCC
15.36SysPTM
Link-
717Phosphothreonine.KVIKTPVVK
CCCCCCCCC
15.36UniProtKB
Link-
723PhosphothreonineVVKKTESPI
CCCCCCCCC
35.66Phosphositeplus
Link-
723PhosphothreonineVVKKTESPI
CCCCCCCCC
35.66SysPTM
Link-
725PhosphoserineKKTESPIKL
CCCCCCCCC
36.84PhosphoELM
Link-
725PhosphoserineKKTESPIKL
CCCCCCCCC
36.84Phosphositeplus
Link-
725PhosphoserineKKTESPIKL
CCCCCCCCC
36.84SysPTM
Link-
725Phosphoserine.KKTESPIKL
CCCCCCCCC
36.84UniProtKB
Link-
730PhosphoserinePIKLSPATP
CCCCCCCCC
13.90PhosphoELM
Link-
730PhosphoserinePIKLSPATP
CCCCCCCCC
13.90Phosphositeplus
Link-
730PhosphoserinePIKLSPATP
CCCCCCCCC
13.90SysPTM
Link-
730Phosphoserine.PIKLSPATP
CCCCCCCCC
13.90UniProtKB
Link-
733PhosphothreonineLSPATPSRK
CCCCCCCCC
25.77PhosphoELM
Link-
733PhosphothreonineLSPATPSRK
CCCCCCCCC
25.77Phosphositeplus
Link-
733PhosphothreonineLSPATPSRK
CCCCCCCCC
25.77SysPTM
Link-
733Phosphothreonine.LSPATPSRK
CCCCCCCCC
25.77UniProtKB
Link-
735PhosphoserinePATPSRKRS
CCCCCCCCC
46.19PhosphoELM
Link-
735PhosphoserinePATPSRKRS
CCCCCCCCC
46.19Phosphositeplus
Link-
735Phosphoserine.PATPSRKRS
CCCCCCCCC
46.19UniProtKB
Link-
739PhosphoserineSRKRSVAVS
CCCCCCCCC
19.91PhosphoELM
Link-
739PhosphoserineSRKRSVAVS
CCCCCCCCC
19.91Phosphositeplus
Link-
739PhosphoserineSRKRSVAVS
CCCCCCCCC
19.91SysPTM
Link-
739Phosphoserine.SRKRSVAVS
CCCCCCCCC
19.91UniProtKB
Link-
743PhosphoserineSVAVSDEEE
CCCCCCCCC
29.57PhosphoELM
Link-
743PhosphoserineSVAVSDEEE
CCCCCCCCC
29.57Phosphositeplus
Link-
743PhosphoserineSVAVSDEEE
CCCCCCCCC
29.57SysPTM
Link-
743Phosphoserine.SVAVSDEEE
CCCCCCCCC
29.57UniProtKB
Link-
767N6-acetyllysineRFVVKEEKK
CCCCCCCCC
55.65Phosphositeplus
Link-
767N6-acetyllysine.RFVVKEEKK
CCCCCCCCC
55.65UniProtKB
Link-
773PhosphoserineEKKDSNELS
CCCCCCCCC
40.87PhosphoELM
Link-
773PhosphoserineEKKDSNELS
CCCCCCCCC
40.87Phosphositeplus
Link-
777PhosphoserineSNELSDSAG
CCCCCCCCC
24.28PhosphoELM
Link-
777PhosphoserineSNELSDSAG
CCCCCCCCC
24.28Phosphositeplus
Link-
777PhosphoserineSNELSDSAG
CCCCCCCCC
24.28SysPTM
Link-
777Phosphoserine.SNELSDSAG
CCCCCCCCC
24.28UniProtKB
Link-
779PhosphoserineELSDSAGEE
CCCCCCCCC
34.49PhosphoELM
Link-
779PhosphoserineELSDSAGEE
CCCCCCCCC
34.49Phosphositeplus
Link-
779PhosphoserineELSDSAGEE
CCCCCCCCC
34.49SysPTM
Link-
779Phosphoserine.ELSDSAGEE
CCCCCCCCC
34.49UniProtKB
Link-
827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RWKVKFDYV
CCCCCCCCC
28.88Phosphositeplus
Link-
836PhosphothreoninePTDTTPRDR
CCCCCCCCC
21.09PhosphoELM
Link-
856PhosphoserineMKPPSPEHQ
CCCCCCCCC
51.99Phosphositeplus
Link-
861PhosphoserinePEHQSLDTQ
CCCCCCCCC
30.07Phosphositeplus
Link-
864PhosphothreonineQSLDTQQEG
CCCCCCCCC
37.13PhosphoELM
Link-
864PhosphothreonineQSLDTQQEG
CCCCCCCCC
37.13Phosphositeplus
Link-
932Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PISKKQLSA
CCCHHHHHC
50.08Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-767, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; SER-725; SER-730AND SER-735, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; SER-696; SER-705;THR-717; SER-725; SER-730; THR-733; SER-739; SER-743; SER-777 ANDSER-779, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND SER-743, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739 AND SER-743, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND SER-743, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; SER-777 ANDSER-779, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures