ZN267_HUMAN - dbPTM
ZN267_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN267_HUMAN
UniProt AC Q14586
Protein Name Zinc finger protein 267
Gene Name ZNF267
Organism Homo sapiens (Human).
Sequence Length 743
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MGLLTFRDVAVEFSLEEWEHLEPAQKNLYQDVMLENYRNLVSLGLVVSKPDLITFLEQRKEPWNVKSEETVAIQPDVFSHYNKDLLTEHCTEASFQKVISRRHGSCDLENLHLRKRWKREECEGHNGCYDEKTFKYDQFDESSVESLFHQQILSSCAKSYNFDQYRKVFTHSSLLNQQEEIDIWGKHHIYDKTSVLFRQVSTLNSYRNVFIGEKNYHCNNSEKTLNQSSSPKNHQENYFLEKQYKCKEFEEVFLQSMHGQEKQEQSYKCNKCVEVCTQSLKHIQHQTIHIRENSYSYNKYDKDLSQSSNLRKQIIHNEEKPYKCEKCGDSLNHSLHLTQHQIIPTEEKPCKWKECGKVFNLNCSLYLTKQQQIDTGENLYKCKACSKSFTRSSNLIVHQRIHTGEKPYKCKECGKAFRCSSYLTKHKRIHTGEKPYKCKECGKAFNRSSCLTQHQTTHTGEKLYKCKVCSKSYARSSNLIMHQRVHTGEKPYKCKECGKVFSRSSCLTQHRKIHTGENLYKCKVCAKPFTCFSNLIVHERIHTGEKPYKCKECGKAFPYSSHLIRHHRIHTGEKPYKCKACSKSFSDSSGLTVHRRTHTGEKPYTCKECGKAFSYSSDVIQHRRIHTGQRPYKCEECGKAFNYRSYLTTHQRSHTGERPYKCEECGKAFNSRSYLTTHRRRHTGERPYKCDECGKAFSYRSYLTTHRRSHSGERPYKCEECGKAFNSRSYLIAHQRSHTREKL
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
34UbiquitinationNLYQDVMLENYRNLV
HHHHHHHHHHHHHHH		3.7629967540
51UbiquitinationGLVVSKPDLITFLEQ
CCEECCHHHHHHHHH		55.2129967540
54PhosphorylationVSKPDLITFLEQRKE
ECCHHHHHHHHHCCC		29.4821406692
60UbiquitinationITFLEQRKEPWNVKS
HHHHHHCCCCCCCCC		68.75-
65UbiquitinationQRKEPWNVKSEETVA
HCCCCCCCCCCEEEE		6.7929967540
66SumoylationRKEPWNVKSEETVAI
CCCCCCCCCCEEEEE		49.27-
66UbiquitinationRKEPWNVKSEETVAI
CCCCCCCCCCEEEEE		49.2729967540
66SumoylationRKEPWNVKSEETVAI
CCCCCCCCCCEEEEE		49.2728112733
70PhosphorylationWNVKSEETVAIQPDV
CCCCCCEEEEECCCH		15.9323879269
83UbiquitinationDVFSHYNKDLLTEHC
CHHHHCCHHHHHHHC		42.4629967540
97UbiquitinationCTEASFQKVISRRHG
CCHHHHHHHHHHHCC		39.2529967540
103UbiquitinationQKVISRRHGSCDLEN
HHHHHHHCCCCCHHH		31.2629967540
105PhosphorylationVISRRHGSCDLENLH
HHHHHCCCCCHHHHH		9.8021712546
126UbiquitinationREECEGHNGCYDEKT
HHHCCCCCCCCCCCC		53.7629967540
135SumoylationCYDEKTFKYDQFDES
CCCCCCEECCCCCHH		53.8228112733
135UbiquitinationCYDEKTFKYDQFDES
CCCCCCEECCCCCHH		53.8229967540
154UbiquitinationLFHQQILSSCAKSYN
HHHHHHHHHHHHHCC		25.6329967540
158UbiquitinationQILSSCAKSYNFDQY
HHHHHHHHHCCHHHH		58.7729967540
159PhosphorylationILSSCAKSYNFDQYR
HHHHHHHHCCHHHHH		13.5430108239
160PhosphorylationLSSCAKSYNFDQYRK
HHHHHHHCCHHHHHH		21.1030108239
186UbiquitinationEEIDIWGKHHIYDKT
HHEEECCCCCCCCHH		19.6029967540
191UbiquitinationWGKHHIYDKTSVLFR
CCCCCCCCHHHHHEE		47.3429967540
194PhosphorylationHHIYDKTSVLFRQVS
CCCCCHHHHHEEEHH		23.67-
200UbiquitinationTSVLFRQVSTLNSYR
HHHHEEEHHHHHHCC		4.0429967540
201PhosphorylationSVLFRQVSTLNSYRN
HHHEEEHHHHHHCCC		20.8830576142
210UbiquitinationLNSYRNVFIGEKNYH
HHHCCCEEECCCCEE		7.2929967540
214UbiquitinationRNVFIGEKNYHCNNS
CCEEECCCCEECCCC		58.56-
223UbiquitinationYHCNNSEKTLNQSSS
EECCCCCCCCCCCCC		59.1229967540
224PhosphorylationHCNNSEKTLNQSSSP
ECCCCCCCCCCCCCC		27.2223312004
228PhosphorylationSEKTLNQSSSPKNHQ
CCCCCCCCCCCCCHH		31.5430108239
229PhosphorylationEKTLNQSSSPKNHQE
CCCCCCCCCCCCHHH		40.6830108239
230PhosphorylationKTLNQSSSPKNHQEN
CCCCCCCCCCCHHHH		45.1825849741
230UbiquitinationKTLNQSSSPKNHQEN
CCCCCCCCCCCHHHH		45.1829967540
232UbiquitinationLNQSSSPKNHQENYF
CCCCCCCCCHHHHHH		69.8429967540
238PhosphorylationPKNHQENYFLEKQYK
CCCHHHHHHHHHHHH		14.5930108239
242UbiquitinationQENYFLEKQYKCKEF
HHHHHHHHHHHCHHH		62.1629967540
262UbiquitinationQSMHGQEKQEQSYKC
HHHCCHHHHHHHHCC		51.7729967540
270UbiquitinationQEQSYKCNKCVEVCT
HHHHHCCCHHHHHHH		36.2929967540
280UbiquitinationVEVCTQSLKHIQHQT
HHHHHHHHHHHCCCE		3.1729967540
288UbiquitinationKHIQHQTIHIRENSY
HHHCCCEEEEECCCC		1.7329967540
302UbiquitinationYSYNKYDKDLSQSSN
CCCCCCCCCCHHCCC		58.4429967540
312UbiquitinationSQSSNLRKQIIHNEE
HHCCCHHHHHHHCCC		49.3629967540
320UbiquitinationQIIHNEEKPYKCEKC
HHHHCCCCCCCCCCC		47.6829967540
337UbiquitinationSLNHSLHLTQHQIIP
CCCCCEECCCCCCCC		6.3029967540
349UbiquitinationIIPTEEKPCKWKECG
CCCCCCCCCCCCCCC		28.3529967540
364PhosphorylationKVFNLNCSLYLTKQQ
CEEECCCEEEEEECC		20.9830108239
366PhosphorylationFNLNCSLYLTKQQQI
EECCCEEEEEECCCC		8.9530108239
368PhosphorylationLNCSLYLTKQQQIDT
CCCEEEEEECCCCCC		17.1630108239
369UbiquitinationNCSLYLTKQQQIDTG
CCEEEEEECCCCCCC		43.4429967540
381UbiquitinationDTGENLYKCKACSKS
CCCCCCEECCCCCCC		32.2129967540
403PhosphorylationIVHQRIHTGEKPYKC
EEEEEEECCCCCCCC		44.6729496963
408PhosphorylationIHTGEKPYKCKECGK
EECCCCCCCCCCCCC		39.83-
424PhosphorylationFRCSSYLTKHKRIHT
CCCHHHHHCCCCCCC		23.9122817900
430UbiquitinationLTKHKRIHTGEKPYK
HHCCCCCCCCCCCCC		31.6729967540
431PhosphorylationTKHKRIHTGEKPYKC
HCCCCCCCCCCCCCC		44.6729496963
436PhosphorylationIHTGEKPYKCKECGK
CCCCCCCCCCCHHHC		39.83-
456PhosphorylationSCLTQHQTTHTGEKL
HCCCCCCCCCCCCEE		20.5828555341
462UbiquitinationQTTHTGEKLYKCKVC
CCCCCCCEEEECEEC		59.4629967540
487PhosphorylationIMHQRVHTGEKPYKC
EEEEECCCCCCCCCC		44.1529496963
490SumoylationQRVHTGEKPYKCKEC
EECCCCCCCCCCCCC		55.80-
490UbiquitinationQRVHTGEKPYKCKEC
EECCCCCCCCCCCCC		55.80-
490SumoylationQRVHTGEKPYKCKEC
EECCCCCCCCCCCCC		55.80-
502PhosphorylationKECGKVFSRSSCLTQ
CCCCCEECCHHHHHC		33.9524719451
505PhosphorylationGKVFSRSSCLTQHRK
CCEECCHHHHHCCCC		16.4324719451
512UbiquitinationSCLTQHRKIHTGENL
HHHHCCCCCCCCCCC		36.39-
515PhosphorylationTQHRKIHTGENLYKC
HCCCCCCCCCCCEEC		50.0625159151
520PhosphorylationIHTGENLYKCKVCAK
CCCCCCCEECEECCC		26.3922817900
543PhosphorylationIVHERIHTGEKPYKC
EEEEECCCCCCCEEC		44.6729496963
548PhosphorylationIHTGEKPYKCKECGK
CCCCCCCEECCCCCC		39.83-
568MethylationSHLIRHHRIHTGEKP
HHHHHCCCCCCCCCC		19.0924381517
571PhosphorylationIRHHRIHTGEKPYKC
HHCCCCCCCCCCCCC		44.6729496963
582PhosphorylationPYKCKACSKSFSDSS
CCCCCCCCCCCCCCC		35.8728842319
584PhosphorylationKCKACSKSFSDSSGL
CCCCCCCCCCCCCCC		17.4328555341
586PhosphorylationKACSKSFSDSSGLTV
CCCCCCCCCCCCCEE		43.6130108239
588PhosphorylationCSKSFSDSSGLTVHR
CCCCCCCCCCCEEEC		25.7130108239
589PhosphorylationSKSFSDSSGLTVHRR
CCCCCCCCCCEEECC		42.6930108239
597PhosphorylationGLTVHRRTHTGEKPY
CCEEECCCCCCCCCE		24.60-
599PhosphorylationTVHRRTHTGEKPYTC
EEECCCCCCCCCEEC		46.56-
604PhosphorylationTHTGEKPYTCKECGK
CCCCCCCEECCCCCC		35.52-
605PhosphorylationHTGEKPYTCKECGKA
CCCCCCEECCCCCCE		26.15-
614PhosphorylationKECGKAFSYSSDVIQ
CCCCCEEECCCCCHH		29.0330301811
615PhosphorylationECGKAFSYSSDVIQH
CCCCEEECCCCCHHC		13.0222817900
616PhosphorylationCGKAFSYSSDVIQHR
CCCEEECCCCCHHCC		20.9030301811
617PhosphorylationGKAFSYSSDVIQHRR
CCEEECCCCCHHCCC		27.8830301811
633SumoylationHTGQRPYKCEECGKA
CCCCCCEECHHCCCC		37.54-
633UbiquitinationHTGQRPYKCEECGKA
CCCCCCEECHHCCCC		37.54-
633SumoylationHTGQRPYKCEECGKA
CCCCCCEECHHCCCC		37.54-
653PhosphorylationYLTTHQRSHTGERPY
HCCCCCCCCCCCCCE		20.8727251275
655PhosphorylationTTHQRSHTGERPYKC
CCCCCCCCCCCCEEH		41.8227251275
661SumoylationHTGERPYKCEECGKA
CCCCCCEEHHHCCHH		37.54-
661SumoylationHTGERPYKCEECGKA
CCCCCCEEHHHCCHH		37.54-
661UbiquitinationHTGERPYKCEECGKA
CCCCCCEEHHHCCHH		37.54-
667UbiquitinationYKCEECGKAFNSRSY
EEHHHCCHHHCCCCC		62.56-
688PhosphorylationRHTGERPYKCDECGK
CCCCCCCCCCCCCCC		30.39-
699PhosphorylationECGKAFSYRSYLTTH
CCCCCEEEHHHHHCC		9.34-
717UbiquitinationHSGERPYKCEECGKA
CCCCCCCCHHHHHHH		37.54-
717SumoylationHSGERPYKCEECGKA
CCCCCCCCHHHHHHH		37.54-
717SumoylationHSGERPYKCEECGKA
CCCCCCCCHHHHHHH		37.54-
723UbiquitinationYKCEECGKAFNSRSY
CCHHHHHHHHCCCCH		62.56-
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 ZN267_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN267_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 ZN267_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN267_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 ZN267_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 THR-424, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-520, AND MASSSPECTROMETRY.

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