TYY1_HUMAN - dbPTM
TYY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TYY1_HUMAN
UniProt AC P25490
Protein Name Transcriptional repressor protein YY1
Gene Name YY1
Organism Homo sapiens (Human).
Sequence Length 414
Subcellular Localization Nucleus matrix . Associated with the nuclear matrix.
Protein Description Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. [PubMed: 15329343 Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions Plays a role in regulating enhancer activation]
Protein Sequence MASGDTLYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGEEEEEDDDDEDGGGGDHGGGGGHGHAGHHHHHHHHHHHPPMIALQPLVTDDPTQVHHHQEVILVQTREEVVGGDDSDGLRAEDGFEDQILIPVPAPAGGDDDYIEQTLVTVAAAGKSGGGGSSSSGGGRVKKGGGKKSGKKSYLSGGAGAAGGGGADPGNKKWEQKQVQIKTLEGEFSVTMWSSDEKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ
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
8PhosphorylationMASGDTLYIATDGSE
CCCCCEEEEECCCCC		7.21-
39PhosphorylationPVETIETTVVGEEEE
ECEEEEEEEECCCCC		10.6221253604
118PhosphorylationEVVGGDDSDGLRAED
EECCCCCCCCCCCCC		38.0129255136
145PhosphorylationPAGGDDDYIEQTLVT
CCCCCCHHHHHHEEE		17.2229496963
158SumoylationVTVAAAGKSGGGGSS
EEEECCCCCCCCCCC		41.00-
165PhosphorylationKSGGGGSSSSGGGRV
CCCCCCCCCCCCCCC		31.62-
173UbiquitinationSSGGGRVKKGGGKKS
CCCCCCCCCCCCCCC		44.3229967540
174AcetylationSGGGRVKKGGGKKSG
CCCCCCCCCCCCCCC		60.9988987
180PhosphorylationKKGGGKKSGKKSYLS
CCCCCCCCCCCCCCC		60.37-
182SumoylationGGGKKSGKKSYLSGG
CCCCCCCCCCCCCCC		45.7128112733
183UbiquitinationGGKKSGKKSYLSGGA
CCCCCCCCCCCCCCC		48.1029967540
183SumoylationGGKKSGKKSYLSGGA
CCCCCCCCCCCCCCC		48.1028112733
183AcetylationGGKKSGKKSYLSGGA
CCCCCCCCCCCCCCC		48.1026051181
183MethylationGGKKSGKKSYLSGGA
CCCCCCCCCCCCCCC		48.1054431537
183SumoylationGGKKSGKKSYLSGGA
CCCCCCCCCCCCCCC		48.10-
184PhosphorylationGKKSGKKSYLSGGAG
CCCCCCCCCCCCCCC		34.4925159151
185PhosphorylationKKSGKKSYLSGGAGA
CCCCCCCCCCCCCCC		17.4829978859
187PhosphorylationSGKKSYLSGGAGAAG
CCCCCCCCCCCCCCC		27.2625159151
203UbiquitinationGGADPGNKKWEQKQV
CCCCCCCCCCEECEE		66.2421906983
203SumoylationGGADPGNKKWEQKQV
CCCCCCCCCCEECEE		66.24-
203SumoylationGGADPGNKKWEQKQV
CCCCCCCCCCEECEE		66.24-
203AcetylationGGADPGNKKWEQKQV
CCCCCCCCCCEECEE		66.2426051181
204AcetylationGADPGNKKWEQKQVQ
CCCCCCCCCEECEEE		61.0224471081
204UbiquitinationGADPGNKKWEQKQVQ
CCCCCCCCCEECEEE		61.0222817900
208SumoylationGNKKWEQKQVQIKTL
CCCCCEECEEEEEEE		40.7028112733
208UbiquitinationGNKKWEQKQVQIKTL
CCCCCEECEEEEEEE		40.7022817900
225PhosphorylationEFSVTMWSSDEKKDI
EEEEEEEECCCCCCC		19.65-
226PhosphorylationFSVTMWSSDEKKDID
EEEEEEECCCCCCCC		33.99-
230SumoylationMWSSDEKKDIDHETV
EEECCCCCCCCCCEE		58.8428112733
236O-linked_GlycosylationKKDIDHETVVEEQII
CCCCCCCEEEEEHHC		26.8216027160
236PhosphorylationKKDIDHETVVEEQII
CCCCCCCEEEEEHHC		26.8222496350
247PhosphorylationEQIIGENSPPDYSEY
EHHCCCCCCCCHHHH		33.2425159151
251PhosphorylationGENSPPDYSEYMTGK
CCCCCCCHHHHHCCC		14.8030266825
252PhosphorylationENSPPDYSEYMTGKK
CCCCCCHHHHHCCCC		29.6328176443
254PhosphorylationSPPDYSEYMTGKKLP
CCCCHHHHHCCCCCC		8.2728176443
256PhosphorylationPDYSEYMTGKKLPPG
CCHHHHHCCCCCCCC		44.9728176443
258AcetylationYSEYMTGKKLPPGGI
HHHHHCCCCCCCCCC		41.8125953088
258UbiquitinationYSEYMTGKKLPPGGI
HHHHHCCCCCCCCCC		41.8121906983
259UbiquitinationSEYMTGKKLPPGGIP
HHHHCCCCCCCCCCC		68.5222817900
274UbiquitinationGIDLSDPKQLAEFAR
CCCCCCHHHHHHHHH		64.0322817900
283UbiquitinationLAEFARMKPRKIKED
HHHHHHCCCCCCCCC		35.8022817900
286SumoylationFARMKPRKIKEDDAP
HHHCCCCCCCCCCCC		67.6628112733
286UbiquitinationFARMKPRKIKEDDAP
HHHCCCCCCCCCCCC		67.6622817900
286SumoylationFARMKPRKIKEDDAP
HHHCCCCCCCCCCCC		67.66-
288SumoylationRMKPRKIKEDDAPRT
HCCCCCCCCCCCCCC		59.11-
288SumoylationRMKPRKIKEDDAPRT
HCCCCCCCCCCCCCC		59.1128112733
288UbiquitinationRMKPRKIKEDDAPRT
HCCCCCCCCCCCCCC		59.1122817900
295PhosphorylationKEDDAPRTIACPHKG
CCCCCCCCCCCCCCC		16.3328555341
301UbiquitinationRTIACPHKGCTKMFR
CCCCCCCCCHHHHHC		40.6029967540
301MethylationRTIACPHKGCTKMFR
CCCCCCCCCHHHHHC		40.60115920241
305MethylationCPHKGCTKMFRDNSA
CCCCCHHHHHCCCHH		39.8783044799
305UbiquitinationCPHKGCTKMFRDNSA
CCCCCHHHHHCCCHH		39.87-
308MethylationKGCTKMFRDNSAMRK
CCHHHHHCCCHHHHH		38.41115920249
311PhosphorylationTKMFRDNSAMRKHLH
HHHHCCCHHHHHHHH		27.9430001349
315UbiquitinationRDNSAMRKHLHTHGP
CCCHHHHHHHHHCCC		37.1229967540
315MethylationRDNSAMRKHLHTHGP
CCCHHHHHHHHHCCC		37.12116252203
315AcetylationRDNSAMRKHLHTHGP
CCCHHHHHHHHHCCC		37.1226210075
332UbiquitinationHVCAECGKAFVESSK
EEECCCCHHHHHHHC		50.7621963094
337PhosphorylationCGKAFVESSKLKRHQ
CCHHHHHHHCCCCCC		27.7229214152
339UbiquitinationKAFVESSKLKRHQLV
HHHHHHHCCCCCCCC		68.2733845483
339SumoylationKAFVESSKLKRHQLV
HHHHHHHCCCCCCCC		68.27-
339AcetylationKAFVESSKLKRHQLV
HHHHHHHCCCCCCCC		68.2726822725
339SumoylationKAFVESSKLKRHQLV
HHHHHHHCCCCCCCC		68.27-
341UbiquitinationFVESSKLKRHQLVHT
HHHHHCCCCCCCCCC		52.12-
348PhosphorylationKRHQLVHTGEKPFQC
CCCCCCCCCCCCEEE		39.2925159151
351UbiquitinationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC		53.1033845483
351SumoylationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC		53.10-
351AcetylationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC		53.1068713
351SumoylationQLVHTGEKPFQCTFE
CCCCCCCCCEEEEEC		53.10-
356PhosphorylationGEKPFQCTFEGCGKR
CCCCEEEEECCCCCE		17.5924732914
362MethylationCTFEGCGKRFSLDFN
EEECCCCCEEEEEEE		55.11-
362UbiquitinationCTFEGCGKRFSLDFN
EEECCCCCEEEEEEE		55.1133845483
365PhosphorylationEGCGKRFSLDFNLRT
CCCCCEEEEEEECCE		30.9428450419
378PhosphorylationRTHVRIHTGDRPYVC
CEEEEEECCCCCEEC		38.1027273156
381MethylationVRIHTGDRPYVCPFD
EEEECCCCCEECCCC		26.29115920253
383PhosphorylationIHTGDRPYVCPFDGC
EECCCCCEECCCCCC		18.6424732914
393UbiquitinationPFDGCNKKFAQSTNL
CCCCCCHHHHHHHCC		31.7629967540
393SumoylationPFDGCNKKFAQSTNL
CCCCCCHHHHHHHCC		31.76-
393SumoylationPFDGCNKKFAQSTNL
CCCCCCHHHHHHHCC		31.76-
401SumoylationFAQSTNLKSHILTHA
HHHHHCCHHHHHHHH		41.90-
401UbiquitinationFAQSTNLKSHILTHA
HHHHHCCHHHHHHHH		41.9023000965
401SumoylationFAQSTNLKSHILTHA
HHHHHCCHHHHHHHH		41.90-
409SumoylationSHILTHAKAKNNQ--
HHHHHHHHHHCCC--		52.9028112733
409UbiquitinationSHILTHAKAKNNQ--
HHHHHHHHHHCCC--		52.9033845483
411SumoylationILTHAKAKNNQ----
HHHHHHHHCCC----		56.5828112733
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
8YPhosphorylationKinaseLYNP07948
PSP
39TPhosphorylationKinasePLK1P53350
PSP
118SPhosphorylationKinaseCSNK2A1P68400
GPS
184SPhosphorylationKinaseAURKBQ96GD4
GPS
254YPhosphorylationKinaseABL1P00519
GPS
254YPhosphorylationKinaseLYNP07948
PSP
365SPhosphorylationKinaseAURKAO14965
GPS
383YPhosphorylationKinaseLYNP07948
PSP
-KUbiquitinationE3 ubiquitin ligasePIAS4Q8N2W9
PMID:17353273
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TYY1_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 TYY1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FKB1A_HUMANFKBP1Aphysical
7541038
MTA2_HUMANMTA2physical
12920132
NOTC1_HUMANNOTCH1physical
12913000
SAP30_HUMANSAP30physical
12788099
HDAC2_HUMANHDAC2physical
11486036
HDAC3_HUMANHDAC3physical
11486036
FKBP3_HUMANFKBP3physical
11532945
EP300_HUMANEP300physical
7758944
SP1_HUMANSP1physical
10224053
SRBP1_HUMANSREBF1physical
10224053
MYC_HUMANMYCphysical
8266081
ATF6A_HUMANATF6physical
10866666
PPIA_HUMANPPIAphysical
7541038
HDAC3_HUMANHDAC3physical
19279113
EP300_HUMANEP300physical
19279113
HDAC2_HUMANHDAC2physical
19139378
CTCF_HUMANCTCFphysical
17218270
HDAC4_HUMANHDAC4physical
19013255
ZN232_HUMANZNF232physical
20211142
HXA11_MOUSEHoxa11physical
16963455
HXA11_HUMANHOXA11physical
16963455
HDAC4_HUMANHDAC4physical
16922677
MAX_HUMANMAXphysical
16878156
CBP_HUMANCREBBPphysical
16878156
HDAC5_HUMANHDAC5physical
16822951
MDM2_HUMANMDM2physical
15210108
P53_HUMANTP53physical
15210108
CDN2A_HUMANCDKN2Aphysical
15210108
ARF_HUMANCDKN2Aphysical
15210108
HDAC1_HUMANHDAC1physical
18634613
HDAC5_HUMANHDAC5physical
18632988
HDAC4_HUMANHDAC4physical
18558095
EP300_HUMANEP300physical
18542060
HDAC3_HUMANHDAC3physical
18542060
SMAD4_HUMANSMAD4physical
12808092
ILF3_HUMANILF3physical
12704081
ANM1_HUMANPRMT1physical
12704081
NPM_HUMANNPM1physical
16170350
ATF6A_HUMANATF6physical
15899857
ANM1_HUMANPRMT1physical
15899857
EZH2_HUMANEZH2physical
15520282
TFCP2_HUMANTFCP2physical
10888618
PRKDC_HUMANPRKDCphysical
18026119
INO80_HUMANINO80physical
18026119
ARP8_HUMANACTR8physical
18026119
HSP74_HUMANHSPA4physical
18026119
ARP5_HUMANACTR5physical
18026119
ACL6A_HUMANACTL6Aphysical
18026119
RUVB1_HUMANRUVBL1physical
18026119
RUVB2_HUMANRUVBL2physical
18026119
P53_HUMANTP53physical
18026119
SP1_HUMANSP1physical
17990281
RELB_HUMANRELBphysical
14707079
HDAC1_HUMANHDAC1physical
17827154
HDAC2_HUMANHDAC2physical
17827154
EP300_HUMANEP300physical
17510411
TYY1_HUMANYY1physical
17510411
RB_HUMANRB1physical
17287852
NF2L2_HUMANNFE2L2physical
20309604
MECP2_HUMANMECP2physical
20504995
RUVB1_HUMANRUVBL1physical
17721549
RUVB2_HUMANRUVBL2physical
17721549
ACL6A_HUMANACTL6Aphysical
17721549
IN80C_HUMANINO80Cphysical
17721549
INO80_HUMANINO80physical
17721549
NFRKB_HUMANNFRKBphysical
17721549
TFE2_HUMANTCF3physical
17721549
ARP5_HUMANACTR5physical
17721549
ARP8_HUMANACTR8physical
17721549
IN80B_HUMANINO80Bphysical
17721549
IN80E_HUMANINO80Ephysical
17721549
UCHL5_HUMANUCHL5physical
17721549
IN80D_HUMANINO80Dphysical
17721549
MCRS1_HUMANMCRS1physical
17721549
TYY1_HUMANYY1physical
17721549
TFPT_HUMANTFPTphysical
17721549
GRP78_HUMANHSPA5physical
17721549
SP1_HUMANSP1physical
17556661
CREB1_HUMANCREB1physical
7769693
ATF2_HUMANATF2physical
7769693
ATF7_HUMANATF7physical
7769693
BAP1_HUMANBAP1physical
20805357
HCFC1_HUMANHCFC1physical
20805357
XRCC6_HUMANXRCC6physical
15367688
XRCC5_HUMANXRCC5physical
15367688
NEDD4_HUMANNEDD4physical
19953087
NED4L_HUMANNEDD4Lphysical
19953087
ARP8_HUMANACTR8physical
22210892
DDX5_HUMANDDX5physical
22210892
DDX3X_HUMANDDX3Xphysical
22210892
RUVB2_HUMANRUVBL2physical
22210892
MDM2_HUMANMDM2physical
22659184
EED_HUMANEEDphysical
11158321
EZH2_HUMANEZH2physical
11158321
A4_HUMANAPPphysical
21832049
ZN830_HUMANZNF830physical
22939629
ZN638_HUMANZNF638physical
22939629
WDHD1_HUMANWDHD1physical
22939629
ZNF24_HUMANZNF24physical
22939629
SP1_HUMANSP1physical
8327494
ARRB1_HUMANARRB1physical
19879840
EP300_HUMANEP300physical
9199306
RYBP_HUMANRYBPphysical
11953439
SMUF2_HUMANSMURF2physical
24803334
AGO2_HUMANAGO2physical
29120412
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 TYY1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-247 ANDTHR-348, AND MASS SPECTROMETRY.
"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-247; THR-348 ANDTHR-378, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-247, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348, AND MASSSPECTROMETRY.

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