ZN142_HUMAN - dbPTM
ZN142_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN142_HUMAN
UniProt AC P52746
Protein Name Zinc finger protein 142
Gene Name ZNF142
Organism Homo sapiens (Human).
Sequence Length 1687
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTDPLLDSQPASSTGEMDGLCPELLLIPPPLSNRGILGPVQSPCPSRDPAPIPTEPGCLLVEATATEEGPGNMEIIVETVAGTLTPGAPGETPAPKLPPGEREPSQEAGTPLPGQETAEEENVEKEEKSDTQKDSQKAVDKGQGAQRLEGDVVSGTESLFKTHMCPECKRCFKKRTHLVEHLHLHFPDPSLQCPNCQKFFTSKSKLKTHLLRELGEKAHHCPLCHYSAVERNALNRHMASMHEDISNFYSDTYACPVCREEFRLSQALKEHLKSHTAAAAAEPLPLRCFQEGCSYAAPDRKAFIKHLKETHGVRAVECRHHSCPMLFATAEAMEAHHKSHYAFHCPHCDFACSNKHLFRKHKKQGHPGSEELRCTFCPFATFNPVAYQDHVGKMHAHEKIHQCPECNFATAHKRVLIRHMLLHTGEKPHKCELCDFTCRDVSYLSKHMLTHSNTKDYMCTECGYVTKWKHYLRVHMRKHAGDLRYQCNQCSYRCHRADQLSSHKLRHQGKSLMCEVCAFACKRKYELQKHMASQHHPGTPAPLYPCHYCSYQSRHKQAVLSHENCKHTRLREFHCALCDYRTFSNTTLLFHKRKAHGYVPGDQAWQLRYASQEPEGAMQGPTPPPDSEPSNQLSARPEGPGHEPGTVVDPSLDQALPEMSEEVNTGRQEGSEAPHGGDLGGSPSPAEVEEGSCTLHLEALGVELESVTEPPLEEVTETAPMEFRPLGLEGPDGLEGPELSSFEGIGTSDLSAEENPLLEKPVSEPSTNPPSLEEAPNNWVGTFKTTPPAETAPLPPLPESESLLKALRRQDKEQAEALVLEGRVQMVVIQGEGRAFRCPHCPFITRREKALNLHSRTGCQGRREPLLCPECGASFKQQRGLSTHLLKKCPVLLRKNKGLPRPDSPIPLQPVLPGTQASEDTESGKPPPASQEAELLLPKDAPLELPREPEETEEPLATVSGSPVPPAGNSLPTEAPKKHCFDPVPPAGNSSPTEAPKKHHLDPVPPAGNSSPTEALKKHRFEQGKFHCNSCPFLCSRLSSITSHVAEGCRGGRGGGGKRGTPQTQPDVSPLSNGDSAPPKNGSTESSSGDGDTVLVQKQKGARFSCPTCPFSCQQERALRTHQIRGCPLEESGELHCSLCPFTAPAATALRLHQKRRHPTAAPARGPRPHLQCGDCGFTCKQSRCMQQHRRLKHEGVKPHQCPFCDFSTTRRYRLEAHQSRHTGIGRIPCSSCPQTFGTNSKLRLHRLRVHDKTPTHFCPLCDYSGYLRHDITRHVNSCHQGTPAFACSQCEAQFSSETALKQHALRRHPEPAQPAPGSPAETTEGPLHCSRCGLLCPSPASLRGHTRKQHPRLECGACQEAFPSRLALDEHRRQQHFSHRCQLCDFAARERVGLVKHYLEQHEETSAAVAASDGDGDAGQPPLHCPFCDFTCRHQLVLDHHVKGHGGTRLYKCTDCAYSTKNRQKITWHSRIHTGEKPYHCHLCPYACADPSRLKYHMRIHKEERKYLCPECGYKCKWVNQLKYHMTKHTGLKPYQCPECEYCTNRADALRVHQETRHREARAFMCEQCGKAFKTRFLLRTHLRKHSEAKPYVCNVCHRAFRWAAGLRHHALTHTDRHPFFCRLCNYKAKQKFQVVKHVRRHHPDQADPNQGVGKDPTTPTVHLHDVQLEDPSPPAPAAPHTGPEG
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
8PhosphorylationMTDPLLDSQPASSTG
CCCCCCCCCCCCCCC
37.7229759185
154PhosphorylationRLEGDVVSGTESLFK
HCCCCEECCCHHHHH
39.5928112733
156PhosphorylationEGDVVSGTESLFKTH
CCCEECCCHHHHHHC
18.2023186163
158PhosphorylationDVVSGTESLFKTHMC
CEECCCHHHHHHCCC
38.6624719451
201PhosphorylationPNCQKFFTSKSKLKT
CCHHHHHCCHHHHHH
38.0827251275
202PhosphorylationNCQKFFTSKSKLKTH
CHHHHHCCHHHHHHH
29.7627251275
204O-linked_GlycosylationQKFFTSKSKLKTHLL
HHHHCCHHHHHHHHH
42.8830379171
207UbiquitinationFTSKSKLKTHLLREL
HCCHHHHHHHHHHHH
37.3229967540
246PhosphorylationASMHEDISNFYSDTY
HHHCHHHHHHHCCCC
32.9622210691
273UbiquitinationQALKEHLKSHTAAAA
HHHHHHHHHCHHHHH
41.9429967540
276PhosphorylationKEHLKSHTAAAAAEP
HHHHHHCHHHHHCCC
25.6928555341
424PhosphorylationIRHMLLHTGEKPHKC
HHHHHHHCCCCCCCC
47.18-
469SumoylationCGYVTKWKHYLRVHM
CCCCCEEHHHHHHHH
24.75-
469SumoylationCGYVTKWKHYLRVHM
CCCCCEEHHHHHHHH
24.75-
485PhosphorylationKHAGDLRYQCNQCSY
HHCCCHHHHHHCCHH
25.39-
533PhosphorylationELQKHMASQHHPGTP
HHHHHHHHCCCCCCC
23.5924043423
539PhosphorylationASQHHPGTPAPLYPC
HHCCCCCCCCCCCCC
22.2624043423
544PhosphorylationPGTPAPLYPCHYCSY
CCCCCCCCCCCCCCC
11.6224043423
548PhosphorylationAPLYPCHYCSYQSRH
CCCCCCCCCCCHHHH
6.9824043423
550PhosphorylationLYPCHYCSYQSRHKQ
CCCCCCCCCHHHHHH
21.0224043423
551PhosphorylationYPCHYCSYQSRHKQA
CCCCCCCCHHHHHHH
13.6224043423
553PhosphorylationCHYCSYQSRHKQAVL
CCCCCCHHHHHHHHH
28.2824043423
594SumoylationTLLFHKRKAHGYVPG
EEEEECCCCCCCCCC
49.9225218447
594SumoylationTLLFHKRKAHGYVPG
EEEEECCCCCCCCCC
49.92-
785PhosphorylationNWVGTFKTTPPAETA
CCCCCCCCCCCHHCC
40.1028348404
786PhosphorylationWVGTFKTTPPAETAP
CCCCCCCCCCHHCCC
28.0621712546
791PhosphorylationKTTPPAETAPLPPLP
CCCCCHHCCCCCCCC
35.3621712546
802PhosphorylationPPLPESESLLKALRR
CCCCCCHHHHHHHHH
48.5624719451
805UbiquitinationPESESLLKALRRQDK
CCCHHHHHHHHHCCH
51.1429967540
874PhosphorylationLCPECGASFKQQRGL
CCCCCCCCHHHHCCC
20.4724719451
904PhosphorylationKGLPRPDSPIPLQPV
CCCCCCCCCCCCCCC
27.6727050516
915PhosphorylationLQPVLPGTQASEDTE
CCCCCCCCCCCCCCC
21.0129083192
918PhosphorylationVLPGTQASEDTESGK
CCCCCCCCCCCCCCC
26.6229083192
958PhosphorylationETEEPLATVSGSPVP
CCCCCCCEECCCCCC
23.9228348404
960PhosphorylationEEPLATVSGSPVPPA
CCCCCEECCCCCCCC
29.2428348404
962PhosphorylationPLATVSGSPVPPAGN
CCCEECCCCCCCCCC
18.4130576142
990PhosphorylationPVPPAGNSSPTEAPK
CCCCCCCCCCCCCCC
36.4623663014
991PhosphorylationVPPAGNSSPTEAPKK
CCCCCCCCCCCCCCH
39.5825159151
993PhosphorylationPAGNSSPTEAPKKHH
CCCCCCCCCCCCHHC
46.8823663014
1010PhosphorylationPVPPAGNSSPTEALK
CCCCCCCCCHHHHHH
36.4630576142
1011PhosphorylationVPPAGNSSPTEALKK
CCCCCCCCHHHHHHH
39.5827050516
1013PhosphorylationPAGNSSPTEALKKHR
CCCCCCHHHHHHHHH
35.5227050516
1039PhosphorylationPFLCSRLSSITSHVA
HHHHHHHHHHHHHHH
20.70-
1040PhosphorylationFLCSRLSSITSHVAE
HHHHHHHHHHHHHHC
34.1828555341
1042PhosphorylationCSRLSSITSHVAEGC
HHHHHHHHHHHHCCC
18.09-
1043PhosphorylationSRLSSITSHVAEGCR
HHHHHHHHHHHCCCC
17.81-
1050MethylationSHVAEGCRGGRGGGG
HHHHCCCCCCCCCCC
62.5554560817
1069PhosphorylationPQTQPDVSPLSNGDS
CCCCCCCCCCCCCCC
27.7428985074
1183PhosphorylationCGFTCKQSRCMQQHR
CCCCCCHHHHHHHHH
16.9730631047
1193SumoylationMQQHRRLKHEGVKPH
HHHHHHHHHCCCCCC
37.4928112733
1242UbiquitinationQTFGTNSKLRLHRLR
CCCCCCCCEEEEEEE
39.43-
1242SumoylationQTFGTNSKLRLHRLR
CCCCCCCCEEEEEEE
39.4328112733
1254PhosphorylationRLRVHDKTPTHFCPL
EEECCCCCCCCCCCC
39.2025627689
1256PhosphorylationRVHDKTPTHFCPLCD
ECCCCCCCCCCCCCC
32.5825627689
1319PhosphorylationPAQPAPGSPAETTEG
CCCCCCCCCCCCCCC
21.6323401153
1323PhosphorylationAPGSPAETTEGPLHC
CCCCCCCCCCCCCCC
32.0530243723
1324PhosphorylationPGSPAETTEGPLHCS
CCCCCCCCCCCCCCC
30.3730243723
1331PhosphorylationTEGPLHCSRCGLLCP
CCCCCCCCCCCEECC
21.6230243723
1339PhosphorylationRCGLLCPSPASLRGH
CCCEECCCHHHHCCC
31.9127134283
1453SumoylationHGGTRLYKCTDCAYS
CCCCEEEEECCCCCC
34.94-
1453SumoylationHGGTRLYKCTDCAYS
CCCCEEEEECCCCCC
34.94-
1455PhosphorylationGTRLYKCTDCAYSTK
CCEEEEECCCCCCCC
29.93-
1462UbiquitinationTDCAYSTKNRQKITW
CCCCCCCCCCCEEEE
44.1629967540
1466SumoylationYSTKNRQKITWHSRI
CCCCCCCEEEEECEE
38.58-
1466SumoylationYSTKNRQKITWHSRI
CCCCCCCEEEEECEE
38.58-
1475PhosphorylationTWHSRIHTGEKPYHC
EEECEEECCCCCEEE
44.6728111955
1507SumoylationRIHKEERKYLCPECG
ECCHHHHCCCCCCCC
45.94-
1507SumoylationRIHKEERKYLCPECG
ECCHHHHCCCCCCCC
45.94-
1531PhosphorylationKYHMTKHTGLKPYQC
HHEECCCCCCCCCCC
45.8528555341
1543PhosphorylationYQCPECEYCTNRADA
CCCCCCCHHCCHHHH
19.07-
1545PhosphorylationCPECEYCTNRADALR
CCCCCHHCCHHHHHH
27.17-
1557PhosphorylationALRVHQETRHREARA
HHHHCHHHHHHHHHH
25.79-
1591SumoylationLRKHSEAKPYVCNVC
HHHHCCCCCCHHHHH
32.6028112733
1638UbiquitinationKQKFQVVKHVRRHHP
HHHHHHHHHHHHHCC
37.2129967540
1674PhosphorylationDVQLEDPSPPAPAAP
ECCCCCCCCCCCCCC
56.7025159151

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 ZN142_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN142_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 ZN142_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN142_HUMAN !!

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 ZN142_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1319, AND MASSSPECTROMETRY.

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