ZBTB1_HUMAN - dbPTM
ZBTB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBTB1_HUMAN
UniProt AC Q9Y2K1
Protein Name Zinc finger and BTB domain-containing protein 1
Gene Name ZBTB1
Organism Homo sapiens (Human).
Sequence Length 713
Subcellular Localization Nucleus . Nucleus, nucleoplasm . Localized in dot-like structures in the nucleus (PubMed:21706167). Colocalized with SMRT in nuclear bodies (PubMed:20797634). The sumoylated form is preferentially located in the nucleoplasm outside the nuclear bodies
Protein Description Acts as a transcriptional repressor. [PubMed: 20797634 Represses cAMP-responsive element (CRE)-mediated transcriptional activation]
Protein Sequence MAKPSHSSYVLQQLNNQREWGFLCDCCIAIDDIYFQAHKAVLAACSSYFRMFFMNHQHSTAQLNLSNMKISAECFDLILQFMYLGKIMTAPSSFEQFKVAMNYLQLYNVPDCLEDIQDADCSSSKCSSSASSKQNSKMIFGVRMYEDTVARNGNEANRWCAEPSSTVNTPHNREADEESLQLGNFPEPLFDVCKKSSVSKLSTPKERVSRRFGRSFTCDSCGFGFSCEKLLDEHVLTCTNRHLYQNTRSYHRIVDIRDGKDSNIKAEFGEKDSSKTFSAQTDKYRGDTSQAADDSASTTGSRKSSTVESEIASEEKSRAAERKRIIIKMEPEDIPTDELKDFNIIKVTDKDCNESTDNDELEDEPEEPFYRYYVEEDVSIKKSGRKTLKPRMSVSADERGGLENMRPPNNSSPVQEDAENASCELCGLTITEEDLSSHYLAKHIENICACGKCGQILVKGRQLQEHAQRCGEPQDLTMNGLGNTEEKMDLEENPDEQSEIRDMFVEMLDDFRDNHYQINSIQKKQLFKHSACPFRCPNCGQRFETENLVVEHMSSCLDQDMFKSAIMEENERDHRRKHFCNLCGKGFYQRCHLREHYTVHTKEKQFVCQTCGKQFLRERQLRLHNDMHKGMARYVCSICDQGNFRKHDHVRHMISHLSAGETICQVCFQIFPNNEQLEQHMDVHLYTCGICGAKFNLRKDMRSHYNAKHLKRT
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
3Sumoylation-----MAKPSHSSYV
-----CCCCCCHHHH		45.84-
3Ubiquitination-----MAKPSHSSYV
-----CCCCCCHHHH		45.8423000965
3Sumoylation-----MAKPSHSSYV
-----CCCCCCHHHH		45.8428112733
125UbiquitinationDADCSSSKCSSSASS
CCCCCCCCCCCCCCC		39.8321963094
137SumoylationASSKQNSKMIFGVRM
CCCCCCCEEEEEEEE		43.49-
137UbiquitinationASSKQNSKMIFGVRM
CCCCCCCEEEEEEEE		43.49-
137SumoylationASSKQNSKMIFGVRM
CCCCCCCEEEEEEEE		43.49-
164PhosphorylationNRWCAEPSSTVNTPH
CCCCCCCCCCCCCCC		30.1027251275
165PhosphorylationRWCAEPSSTVNTPHN
CCCCCCCCCCCCCCC		47.2721712546
166PhosphorylationWCAEPSSTVNTPHNR
CCCCCCCCCCCCCCH		23.3223312004
169PhosphorylationEPSSTVNTPHNREAD
CCCCCCCCCCCHHCC		22.9128985074
179PhosphorylationNREADEESLQLGNFP
CHHCCHHHHHCCCCC		21.2626657352
194UbiquitinationEPLFDVCKKSSVSKL
HHHHHHHHHCCCCCC		56.3829967540
195UbiquitinationPLFDVCKKSSVSKLS
HHHHHHHHCCCCCCC		42.72-
196PhosphorylationLFDVCKKSSVSKLST
HHHHHHHCCCCCCCC		22.8229457462
197PhosphorylationFDVCKKSSVSKLSTP
HHHHHHCCCCCCCCH		39.0129457462
199PhosphorylationVCKKSSVSKLSTPKE
HHHHCCCCCCCCHHH		29.8129457462
200SumoylationCKKSSVSKLSTPKER
HHHCCCCCCCCHHHH		44.28-
200SumoylationCKKSSVSKLSTPKER
HHHCCCCCCCCHHHH		44.2828112733
202PhosphorylationKSSVSKLSTPKERVS
HCCCCCCCCHHHHHH		46.5324719451
203PhosphorylationSSVSKLSTPKERVSR
CCCCCCCCHHHHHHH		49.1424719451
205SumoylationVSKLSTPKERVSRRF
CCCCCCHHHHHHHHH		59.2328112733
215PhosphorylationVSRRFGRSFTCDSCG
HHHHHCCCEECCCCC		25.8627080861
217PhosphorylationRRFGRSFTCDSCGFG
HHHCCCEECCCCCCC		19.3627080861
229UbiquitinationGFGFSCEKLLDEHVL
CCCCCHHHHHHCCCH		59.69-
239PhosphorylationDEHVLTCTNRHLYQN
HCCCHHCCCHHHHCC		30.0128555341
244PhosphorylationTCTNRHLYQNTRSYH
HCCCHHHHCCCCCEE		8.1328796482
260SumoylationIVDIRDGKDSNIKAE
EEECCCCCCCCEEEE		63.3728112733
262PhosphorylationDIRDGKDSNIKAEFG
ECCCCCCCCEEEEEC		43.8928555341
265UbiquitinationDGKDSNIKAEFGEKD
CCCCCCEEEEECCCC		46.2229967540
265SumoylationDGKDSNIKAEFGEKD
CCCCCCEEEEECCCC		46.2228112733
265SumoylationDGKDSNIKAEFGEKD
CCCCCCEEEEECCCC		46.22-
271AcetylationIKAEFGEKDSSKTFS
EEEEECCCCCCCCEE		64.3925953088
273PhosphorylationAEFGEKDSSKTFSAQ
EEECCCCCCCCEEEE		44.8127251275
274PhosphorylationEFGEKDSSKTFSAQT
EECCCCCCCCEEEEC		45.9427251275
275UbiquitinationFGEKDSSKTFSAQTD
ECCCCCCCCEEEECH		58.50-
275SumoylationFGEKDSSKTFSAQTD
ECCCCCCCCEEEECH		58.5025218447
275SumoylationFGEKDSSKTFSAQTD
ECCCCCCCCEEEECH		58.50-
276PhosphorylationGEKDSSKTFSAQTDK
CCCCCCCCEEEECHH		25.4427251275
278PhosphorylationKDSSKTFSAQTDKYR
CCCCCCEEEECHHCC		25.3827251275
281PhosphorylationSKTFSAQTDKYRGDT
CCCEEEECHHCCCCC		33.8927251275
283SumoylationTFSAQTDKYRGDTSQ
CEEEECHHCCCCCCH		39.9928112733
283UbiquitinationTFSAQTDKYRGDTSQ
CEEEECHHCCCCCCH		39.9929967540
284PhosphorylationFSAQTDKYRGDTSQA
EEEECHHCCCCCCHH		23.7329449344
288PhosphorylationTDKYRGDTSQAADDS
CHHCCCCCCHHCCCC		26.0920068231
289PhosphorylationDKYRGDTSQAADDSA
HHCCCCCCHHCCCCC		23.6721815630
295PhosphorylationTSQAADDSASTTGSR
CCHHCCCCCCCCCCC		25.3530576142
297PhosphorylationQAADDSASTTGSRKS
HHCCCCCCCCCCCCC		30.3830576142
298PhosphorylationAADDSASTTGSRKSS
HCCCCCCCCCCCCCH		34.5930108239
299PhosphorylationADDSASTTGSRKSST
CCCCCCCCCCCCCHH		30.5728450419
301PhosphorylationDSASTTGSRKSSTVE
CCCCCCCCCCCHHHH		34.1528450419
303SumoylationASTTGSRKSSTVESE
CCCCCCCCCHHHHHH		50.91-
303UbiquitinationASTTGSRKSSTVESE
CCCCCCCCCHHHHHH		50.91-
303SumoylationASTTGSRKSSTVESE
CCCCCCCCCHHHHHH		50.9128112733
304PhosphorylationSTTGSRKSSTVESEI
CCCCCCCCHHHHHHH		30.0825159151
305PhosphorylationTTGSRKSSTVESEIA
CCCCCCCHHHHHHHH		39.2425159151
306PhosphorylationTGSRKSSTVESEIAS
CCCCCCHHHHHHHHC		35.0725159151
309PhosphorylationRKSSTVESEIASEEK
CCCHHHHHHHHCHHH		29.9328450419
313PhosphorylationTVESEIASEEKSRAA
HHHHHHHCHHHHHHH		52.5325159151
316SumoylationSEIASEEKSRAAERK
HHHHCHHHHHHHHHC		40.9928112733
316SumoylationSEIASEEKSRAAERK
HHHHCHHHHHHHHHC		40.99-
316UbiquitinationSEIASEEKSRAAERK
HHHHCHHHHHHHHHC		40.99-
317PhosphorylationEIASEEKSRAAERKR
HHHCHHHHHHHHHCC		30.3623312004
328SumoylationERKRIIIKMEPEDIP
HHCCEEEECCHHCCC		27.1428112733
328SumoylationERKRIIIKMEPEDIP
HHCCEEEECCHHCCC		27.14-
340UbiquitinationDIPTDELKDFNIIKV
CCCCHHHCCCCEEEE		59.22-
340SumoylationDIPTDELKDFNIIKV
CCCCHHHCCCCEEEE		59.2228112733
346SumoylationLKDFNIIKVTDKDCN
HCCCCEEEECCCCCC		34.9728112733
346UbiquitinationLKDFNIIKVTDKDCN
HCCCCEEEECCCCCC		34.9729967540
346SumoylationLKDFNIIKVTDKDCN
HCCCCEEEECCCCCC		34.97-
348PhosphorylationDFNIIKVTDKDCNES
CCCEEEECCCCCCCC		32.1222617229
355PhosphorylationTDKDCNESTDNDELE
CCCCCCCCCCCCCCC		27.3723401153
356PhosphorylationDKDCNESTDNDELED
CCCCCCCCCCCCCCC		32.4222617229
373PhosphorylationEEPFYRYYVEEDVSI
CCCCHHHHHHCCEEE		7.7422210691
379PhosphorylationYYVEEDVSIKKSGRK
HHHHCCEEECCCCCC		40.8022210691
381UbiquitinationVEEDVSIKKSGRKTL
HHCCEEECCCCCCCC		33.1233845483
381SumoylationVEEDVSIKKSGRKTL
HHCCEEECCCCCCCC		33.1228112733
393PhosphorylationKTLKPRMSVSADERG
CCCCCCCCCCHHHCC		17.7529255136
395PhosphorylationLKPRMSVSADERGGL
CCCCCCCCHHHCCCC		23.7730108239
411PhosphorylationNMRPPNNSSPVQEDA
CCCCCCCCCCCHHHH		42.5328731282
412PhosphorylationMRPPNNSSPVQEDAE
CCCCCCCCCCHHHHH		31.0830576142
422PhosphorylationQEDAENASCELCGLT
HHHHHHCCCEECCCE		21.5027080861
429PhosphorylationSCELCGLTITEEDLS
CCEECCCEEEHHHHH		15.9027080861
437PhosphorylationITEEDLSSHYLAKHI
EEHHHHHHHHHHHHH		24.3722210691
439PhosphorylationEEDLSSHYLAKHIEN
HHHHHHHHHHHHHHH		15.4222210691
459SumoylationKCGQILVKGRQLQEH
CCCCEEECCHHHHHH		44.95-
459SumoylationKCGQILVKGRQLQEH
CCCCEEECCHHHHHH		44.95-
459UbiquitinationKCGQILVKGRQLQEH
CCCCEEECCHHHHHH		44.95-
516PhosphorylationDDFRDNHYQINSIQK
HHHHHCCCCCCCCCH		19.8327642862
520PhosphorylationDNHYQINSIQKKQLF
HCCCCCCCCCHHHHH		28.2025159151
523UbiquitinationYQINSIQKKQLFKHS
CCCCCCCHHHHHCCC		40.6029967540
528UbiquitinationIQKKQLFKHSACPFR
CCHHHHHCCCCCCCC		45.2929967540
528SumoylationIQKKQLFKHSACPFR
CCHHHHHCCCCCCCC		45.2928112733
563SumoylationCLDQDMFKSAIMEEN
HCCHHHHHHHHHHHH		32.1328112733
564PhosphorylationLDQDMFKSAIMEENE
CCHHHHHHHHHHHHH		16.2620860994
577UbiquitinationNERDHRRKHFCNLCG
HHHHHHHHHHHHHCC		40.78-
585UbiquitinationHFCNLCGKGFYQRCH
HHHHHCCCCHHHHHH		44.87-
601PhosphorylationREHYTVHTKEKQFVC
HCCEEEECCCCEEEE		36.2420068231
604UbiquitinationYTVHTKEKQFVCQTC
EEEECCCCEEEEHHC		51.06-
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 ZBTB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
265KSumoylation

20797634
328KSumoylation

20797634
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 ZBTB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAML3_HUMANMAML3physical
20211142
PCNA_HUMANPCNAphysical
24657165
MTA2_HUMANMTA2physical
24657165
TIF1B_HUMANTRIM28physical
24657165
ZBTB2_HUMANZBTB2physical
24657165
MEP50_HUMANWDR77physical
24657165
TRI33_HUMANTRIM33physical
24657165
RBM10_HUMANRBM10physical
24657165
RS14_HUMANRPS14physical
24657165
CCAR2_HUMANCCAR2physical
24657165
HSP7C_HUMANHSPA8physical
24657165
FLNA_HUMANFLNAphysical
24657165
DDX1_HUMANDDX1physical
24657165
BCLF1_HUMANBCLAF1physical
24657165
RS16_HUMANRPS16physical
24657165
RL27A_HUMANRPL27Aphysical
24657165
PSMD2_HUMANPSMD2physical
24657165
RS23_HUMANRPS23physical
24657165
TGM3_HUMANTGM3physical
24657165
RL11_HUMANRPL11physical
24657165
RL30_HUMANRPL30physical
24657165
RS29_HUMANRPS29physical
24657165
H15_HUMANHIST1H1Bphysical
24657165
RL13A_HUMANRPL13Aphysical
24657165
STK38_HUMANSTK38physical
24657165
SRSF1_HUMANSRSF1physical
24657165
SRSF7_HUMANSRSF7physical
24657165
SPR2E_HUMANSPRR2Ephysical
24657165
O51B4_HUMANOR51B4physical
24657165
RL34_HUMANRPL34physical
24657165
H2AZ_HUMANH2AFZphysical
24657165
RL24_HUMANRPL24physical
24657165
RL27_HUMANRPL27physical
24657165
IF4B_HUMANEIF4Bphysical
24657165
MUCL1_HUMANMUCL1physical
24657165
HSPB1_HUMANHSPB1physical
24657165
PEO1_HUMANC10orf2physical
24657165
RL3_HUMANRPL3physical
24657165
RLA0_HUMANRPLP0physical
24657165
ROA3_HUMANHNRNPA3physical
24657165
MPCP_HUMANSLC25A3physical
24657165
HNRPR_HUMANHNRNPRphysical
24657165
BLMH_HUMANBLMHphysical
24657165
RL18_HUMANRPL18physical
24657165
RS13_HUMANRPS13physical
24657165
DESP_HUMANDSPphysical
24657165
CS043_HUMANC19orf43physical
24657165
WIZ_HUMANWIZphysical
24657165
ECHA_HUMANHADHAphysical
24657165
RS27_HUMANRPS27physical
24657165
RL14_HUMANRPL14physical
24657165
TBB4B_HUMANTUBB4Bphysical
24657165
RSMN_HUMANSNRPNphysical
24657165
ANXA1_HUMANANXA1physical
24657165
HS71L_HUMANHSPA1Lphysical
24657165
RSSA_HUMANRPSAphysical
24657165
PDE4D_HUMANPDE4Dphysical
24657165
GDIR2_HUMANARHGDIBphysical
24657165
ADT3_HUMANSLC25A6physical
24657165
MTCL1_HUMANMTCL1physical
24657165
CCD42_HUMANCCDC42physical
24657165
RL8_HUMANRPL8physical
24657165
P66B_HUMANGATAD2Bphysical
24657165
RS15A_HUMANRPS15Aphysical
24657165
KIF14_HUMANKIF14physical
24657165
TESK2_HUMANTESK2physical
24657165
RS9_HUMANRPS9physical
24657165
RS25_HUMANRPS25physical
24657165
RS4X_HUMANRPS4Xphysical
24657165
SPTN1_HUMANSPTAN1physical
24657165
CRNN_HUMANCRNNphysical
24657165
SMD3_HUMANSNRPD3physical
24657165
NUCL_HUMANNCLphysical
24657165
RS11_HUMANRPS11physical
24657165
RU2A_HUMANSNRPA1physical
24657165
RS8_HUMANRPS8physical
24657165
TBA1B_HUMANTUBA1Bphysical
24657165
SF3A1_HUMANSF3A1physical
24657165
ACTB_HUMANACTBphysical
24657165
TBB5_HUMANTUBBphysical
24657165
F161A_HUMANFAM161Aphysical
25416956
ZN572_HUMANZNF572physical
25416956
ZN417_HUMANZNF417physical
25416956
TRI42_HUMANTRIM42physical
25416956
UBC_HUMANUBCphysical
24657165
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 ZBTB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND THR-356, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND MASSSPECTROMETRY.

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