ZN473_HUMAN - dbPTM
ZN473_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN473_HUMAN
UniProt AC Q8WTR7
Protein Name Zinc finger protein 473
Gene Name ZNF473
Organism Homo sapiens (Human).
Sequence Length 871
Subcellular Localization Nucleus . Stable component of Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA.
Protein Description Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases..
Protein Sequence MAEEFVTLKDVGMDFTLGDWEQLGLEQGDTFWDTALDNCQDLFLLDPPRPNLTSHPDGSEDLEPLAGGSPEATSPDVTETKNSPLMEDFFEEGFSQEIIEMLSKDGFWNSNFGEACIEDTWLDSLLGDPESLLRSDIATNGESPTECKSHELKRGLSPVSTVSTGEDSMVHNVSEKTLTPAKSKEYRGEFFSYSDHSQQDSVQEGEKPYQCSECGKSFSGSYRLTQHWITHTREKPTVHQECEQGFDRNASLSVYPKTHTGYKFYVCNEYGTTFSQSTYLWHQKTHTGEKPCKSQDSDHPPSHDTQPGEHQKTHTDSKSYNCNECGKAFTRIFHLTRHQKIHTRKRYECSKCQATFNLRKHLIQHQKTHAAKTTSECQECGKIFRHSSLLIEHQALHAGEEPYKCNERGKSFRHNSTLKIHQRVHSGEKPYKCSECGKAFHRHTHLNEHRRIHTGYRPHKCQECVRSFSRPSHLMRHQAIHTAEKPYSCAECKETFSDNNRLVQHQKMHTVKTPYECQECGERFICGSTLKCHESVHAREKQGFFVSGKILDQNPEQKEKCFKCNKCEKTFSCSKYLTQHERIHTRGVKPFECDQCGKAFGQSTRLIHHQRIHSRVRLYKWGEQGKAISSASLIKLQSFHTKEHPFKCNECGKTFSHSAHLSKHQLIHAGENPFKCSKCDRVFTQRNYLVQHERTHARKKPLVCNECGKTFRQSSCLSKHQRIHSGEKPYVCDYCGKAFGLSAELVRHQRIHTGEKPYVCQECGKAFTQSSCLSIHRRVHTGEKPYRCGECGKAFAQKANLTQHQRIHTGEKPYSCNVCGKAFVLSAHLNQHLRVHTQETLYQCQRCQKAFRCHSSLSRHQRVHNKQQYCL
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
83PhosphorylationDVTETKNSPLMEDFF
CCCCCCCCCCHHHHH		22.44-
103PhosphorylationQEIIEMLSKDGFWNS
HHHHHHHHCCCCCCC		27.65-
135PhosphorylationDPESLLRSDIATNGE
CHHHHHHCCCCCCCC		33.0830206219
143PhosphorylationDIATNGESPTECKSH
CCCCCCCCCCHHHHH		38.2221815630
148SumoylationGESPTECKSHELKRG
CCCCCHHHHHHHHCC		48.9228112733
148AcetylationGESPTECKSHELKRG
CCCCCHHHHHHHHCC		48.9225953088
148UbiquitinationGESPTECKSHELKRG
CCCCCHHHHHHHHCC		48.92-
153AcetylationECKSHELKRGLSPVS
HHHHHHHHCCCCCCC		41.2426051181
157PhosphorylationHELKRGLSPVSTVST
HHHHCCCCCCCEEEC		26.5325849741
160PhosphorylationKRGLSPVSTVSTGED
HCCCCCCCEEECCCC		26.8625850435
161PhosphorylationRGLSPVSTVSTGEDS
CCCCCCCEEECCCCC		20.7925850435
163PhosphorylationLSPVSTVSTGEDSMV
CCCCCEEECCCCCCC		30.6822115753
164PhosphorylationSPVSTVSTGEDSMVH
CCCCEEECCCCCCCC		40.0122115753
176AcetylationMVHNVSEKTLTPAKS
CCCCCCCCCCCCCCC		41.1325953088
182AcetylationEKTLTPAKSKEYRGE
CCCCCCCCCCCCCCC		64.3626051181
184AcetylationTLTPAKSKEYRGEFF
CCCCCCCCCCCCCCC		59.0426051181
207SumoylationDSVQEGEKPYQCSEC
CCCCCCCCCEECCCC		60.94-
207SumoylationDSVQEGEKPYQCSEC
CCCCCCCCCEECCCC		60.94-
216AcetylationYQCSECGKSFSGSYR
EECCCCCCCCCCCEE		61.0526051181
235UbiquitinationWITHTREKPTVHQEC
EEEECCCCCCCHHHH		42.57-
235AcetylationWITHTREKPTVHQEC
EEEECCCCCCCHHHH		42.5725953088
262PhosphorylationYPKTHTGYKFYVCNE
ECCCCCCCEEEEECC		10.08-
265PhosphorylationTHTGYKFYVCNEYGT
CCCCCEEEEECCCCC		10.4329759185
270PhosphorylationKFYVCNEYGTTFSQS
EEEEECCCCCCCEEC		13.0429759185
279PhosphorylationTTFSQSTYLWHQKTH
CCCEECCEEEEECCC		17.03-
312UbiquitinationTQPGEHQKTHTDSKS
CCCCCCCCCCCCCCC		44.1521906983
318UbiquitinationQKTHTDSKSYNCNEC
CCCCCCCCCEECCHH		60.82-
318SumoylationQKTHTDSKSYNCNEC
CCCCCCCCCEECCHH		60.82-
318SumoylationQKTHTDSKSYNCNEC
CCCCCCCCCEECCHH		60.82-
327AcetylationYNCNECGKAFTRIFH
EECCHHHHHHHHHHH		52.5726051181
382AcetylationSECQECGKIFRHSSL
HHHHHHHHHHHCHHH		50.7826051181
382UbiquitinationSECQECGKIFRHSSL
HHHHHHHHHHHCHHH		50.78-
419SumoylationFRHNSTLKIHQRVHS
CCCCCCEEEEEECCC		37.9328112733
426PhosphorylationKIHQRVHSGEKPYKC
EEEEECCCCCCCEEC		45.8730177828
469PhosphorylationQECVRSFSRPSHLMR
HHHHHHCCCCHHHHH		44.5217081983
485AcetylationQAIHTAEKPYSCAEC
HHHCCCCCCCCHHHH		46.9526051181
485UbiquitinationQAIHTAEKPYSCAEC
HHHCCCCCCCCHHHH		46.95-
493UbiquitinationPYSCAECKETFSDNN
CCCHHHHHHHHCCCC		51.82-
493SumoylationPYSCAECKETFSDNN
CCCHHHHHHHHCCCC		51.82-
493SumoylationPYSCAECKETFSDNN
CCCHHHHHHHHCCCC		51.82-
507UbiquitinationNRLVQHQKMHTVKTP
CCEEEEEECCCCCCC		30.44-
512UbiquitinationHQKMHTVKTPYECQE
EEECCCCCCCCCHHH		44.96-
531UbiquitinationFICGSTLKCHESVHA
EEECCEEEECCCCCC		33.36-
541UbiquitinationESVHAREKQGFFVSG
CCCCCHHCCCEEEEC		50.60-
541AcetylationESVHAREKQGFFVSG
CCCCCHHCCCEEEEC		50.6025953088
549UbiquitinationQGFFVSGKILDQNPE
CCEEEECEECCCCHH		32.37-
549AcetylationQGFFVSGKILDQNPE
CCEEEECEECCCCHH		32.3725953088
549SumoylationQGFFVSGKILDQNPE
CCEEEECEECCCCHH		32.3728112733
558UbiquitinationLDQNPEQKEKCFKCN
CCCCHHHHHHHEECC		58.44-
558SumoylationLDQNPEQKEKCFKCN
CCCCHHHHHHHEECC		58.4428112733
558SumoylationLDQNPEQKEKCFKCN
CCCCHHHHHHHEECC		58.44-
598AcetylationFECDQCGKAFGQSTR
CCCCCCCHHHCCCHH		48.4426051181
620SumoylationHSRVRLYKWGEQGKA
HHHEEEEECCCCCCC		54.00-
620SumoylationHSRVRLYKWGEQGKA
HHHEEEEECCCCCCC		54.00-
632PhosphorylationGKAISSASLIKLQSF
CCCCCHHHEEEHHHC		32.3524719451
635SumoylationISSASLIKLQSFHTK
CCHHHEEEHHHCCCC		45.8528112733
635SumoylationISSASLIKLQSFHTK
CCHHHEEEHHHCCCC		45.85-
675SumoylationHAGENPFKCSKCDRV
ECCCCCCCCCCCCCE		38.56-
675SumoylationHAGENPFKCSKCDRV
ECCCCCCCCCCCCCE		38.56-
728SumoylationQRIHSGEKPYVCDYC
CHHHCCCCCEECCCC		45.21-
728SumoylationQRIHSGEKPYVCDYC
CHHHCCCCCEECCCC		45.21-
753PhosphorylationVRHQRIHTGEKPYVC
HHHCCCCCCCCCEEH		44.6728111955
756SumoylationQRIHTGEKPYVCQEC
CCCCCCCCCEEHHHH		42.89-
756SumoylationQRIHTGEKPYVCQEC
CCCCCCCCCEEHHHH		42.89-
781PhosphorylationSIHRRVHTGEKPYRC
HHHCCCCCCCCCEEC		44.15-
784UbiquitinationRRVHTGEKPYRCGEC
CCCCCCCCCEECCHH		49.01-
809PhosphorylationTQHQRIHTGEKPYSC
CCCCHHHCCCCCEEC		44.6728111955
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 ZN473_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN473_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 ZN473_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI41_HUMANTRIM41physical
16189514
GPT2L_HUMANGPATCH2Lphysical
25416956
ZN250_HUMANZNF250physical
25416956
AEN_HUMANAENphysical
25416956
DHX57_HUMANDHX57physical
25416956
ZN792_HUMANZNF792physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
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 ZN473_HUMAN

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Related Literatures of Post-Translational Modification

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