I2BP1_HUMAN - dbPTM
I2BP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I2BP1_HUMAN
UniProt AC Q8IU81
Protein Name Interferon regulatory factor 2-binding protein 1
Gene Name IRF2BP1
Organism Homo sapiens (Human).
Sequence Length 584
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation..
Protein Sequence MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPPALKHPATKDLAAAAAQGPQLPPPQAQPQPSGTGGGVSGQDRYDRATSSGRLPLPSPALEYTLGSRLANGLGREEAVAEGARRALLGSMPGLMPPGLLAAAVSGLGSRGLTLAPGLSPARPLFGSDFEKEKQQRNADCLAELNEAMRGRAEEWHGRPKAVREQLLALSACAPFNVRFKKDHGLVGRVFAFDATARPPGYEFELKLFTEYPCGSGNVYAGVLAVARQMFHDALREPGKALASSGFKYLEYERRHGSGEWRQLGELLTDGVRSFREPAPAEALPQQYPEPAPAALCGPPPRAPSRNLAPTPRRRKASPEPEGEAAGKMTTEEQQQRHWVAPGGPYSAETPGVPSPIAALKNVAEALGHSPKDPGGGGGPVRAGGASPAASSTAQPPTQHRLVARNGEAEVSPTAGAEAVSGGGSGTGATPGAPLCCTLCRERLEDTHFVQCPSVPGHKFCFPCSREFIKAQGPAGEVYCPSGDKCPLVGSSVPWAFMQGEIATILAGDIKVKKERDP
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------MASVQASRR
------CCCCCCCCC		20.57-
58PhosphorylationAARQLKRSHVLPEGR
HHHHHHHHCCCCCCC		19.1623403867
66PhosphorylationHVLPEGRSPGPPALK
CCCCCCCCCCCCCCC		45.1023927012
73AcetylationSPGPPALKHPATKDL
CCCCCCCCCCCHHHH		50.0425953088
73UbiquitinationSPGPPALKHPATKDL
CCCCCCCCCCCHHHH		50.0429967540
77PhosphorylationPALKHPATKDLAAAA
CCCCCCCHHHHHHHH		29.5521949786
116PhosphorylationQDRYDRATSSGRLPL
CCCCCCCCCCCCCCC		25.0728450419
117PhosphorylationDRYDRATSSGRLPLP
CCCCCCCCCCCCCCC		29.7930576142
118PhosphorylationRYDRATSSGRLPLPS
CCCCCCCCCCCCCCC		24.4728464451
120MethylationDRATSSGRLPLPSPA
CCCCCCCCCCCCCHH		34.77115480483
125PhosphorylationSGRLPLPSPALEYTL
CCCCCCCCHHHHHHH		30.4122617229
130PhosphorylationLPSPALEYTLGSRLA
CCCHHHHHHHHHHHH		14.2322199227
131PhosphorylationPSPALEYTLGSRLAN
CCHHHHHHHHHHHHC		18.4426074081
134PhosphorylationALEYTLGSRLANGLG
HHHHHHHHHHHCCCC		27.5126074081
157PhosphorylationARRALLGSMPGLMPP
HHHHHHHCCCCCCCH		23.0528348404
177MethylationAVSGLGSRGLTLAPG
HHHCCCCCCCCCCCC		42.2024129315
180PhosphorylationGLGSRGLTLAPGLSP
CCCCCCCCCCCCCCC		24.5730266825
186PhosphorylationLTLAPGLSPARPLFG
CCCCCCCCCCCCCCC		23.5630266825
189MethylationAPGLSPARPLFGSDF
CCCCCCCCCCCCCHH		31.66115480491
194PhosphorylationPARPLFGSDFEKEKQ
CCCCCCCCHHHHHHH		31.6230266825
198UbiquitinationLFGSDFEKEKQQRNA
CCCCHHHHHHHHHHH		70.9233845483
200UbiquitinationGSDFEKEKQQRNADC
CCHHHHHHHHHHHHH		63.90-
207GlutathionylationKQQRNADCLAELNEA
HHHHHHHHHHHHHHH		3.4422555962
227SumoylationEEWHGRPKAVREQLL
HHHCCCCHHHHHHHH		59.1428112733
227UbiquitinationEEWHGRPKAVREQLL
HHHCCCCHHHHHHHH		59.14-
237PhosphorylationREQLLALSACAPFNV
HHHHHHHHHHCCEEE		18.72-
239GlutathionylationQLLALSACAPFNVRF
HHHHHHHHCCEEEEE		4.4322555962
245MethylationACAPFNVRFKKDHGL
HHCCEEEEECCCCCC		38.48115387527
247UbiquitinationAPFNVRFKKDHGLVG
CCEEEEECCCCCCCC		46.8829967540
248UbiquitinationPFNVRFKKDHGLVGR
CEEEEECCCCCCCCE		52.8529967540
268PhosphorylationATARPPGYEFELKLF
CCCCCCCEEEEEEEE		24.1817360941
306UbiquitinationDALREPGKALASSGF
HHHHCCHHHHHHCCC		51.4433845483
314UbiquitinationALASSGFKYLEYERR
HHHHCCCCEEEEEHH		53.0722817900
314SumoylationALASSGFKYLEYERR
HHHHCCCCEEEEEHH		53.07-
314AcetylationALASSGFKYLEYERR
HHHHCCCCEEEEEHH		53.0726051181
314SumoylationALASSGFKYLEYERR
HHHHCCCCEEEEEHH		53.07-
340PhosphorylationLLTDGVRSFREPAPA
HHHHHHHHCCCCCCH		26.6727251275
354PhosphorylationAEALPQQYPEPAPAA
HHHCCCCCCCCCCHH		12.3326552605
371PhosphorylationGPPPRAPSRNLAPTP
CCCCCCCCCCCCCCC		32.5821712546
377PhosphorylationPSRNLAPTPRRRKAS
CCCCCCCCCCCCCCC		24.6621712546
382SumoylationAPTPRRRKASPEPEG
CCCCCCCCCCCCCCC		51.94-
382SumoylationAPTPRRRKASPEPEG
CCCCCCCCCCCCCCC		51.94-
384PhosphorylationTPRRRKASPEPEGEA
CCCCCCCCCCCCCCC		32.6029255136
394UbiquitinationPEGEAAGKMTTEEQQ
CCCCCCCCCCHHHHH		28.4824816145
396PhosphorylationGEAAGKMTTEEQQQR
CCCCCCCCHHHHHHH		34.2429978859
397PhosphorylationEAAGKMTTEEQQQRH
CCCCCCCHHHHHHHC		33.7429978859
412PhosphorylationWVAPGGPYSAETPGV
CCCCCCCCCCCCCCC		24.6430266825
413PhosphorylationVAPGGPYSAETPGVP
CCCCCCCCCCCCCCC		23.8230266825
416PhosphorylationGGPYSAETPGVPSPI
CCCCCCCCCCCCCHH		25.6730266825
421PhosphorylationAETPGVPSPIAALKN
CCCCCCCCHHHHHHH		26.9122167270
427UbiquitinationPSPIAALKNVAEALG
CCHHHHHHHHHHHHC		44.6532015554
436PhosphorylationVAEALGHSPKDPGGG
HHHHHCCCCCCCCCC		31.6729255136
438UbiquitinationEALGHSPKDPGGGGG
HHHCCCCCCCCCCCC		78.5422817900
438SumoylationEALGHSPKDPGGGGG
HHHCCCCCCCCCCCC		78.5428112733
453PhosphorylationPVRAGGASPAASSTA
CCCCCCCCCCCCCCC		20.5329255136
457PhosphorylationGGASPAASSTAQPPT
CCCCCCCCCCCCCCC		30.2623927012
458PhosphorylationGASPAASSTAQPPTQ
CCCCCCCCCCCCCCC		24.0423927012
458O-linked_GlycosylationGASPAASSTAQPPTQ
CCCCCCCCCCCCCCC		24.0430059200
459PhosphorylationASPAASSTAQPPTQH
CCCCCCCCCCCCCCC		27.1523927012
459O-linked_GlycosylationASPAASSTAQPPTQH
CCCCCCCCCCCCCCC		27.1530059200
464O-linked_GlycosylationSSTAQPPTQHRLVAR
CCCCCCCCCCCEEEE		43.6330059200
464PhosphorylationSSTAQPPTQHRLVAR
CCCCCCCCCCCEEEE		43.6326074081
478PhosphorylationRNGEAEVSPTAGAEA
ECCCEEECCCCCCCC		14.1925159151
480PhosphorylationGEAEVSPTAGAEAVS
CCEEECCCCCCCCCC		30.1625159151
487PhosphorylationTAGAEAVSGGGSGTG
CCCCCCCCCCCCCCC		38.4830576142
491PhosphorylationEAVSGGGSGTGATPG
CCCCCCCCCCCCCCC		36.1320068231
493PhosphorylationVSGGGSGTGATPGAP
CCCCCCCCCCCCCCC		25.9128464451
496PhosphorylationGGSGTGATPGAPLCC
CCCCCCCCCCCCCEE		24.4928464451
504PhosphorylationPGAPLCCTLCRERLE
CCCCCEEHHHHHHHC		28.0920068231
536UbiquitinationPCSREFIKAQGPAGE
ECCHHHHHHHCCCCE		39.7232015554
536NeddylationPCSREFIKAQGPAGE
ECCHHHHHHHCCCCE		39.7232015554
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 I2BP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I2BP1_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 I2BP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JDP2_HUMANJDP2physical
18671972
PHS2_HUMANPCBD2physical
20211142
IRF2_HUMANIRF2physical
12799427
RHG01_HUMANARHGAP1physical
26344197
SYFA_HUMANFARSAphysical
26344197
I2BPL_HUMANIRF2BPLphysical
28514442
I2BP2_HUMANIRF2BP2physical
28514442
DCP1B_HUMANDCP1Bphysical
28514442
FYB2_HUMANC1orf168physical
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 I2BP1_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, 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-125 AND SER-436, ANDMASS 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-66; SER-186; SER-421;SER-436; SER-453 AND SER-457, 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-125 AND SER-453, ANDMASS SPECTROMETRY.
"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-421; SER-436 ANDSER-453, AND MASS SPECTROMETRY.

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