I2BP2_HUMAN - dbPTM
I2BP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I2BP2_HUMAN
UniProt AC Q7Z5L9
Protein Name Interferon regulatory factor 2-binding protein 2
Gene Name IRF2BP2
Organism Homo sapiens (Human).
Sequence Length 587
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle..
Protein Sequence MAAAVAVAAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAHGCFPEGRSPPGAAASAAAKPPPLSAKDILLQQQQQLGHGGPEAAPRAPQALERYPLAAAAERPPRLGSDFGSSRPAASLAQPPTPQPPPVNGILVPNGFSKLEEPPELNRQSPNPRRGHAVPPTLVPLMNGSATPLPTALGLGGRAAASLAAVSGTAAASLGSAQPTDLGAHKRPASVSSSAAVEHEQREAAAKEKQPPPPAHRGPADSLSTAAGAAELSAEGAGKSRGSGEQDWVNRPKTVRDTLLALHQHGHSGPFESKFKKEPALTAGRLLGFEANGANGSKAVARTARKRKPSPEPEGEVGPPKINGEAQPWLSTSTEGLKIPMTPTSSFVSPPPPTASPHSNRTTPPEAAQNGQSPMAALILVADNAGGSHASKDANQVHSTTRRNSNSPPSPSSMNQRRLGPREVGGQGAGNTGGLEPVHPASLPDSSLATSAPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDS
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------MAAAVAVAA
------CHHHHHHHH
12.2522814378
11PhosphorylationAVAVAAASRRQSCYL
HHHHHHHHHCCCEEE
24.2220068231
15PhosphorylationAAASRRQSCYLCDLP
HHHHHCCCEEECCCC
11.6925849741
17PhosphorylationASRRQSCYLCDLPRM
HHHCCCEEECCCCCC
18.6628450419
71PhosphorylationGCFPEGRSPPGAAAS
CCCCCCCCCCCHHHH
46.4323401153
78PhosphorylationSPPGAAASAAAKPPP
CCCCHHHHHHCCCCC
17.4524702127
87PhosphorylationAAKPPPLSAKDILLQ
HCCCCCCCHHHHHHH
38.7624702127
89UbiquitinationKPPPLSAKDILLQQQ
CCCCCCHHHHHHHHH
41.7621890473
89 (in isoform 1)Ubiquitination-41.7621890473
89 (in isoform 2)Ubiquitination-41.7621890473
109MethylationGGPEAAPRAPQALER
CCCCCCCCCCHHHHH
54.92115480507
116MethylationRAPQALERYPLAAAA
CCCHHHHHCCCHHHH
38.9480702545
125MethylationPLAAAAERPPRLGSD
CCHHHHCCCCCCCCC
41.62115480499
131PhosphorylationERPPRLGSDFGSSRP
CCCCCCCCCCCCCCC
34.0723401153
135PhosphorylationRLGSDFGSSRPAASL
CCCCCCCCCCCCHHH
24.1423312004
136PhosphorylationLGSDFGSSRPAASLA
CCCCCCCCCCCHHHC
42.5427794612
141PhosphorylationGSSRPAASLAQPPTP
CCCCCCHHHCCCCCC
26.7528450419
147PhosphorylationASLAQPPTPQPPPVN
HHHCCCCCCCCCCCC
41.0428450419
163PhosphorylationILVPNGFSKLEEPPE
EECCCCCCCCCCCCC
37.4222210691
175PhosphorylationPPELNRQSPNPRRGH
CCCCCCCCCCCCCCC
24.3329255136
195PhosphorylationLVPLMNGSATPLPTA
CCCCCCCCCCCCCCH
24.7821712546
197PhosphorylationPLMNGSATPLPTALG
CCCCCCCCCCCCHHC
27.3625159151
212O-linked_GlycosylationLGGRAAASLAAVSGT
CCHHHHHHHHHHHCC
17.5130059200
212PhosphorylationLGGRAAASLAAVSGT
CCHHHHHHHHHHHCC
17.5128555341
217O-linked_GlycosylationAASLAAVSGTAAASL
HHHHHHHHCCHHHHC
26.2130059200
217PhosphorylationAASLAAVSGTAAASL
HHHHHHHHCCHHHHC
26.2128555341
219O-linked_GlycosylationSLAAVSGTAAASLGS
HHHHHHCCHHHHCCC
12.9630059200
223O-linked_GlycosylationVSGTAAASLGSAQPT
HHCCHHHHCCCCCCC
28.6530059200
223PhosphorylationVSGTAAASLGSAQPT
HHCCHHHHCCCCCCC
28.6522210691
226O-linked_GlycosylationTAAASLGSAQPTDLG
CHHHHCCCCCCCCCC
29.0830059200
226PhosphorylationTAAASLGSAQPTDLG
CHHHHCCCCCCCCCC
29.0822210691
230O-linked_GlycosylationSLGSAQPTDLGAHKR
HCCCCCCCCCCCCCC
31.6030059200
230PhosphorylationSLGSAQPTDLGAHKR
HCCCCCCCCCCCCCC
31.6022210691
236AcetylationPTDLGAHKRPASVSS
CCCCCCCCCCCCCCH
60.5925953088
240O-linked_GlycosylationGAHKRPASVSSSAAV
CCCCCCCCCCHHHHH
25.8030059200
240PhosphorylationGAHKRPASVSSSAAV
CCCCCCCCCCHHHHH
25.8029255136
242O-linked_GlycosylationHKRPASVSSSAAVEH
CCCCCCCCHHHHHHH
18.9730059200
242PhosphorylationHKRPASVSSSAAVEH
CCCCCCCCHHHHHHH
18.9729255136
243PhosphorylationKRPASVSSSAAVEHE
CCCCCCCHHHHHHHH
23.1129255136
244PhosphorylationRPASVSSSAAVEHEQ
CCCCCCHHHHHHHHH
16.8530278072
272PhosphorylationAHRGPADSLSTAAGA
CCCCCCCHHHHHHHH
26.7328555341
274PhosphorylationRGPADSLSTAAGAAE
CCCCCHHHHHHHHHH
21.6921601212
275PhosphorylationGPADSLSTAAGAAEL
CCCCHHHHHHHHHHH
26.3123312004
283PhosphorylationAAGAAELSAEGAGKS
HHHHHHHHHCCCCCC
18.7723312004
289AcetylationLSAEGAGKSRGSGEQ
HHHCCCCCCCCCCCC
36.1225953088
289SumoylationLSAEGAGKSRGSGEQ
HHHCCCCCCCCCCCC
36.1228112733
289UbiquitinationLSAEGAGKSRGSGEQ
HHHCCCCCCCCCCCC
36.1232015554
290PhosphorylationSAEGAGKSRGSGEQD
HHCCCCCCCCCCCCC
40.7425159151
291MethylationAEGAGKSRGSGEQDW
HCCCCCCCCCCCCCC
46.94115480511
293PhosphorylationGAGKSRGSGEQDWVN
CCCCCCCCCCCCCCC
37.7425159151
303SumoylationQDWVNRPKTVRDTLL
CCCCCCCHHHHHHHH
57.3128112733
303UbiquitinationQDWVNRPKTVRDTLL
CCCCCCCHHHHHHHH
57.3129967540
308PhosphorylationRPKTVRDTLLALHQH
CCHHHHHHHHHHHHH
17.0722210691
318PhosphorylationALHQHGHSGPFESKF
HHHHHCCCCCCHHHC
53.4023401153
323PhosphorylationGHSGPFESKFKKEPA
CCCCCCHHHCCCCCC
43.7123401153
324SumoylationHSGPFESKFKKEPAL
CCCCCHHHCCCCCCC
54.7428112733
324UbiquitinationHSGPFESKFKKEPAL
CCCCCHHHCCCCCCC
54.7432015554
326SumoylationGPFESKFKKEPALTA
CCCHHHCCCCCCCCH
61.0228112733
326UbiquitinationGPFESKFKKEPALTA
CCCHHHCCCCCCCCH
61.0229967540
327UbiquitinationPFESKFKKEPALTAG
CCHHHCCCCCCCCHH
72.5529967540
344PhosphorylationLGFEANGANGSKAVA
HCCCCCCCCCHHHHH
19.6132142685
344 (in isoform 2)Phosphorylation-19.6125849741
347PhosphorylationEANGANGSKAVARTA
CCCCCCCHHHHHHHH
19.7626074081
348AcetylationANGANGSKAVARTAR
CCCCCCHHHHHHHHH
48.5625953088
348SumoylationANGANGSKAVARTAR
CCCCCCHHHHHHHHH
48.5628112733
348UbiquitinationANGANGSKAVARTAR
CCCCCCHHHHHHHHH
48.5633845483
353PhosphorylationGSKAVARTARKRKPS
CHHHHHHHHHHCCCC
22.5226074081
360PhosphorylationTARKRKPSPEPEGEV
HHHHCCCCCCCCCCC
44.9529255136
380PhosphorylationNGEAQPWLSTSTEGL
CCCCCCCCCCCCCCC
5.2132142685
381O-linked_GlycosylationGEAQPWLSTSTEGLK
CCCCCCCCCCCCCCC
19.2230059200
381PhosphorylationGEAQPWLSTSTEGLK
CCCCCCCCCCCCCCC
19.2228450419
382O-linked_GlycosylationEAQPWLSTSTEGLKI
CCCCCCCCCCCCCCC
37.1830059200
382PhosphorylationEAQPWLSTSTEGLKI
CCCCCCCCCCCCCCC
37.1828450419
383O-linked_GlycosylationAQPWLSTSTEGLKIP
CCCCCCCCCCCCCCC
22.5330059200
383PhosphorylationAQPWLSTSTEGLKIP
CCCCCCCCCCCCCCC
22.5321815630
384PhosphorylationQPWLSTSTEGLKIPM
CCCCCCCCCCCCCCC
33.8728450419
392O-linked_GlycosylationEGLKIPMTPTSSFVS
CCCCCCCCCCCCCCC
20.3330059200
392PhosphorylationEGLKIPMTPTSSFVS
CCCCCCCCCCCCCCC
20.3323927012
394PhosphorylationLKIPMTPTSSFVSPP
CCCCCCCCCCCCCCC
28.0323927012
395O-linked_GlycosylationKIPMTPTSSFVSPPP
CCCCCCCCCCCCCCC
24.0030059200
395PhosphorylationKIPMTPTSSFVSPPP
CCCCCCCCCCCCCCC
24.0023927012
396PhosphorylationIPMTPTSSFVSPPPP
CCCCCCCCCCCCCCC
31.9530266825
399PhosphorylationTPTSSFVSPPPPTAS
CCCCCCCCCCCCCCC
29.6730266825
404PhosphorylationFVSPPPPTASPHSNR
CCCCCCCCCCCCCCC
45.6129255136
406PhosphorylationSPPPPTASPHSNRTT
CCCCCCCCCCCCCCC
26.1429255136
409PhosphorylationPPTASPHSNRTTPPE
CCCCCCCCCCCCCHH
31.2430266825
412PhosphorylationASPHSNRTTPPEAAQ
CCCCCCCCCCHHHHH
48.1530278072
413PhosphorylationSPHSNRTTPPEAAQN
CCCCCCCCCHHHHHC
33.3430278072
423PhosphorylationEAAQNGQSPMAALIL
HHHHCCCCCCEEEEE
20.3123401153
438PhosphorylationVADNAGGSHASKDAN
EEECCCCCCCCCCHH
18.2423927012
441PhosphorylationNAGGSHASKDANQVH
CCCCCCCCCCHHHHC
26.1620068231
444PhosphorylationGSHASKDANQVHSTT
CCCCCCCHHHHCCCC
16.4632645325
446PhosphorylationHASKDANQVHSTTRR
CCCCCHHHHCCCCCC
35.7033259812
449PhosphorylationKDANQVHSTTRRNSN
CCHHHHCCCCCCCCC
32.3929514088
450PhosphorylationDANQVHSTTRRNSNS
CHHHHCCCCCCCCCC
14.9429514088
451PhosphorylationANQVHSTTRRNSNSP
HHHHCCCCCCCCCCC
30.5529514088
455PhosphorylationHSTTRRNSNSPPSPS
CCCCCCCCCCCCCCC
36.5529255136
457PhosphorylationTTRRNSNSPPSPSSM
CCCCCCCCCCCCCHH
37.7029255136
460PhosphorylationRNSNSPPSPSSMNQR
CCCCCCCCCCHHHCC
40.5829255136
462PhosphorylationSNSPPSPSSMNQRRL
CCCCCCCCHHHCCCC
46.7029255136
463PhosphorylationNSPPSPSSMNQRRLG
CCCCCCCHHHCCCCC
25.7429255136
492PhosphorylationLEPVHPASLPDSSLA
CCCCCCCCCCCCHHC
44.9022817901
496PhosphorylationHPASLPDSSLATSAP
CCCCCCCCHHCCCCC
25.8822210691
497PhosphorylationPASLPDSSLATSAPL
CCCCCCCHHCCCCCE
29.4227080861
500PhosphorylationLPDSSLATSAPLCCT
CCCCHHCCCCCEEHH
30.6227080861
523NeddylationTHFVQCPSVPSHKFC
CCCCCCCCCCCCCCE
55.0432015554
523UbiquitinationTHFVQCPSVPSHKFC
CCCCCCCCCCCCCCE
55.0432015554
539NeddylationPCSRQSIKQQGASGE
ECCHHHHHHCCCCCE
41.6432015554
539UbiquitinationPCSRQSIKQQGASGE
ECCHHHHHHCCCCCE
41.6432015554
587PhosphorylationKVKKERDS-------
EEECCCCC-------
48.6326074081

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 I2BP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
360SPhosphorylation

17081983

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 I2BP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IRF2_HUMANIRF2physical
12799427
NFAC2_HUMANNFATC2physical
21576369
VGLL4_HUMANVGLL4physical
20702774
IF4H_HUMANEIF4Hphysical
26344197

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 I2BP2_HUMAN

loading...

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-455; SER-457; SER-460 AND SER-462, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Identification of a phosphorylation-dependent nuclear localizationmotif in interferon regulatory factor 2 binding protein 2.";
Teng A.C., Al-Montashiri N.A., Cheng B.L., Lou P., Ozmizrak P.,Chen H.H., Stewart A.F.;
PLoS ONE 6:E24100-E24100(2011).
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND PHOSPHORYLATIONAT SER-360.
"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-360; THR-392 ANDSER-457, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, 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-455; SER-457; SER-460 AND SER-462, AND MASSSPECTROMETRY.
"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-175; SER-360; SER-455;SER-457 AND SER-460, AND MASS SPECTROMETRY.

TOP