ZKSC1_HUMAN - dbPTM
ZKSC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZKSC1_HUMAN
UniProt AC P17029
Protein Name Zinc finger protein with KRAB and SCAN domains 1
Gene Name ZKSCAN1
Organism Homo sapiens (Human).
Sequence Length 563
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MMTAESREATGLSPQAAQEKDGIVIVKVEEEDEEDHMWGQDSTLQDTPPPDPEIFRQRFRRFCYQNTFGPREALSRLKELCHQWLRPEINTKEQILELLVLEQFLSILPKELQVWLQEYRPDSGEEAVTLLEDLELDLSGQQVPGQVHGPEMLARGMVPLDPVQESSSFDLHHEATQSHFKHSSRKPRLLQSRALPAAHIPAPPHEGSPRDQAMASALFTADSQAMVKIEDMAVSLILEEWGCQNLARRNLSRDNRQENYGSAFPQGGENRNENEESTSKAETSEDSASRGETTGRSQKEFGEKRDQEGKTGERQQKNPEEKTRKEKRDSGPAIGKDKKTITGERGPREKGKGLGRSFSLSSNFTTPEEVPTGTKSHRCDECGKCFTRSSSLIRHKIIHTGEKPYECSECGKAFSLNSNLVLHQRIHTGEKPHECNECGKAFSHSSNLILHQRIHSGEKPYECNECGKAFSQSSDLTKHQRIHTGEKPYECSECGKAFNRNSYLILHRRIHTREKPYKCTKCGKAFTRSSTLTLHHRIHARERASEYSPASLDAFGAFLKSCV
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
6Phosphorylation--MMTAESREATGLS
--CCCHHHHHHHCCC		32.72-
10PhosphorylationTAESREATGLSPQAA
CHHHHHHHCCCHHHH		33.6230266825
13PhosphorylationSREATGLSPQAAQEK
HHHHHCCCHHHHHHC		19.1329255136
20UbiquitinationSPQAAQEKDGIVIVK
CHHHHHHCCCEEEEE		49.53-
27SumoylationKDGIVIVKVEEEDEE
CCCEEEEECCCCCCC		32.5728112733
42PhosphorylationDHMWGQDSTLQDTPP
CCCCCCCCCCCCCCC		24.1127732954
43PhosphorylationHMWGQDSTLQDTPPP
CCCCCCCCCCCCCCC		36.4127732954
47PhosphorylationQDSTLQDTPPPDPEI
CCCCCCCCCCCCHHH		25.4130576142
166PhosphorylationPLDPVQESSSFDLHH
ECCCCCCCCCCCCCC		17.7528348404
167PhosphorylationLDPVQESSSFDLHHE
CCCCCCCCCCCCCCH		33.9828348404
168PhosphorylationDPVQESSSFDLHHEA
CCCCCCCCCCCCCHH		31.8728348404
178PhosphorylationLHHEATQSHFKHSSR
CCCHHHHHHHCCCCC		26.9128555341
181UbiquitinationEATQSHFKHSSRKPR
HHHHHHHCCCCCCCC		36.83-
181SumoylationEATQSHFKHSSRKPR
HHHHHHHCCCCCCCC		36.8328112733
184PhosphorylationQSHFKHSSRKPRLLQ
HHHHCCCCCCCCHHH		44.00-
208PhosphorylationPAPPHEGSPRDQAMA
CCCCCCCCHHHHHHH		17.4929255136
216PhosphorylationPRDQAMASALFTADS
HHHHHHHHHHHCCCC		16.6624247654
223PhosphorylationSALFTADSQAMVKIE
HHHHCCCCCCCHHHH		19.85-
228SumoylationADSQAMVKIEDMAVS
CCCCCCHHHHHHHHH		27.5628112733
252PhosphorylationNLARRNLSRDNRQEN
HHHHCCCCCCCCHHH		40.9327251275
262PhosphorylationNRQENYGSAFPQGGE
CCHHHCCCCCCCCCC		19.1727251275
279PhosphorylationNENEESTSKAETSED
CCCHHHCCCCCCCHH		38.8628555341
280SumoylationENEESTSKAETSEDS
CCHHHCCCCCCCHHH		50.7828112733
280UbiquitinationENEESTSKAETSEDS
CCHHHCCCCCCCHHH		50.7821906983
280SumoylationENEESTSKAETSEDS
CCHHHCCCCCCCHHH		50.78-
283PhosphorylationESTSKAETSEDSASR
HHCCCCCCCHHHHHC		42.1325850435
284PhosphorylationSTSKAETSEDSASRG
HCCCCCCCHHHHHCC		30.8025850435
287PhosphorylationKAETSEDSASRGETT
CCCCCHHHHHCCCCC		24.8829255136
289PhosphorylationETSEDSASRGETTGR
CCCHHHHHCCCCCCC		44.7829255136
293PhosphorylationDSASRGETTGRSQKE
HHHHCCCCCCCCHHH		37.0629255136
294PhosphorylationSASRGETTGRSQKEF
HHHCCCCCCCCHHHH		26.7129255136
299SumoylationETTGRSQKEFGEKRD
CCCCCCHHHHHHHHC		57.1528112733
304SumoylationSQKEFGEKRDQEGKT
CHHHHHHHHCCCCCC		62.7528112733
310AcetylationEKRDQEGKTGERQQK
HHHCCCCCCCHHHHC		53.2418586575
330PhosphorylationTRKEKRDSGPAIGKD
HHHHHHCCCCCCCCC		51.1930576142
336AcetylationDSGPAIGKDKKTITG
CCCCCCCCCCCCCCC		61.3325953088
339SumoylationPAIGKDKKTITGERG
CCCCCCCCCCCCCCC		56.1228112733
339SumoylationPAIGKDKKTITGERG
CCCCCCCCCCCCCCC		56.12-
357PhosphorylationKGKGLGRSFSLSSNF
CCCCCCCCEECCCCC		19.8625159151
359PhosphorylationKGLGRSFSLSSNFTT
CCCCCCEECCCCCCC		28.7025159151
361PhosphorylationLGRSFSLSSNFTTPE
CCCCEECCCCCCCCC		23.2628348404
362PhosphorylationGRSFSLSSNFTTPEE
CCCEECCCCCCCCCC		41.0528348404
365PhosphorylationFSLSSNFTTPEEVPT
EECCCCCCCCCCCCC		45.7730108239
366PhosphorylationSLSSNFTTPEEVPTG
ECCCCCCCCCCCCCC		25.2725159151
372PhosphorylationTTPEEVPTGTKSHRC
CCCCCCCCCCCCCCC		63.7622199227
374PhosphorylationPEEVPTGTKSHRCDE
CCCCCCCCCCCCCCC		31.6726074081
375UbiquitinationEEVPTGTKSHRCDEC
CCCCCCCCCCCCCCC		45.68-
375SumoylationEEVPTGTKSHRCDEC
CCCCCCCCCCCCCCC		45.6828112733
384UbiquitinationHRCDECGKCFTRSSS
CCCCCCCCCCCCCHH		37.52-
390PhosphorylationGKCFTRSSSLIRHKI
CCCCCCCHHHHCCEE		26.3524719451
391PhosphorylationKCFTRSSSLIRHKII
CCCCCCHHHHCCEEE		29.1224719451
396UbiquitinationSSSLIRHKIIHTGEK
CHHHHCCEEEECCCC		33.24-
400PhosphorylationIRHKIIHTGEKPYEC
HCCEEEECCCCCEEC		36.3129496963
403UbiquitinationKIIHTGEKPYECSEC
EEEECCCCCEECCCC		55.00-
405PhosphorylationIHTGEKPYECSECGK
EECCCCCEECCCCCC		40.41-
408PhosphorylationGEKPYECSECGKAFS
CCCCEECCCCCCEEE		24.7927251275
412SumoylationYECSECGKAFSLNSN
EECCCCCCEEECCCC		58.9028112733
412SumoylationYECSECGKAFSLNSN
EECCCCCCEEECCCC		58.90-
415PhosphorylationSECGKAFSLNSNLVL
CCCCCEEECCCCEEE		31.3428555341
418PhosphorylationGKAFSLNSNLVLHQR
CCEEECCCCEEEEEE		36.5128555341
428PhosphorylationVLHQRIHTGEKPHEC
EEEEEECCCCCCCCC		44.6727282143
440SumoylationHECNECGKAFSHSSN
CCCCCCHHCCCCCCC		58.9028112733
443PhosphorylationNECGKAFSHSSNLIL
CCCHHCCCCCCCEEE		27.5923312004
445PhosphorylationCGKAFSHSSNLILHQ
CHHCCCCCCCEEEEE		21.5223312004
446PhosphorylationGKAFSHSSNLILHQR
HHCCCCCCCEEEEEE		30.1723312004
456PhosphorylationILHQRIHSGEKPYEC
EEEEECCCCCCCEEC		46.4026657352
459UbiquitinationQRIHSGEKPYECNEC
EECCCCCCCEECCCC		57.32-
461PhosphorylationIHSGEKPYECNECGK
CCCCCCCEECCCCHH		44.1523312004
468UbiquitinationYECNECGKAFSQSSD
EECCCCHHHHHCCCC		58.90-
471PhosphorylationNECGKAFSQSSDLTK
CCCHHHHHCCCCCCC		33.7317525332
473PhosphorylationCGKAFSQSSDLTKHQ
CHHHHHCCCCCCCCC		25.3123312004
478SumoylationSQSSDLTKHQRIHTG
HCCCCCCCCCCCCCC		45.0728112733
478UbiquitinationSQSSDLTKHQRIHTG
HCCCCCCCCCCCCCC		45.07-
478SumoylationSQSSDLTKHQRIHTG
HCCCCCCCCCCCCCC		45.07-
484PhosphorylationTKHQRIHTGEKPYEC
CCCCCCCCCCCCCCC		44.6729496963
489PhosphorylationIHTGEKPYECSECGK
CCCCCCCCCCCHHHH		40.41-
492PhosphorylationGEKPYECSECGKAFN
CCCCCCCCHHHHCCC		24.7927251275
496SumoylationYECSECGKAFNRNSY
CCCCHHHHCCCCCCE		62.56-
496UbiquitinationYECSECGKAFNRNSY
CCCCHHHHCCCCCCE		62.56-
496SumoylationYECSECGKAFNRNSY
CCCCHHHHCCCCCCE		62.56-
502PhosphorylationGKAFNRNSYLILHRR
HHCCCCCCEEEEECC		20.3430108239
503PhosphorylationKAFNRNSYLILHRRI
HCCCCCCEEEEECCE		11.0030108239
527PhosphorylationTKCGKAFTRSSTLTL
CCCCCEEECCCCEEH		34.2028555341
529PhosphorylationCGKAFTRSSTLTLHH
CCCEEECCCCEEHHH		25.3123312004
530PhosphorylationGKAFTRSSTLTLHHR
CCEEECCCCEEHHHH		24.9328555341
531PhosphorylationKAFTRSSTLTLHHRI
CEEECCCCEEHHHHH		25.6323312004
533PhosphorylationFTRSSTLTLHHRIHA
EECCCCEEHHHHHHH		24.9223312004
545PhosphorylationIHARERASEYSPASL
HHHHHHHHHCCCHHH		43.2023403867
547PhosphorylationARERASEYSPASLDA
HHHHHHHCCCHHHHH		19.9123403867
548PhosphorylationRERASEYSPASLDAF
HHHHHHCCCHHHHHH		15.2228176443
551PhosphorylationASEYSPASLDAFGAF
HHHCCCHHHHHHHHH		30.1128176443
560UbiquitinationDAFGAFLKSCV----
HHHHHHHHHCC----		35.04-
560SumoylationDAFGAFLKSCV----
HHHHHHHHHCC----		35.0428112733
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 ZKSC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZKSC1_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 ZKSC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ZSC32_HUMANZSCAN32physical
25416956
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZKSC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-13, AND MASSSPECTROMETRY.
"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-13, 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-13, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-208, 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-13, AND MASSSPECTROMETRY.
"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-471, AND MASSSPECTROMETRY.
"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-13, AND MASSSPECTROMETRY.

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