Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Zinc finger CCHC domain-containing protein 8  

UniProtKB / Swiss-Prot ID :  ZCHC8_HUMAN

Gene Name (Synonyms) : 
ZCCHC8  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  May be involved in pre-mRNA splicing. 

Protein Sequence MAAEVYFGDLELFEPFDHPEESIPKPVHTRFKDDDGDEEDENGVGDAELRERLRQCEETIEQLRAENQEL...
Predicted Secondary Structure CCCCCCCCHHHHHHHCCCCCCCCCCCEEEEECCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
672P -> A (in dbSNP:rs1063155). VAR_034585
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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
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
2N-acetylalanine.---MAAEVY
---CCCCCC
16.60UniProtKB
Link-
88PhosphothreonineLVNDTKLDG
EECCCCCCC
28.44HPRD
Link-
88PhosphothreonineLVNDTKLDG
EECCCCCCC
28.44Phosphositeplus
Link-
252PhosphoserineAARISEKRK
HHHHHHHHH
31.35HPRD
Link-
252PhosphoserineAARISEKRK
HHHHHHHHH
31.35Phosphositeplus
Link-
342PhosphothreonineGKDGTDGET
CCCCCCCCC
51.47Phosphositeplus
Link-
363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YDLSKLVNY
EEHHHHHHC
64.85Phosphositeplus
Link-
420PhosphoserineNKRSSSHSS
CCCCCCCCC
35.78SysPTM
Link-
424PhosphoserineSSHSSPGSP
CCCCCCCCC
28.05HPRD
Link-
424PhosphoserineSSHSSPGSP
CCCCCCCCC
28.05Phosphositeplus
Link-
427PhosphoserineSSPGSPKKQ
CCCCCCCCC
36.61Phosphositeplus
Link-
479PhosphothreonineLPRGTPPPV
CCCCCCCCC
33.62HPRD
Link-
479PhosphothreonineLPRGTPPPV
CCCCCCCCC
33.62PhosphoELM
Link-
479PhosphothreonineLPRGTPPPV
CCCCCCCCC
33.62Phosphositeplus
Link-
479PhosphothreonineLPRGTPPPV
CCCCCCCCC
33.62SysPTM
Link-
479Phosphothreonine.LPRGTPPPV
CCCCCCCCC
33.62UniProtKB
Link-
485PhosphothreoninePPVFTPPLP
CCCCCCCCC
25.00HPRD
Link-
485PhosphothreoninePPVFTPPLP
CCCCCCCCC
25.00PhosphoELM
Link-
485PhosphothreoninePPVFTPPLP
CCCCCCCCC
25.00Phosphositeplus
Link-
485PhosphothreoninePPVFTPPLP
CCCCCCCCC
25.00SysPTM
Link-
485Phosphothreonine.PPVFTPPLP
CCCCCCCCC
25.00UniProtKB
Link-
492PhosphothreonineLPKGTPPLT
CCCCCCCCC
28.05HPRD
Link-
492PhosphothreonineLPKGTPPLT
CCCCCCCCC
28.05PhosphoELM
Link-
492PhosphothreonineLPKGTPPLT
CCCCCCCCC
28.05Phosphositeplus
Link-
492PhosphothreonineLPKGTPPLT
CCCCCCCCC
28.05SysPTM
Link-
492Phosphothreonine.LPKGTPPLT
CCCCCCCCC
28.05UniProtKB
Link-
496PhosphothreonineTPPLTPSDS
CCCCCCCCC
26.90HPRD
Link-
496PhosphothreonineTPPLTPSDS
CCCCCCCCC
26.90PhosphoELM
Link-
496PhosphothreonineTPPLTPSDS
CCCCCCCCC
26.90Phosphositeplus
Link-
496PhosphothreonineTPPLTPSDS
CCCCCCCCC
26.90SysPTM
Link-
496Phosphothreonine.TPPLTPSDS
CCCCCCCCC
26.90UniProtKB
Link-
498PhosphoserinePLTPSDSPQ
CCCCCCCCC
45.55HPRD
Link-
498PhosphoserinePLTPSDSPQ
CCCCCCCCC
45.55Phosphositeplus
Link-
500PhosphoserineTPSDSPQTR
CCCCCCCCC
24.20HPRD
Link-
500PhosphoserineTPSDSPQTR
CCCCCCCCC
24.20PhosphoELM
Link-
500PhosphoserineTPSDSPQTR
CCCCCCCCC
24.20Phosphositeplus
Link-
500PhosphoserineTPSDSPQTR
CCCCCCCCC
24.20SysPTM
Link-
500Phosphoserine.TPSDSPQTR
CCCCCCCCC
24.20UniProtKB
Link-
597PhosphoserineAGHASSPDS
CCCCCCCCC
36.41HPRD
Link-
597PhosphoserineAGHASSPDS
CCCCCCCCC
36.41PhosphoELM
Link-
597Phosphoserine.AGHASSPDS
CCCCCCCCC
36.41UniProtKB
Link-
598PhosphoserineGHASSPDSE
CCCCCCCCC
33.25HPRD
Link-
598PhosphoserineGHASSPDSE
CCCCCCCCC
33.25PhosphoELM
Link-
598PhosphoserineGHASSPDSE
CCCCCCCCC
33.25Phosphositeplus
Link-
598PhosphoserineGHASSPDSE
CCCCCCCCC
33.25SysPTM
Link-
598Phosphoserine.GHASSPDSE
CCCCCCCCC
33.25UniProtKB
Link-
601PhosphoserineSSPDSEVTS
CCCCCCCCC
37.03HPRD
Link-
601PhosphoserineSSPDSEVTS
CCCCCCCCC
37.03Phosphositeplus
Link-
601PhosphoserineSSPDSEVTS
CCCCCCCCC
37.03SysPTM
Link-
640PhosphoserineSNGGSQKLF
CCCCCCCCC
26.07HPRD
Link-
640PhosphoserineSNGGSQKLF
CCCCCCCCC
26.07PhosphoELM
Link-
640PhosphoserineSNGGSQKLF
CCCCCCCCC
26.07Phosphositeplus
Link-
640Phosphoserine.SNGGSQKLF
CCCCCCCCC
26.07UniProtKB
Link-
648PhosphothreonineFPADTSPST
CCCCCCCCC
44.64HPRD
Link-
648PhosphothreonineFPADTSPST
CCCCCCCCC
44.64Phosphositeplus
Link-
649PhosphoserinePADTSPSTA
CCCCCCCCC
19.87HPRD
Link-
649PhosphoserinePADTSPSTA
CCCCCCCCC
19.87Phosphositeplus
Link-
649PhosphoserinePADTSPSTA
CCCCCCCCC
19.87SysPTM
Link-
649Phosphoserine.PADTSPSTA
CCCCCCCCC
19.87UniProtKB
Link-
652PhosphothreonineTSPSTATKI
CCCCCCCCC
41.55Phosphositeplus
Link-
652PhosphothreonineTSPSTATKI
CCCCCCCCC
41.55SysPTM
Link-
658PhosphoserineTKIHSPIPD
CCCCCCCCC
28.18HPRD
Link-
658PhosphoserineTKIHSPIPD
CCCCCCCCC
28.18PhosphoELM
Link-
658PhosphoserineTKIHSPIPD
CCCCCCCCC
28.18Phosphositeplus
Link-
658Phosphoserine.TKIHSPIPD
CCCCCCCCC
28.18UniProtKB
Link-
685PhosphotyrosineSTGMYLRIR
HCCHHEEEH
8.32Phosphositeplus
Link-
695PhosphoserineLLKNSPRNQ
HHHCCCHHH
24.53HPRD
Link-
695PhosphoserineLLKNSPRNQ
HHHCCCHHH
24.53Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PR40A_HUMANphysical interactionMINT-61861MINT15231748
PR40A_HUMANphysical interactionMINT-61872MINT15231748
PR40A_HUMANyeast 2-hybridHPRD:11698HPRD15231748
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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
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-479; SER-597; SER-598 AND SER-649, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-479; SER-597; SER-598 AND SER-649, AND MASSSPECTROMETRY.
"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 THR-479; SER-649 ANDSER-658, AND MASS 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 THR-479, AND MASSSPECTROMETRY.
"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 THR-479; THR-485; THR-492;THR-496 AND SER-500, AND MASS 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-640, 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 THR-485, AND MASSSPECTROMETRY.
"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 THR-479; THR-485; SER-598AND SER-658, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures