Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Zinc finger C3H1 domain-containing protein  

UniProtKB / Swiss-Prot ID :  ZC3H1_HUMAN

Gene Name (Synonyms) : 
ZFC3H1, CCDC131, KIAA0546, PSRC2  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MATADTPAPASSGLSPKEEGELEDGEISDDDNNSQIRSRSSSSSSGGGLLPYPRRRPPHSARGGGSGGGG...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
1006E -> K (in dbSNP:rs1011332). VAR_032070
1807K -> R (in dbSNP:rs11541286). VAR_032071
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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
Protein Variant
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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
15PhosphoserineSSGLSPKEE
37.13HPRD
Link-
15PhosphoserineSSGLSPKEE
37.13Phosphositeplus
Link-
28PhosphoserineDGEISDDDN
30.59HPRD
Link-
28PhosphoserineDGEISDDDN
30.59PhosphoELM
Link-
28PhosphoserineDGEISDDDN
30.59Phosphositeplus
Link-
28PhosphoserineDGEISDDDN
30.59SysPTM
Link-
28Phosphoserine.DGEISDDDN
30.59UniProtKB
Link-
34PhosphoserineDDNNSQIRS
32.99HPRD
Link-
34PhosphoserineDDNNSQIRS
32.99Phosphositeplus
Link-
34Phosphoserine.DDNNSQIRS
32.99UniProtKB
Link-
40PhosphoserineIRSRSSSSS
35.50HPRD
Link-
41PhosphoserineRSRSSSSSS
32.88HPRD
Link-
42PhosphoserineSRSSSSSSG
35.17HPRD
Link-
43PhosphoserineRSSSSSSGG
30.39HPRD
Link-
44PhosphoserineSSSSSSGGG
34.64HPRD
Link-
127PhosphoserineSLSESSPRP
42.12HPRD
Link-
127PhosphoserineSLSESSPRP
42.12PhosphoELM
Link-
128PhosphoserineLSESSPRPS
22.37HPRD
Link-
128PhosphoserineLSESSPRPS
22.37PhosphoELM
Link-
352PhosphoserineTRRISTSDI
21.76HPRD
Link-
352PhosphoserineTRRISTSDI
21.76PhosphoELM
Link-
352PhosphoserineTRRISTSDI
21.76Phosphositeplus
Link-
352PhosphoserineTRRISTSDI
21.76SysPTM
Link-
352Phosphoserine.TRRISTSDI
21.76UniProtKB
Link-
655PhosphoserineSDPPSPPVL
47.42Phosphositeplus
Link-
714PhosphoserineTLNDSDDSE
42.09HPRD
Link-
714PhosphoserineTLNDSDDSE
42.09PhosphoELM
Link-
714PhosphoserineTLNDSDDSE
42.09Phosphositeplus
Link-
714PhosphoserineTLNDSDDSE
42.09SysPTM
Link-
714Phosphoserine.TLNDSDDSE
42.09UniProtKB
Link-
717PhosphoserineDSDDSESDG
43.95HPRD
Link-
717PhosphoserineDSDDSESDG
43.95PhosphoELM
Link-
717PhosphoserineDSDDSESDG
43.95Phosphositeplus
Link-
717PhosphoserineDSDDSESDG
43.95SysPTM
Link-
717Phosphoserine.DSDDSESDG
43.95UniProtKB
Link-
719PhosphoserineDDSESDGEA
55.67HPRD
Link-
719PhosphoserineDDSESDGEA
55.67PhosphoELM
Link-
719PhosphoserineDDSESDGEA
55.67Phosphositeplus
Link-
719PhosphoserineDDSESDGEA
55.67SysPTM
Link-
719Phosphoserine.DDSESDGEA
55.67UniProtKB
Link-
724PhosphoserineDGEASKSTN
23.88HPRD
Link-
724PhosphoserineDGEASKSTN
23.88PhosphoELM
Link-
766PhosphothreonineDPLRTPEAL
32.91HPRD
Link-
766PhosphothreonineDPLRTPEAL
32.91PhosphoELM
Link-
766PhosphothreonineDPLRTPEAL
32.91Phosphositeplus
Link-
766PhosphothreonineDPLRTPEAL
32.91SysPTM
Link-
766Phosphothreonine.DPLRTPEAL
32.91UniProtKB
Link-
778PhosphotyrosineKKIEYRLLK
15.27Phosphositeplus
Link-
801PhosphothreonineDQLKTSSSS
42.29HPRD
Link-
801PhosphothreonineDQLKTSSSS
42.29PhosphoELM
Link-
803PhosphoserineLKTSSSSPA
39.81HPRD
Link-
803PhosphoserineLKTSSSSPA
39.81PhosphoELM
Link-
804PhosphoserineKTSSSSPAN
39.86HPRD
Link-
804PhosphoserineKTSSSSPAN
39.86PhosphoELM
Link-
805PhosphoserineTSSSSPANS
29.94HPRD
Link-
805PhosphoserineTSSSSPANS
29.94PhosphoELM
Link-
805PhosphoserineTSSSSPANS
29.94Phosphositeplus
Link-
809PhosphoserineSPANSDVEI
45.18HPRD
Link-
809PhosphoserineSPANSDVEI
45.18PhosphoELM
Link-
809PhosphoserineSPANSDVEI
45.18Phosphositeplus
Link-
809PhosphoserineSPANSDVEI
45.18SysPTM
Link-
809Phosphoserine.SPANSDVEI
45.18UniProtKB
Link-
880Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QATEKILNV
48.41Phosphositeplus
Link-
948PhosphoserineMRLDSSPVS
40.93HPRD
Link-
948PhosphoserineMRLDSSPVS
40.93Phosphositeplus
Link-
948PhosphoserineMRLDSSPVS
40.93SysPTM
Link-
949PhosphoserineRLDSSPVSS
29.05HPRD
Link-
949PhosphoserineRLDSSPVSS
29.05PhosphoELM
Link-
949PhosphoserineRLDSSPVSS
29.05Phosphositeplus
Link-
949PhosphoserineRLDSSPVSS
29.05SysPTM
Link-
949Phosphoserine.RLDSSPVSS
29.05UniProtKB
Link-
952PhosphoserineSSPVSSPRK
37.70HPRD
Link-
952PhosphoserineSSPVSSPRK
37.70Phosphositeplus
Link-
953PhosphoserineSPVSSPRKH
29.02HPRD
Link-
953PhosphoserineSPVSSPRKH
29.02PhosphoELM
Link-
953PhosphoserineSPVSSPRKH
29.02Phosphositeplus
Link-
953PhosphoserineSPVSSPRKH
29.02SysPTM
Link-
953Phosphoserine.SPVSSPRKH
29.02UniProtKB
Link-
974PhosphotyrosineQKLEYEYAL
25.36Phosphositeplus
Link-
976PhosphotyrosineLEYEYALKI
19.14Phosphositeplus
Link-
998PhosphoserineQQNISPVVE
21.13HPRD
Link-
998PhosphoserineQQNISPVVE
21.13PhosphoELM
Link-
998PhosphoserineQQNISPVVE
21.13Phosphositeplus
Link-
998PhosphoserineQQNISPVVE
21.13SysPTM
Link-
998Phosphoserine.QQNISPVVE
21.13UniProtKB
Link-
1046PhosphoserineERRRSFLES
32.16HPRD
Link-
1046PhosphoserineERRRSFLES
32.16PhosphoELM
Link-
1046PhosphoserineERRRSFLES
32.16Phosphositeplus
Link-
1046PhosphoserineERRRSFLES
32.16SysPTM
Link-
1046Phosphoserine.ERRRSFLES
32.16UniProtKB
Link-
1244PhosphotyrosineSAEKYVEKL
12.83Phosphositeplus
Link-
1298PhosphoserineRKPISDNSF
38.99HPRD
Link-
1298PhosphoserineRKPISDNSF
38.99PhosphoELM
Link-
1298PhosphoserineRKPISDNSF
38.99Phosphositeplus
Link-
1301PhosphoserineISDNSFSSD
31.34HPRD
Link-
1301PhosphoserineISDNSFSSD
31.34PhosphoELM
Link-
1301PhosphoserineISDNSFSSD
31.34Phosphositeplus
Link-
1303PhosphoserineDNSFSSDEE
36.38HPRD
Link-
1303PhosphoserineDNSFSSDEE
36.38PhosphoELM
Link-
1303PhosphoserineDNSFSSDEE
36.38Phosphositeplus
Link-
1303PhosphoserineDNSFSSDEE
36.38SysPTM
Link-
1303Phosphoserine.DNSFSSDEE
36.38UniProtKB
Link-
1304PhosphoserineNSFSSDEEQ
47.21HPRD
Link-
1304PhosphoserineNSFSSDEEQ
47.21PhosphoELM
Link-
1304PhosphoserineNSFSSDEEQ
47.21Phosphositeplus
Link-
1304PhosphoserineNSFSSDEEQ
47.21SysPTM
Link-
1304Phosphoserine.NSFSSDEEQ
47.21UniProtKB
Link-
1309PhosphoserineDEEQSTGPI
38.31SysPTM
Link-
1310PhosphothreonineEEQSTGPIK
46.82SysPTM
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
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-949 AND SER-998, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-34, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-953, ANDMASS 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-28; SER-352; SER-714;SER-717; SER-719; THR-766; SER-809; SER-949; SER-953; SER-998;SER-1046; SER-1303 AND SER-1304, AND MASS 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-809 AND SER-949, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures