ZN207_HUMAN - dbPTM
ZN207_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN207_HUMAN
UniProt AC O43670
Protein Name BUB3-interacting and GLEBS motif-containing protein ZNF207 {ECO:0000303|PubMed:24462186, ECO:0000303|PubMed:24462187}
Gene Name ZNF207 {ECO:0000312|HGNC:HGNC:12998}
Organism Homo sapiens (Human).
Sequence Length 478
Subcellular Localization Nucleus . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from k
Protein Description Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly. [PubMed: 24462186]
Protein Sequence MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQAPIGNPPVGPIGGMMPPQPGIPQQQGMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY
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
10AcetylationRKKKKQLKPWCWYCN
CCCCCCCCCCCEECC		33.7026051181
24UbiquitinationNRDFDDEKILIQHQK
CCCCCCHHHHHHHHH		50.2121906983
24 (in isoform 3)Ubiquitination-50.2121906983
24 (in isoform 2)Ubiquitination-50.2121906983
24 (in isoform 1)Ubiquitination-50.2121906983
24AcetylationNRDFDDEKILIQHQK
CCCCCCHHHHHHHHH		50.2125953088
31AcetylationKILIQHQKAKHFKCH
HHHHHHHHCCCCCCE		58.2225953088
31UbiquitinationKILIQHQKAKHFKCH
HHHHHHHHCCCCCCE		58.2233845483
36AcetylationHQKAKHFKCHICHKK
HHHCCCCCCEECCCC		25.3123749302
42AcetylationFKCHICHKKLYTGPG
CCCEECCCCCCCCCC		39.8130593627
43AcetylationKCHICHKKLYTGPGL
CCEECCCCCCCCCCH		24.0626051181
45PhosphorylationHICHKKLYTGPGLAI
EECCCCCCCCCCHHH		20.6628442448
46PhosphorylationICHKKLYTGPGLAIH
ECCCCCCCCCCHHHE		47.5428442448
59UbiquitinationIHCMQVHKETIDAVP
HEEEEHHHHHHHCCC		58.6633845483
88UbiquitinationGMEGIPEKDMDERRR
CCCCCCHHCHHHHHH		53.6632015554
100 (in isoform 2)Ubiquitination-42.6821906983
100UbiquitinationRRRLLEQKTQESQKK
HHHHHHHHHHHHHHH		42.6833845483
100 (in isoform 1)Ubiquitination-42.6821906983
100AcetylationRRRLLEQKTQESQKK
HHHHHHHHHHHHHHH		42.6826051181
101PhosphorylationRRLLEQKTQESQKKK
HHHHHHHHHHHHHHH		36.9426074081
104PhosphorylationLEQKTQESQKKKQQD
HHHHHHHHHHHHHHC		37.1726074081
113PhosphorylationKKKQQDDSDEYDDDD
HHHHHCCCCCCCCCC		40.4026074081
116PhosphorylationQQDDSDEYDDDDSAA
HHCCCCCCCCCCCCC		29.6626074081
273 (in isoform 2)Phosphorylation-41.7425159151
314O-linked_GlycosylationLNSTPATTTEPPKPT
CCCCCCCCCCCCCCC		31.1330059200
315O-linked_GlycosylationNSTPATTTEPPKPTF
CCCCCCCCCCCCCCC		41.9830059200
321O-linked_GlycosylationTTEPPKPTFPAYTQS
CCCCCCCCCCCCCCC		48.6730059200
328PhosphorylationTFPAYTQSTASTTST
CCCCCCCCCCCCCCC		20.3830576142
335UbiquitinationSTASTTSTTNSTAAK
CCCCCCCCCCCCCCC		28.0933845483
335PhosphorylationSTASTTSTTNSTAAK
CCCCCCCCCCCCCCC		28.0930576142
336PhosphorylationTASTTSTTNSTAAKP
CCCCCCCCCCCCCCC		27.2630576142
346PhosphorylationTAAKPAASITSKPAT
CCCCCCCCCCCCCEE		28.6225159151
347UbiquitinationAAKPAASITSKPATL
CCCCCCCCCCCCEEE		4.2929967540
348PhosphorylationAKPAASITSKPATLT
CCCCCCCCCCCEEEE		28.3623312004
349O-linked_GlycosylationKPAASITSKPATLTT
CCCCCCCCCCEEEEC		34.6630059200
349PhosphorylationKPAASITSKPATLTT
CCCCCCCCCCEEEEC		34.6623312004
350AcetylationPAASITSKPATLTTT
CCCCCCCCCEEEECC		29.9825953088
350UbiquitinationPAASITSKPATLTTT
CCCCCCCCCEEEECC		29.9833845483
353PhosphorylationSITSKPATLTTTSAT
CCCCCCEEEECCCCC		32.9121406692
355PhosphorylationTSKPATLTTTSATSK
CCCCEEEECCCCCCC		24.5521406692
356PhosphorylationSKPATLTTTSATSKL
CCCEEEECCCCCCCC		23.1321406692
357PhosphorylationKPATLTTTSATSKLI
CCEEEECCCCCCCCC		15.8921406692
358PhosphorylationPATLTTTSATSKLIH
CEEEECCCCCCCCCC		27.7021406692
360PhosphorylationTLTTTSATSKLIHPD
EEECCCCCCCCCCCC		26.6021406692
361PhosphorylationLTTTSATSKLIHPDE
EECCCCCCCCCCCCC		25.7721406692
362AcetylationTTTSATSKLIHPDED
ECCCCCCCCCCCCCC		47.2923236377
362UbiquitinationTTTSATSKLIHPDED
ECCCCCCCCCCCCCC		47.2929967540
366UbiquitinationATSKLIHPDEDISLE
CCCCCCCCCCCCCHH		39.4333845483
371PhosphorylationIHPDEDISLEERRAQ
CCCCCCCCHHHHHHH		41.89-
378UbiquitinationSLEERRAQLPKYQRN
CHHHHHHHCCHHHHC		57.3929967540
381UbiquitinationERRAQLPKYQRNLPR
HHHHHCCHHHHCCCC		63.7129967540
397UbiquitinationGQAPIGNPPVGPIGG
CCCCCCCCCCCCCCC		21.5329967540
468MethylationPRPPMGMRPPVMSQG
CCCCCCCCCCCCCCC		27.0054561931
468DimethylationPRPPMGMRPPVMSQG
CCCCCCCCCCCCCCC		27.00-
477DimethylationPVMSQGGRY------
CCCCCCCCC------		40.59-
477MethylationPVMSQGGRY------
CCCCCCCCC------		40.5954561937
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 ZN207_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN207_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 ZN207_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUB3_HUMANBUB3physical
22365833
HNRL1_HUMANHNRNPUL1physical
22365833
MEP50_HUMANWDR77physical
22365833
HNRPM_HUMANHNRNPMphysical
22365833
BUB3_HUMANBUB3physical
26344197
UBR5_HUMANUBR5physical
26438829
IMB1_HUMANKPNB1physical
26438829
BUB3_HUMANBUB3physical
26438829
BUB3_HUMANBUB3physical
26472760
HS105_HUMANHSPH1physical
26472760
ZN207_HUMANZNF207physical
26472760
PUF60_HUMANPUF60physical
26472760
SRS11_HUMANSRSF11physical
26472760
DPY30_HUMANDPY30physical
26472760
S10A9_HUMANS100A9physical
26472760
SET1A_HUMANSETD1Aphysical
26472760
TRAP1_HUMANTRAP1physical
27173435
SND1_HUMANSND1physical
27173435
ANXA5_HUMANANXA5physical
27173435
IF2P_HUMANEIF5Bphysical
27173435
G6PI_HUMANGPIphysical
27173435
IDHP_HUMANIDH2physical
27173435
PDIA3_HUMANPDIA3physical
27173435
UBE2N_HUMANUBE2Nphysical
27173435
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 ZN207_HUMAN

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Related Literatures of Post-Translational Modification

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