ZN33B_HUMAN - dbPTM
ZN33B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN33B_HUMAN
UniProt AC Q06732
Protein Name Zinc finger protein 33B
Gene Name ZNF33B
Organism Homo sapiens (Human).
Sequence Length 778
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNKVDQKFQGSVSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVGYCAHKPEVIFRLEQGEEPWRLEEEFPSQSFPEVWTADHLKERSQENQSKHLWEVVFINNEMLTKEQGNVIGIPFNMDVSSFPSRKMFCQYDSRGMSFNTVSELVISKINYLGKKSDEFNACGKLLLNIKHDETHTREKNEVLKNRNTLSHRENTLQHEKIQTLDHNFEYSICQETLLEKAVFNTRKRENAEENNCDYNEFGRTFCDSSSLLFHQIPPSKDSHYEFSDCEKFLCVKSTLSKHDGVPVKHYDCGESGNNFRRKLCLSQLQKGDKGEKHFECNECGKAFWEKSHLTRHQRVHTGEKHFQCNQCGKTFWEKSNLTKHQRSHTGEKPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNACGKTFYQKSDLTKHQRTHTGQKPYECYECGKSFCMNSHLTVHQRTHTGEKPFECLECGKSFCQKSHLTQHQRTHIGDKPYECNACGKTFYHKSVLTRHQIIHTGLKPYECYECGKTFCLKSDLTIHQRTHTGEKPFACPECGKFFSHKSTLSQHYRTHTGEKPYECHECGKIFYNKSYLTKHNRTHTGEKPYECNECGKTFCQKSQLTQHQRIHIGEKPYECNECGKAFCHKSALIVHQRTHTQEKPYKCNECGKSFCVKSGLILHERKHTGEKPYECNECGKSFSHKSSLTVHHRAHTGEKSCQCNECGKIFYRKSDLAKHQRSHTGEKPYECNTCRKTFSQKSNLIVHQRTHIGEKPYE
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
13PhosphorylationQKFQGSVSFKDVTVG
HHHCCCEEEEEEEEE		28.4224719451
18PhosphorylationSVSFKDVTVGFTQEE
CEEEEEEEEEECHHH		25.6625002506
22PhosphorylationKDVTVGFTQEEWQHL
EEEEEEECHHHHHHC		29.1925002506
32PhosphorylationEWQHLDPSQRALYRD
HHHHCCHHHHHHHHH		31.7825002506
167PhosphorylationINYLGKKSDEFNACG
HHHCCCCCHHCCCHH		45.9528555341
173UbiquitinationKSDEFNACGKLLLNI
CCHHCCCHHHHHHHC		5.32-
181SumoylationGKLLLNIKHDETHTR
HHHHHHCCCCCCCHH		43.8828112733
202UbiquitinationKNRNTLSHRENTLQH
HCCHHCCHHHHHHHH		44.16-
287UbiquitinationCEKFLCVKSTLSKHD
CCEEEEEHHHHCCCC		36.4029967540
294UbiquitinationKSTLSKHDGVPVKHY
HHHHCCCCCCEECCC		64.62-
321SumoylationLCLSQLQKGDKGEKH
HHHHHHHCCCCCCCC		77.12-
328SumoylationKGDKGEKHFECNECG
CCCCCCCCEEECHHH		21.31-
341SumoylationCGKAFWEKSHLTRHQ
HHHHHHHHHCCCHHC		33.50-
343UbiquitinationKAFWEKSHLTRHQRV
HHHHHHHCCCHHCCC		42.14-
348UbiquitinationKSHLTRHQRVHTGEK
HHCCCHHCCCCCCCC		45.89-
348SumoylationKSHLTRHQRVHTGEK
HHCCCHHCCCCCCCC		45.89-
355AcetylationQRVHTGEKHFQCNQC
CCCCCCCCEEEECCC		51.5720167786
362AcetylationKHFQCNQCGKTFWEK
CEEEECCCCCCHHHH		3.62-
364AcetylationFQCNQCGKTFWEKSN
EEECCCCCCHHHHCC		48.4520167786
371AcetylationKTFWEKSNLTKHQRS
CCHHHHCCCCCCCCC		63.90-
383AcetylationQRSHTGEKPFECNEC
CCCCCCCCCEECCCC		57.2525443231
390UbiquitinationKPFECNECGKAFSHK
CCEECCCCCCCCCCC		4.16-
390AcetylationKPFECNECGKAFSHK
CCEECCCCCCCCCCC		4.16-
406PhosphorylationALTLHQRTHTGEKPY
CEEEECCCCCCCCCE		19.74-
408PhosphorylationTLHQRTHTGEKPYQC
EEECCCCCCCCCEEC		46.56-
418UbiquitinationKPYQCNACGKTFYQK
CCEECCCCCCEEECC		3.41-
434PhosphorylationDLTKHQRTHTGQKPY
CCCCCCCCCCCCCCE		19.7428258704
462PhosphorylationHLTVHQRTHTGEKPF
CEEEEECCCCCCCCE		19.74-
464PhosphorylationTVHQRTHTGEKPFEC
EEEECCCCCCCCEEH		46.56-
474UbiquitinationKPFECLECGKSFCQK
CCEEHHHCCHHHHHH		5.55-
546PhosphorylationDLTIHQRTHTGEKPF
CCEEEECCCCCCCCE		19.74-
548PhosphorylationTIHQRTHTGEKPFAC
EEEECCCCCCCCEEC		46.56-
574PhosphorylationTLSQHYRTHTGEKPY
HHHHHHHHCCCCCCE		19.34-
576PhosphorylationSQHYRTHTGEKPYEC
HHHHHHCCCCCCEEE		46.56-
591PhosphorylationHECGKIFYNKSYLTK
CCCCCEEECHHHHCC		25.75-
593SumoylationCGKIFYNKSYLTKHN
CCCEEECHHHHCCCC		29.15-
595PhosphorylationKIFYNKSYLTKHNRT
CEEECHHHHCCCCCC		21.72-
600SumoylationKSYLTKHNRTHTGEK
HHHHCCCCCCCCCCC		52.69-
602PhosphorylationYLTKHNRTHTGEKPY
HHCCCCCCCCCCCCC		29.1628348404
604PhosphorylationTKHNRTHTGEKPYEC
CCCCCCCCCCCCCCC		46.5629496963
614UbiquitinationKPYECNECGKTFCQK
CCCCCCCCCCCCCCH		4.16-
642UbiquitinationKPYECNECGKAFCHK
CCCCCCCCCCCEECC		4.16-
666SumoylationHTQEKPYKCNECGKS
CCCCCCCCCCCCCCE		38.83-
673SumoylationKCNECGKSFCVKSGL
CCCCCCCEEEEECCC		14.79-
673PhosphorylationKCNECGKSFCVKSGL
CCCCCCCEEEEECCC		14.7930108239
688PhosphorylationILHERKHTGEKPYEC
EEEECCCCCCCCEEC		50.5023532336
698UbiquitinationKPYECNECGKSFSHK
CCEECCCCCCCCCCC		5.31-
703PhosphorylationNECGKSFSHKSSLTV
CCCCCCCCCCCCCEE		36.78-
735UbiquitinationKIFYRKSDLAKHQRS
CEEEEHHHHHHHHHH		54.39-
761SumoylationCRKTFSQKSNLIVHQ
CCCCCCCCCCEEEEE		39.86-
768SumoylationKSNLIVHQRTHIGEK
CCCEEEEECCCCCCC		40.86-
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 ZN33B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN33B_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 ZN33B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAP1_HUMANHAP1physical
15383276
ZHX1_HUMANZHX1physical
15383276
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 ZN33B_HUMAN

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Related Literatures of Post-Translational Modification

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