ZN431_HUMAN - dbPTM
ZN431_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN431_HUMAN
UniProt AC Q8TF32
Protein Name Zinc finger protein 431
Gene Name ZNF431
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization Nucleus.
Protein Description Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling response. Binds to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1 (By similarity)..
Protein Sequence MDDLKYGVYPLKEASGCPGAERNLLVYSYFEKETLTFRDVAIEFSLEEWECLNPAQQNLYMNVMLENYKNLVFLGVAVSKQDPVTCLEQEKEPWNMKRHEMVDEPPAMCSYFTKDLWPEQDIKDSFQQVILRRYGKCEHENLQLRKGSASVDEYKVHKEGYNELNQCLTTTQSKIFPCDKYVKVFHKFLNANRHKTRHTGKKPFKCKKCGKSFCMLLHLSQHKRIHIRENSYQCEECGKAFKWFSTLTRHKRIHTGEKPFKCEECGKAFKQSSTLTTHKIIHTGEKPYRCEECGKAFNRSSHLTTHKIIHTGEKPYKCEECGKAFNQSSTLSTHKFIHAGEKPYKCEECDKAFNRFSYLTKHKIIHTGEKSYKCEECGKGFNWSSTLTKHKRIHTGEKPYKCEVCGKAFNESSNLTTHKMIHTGEKPYKCEECGKAFNRSPQLTAHKIIHTGEKPYKCEECGKAFSQSSILTTHKRIHTGEKPYKCEECGKAFNRSSNLTKHKIIHTGEKSYKCEECGKAFNQSSTLTKHRKIHTRQKPYNCEECDNTFNQSSNLIKQNNSYWRETLQMSRMWESL
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
5Ubiquitination---MDDLKYGVYPLK
---CCCCCCEEEECH		47.13-
12UbiquitinationKYGVYPLKEASGCPG
CCEEEECHHHCCCCC		46.89-
29PhosphorylationRNLLVYSYFEKETLT
CCEEEEEEEECCEEE		9.70-
114UbiquitinationAMCSYFTKDLWPEQD
CHHHHHCCCCCCHHH		40.71-
136UbiquitinationVILRRYGKCEHENLQ
HHHHHHCCCHHHCCE		27.75-
148PhosphorylationNLQLRKGSASVDEYK
CCEECCCCCCCCCHH		22.02-
150PhosphorylationQLRKGSASVDEYKVH
EECCCCCCCCCHHHH		31.62-
158UbiquitinationVDEYKVHKEGYNELN
CCCHHHHHCCHHHHH		56.68-
183UbiquitinationFPCDKYVKVFHKFLN
CCCHHHHHHHHHHHH		35.77-
255PhosphorylationTRHKRIHTGEKPFKC
HCCCCCCCCCCCCCH		44.6718669648
261SumoylationHTGEKPFKCEECGKA
CCCCCCCCHHHHHHH		49.62-
261SumoylationHTGEKPFKCEECGKA
CCCCCCCCHHHHHHH		49.62-
270UbiquitinationEECGKAFKQSSTLTT
HHHHHHHHCCCCCEE		54.88-
270SumoylationEECGKAFKQSSTLTT
HHHHHHHHCCCCCEE		54.88-
270SumoylationEECGKAFKQSSTLTT
HHHHHHHHCCCCCEE		54.88-
272PhosphorylationCGKAFKQSSTLTTHK
HHHHHHCCCCCEEEE		26.36-
273PhosphorylationGKAFKQSSTLTTHKI
HHHHHCCCCCEEEEE		25.58-
276PhosphorylationFKQSSTLTTHKIIHT
HHCCCCCEEEEEEEC		27.26-
279SumoylationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
279UbiquitinationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
279SumoylationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
283PhosphorylationTTHKIIHTGEKPYRC
EEEEEEECCCCCCCH		36.3129496963
286SumoylationKIIHTGEKPYRCEEC
EEEECCCCCCCHHHH		49.01-
286SumoylationKIIHTGEKPYRCEEC
EEEECCCCCCCHHHH		49.01-
286UbiquitinationKIIHTGEKPYRCEEC
EEEECCCCCCCHHHH		49.01-
295UbiquitinationYRCEECGKAFNRSSH
CCHHHHHHCCCCCCC		62.56-
307UbiquitinationSSHLTTHKIIHTGEK
CCCCCCCEEEECCCC		41.06-
311PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCEEH		36.3129496963
314UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEEHHHH		55.80-
316PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		39.06-
317UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
317SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
317AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.6319825793
317SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
323AcetylationYKCEECGKAFNQSST
EEHHHHHHCCCCCCC		62.5628733145
345SumoylationHAGEKPYKCEECDKA
CCCCCCCCCHHHHHH		43.63-
345SumoylationHAGEKPYKCEECDKA
CCCCCCCCCHHHHHH		43.63-
360PhosphorylationFNRFSYLTKHKIIHT
HHHHHHHHHCCEEEC		23.91-
367PhosphorylationTKHKIIHTGEKSYKC
HHCCEEECCCCEEEC		36.3127251275
370UbiquitinationKIIHTGEKSYKCEEC
CEEECCCCEEECCCC		61.50-
373SumoylationHTGEKSYKCEECGKG
ECCCCEEECCCCCCC		42.11-
373SumoylationHTGEKSYKCEECGKG
ECCCCEEECCCCCCC		42.11-
389UbiquitinationNWSSTLTKHKRIHTG
CCCHHCCCCCCCCCC		50.68-
395PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCEEC		44.6729496963
401SumoylationHTGEKPYKCEVCGKA
CCCCCCEECEECCCC		32.23-
401SumoylationHTGEKPYKCEVCGKA
CCCCCCEECEECCCC		32.23-
401UbiquitinationHTGEKPYKCEVCGKA
CCCCCCEECEECCCC		32.23-
419UbiquitinationSSNLTTHKMIHTGEK
CCCCCCCCEEECCCC		37.14-
423PhosphorylationTTHKMIHTGEKPYKC
CCCCEEECCCCCEEC		35.7929496963
426UbiquitinationKMIHTGEKPYKCEEC
CEEECCCCCEECHHH		55.80-
428PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECHHHHH		39.06-
429SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.63-
429UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.63-
429SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.63-
435UbiquitinationYKCEECGKAFNRSPQ
EECHHHHHHCCCCCC		62.56-
440PhosphorylationCGKAFNRSPQLTAHK
HHHHCCCCCCCCEEE		20.3625849741
444PhosphorylationFNRSPQLTAHKIIHT
CCCCCCCCEEEEEEC		22.8229083192
447UbiquitinationSPQLTAHKIIHTGEK
CCCCCEEEEEECCCC		40.67-
451PhosphorylationTAHKIIHTGEKPYKC
CEEEEEECCCCCEEC		36.3129496963
454UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEECHHH		55.80-
456PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECHHHHH		39.06-
457SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		43.63-
457AcetylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		43.6319825799
457SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		43.63-
457UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		43.63-
473PhosphorylationSQSSILTTHKRIHTG
CCCCCHHCCCCCCCC		23.1924719451
479PhosphorylationTTHKRIHTGEKPYKC
HCCCCCCCCCCCCCH		44.6729496963
482UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
484PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
485SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
485SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
485UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
491UbiquitinationYKCEECGKAFNRSSN
CCHHHHHHCCCCCCC		62.56-
500PhosphorylationFNRSSNLTKHKIIHT
CCCCCCCCCCCEEEC		35.0428555341
507PhosphorylationTKHKIIHTGEKSYKC
CCCCEEECCCCEEEH		36.3128555341
510UbiquitinationKIIHTGEKSYKCEEC
CEEECCCCEEEHHHH		61.50-
513SumoylationHTGEKSYKCEECGKA
ECCCCEEEHHHHHHH		42.11-
513SumoylationHTGEKSYKCEECGKA
ECCCCEEEHHHHHHH		42.11-
519AcetylationYKCEECGKAFNQSST
EEHHHHHHHHCCCCC		62.56-
524PhosphorylationCGKAFNQSSTLTKHR
HHHHHCCCCCCCCCC		26.7929978859
525PhosphorylationGKAFNQSSTLTKHRK
HHHHCCCCCCCCCCC		20.0629978859
526PhosphorylationKAFNQSSTLTKHRKI
HHHCCCCCCCCCCCC		43.6329978859
529UbiquitinationNQSSTLTKHRKIHTR
CCCCCCCCCCCCCCC		44.52-
538UbiquitinationRKIHTRQKPYNCEEC
CCCCCCCCCCCHHHC		46.29-
552PhosphorylationCDNTFNQSSNLIKQN
CCCCCCCCHHHHHHC		23.4627251275
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 ZN431_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN431_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 ZN431_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYRP1_HUMANTYRP1physical
28514442
ICAM3_HUMANICAM3physical
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 ZN431_HUMAN

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Related Literatures of Post-Translational Modification

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