ZN800_HUMAN - dbPTM
ZN800_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN800_HUMAN
UniProt AC Q2TB10
Protein Name Zinc finger protein 800
Gene Name ZNF800
Organism Homo sapiens (Human).
Sequence Length 664
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MPLRDKYCQTDHHHHGCCEPVYILEPGDPPLLQQPLQTSKSGIQQIIECFRSGTKQLKHILLKDVDTIFECKLCRSLFRGLPNLITHKKFYCPPSLQMDDNLPDVNDKQSQAINDLLEAIYPSVDKREYIIKLEPIETNQNAVFQYISRTDNPIEVTESSSTPEQTEVQIQETSTEQSKTVPVTDTEVETVEPPPVEIVTDEVAPTSDEQPQESQADLETSDNSDFGHQLICCLCRKEFNSRRGVRRHIRKVHKKKMEELKKYIETRKNPNQSSKGRSKNVLVPLSRSCPVCCKSFATKANVRRHFDEVHRGLRRDSITPDIATKPGQPLFLDSISPKKSFKTRKQKSSSKAEYNLTACKCLLCKRKYSSQIMLKRHMQIVHKITLSGTNSKREKGPNNTANSSEIKVKVEPADSVESSPPSITHSPQNELKGTNHSNEKKNTPAAQKNKVKQDSESPKSTSPSAAGGQQKTRKPKLSAGFDFKQLYCKLCKRQFTSKQNLTKHIELHTDGNNIYVKFYKCPLCTYETRRKRDVIRHITVVHKKSSRYLGKITASLEIRAIKKPIDFVLNKVAKRGPSRDEAKHSDSKHDGTSNSPSKKYEVADVGIEVKVTKNFSLHRCNKCGKAFAKKTYLEHHKKTHKANASNSPEGNKTKGRSTRSKALV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
63AcetylationQLKHILLKDVDTIFE
HHHHHHHCCCCHHHH		52.8726051181
91PhosphorylationLITHKKFYCPPSLQM
CHHCCCCCCCCCCCC		16.9627642862
95PhosphorylationKKFYCPPSLQMDDNL
CCCCCCCCCCCCCCC		19.17-
126UbiquitinationAIYPSVDKREYIIKL
HHCCCCCCCCEEEEE		45.0029967540
132SumoylationDKREYIIKLEPIETN
CCCCEEEEEEECCCC		36.92-
132SumoylationDKREYIIKLEPIETN
CCCCEEEEEEECCCC		36.9228112733
150PhosphorylationVFQYISRTDNPIEVT
HHHHHHCCCCCEEEE		33.0828450419
157PhosphorylationTDNPIEVTESSSTPE
CCCCEEEECCCCCCC		19.8428450419
159PhosphorylationNPIEVTESSSTPEQT
CCEEEECCCCCCCCE		21.8930576142
160PhosphorylationPIEVTESSSTPEQTE
CEEEECCCCCCCCEE		31.8130576142
161PhosphorylationIEVTESSSTPEQTEV
EEEECCCCCCCCEEE		58.2125627689
162PhosphorylationEVTESSSTPEQTEVQ
EEECCCCCCCCEEEE		32.5628450419
166PhosphorylationSSSTPEQTEVQIQET
CCCCCCCEEEEEEEC		36.1428450419
173PhosphorylationTEVQIQETSTEQSKT
EEEEEEECCCCCCCE		25.2730576142
174PhosphorylationEVQIQETSTEQSKTV
EEEEEECCCCCCCEE		29.2425627689
175PhosphorylationVQIQETSTEQSKTVP
EEEEECCCCCCCEEC		45.5230576142
279SumoylationQSSKGRSKNVLVPLS
CCCCCCCCCEEEECC		50.1128112733
317PhosphorylationHRGLRRDSITPDIAT
HHHHCCCCCCCCCCC		26.9229255136
319PhosphorylationGLRRDSITPDIATKP
HHCCCCCCCCCCCCC		20.8929255136
324PhosphorylationSITPDIATKPGQPLF
CCCCCCCCCCCCCCC		37.8029255136
334PhosphorylationGQPLFLDSISPKKSF
CCCCCCCCCCCCCCC		27.4129255136
336PhosphorylationPLFLDSISPKKSFKT
CCCCCCCCCCCCCCC		34.3229255136
350PhosphorylationTRKQKSSSKAEYNLT
CCCCCCCCHHHHHHH		42.8722817900
368PhosphorylationCLLCKRKYSSQIMLK
HHHCCCCCCHHHHHH		20.00-
369PhosphorylationLLCKRKYSSQIMLKR
HHCCCCCCHHHHHHH		20.8525159151
385PhosphorylationMQIVHKITLSGTNSK
HHEEEEEECCCCCCC		21.4818452278
387PhosphorylationIVHKITLSGTNSKRE
EEEEEECCCCCCCCC		34.6225159151
389PhosphorylationHKITLSGTNSKREKG
EEEECCCCCCCCCCC		32.7019691289
391PhosphorylationITLSGTNSKREKGPN
EECCCCCCCCCCCCC		32.6924732914
392SumoylationTLSGTNSKREKGPNN
ECCCCCCCCCCCCCC		67.6528112733
403PhosphorylationGPNNTANSSEIKVKV
CCCCCCCCCCEEEEE		27.2125159151
404PhosphorylationPNNTANSSEIKVKVE
CCCCCCCCCEEEEEE		43.0525627689
408UbiquitinationANSSEIKVKVEPADS
CCCCCEEEEEECCCC		11.7425015289
409SumoylationNSSEIKVKVEPADSV
CCCCEEEEEECCCCC		35.5625114211
409UbiquitinationNSSEIKVKVEPADSV
CCCCEEEEEECCCCC		35.5625015289
409AcetylationNSSEIKVKVEPADSV
CCCCEEEEEECCCCC		35.5626051181
409SumoylationNSSEIKVKVEPADSV
CCCCEEEEEECCCCC		35.56-
415PhosphorylationVKVEPADSVESSPPS
EEEECCCCCCCCCCC		29.8629255136
416UbiquitinationKVEPADSVESSPPSI
EEECCCCCCCCCCCC		9.4725015289
418PhosphorylationEPADSVESSPPSITH
ECCCCCCCCCCCCCC		46.0930266825
418UbiquitinationEPADSVESSPPSITH
ECCCCCCCCCCCCCC		46.0925015289
419PhosphorylationPADSVESSPPSITHS
CCCCCCCCCCCCCCC		27.5930266825
422PhosphorylationSVESSPPSITHSPQN
CCCCCCCCCCCCCCC		43.4323401153
424PhosphorylationESSPPSITHSPQNEL
CCCCCCCCCCCCCCC		22.1923401153
426PhosphorylationSPPSITHSPQNELKG
CCCCCCCCCCCCCCC		21.3823401153
434O-linked_GlycosylationPQNELKGTNHSNEKK
CCCCCCCCCCCCCCC		28.3331492838
440UbiquitinationGTNHSNEKKNTPAAQ
CCCCCCCCCCCHHHH		56.4225015289
441UbiquitinationTNHSNEKKNTPAAQK
CCCCCCCCCCHHHHH		60.9325015289
443PhosphorylationHSNEKKNTPAAQKNK
CCCCCCCCHHHHHHH		24.1628985074
448UbiquitinationKNTPAAQKNKVKQDS
CCCHHHHHHHCCCCC		54.7525015289
450UbiquitinationTPAAQKNKVKQDSES
CHHHHHHHCCCCCCC		58.8225015289
455PhosphorylationKNKVKQDSESPKSTS
HHHCCCCCCCCCCCC		37.1623401153
457PhosphorylationKVKQDSESPKSTSPS
HCCCCCCCCCCCCCC		41.3922167270
460PhosphorylationQDSESPKSTSPSAAG
CCCCCCCCCCCCCCC		37.1923401153
461PhosphorylationDSESPKSTSPSAAGG
CCCCCCCCCCCCCCC		51.2722167270
462PhosphorylationSESPKSTSPSAAGGQ
CCCCCCCCCCCCCCC		24.7722167270
464PhosphorylationSPKSTSPSAAGGQQK
CCCCCCCCCCCCCCC		30.4422167270
476SumoylationQQKTRKPKLSAGFDF
CCCCCCCCCCCCCCH		59.1028112733
478PhosphorylationKTRKPKLSAGFDFKQ
CCCCCCCCCCCCHHH		32.2624732914
509PhosphorylationTKHIELHTDGNNIYV
CCEEEEECCCCCEEE		59.2228555341
547MethylationVVHKKSSRYLGKITA
EEECCCCCCCCEEEE		37.4724411221
555PhosphorylationYLGKITASLEIRAIK
CCCEEEEEEEHHCCC		20.2024719451
585PhosphorylationSRDEAKHSDSKHDGT
CHHHHCCCCCCCCCC		42.7623312004
587PhosphorylationDEAKHSDSKHDGTSN
HHHCCCCCCCCCCCC		34.6030576142
592PhosphorylationSDSKHDGTSNSPSKK
CCCCCCCCCCCCCCC		30.6930576142
593PhosphorylationDSKHDGTSNSPSKKY
CCCCCCCCCCCCCCE		40.6230576142
595PhosphorylationKHDGTSNSPSKKYEV
CCCCCCCCCCCCEEE		30.2530576142
597PhosphorylationDGTSNSPSKKYEVAD
CCCCCCCCCCEEEEC		41.4220068231
599SumoylationTSNSPSKKYEVADVG
CCCCCCCCEEEECCC		51.4828112733
600PhosphorylationSNSPSKKYEVADVGI
CCCCCCCEEEECCCC		21.2624114839
632PhosphorylationKAFAKKTYLEHHKKT
HHHHHHHHHHHHHHH		20.97-
645PhosphorylationKTHKANASNSPEGNK
HHCCCCCCCCCCCCC		37.3328176443
647PhosphorylationHKANASNSPEGNKTK
CCCCCCCCCCCCCCC		23.1028176443
658PhosphorylationNKTKGRSTRSKALV-
CCCCCCCCCCCCCC-		37.29-
660PhosphorylationTKGRSTRSKALV---
CCCCCCCCCCCC---		23.51-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ZN800_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN800_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ZN800_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTA2_HUMANMTA2physical
28514442
MTA3_HUMANMTA3physical
28514442
MBD3_HUMANMBD3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN800_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASSSPECTROMETRY.
"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-336, 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 SER-317; THR-319; SER-334;SER-336; SER-455; SER-457 AND SER-462, AND MASS SPECTROMETRY.
"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-317; SER-336; SER-387;SER-403; SER-426; SER-462 AND SER-595, AND MASS SPECTROMETRY.

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