ZN330_HUMAN - dbPTM
ZN330_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN330_HUMAN
UniProt AC Q9Y3S2
Protein Name Zinc finger protein 330
Gene Name ZNF330
Organism Homo sapiens (Human).
Sequence Length 320
Subcellular Localization Nucleus . Nucleus, nucleolus . Chromosome, centromere . Predominantly expressed in the nucleolus. In mitosis associated with centromeres and concentrated at the midbody in cytokinesis.
Protein Description
Protein Sequence MPKKKTGARKKAENRREREKQLRASRSTIDLAKHPCNASMECDKCQRRQKNRAFCYFCNSVQKLPICAQCGKTKCMMKSSDCVIKHAGVYSTGLAMVGAICDFCEAWVCHGRKCLSTHACACPLTDAECVECERGVWDHGGRIFSCSFCHNFLCEDDQFEHQASCQVLEAETFKCVSCNRLGQHSCLRCKACFCDDHTRSKVFKQEKGKQPPCPKCGHETQETKDLSMSTRSLKFGRQTGGEEGDGASGYDAYWKNLSSDKYGDTSYHDEEEDEYEAEDDEEEEDEGRKDSDTESSDLFTNLNLGRTYASGYAHYEEQEN
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
11UbiquitinationKKTGARKKAENRRER
CCCCHHHHHHHHHHH		56.21-
25PhosphorylationREKQLRASRSTIDLA
HHHHHHHHHHHHHHH		21.9623403867
27PhosphorylationKQLRASRSTIDLAKH
HHHHHHHHHHHHHHC		27.5023911959
28PhosphorylationQLRASRSTIDLAKHP
HHHHHHHHHHHHHCC		19.8723403867
33UbiquitinationRSTIDLAKHPCNASM
HHHHHHHHCCCCCCC		56.21-
33AcetylationRSTIDLAKHPCNASM
HHHHHHHHCCCCCCC		56.2125953088
44UbiquitinationNASMECDKCQRRQKN
CCCCCCHHHHHHHCC		43.88-
60PhosphorylationAFCYFCNSVQKLPIC
EEHHHCCCCCCCCEE		27.4027080861
72UbiquitinationPICAQCGKTKCMMKS
CEEHHCCCCEEEECC		53.06-
72AcetylationPICAQCGKTKCMMKS
CEEHHCCCCEEEECC		53.0625953088
78UbiquitinationGKTKCMMKSSDCVIK
CCCEEEECCCCEEEE		21.66-
113UbiquitinationAWVCHGRKCLSTHAC
HHHCCCCCCCCCCCE		44.0821890473
114S-palmitoylationWVCHGRKCLSTHACA
HHCCCCCCCCCCCEE		3.3221044946
120S-palmitoylationKCLSTHACACPLTDA
CCCCCCCEECCCCCH		2.8821044946
122S-palmitoylationLSTHACACPLTDAEC
CCCCCEECCCCCHHH		2.6021044946
129S-palmitoylationCPLTDAECVECERGV
CCCCCHHHEECCCCC		3.1521044946
132S-palmitoylationTDAECVECERGVWDH
CCHHHEECCCCCCCC		1.8421044946
201AcetylationCDDHTRSKVFKQEKG
ECCCCHHHHHHHHCC		48.6924848155
201UbiquitinationCDDHTRSKVFKQEKG
ECCCCHHHHHHHHCC		48.69-
204SumoylationHTRSKVFKQEKGKQP
CCHHHHHHHHCCCCC		61.61-
204SumoylationHTRSKVFKQEKGKQP
CCHHHHHHHHCCCCC		61.61-
215UbiquitinationGKQPPCPKCGHETQE
CCCCCCCCCCCCCHH		60.61-
227PhosphorylationTQETKDLSMSTRSLK
CHHHCCCCHHHCCEE		22.3321815630
229PhosphorylationETKDLSMSTRSLKFG
HHCCCCHHHCCEECC		19.7923403867
230PhosphorylationTKDLSMSTRSLKFGR
HCCCCHHHCCEECCC		18.6823403867
232PhosphorylationDLSMSTRSLKFGRQT
CCCHHHCCEECCCCC		35.6825159151
234UbiquitinationSMSTRSLKFGRQTGG
CHHHCCEECCCCCCC		47.20-
237MethylationTRSLKFGRQTGGEEG
HCCEECCCCCCCCCC		33.74115920477
239PhosphorylationSLKFGRQTGGEEGDG
CEECCCCCCCCCCCC		45.8828555341
248PhosphorylationGEEGDGASGYDAYWK
CCCCCCCCCCCHHHC		43.3328796482
250PhosphorylationEGDGASGYDAYWKNL
CCCCCCCCCHHHCCC		8.5628796482
253PhosphorylationGASGYDAYWKNLSSD
CCCCCCHHHCCCCCC		17.6428796482
255UbiquitinationSGYDAYWKNLSSDKY
CCCCHHHCCCCCCCC		35.0221906983
258PhosphorylationDAYWKNLSSDKYGDT
CHHHCCCCCCCCCCC		45.9827642862
262PhosphorylationKNLSSDKYGDTSYHD
CCCCCCCCCCCCCCC		25.8130576142
265PhosphorylationSSDKYGDTSYHDEEE
CCCCCCCCCCCCCCC		27.1627642862
267PhosphorylationDKYGDTSYHDEEEDE
CCCCCCCCCCCCCCC		18.5130576142
275PhosphorylationHDEEEDEYEAEDDEE
CCCCCCCCCCCCCHH		32.5328796482
289AcetylationEEEDEGRKDSDTESS
HHCCCCCCCCCCCCH		72.8820167786
291PhosphorylationEDEGRKDSDTESSDL
CCCCCCCCCCCCHHH		49.8430266825
293PhosphorylationEGRKDSDTESSDLFT
CCCCCCCCCCHHHHH		41.5430266825
295PhosphorylationRKDSDTESSDLFTNL
CCCCCCCCHHHHHHC		31.1130266825
296PhosphorylationKDSDTESSDLFTNLN
CCCCCCCHHHHHHCC		31.9130266825
300PhosphorylationTESSDLFTNLNLGRT
CCCHHHHHHCCCCCC		46.2027732954
307PhosphorylationTNLNLGRTYASGYAH
HHCCCCCCCCCCCCC		22.9527642862
308PhosphorylationNLNLGRTYASGYAHY
HCCCCCCCCCCCCCC		9.4522817900
310PhosphorylationNLGRTYASGYAHYEE
CCCCCCCCCCCCCCC		23.1729978859
312PhosphorylationGRTYASGYAHYEEQE
CCCCCCCCCCCCCCC		6.4229978859
315PhosphorylationYASGYAHYEEQEN--
CCCCCCCCCCCCC--		17.0028796482
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 ZN330_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN330_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 ZN330_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN330_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 ZN330_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-308 AND TYR-315, ANDMASS SPECTROMETRY.

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