ZN143_HUMAN - dbPTM
ZN143_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN143_HUMAN
UniProt AC P52747
Protein Name Zinc finger protein 143
Gene Name ZNF143
Organism Homo sapiens (Human).
Sequence Length 638
Subcellular Localization Nucleus .
Protein Description Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8..
Protein Sequence MLLAQINRDSQGMTEFPGGGMEAQHVTLCLTEAVTVADGDNLENMEGVSLQAVTLADGSTAYIQHNSKDAKLIDGQVIQLEDGSAAYVQHVPIPKSTGDSLRLEDGQAVQLEDGTTAFIHHTSKDSYDQSALQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGDATIDPDTISALEQYAAKVSIDGSESVAGTGMIGENEQEKKMQIVLQGHATRVTAKSQQSGEKAFRCEYDGCGKLYTTAHHLKVHERSHTGDRPYQCEHAGCGKAFATGYGLKSHVRTHTGEKPYRCSEDNCTKSFKTSGDLQKHIRTHTGERPFKCPFEGCGRSFTTSNIRKVHVRTHTGERPYYCTEPGCGRAFASATNYKNHVRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTHSKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQEAFFEPPPGQGEDVLKGSQITYVTGVEGDDVVSTQVATVTQSGLSQQVTLISQDGTQHVNISQADMQAIGNTITMVTQDGTPITVPAHDAVISSAGTHSVAMVTAEGTEGEQVAIVAQDLAAFHTASSEMGHQQHSHHLVTTETRPLTLVATSNGTQIAVQLGEQPSLEEAIRIASRIQQGETPGLDD
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
1Acetylation-------MLLAQINR
-------CCEEECCC		6.6322814378
32UbiquitinationHVTLCLTEAVTVADG
EEEEEEEECEEECCC		28.3524816145
64UbiquitinationDGSTAYIQHNSKDAK
CCCEEEEEECCCCCE		19.6229967540
71UbiquitinationQHNSKDAKLIDGQVI
EECCCCCEEECCEEE		56.9929967540
82UbiquitinationGQVIQLEDGSAAYVQ
CEEEEECCCCEEEEE		66.0122505724
84PhosphorylationVIQLEDGSAAYVQHV
EEEECCCCEEEEEEC		23.2727642862
87PhosphorylationLEDGSAAYVQHVPIP
ECCCCEEEEEECCCC		10.6025159151
95UbiquitinationVQHVPIPKSTGDSLR
EEECCCCCCCCCCEE		62.4629967540
100PhosphorylationIPKSTGDSLRLEDGQ
CCCCCCCCEEECCCC		19.4128555341
203UbiquitinationSESVAGTGMIGENEQ
CCCCCCCCCCCCCCH		12.5624816145
204UbiquitinationESVAGTGMIGENEQE
CCCCCCCCCCCCCHH		3.4124816145
213SumoylationGENEQEKKMQIVLQG
CCCCHHHHEEEEEEC		34.9728112733
213SumoylationGENEQEKKMQIVLQG
CCCCHHHHEEEEEEC		34.97-
215UbiquitinationNEQEKKMQIVLQGHA
CCHHHHEEEEEECCE		31.3629967540
218UbiquitinationEKKMQIVLQGHATRV
HHHEEEEEECCEEEE		5.5824816145
219UbiquitinationKKMQIVLQGHATRVT
HHEEEEEECCEEEEE		30.6324816145
224UbiquitinationVLQGHATRVTAKSQQ
EEECCEEEEEECHHH		25.2729967540
234UbiquitinationAKSQQSGEKAFRCEY
ECHHHCCCCEEEEEE		46.5924816145
235AcetylationKSQQSGEKAFRCEYD
CHHHCCCCEEEEEEC		57.2426051181
235UbiquitinationKSQQSGEKAFRCEYD
CHHHCCCCEEEEEEC		57.2424816145
241PhosphorylationEKAFRCEYDGCGKLY
CCEEEEEECCCCCEE		22.66-
245UbiquitinationRCEYDGCGKLYTTAH
EEEECCCCCEEEEEH		28.6529967540
246UbiquitinationCEYDGCGKLYTTAHH
EEECCCCCEEEEEHH		42.2529967540
249UbiquitinationDGCGKLYTTAHHLKV
CCCCCEEEEEHHHEE		28.1324816145
250UbiquitinationGCGKLYTTAHHLKVH
CCCCEEEEEHHHEEE		15.5024816145
253UbiquitinationKLYTTAHHLKVHERS
CEEEEEHHHEEECCC		25.5322505724
254UbiquitinationLYTTAHHLKVHERSH
EEEEEHHHEEECCCC		4.4422505724
255UbiquitinationYTTAHHLKVHERSHT
EEEEHHHEEECCCCC		36.8729967540
260PhosphorylationHLKVHERSHTGDRPY
HHEEECCCCCCCCCE		23.5529449344
262PhosphorylationKVHERSHTGDRPYQC
EEECCCCCCCCCEEC		41.8629496963
267PhosphorylationSHTGDRPYQCEHAGC
CCCCCCCEECCCCCC		27.0422817900
268UbiquitinationHTGDRPYQCEHAGCG
CCCCCCEECCCCCCC		28.8922505724
269UbiquitinationTGDRPYQCEHAGCGK
CCCCCEECCCCCCCH		3.2322505724
276UbiquitinationCEHAGCGKAFATGYG
CCCCCCCHHHHCCCC		44.39-
276AcetylationCEHAGCGKAFATGYG
CCCCCCCHHHHCCCC		44.3926051181
280PhosphorylationGCGKAFATGYGLKSH
CCCHHHHCCCCCHHC		25.20-
282PhosphorylationGKAFATGYGLKSHVR
CHHHHCCCCCHHCEE		18.2218083107
284UbiquitinationAFATGYGLKSHVRTH
HHHCCCCCHHCEEEC		3.7622505724
285SumoylationFATGYGLKSHVRTHT
HHCCCCCHHCEEECC		33.87-
285SumoylationFATGYGLKSHVRTHT
HHCCCCCHHCEEECC		33.87-
285UbiquitinationFATGYGLKSHVRTHT
HHCCCCCHHCEEECC		33.8722505724
286PhosphorylationATGYGLKSHVRTHTG
HCCCCCHHCEEECCC		32.05-
290PhosphorylationGLKSHVRTHTGEKPY
CCHHCEEECCCCCCE		23.77-
292PhosphorylationKSHVRTHTGEKPYRC
HHCEEECCCCCCEEC		46.5624719451
295AcetylationVRTHTGEKPYRCSED
EEECCCCCCEECCCC		49.0121339330
297UbiquitinationTHTGEKPYRCSEDNC
ECCCCCCEECCCCCC		35.0129967540
299UbiquitinationTGEKPYRCSEDNCTK
CCCCCEECCCCCCCC		4.2722505724
300UbiquitinationGEKPYRCSEDNCTKS
CCCCEECCCCCCCCC		38.7022505724
306UbiquitinationCSEDNCTKSFKTSGD
CCCCCCCCCEECCCC		56.97-
309MethylationDNCTKSFKTSGDLQK
CCCCCCEECCCCHHH		49.20110925525
309SumoylationDNCTKSFKTSGDLQK
CCCCCCEECCCCHHH		49.20-
309SumoylationDNCTKSFKTSGDLQK
CCCCCCEECCCCHHH		49.20-
315UbiquitinationFKTSGDLQKHIRTHT
EECCCCHHHHHHHCC		39.7729967540
316UbiquitinationKTSGDLQKHIRTHTG
ECCCCHHHHHHHCCC		48.5829967540
320PhosphorylationDLQKHIRTHTGERPF
CHHHHHHHCCCCCCC		24.1628555341
322PhosphorylationQKHIRTHTGERPFKC
HHHHHHCCCCCCCCC		39.8725159151
327UbiquitinationTHTGERPFKCPFEGC
HCCCCCCCCCCCCCC		18.6429967540
328UbiquitinationHTGERPFKCPFEGCG
CCCCCCCCCCCCCCC		43.6229967540
337PhosphorylationPFEGCGRSFTTSNIR
CCCCCCCCEECCCEE		16.5425627689
339PhosphorylationEGCGRSFTTSNIRKV
CCCCCCEECCCEEEE		30.4824719451
340PhosphorylationGCGRSFTTSNIRKVH
CCCCCEECCCEEEEE		20.1224719451
341PhosphorylationCGRSFTTSNIRKVHV
CCCCEECCCEEEEEE		27.4824719451
344UbiquitinationSFTTSNIRKVHVRTH
CEECCCEEEEEEEEC		38.9129967540
350PhosphorylationIRKVHVRTHTGERPY
EEEEEEEECCCCCCE		23.7728450419
352PhosphorylationKVHVRTHTGERPYYC
EEEEEECCCCCCEEE		39.8725159151
354UbiquitinationHVRTHTGERPYYCTE
EEEECCCCCCEEECC		52.1929967540
357PhosphorylationTHTGERPYYCTEPGC
ECCCCCCEEECCCCC		19.8628450419
358PhosphorylationHTGERPYYCTEPGCG
CCCCCCEEECCCCCC		8.7927732954
365UbiquitinationYCTEPGCGRAFASAT
EECCCCCCCCCCCCC		29.8429967540
374UbiquitinationAFASATNYKNHVRIH
CCCCCCCCCCCEEEE		14.6029967540
375SumoylationFASATNYKNHVRIHT
CCCCCCCCCCEEEEC		42.52-
375UbiquitinationFASATNYKNHVRIHT
CCCCCCCCCCEEEEC		42.5229967540
375SumoylationFASATNYKNHVRIHT
CCCCCCCCCCEEEEC		42.52-
382PhosphorylationKNHVRIHTGEKPYVC
CCCEEEECCCCCEEE		44.6729214152
384UbiquitinationHVRIHTGEKPYVCTV
CEEEECCCCCEEEEC		52.6029967540
385UbiquitinationVRIHTGEKPYVCTVP
EEEECCCCCEEEECC		42.8929967540
387PhosphorylationIHTGEKPYVCTVPGC
EECCCCCEEEECCCC		21.1625159151
393UbiquitinationPYVCTVPGCDKRFTE
CEEEECCCCCCCHHH		28.1129967540
395UbiquitinationVCTVPGCDKRFTEYS
EEECCCCCCCHHHHH		51.5929967540
396UbiquitinationCTVPGCDKRFTEYSS
EECCCCCCCHHHHHH		54.1929967540
405UbiquitinationFTEYSSLYKHHVVHT
HHHHHHHHCCCEEEC		15.3829967540
406SumoylationTEYSSLYKHHVVHTH
HHHHHHHCCCEEECC		32.3128112733
415AcetylationHVVHTHSKPYNCNHC
CEEECCCCCCCCCCC		43.8726051181
423UbiquitinationPYNCNHCGKTYKQIS
CCCCCCCCCCHHHHH		20.1429967540
424UbiquitinationYNCNHCGKTYKQIST
CCCCCCCCCHHHHHH		54.8229967540
435UbiquitinationQISTLAMHKRTAHND
HHHHHHHHCCCCCCC		15.7329967540
436UbiquitinationISTLAMHKRTAHNDT
HHHHHHHCCCCCCCC		38.0629967540
466SumoylationGQGEDVLKGSQITYV
CCCCCCCCCCEEEEE		57.26-
633PhosphorylationSRIQQGETPGLDD--
HHHHCCCCCCCCC--		29.4923403867
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 ZN143_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN143_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 ZN143_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PO5F1_HUMANPOU5F1physical
18687992
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 ZN143_HUMAN

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Related Literatures of Post-Translational Modification

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