AEBP2_HUMAN - dbPTM
AEBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AEBP2_HUMAN
UniProt AC Q6ZN18
Protein Name Zinc finger protein AEBP2
Gene Name AEBP2
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization Nucleus .
Protein Description DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3..
Protein Sequence MAAAITDMADLEELSRLSPLPPGSPGSAARGRAEPPEEEEEEEEEEEEAEAEAVAALLLNGGSGGGGGGGGGGVGGGEAETMSEPSPESASQAGEDEDEEEDDEEEEDESSSSGGGEEESSAESLVGSSGGSSSDETRSLSPGAASSSSGDGDGKEGLEEPKGPRGSQGGGGGGSSSSSVVSSGGDEGYGTGGGGSSATSGGRRGSLEMSSDGEPLSRMDSEDSISSTIMDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLSKLPKDTALLLDPNIYRTMPQKRLKRTLIRKVFNLYLSKQ
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
2Acetylation------MAAAITDMA
------CCCCCCCHH		12.9522814378
6Phosphorylation--MAAAITDMADLEE
--CCCCCCCHHHHHH		18.2628464451
15PhosphorylationMADLEELSRLSPLPP
HHHHHHHHHCCCCCC		34.1629255136
18PhosphorylationLEELSRLSPLPPGSP
HHHHHHCCCCCCCCC		24.2329255136
24PhosphorylationLSPLPPGSPGSAARG
CCCCCCCCCCCCCCC		31.6829255136
27PhosphorylationLPPGSPGSAARGRAE
CCCCCCCCCCCCCCC		23.3430266825
87UbiquitinationETMSEPSPESASQAG
CCCCCCCHHHHHHCC		50.7229967540
128PhosphorylationSAESLVGSSGGSSSD
CCHHHCCCCCCCCCC		20.5222468782
131UbiquitinationSLVGSSGGSSSDETR
HHCCCCCCCCCCCCC		26.7122817900
137PhosphorylationGGSSSDETRSLSPGA
CCCCCCCCCCCCCCC		30.4622468782
139PhosphorylationSSSDETRSLSPGAAS
CCCCCCCCCCCCCCC		40.3930266825
141PhosphorylationSDETRSLSPGAASSS
CCCCCCCCCCCCCCC		23.6429255136
144 (in isoform 3)Ubiquitination-13.9321906983
144UbiquitinationTRSLSPGAASSSSGD
CCCCCCCCCCCCCCC		13.9322817900
146PhosphorylationSLSPGAASSSSGDGD
CCCCCCCCCCCCCCC		30.1623403867
147PhosphorylationLSPGAASSSSGDGDG
CCCCCCCCCCCCCCC		24.6423403867
148PhosphorylationSPGAASSSSGDGDGK
CCCCCCCCCCCCCCC		35.5321815630
149PhosphorylationPGAASSSSGDGDGKE
CCCCCCCCCCCCCCC		42.7423927012
155UbiquitinationSSGDGDGKEGLEEPK
CCCCCCCCCCCCCCC		54.0424816145
162UbiquitinationKEGLEEPKGPRGSQG
CCCCCCCCCCCCCCC		82.1227667366
167PhosphorylationEPKGPRGSQGGGGGG
CCCCCCCCCCCCCCC		27.2517525332
174PhosphorylationSQGGGGGGSSSSSVV
CCCCCCCCCCCCCCC		27.8532645325
175PhosphorylationQGGGGGGSSSSSVVS
CCCCCCCCCCCCCCC		30.2630576142
176PhosphorylationGGGGGGSSSSSVVSS
CCCCCCCCCCCCCCC		37.2030177828
177PhosphorylationGGGGGSSSSSVVSSG
CCCCCCCCCCCCCCC		28.4726552605
178PhosphorylationGGGGSSSSSVVSSGG
CCCCCCCCCCCCCCC		29.1530177828
179PhosphorylationGGGSSSSSVVSSGGD
CCCCCCCCCCCCCCC		28.6130177828
182PhosphorylationSSSSSVVSSGGDEGY
CCCCCCCCCCCCCCC		22.5530177828
183PhosphorylationSSSSVVSSGGDEGYG
CCCCCCCCCCCCCCC		34.8730177828
189PhosphorylationSSGGDEGYGTGGGGS
CCCCCCCCCCCCCCC		14.9626552605
191PhosphorylationGGDEGYGTGGGGSSA
CCCCCCCCCCCCCCC		24.9526552605
196PhosphorylationYGTGGGGSSATSGGR
CCCCCCCCCCCCCCC		21.7826552605
197PhosphorylationGTGGGGSSATSGGRR
CCCCCCCCCCCCCCC		38.5526552605
199PhosphorylationGGGGSSATSGGRRGS
CCCCCCCCCCCCCCC		29.8326552605
200PhosphorylationGGGSSATSGGRRGSL
CCCCCCCCCCCCCCE		38.6826552605
206PhosphorylationTSGGRRGSLEMSSDG
CCCCCCCCEEECCCC		21.2429255136
210PhosphorylationRRGSLEMSSDGEPLS
CCCCEEECCCCCCCC		18.8529255136
211PhosphorylationRGSLEMSSDGEPLSR
CCCEEECCCCCCCCC		48.6129255136
217PhosphorylationSSDGEPLSRMDSEDS
CCCCCCCCCCCCCCC		35.9522167270
221PhosphorylationEPLSRMDSEDSISST
CCCCCCCCCCCCCCE		33.6830624053
224PhosphorylationSRMDSEDSISSTIMD
CCCCCCCCCCCEEEC		21.9630624053
226PhosphorylationMDSEDSISSTIMDVD
CCCCCCCCCEEECCC		25.9430624053
227PhosphorylationDSEDSISSTIMDVDS
CCCCCCCCEEECCCC		21.9330624053
228PhosphorylationSEDSISSTIMDVDST
CCCCCCCEEECCCCH		17.3330624053
234PhosphorylationSTIMDVDSTISSGRS
CEEECCCCHHCCCCC		27.7330576142
235PhosphorylationTIMDVDSTISSGRST
EEECCCCHHCCCCCC		22.0330576142
237PhosphorylationMDVDSTISSGRSTPA
ECCCCHHCCCCCCCC		27.1627251275
238PhosphorylationDVDSTISSGRSTPAM
CCCCHHCCCCCCCCC		34.0827251275
241PhosphorylationSTISSGRSTPAMMNG
CHHCCCCCCCCCCCC		42.1228450419
242PhosphorylationTISSGRSTPAMMNGQ
HHCCCCCCCCCCCCC		17.4428450419
251PhosphorylationAMMNGQGSTTSSSKN
CCCCCCCCCCCCCCC		22.1824114839
252PhosphorylationMMNGQGSTTSSSKNI
CCCCCCCCCCCCCCE		37.2124114839
257UbiquitinationGSTTSSSKNIAYNCC
CCCCCCCCCEECCCH		55.0829967540
263UbiquitinationSKNIAYNCCWDQCQA
CCCEECCCHHHHHHH		1.2929967540
303UbiquitinationVCLWKGCKVYNTPST
EEEECCCEEECCCCC		57.3229967540
305PhosphorylationLWKGCKVYNTPSTSQ
EECCCEEECCCCCCH		9.9826074081
307PhosphorylationKGCKVYNTPSTSQSW
CCCEEECCCCCCHHH		10.8326074081
309PhosphorylationCKVYNTPSTSQSWLQ
CEEECCCCCCHHHHH		38.3626074081
310PhosphorylationKVYNTPSTSQSWLQR
EEECCCCCCHHHHHH		31.8026074081
311PhosphorylationVYNTPSTSQSWLQRH
EECCCCCCHHHHHHH		26.9326074081
313PhosphorylationNTPSTSQSWLQRHML
CCCCCCHHHHHHHCC		29.5326074081
341PhosphorylationGCNASFASQGGLARH
CCCHHHHHCCCHHHH		27.6146159965
354PhosphorylationRHVPTHFSQQNSSKV
HHCCCCHHHCCCCCC		24.2128555341
358PhosphorylationTHFSQQNSSKVSSQP
CCHHHCCCCCCCCCC		27.4828555341
360 (in isoform 2)Ubiquitination-46.0521906983
360UbiquitinationFSQQNSSKVSSQPKA
HHHCCCCCCCCCCCC		46.0522817900
360 (in isoform 1)Ubiquitination-46.0521906983
371PhosphorylationQPKAKEESPSKAGMN
CCCCCCCCCCCCCHH		35.2528176443
373PhosphorylationKAKEESPSKAGMNKR
CCCCCCCCCCCHHHH		44.4028176443
390PhosphorylationLKNKRRRSLPRPHDF
HHHHHHHCCCCCCCC		40.7030266825
402PhosphorylationHDFFDAQTLDAIRHR
CCCCCHHHHHHHHHH		28.4622199227
472PhosphorylationSERHQLKTKVVHLSK
HHHHHCEEEEEEHHH		37.3523607784
473UbiquitinationERHQLKTKVVHLSKL
HHHHCEEEEEEHHHC		40.4429967540
478PhosphorylationKTKVVHLSKLPKDTA
EEEEEEHHHCCCCCE		19.7823607784
479UbiquitinationTKVVHLSKLPKDTAL
EEEEEHHHCCCCCEE		75.1529967540
479AcetylationTKVVHLSKLPKDTAL
EEEEEHHHCCCCCEE		75.1523749302
482UbiquitinationVHLSKLPKDTALLLD
EEHHHCCCCCEEECC		77.48-
484PhosphorylationLSKLPKDTALLLDPN
HHHCCCCCEEECCCC		25.9024300666
493PhosphorylationLLLDPNIYRTMPQKR
EECCCCHHHHCCHHH		13.4824300666
513PhosphorylationIRKVFNLYLSKQ---
HHHHHHHHHCCC---		15.2728555341
515PhosphorylationKVFNLYLSKQ-----
HHHHHHHCCC-----		18.5629214152
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 AEBP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AEBP2_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 AEBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RALYL_HUMANRALYLphysical
16189514
SUZ12_HUMANSUZ12physical
15225548
A4_HUMANAPPphysical
21832049
JMJD6_HUMANJMJD6physical
23455924
RBBP7_HUMANRBBP7physical
26186194
EED_HUMANEEDphysical
26186194
EZH2_HUMANEZH2physical
26186194
JARD2_HUMANJARID2physical
26186194
ATX3_HUMANATXN3physical
26186194
KBTB7_HUMANKBTBD7physical
26186194
SUZ12_HUMANSUZ12physical
26186194
THAP1_HUMANTHAP1physical
21516116
SUZ12_HUMANSUZ12physical
28514442
JARD2_HUMANJARID2physical
28514442
RBBP7_HUMANRBBP7physical
28514442
EZH2_HUMANEZH2physical
28514442
EED_HUMANEEDphysical
28514442
ATX3_HUMANATXN3physical
28514442
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 AEBP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-18 AND SER-24, AND MASS SPECTROMETRY.
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-206, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-18 AND SER-24, 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-206; SER-210 ANDSER-211, AND MASS 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 SER-24 AND SER-27, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-24, AND MASSSPECTROMETRY.

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