I2BPL_HUMAN - dbPTM
I2BPL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I2BPL_HUMAN
UniProt AC Q9H1B7
Protein Name Interferon regulatory factor 2-binding protein-like
Gene Name IRF2BPL
Organism Homo sapiens (Human).
Sequence Length 796
Subcellular Localization Nucleus.
Protein Description May contribute to the control of female reproductive function (By similarity). May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter..
Protein Sequence MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAAAAAAAAQQQQQQQQQQQQQQQQQQQQQQQQQLNHVDGSSKPAVLAAPSGLERYGLSAAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHTARLPNGLGGPNGFPKPTPEEGPPELNRQSPNSSSAAASVASRRGTHGGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPPPHALGSRGPPTPAPPGAPGGPACLGGTPGVSATSSSASSSTSSSVAEVGVGAGGKRPGSVSSTDQERELKEKQRNAEALAELSESLRNRAEEWASKPKMVRDTLLTLAGCTPYEVRFKKDHSLLGRVFAFDAVSKPGMDYELKLFIEYPTGSGNVYSSASGVAKQMYQDCMKDFGRGLSSGFKYLEYEKKHGSGDWRLLGDLLPEAVRFFKEGVPGADMLPQPYLDASCPMLPTALVSLSRAPSAPPGTGALPPAAPSGRGAAASLRKRKASPEPPDSAEGALKLGEEQQRQQWMANQSEALKLTMSAGGFAAPGHAAGGPPPPPPPLGPHSNRTTPPESAPQNGPSPMAALMSVADTLGTAHSPKDGSSVHSTTASARRNSSSPVSPASVPGQRRLASRNGDLNLQVAPPPPSAHPGMDQVHPQNIPDSPMANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP
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
2Phosphorylation------MSAAQVSSS
------CCHHHHCCC		32.1021406692
7Phosphorylation-MSAAQVSSSRRQSC
-CCHHHHCCCCCCCE		15.5421406692
8PhosphorylationMSAAQVSSSRRQSCY
CCHHHHCCCCCCCEE		29.0721406692
9PhosphorylationSAAQVSSSRRQSCYL
CHHHHCCCCCCCEEE		24.7921406692
13PhosphorylationVSSSRRQSCYLCDLP
HCCCCCCCEEECCCC		11.6925849741
15PhosphorylationSSRRQSCYLCDLPRM
CCCCCCEEECCCCCC		18.6628450419
69PhosphorylationGCFQDGRSPGPPPPV
CCCCCCCCCCCCCCC		39.4729255136
79SumoylationPPPPVGVKTVALSAK
CCCCCCCEEEEECHH		31.2128112733
79UbiquitinationPPPPVGVKTVALSAK
CCCCCCCEEEEECHH		31.2123000965
135PhosphorylationLNHVDGSSKPAVLAA
HHCCCCCCCCCEEEC		48.46-
152PhosphorylationGLERYGLSAAAAAAA
CHHHHCHHHHHHHHH		16.1127251275
169O-linked_GlycosylationAAAVEQRSRFEYPPP
HHHHHHHHCCCCCCC		40.8030059200
170MethylationAAVEQRSRFEYPPPP
HHHHHHHCCCCCCCC		30.52-
179O-linked_GlycosylationEYPPPPVSLGSSSHT
CCCCCCCCCCCCCCC		32.5530059200
179PhosphorylationEYPPPPVSLGSSSHT
CCCCCCCCCCCCCCC		32.5528555341
182O-linked_GlycosylationPPPVSLGSSSHTARL
CCCCCCCCCCCCCCC		33.6830059200
183O-linked_GlycosylationPPVSLGSSSHTARLP
CCCCCCCCCCCCCCC		25.0830059200
184O-linked_GlycosylationPVSLGSSSHTARLPN
CCCCCCCCCCCCCCC		26.9330059200
186O-linked_GlycosylationSLGSSSHTARLPNGL
CCCCCCCCCCCCCCC		18.5430059200
203PhosphorylationPNGFPKPTPEEGPPE
CCCCCCCCCCCCCCC		49.8430108239
215PhosphorylationPPELNRQSPNSSSAA
CCCCCCCCCCCHHHH		23.8629255136
218PhosphorylationLNRQSPNSSSAAASV
CCCCCCCCHHHHHHH		29.1130266825
219PhosphorylationNRQSPNSSSAAASVA
CCCCCCCHHHHHHHH		30.5430266825
220PhosphorylationRQSPNSSSAAASVAS
CCCCCCHHHHHHHHH		23.0330266825
224PhosphorylationNSSSAAASVASRRGT
CCHHHHHHHHHHCCC		17.3130278072
227PhosphorylationSAAASVASRRGTHGG
HHHHHHHHHCCCCCC		21.9830278072
231PhosphorylationSVASRRGTHGGLVTG
HHHHHCCCCCCEECC		18.6128348404
237PhosphorylationGTHGGLVTGLPNPGG
CCCCCEECCCCCCCC		37.7428348404
251PhosphorylationGGGGPQLTVPPNLLP
CCCCCCCCCCCCCCC		26.2222210691
286PhosphorylationLGSRGPPTPAPPGAP
CCCCCCCCCCCCCCC		34.9027251275
302O-linked_GlycosylationGPACLGGTPGVSATS
CCCCCCCCCCCCCCC		18.3130059200
306O-linked_GlycosylationLGGTPGVSATSSSAS
CCCCCCCCCCCCCCC		31.5730059200
308O-linked_GlycosylationGTPGVSATSSSASSS
CCCCCCCCCCCCCCC		22.9530059200
313PhosphorylationSATSSSASSSTSSSV
CCCCCCCCCCCCCCC		27.1115302935
314O-linked_GlycosylationATSSSASSSTSSSVA
CCCCCCCCCCCCCCE		37.0330059200
319O-linked_GlycosylationASSSTSSSVAEVGVG
CCCCCCCCCEEECCC		25.7230059200
334PhosphorylationAGGKRPGSVSSTDQE
CCCCCCCCCCCHHHH		22.8529255136
336PhosphorylationGKRPGSVSSTDQERE
CCCCCCCCCHHHHHH		29.2629255136
337PhosphorylationKRPGSVSSTDQEREL
CCCCCCCCHHHHHHH		33.5723927012
338PhosphorylationRPGSVSSTDQERELK
CCCCCCCHHHHHHHH		33.9123927012
371UbiquitinationRAEEWASKPKMVRDT
HHHHHHCCCHHHHHH		40.6933845483
373UbiquitinationEEWASKPKMVRDTLL
HHHHCCCHHHHHHHH		54.48-
388PhosphorylationTLAGCTPYEVRFKKD
HHCCCCCEEEEECCC		14.65-
394MalonylationPYEVRFKKDHSLLGR
CEEEEECCCCHHHHH		58.9426320211
397PhosphorylationVRFKKDHSLLGRVFA
EEECCCCHHHHHEEE		35.11-
410UbiquitinationFAFDAVSKPGMDYEL
EEEEECCCCCCCEEE		38.7029967540
454PhosphorylationKDFGRGLSSGFKYLE
HHHCCHHHHHCCEEE		31.1028102081
455PhosphorylationDFGRGLSSGFKYLEY
HHCCHHHHHCCEEEE		53.9828102081
458SumoylationRGLSSGFKYLEYEKK
CHHHHHCCEEEEEHH		53.07-
458UbiquitinationRGLSSGFKYLEYEKK
CHHHHHCCEEEEEHH		53.0729967540
458SumoylationRGLSSGFKYLEYEKK
CHHHHHCCEEEEEHH		53.07-
458MalonylationRGLSSGFKYLEYEKK
CHHHHHCCEEEEEHH		53.0726320211
458AcetylationRGLSSGFKYLEYEKK
CHHHHHCCEEEEEHH		53.0722424773
464UbiquitinationFKYLEYEKKHGSGDW
CCEEEEEHHHCCCCC		49.5229967540
515PhosphorylationPTALVSLSRAPSAPP
CCHHHHHHCCCCCCC		20.9124719451
519PhosphorylationVSLSRAPSAPPGTGA
HHHHCCCCCCCCCCC		53.0430266825
524PhosphorylationAPSAPPGTGALPPAA
CCCCCCCCCCCCCCC		25.6730266825
540PhosphorylationSGRGAAASLRKRKAS
CCCCHHHHHHHCCCC		24.7929396449
547PhosphorylationSLRKRKASPEPPDSA
HHHHCCCCCCCCCCH		32.6029255136
553PhosphorylationASPEPPDSAEGALKL
CCCCCCCCHHHHHHH		33.7123927012
610PhosphorylationLGPHSNRTTPPESAP
CCCCCCCCCCCCCCC		48.1530278072
611PhosphorylationGPHSNRTTPPESAPQ
CCCCCCCCCCCCCCC		33.3430278072
615PhosphorylationNRTTPPESAPQNGPS
CCCCCCCCCCCCCCC		51.5323090842
622PhosphorylationSAPQNGPSPMAALMS
CCCCCCCCHHHHHHH		28.8030278072
629PhosphorylationSPMAALMSVADTLGT
CHHHHHHHHHHHHCC		18.2730278072
633PhosphorylationALMSVADTLGTAHSP
HHHHHHHHHCCCCCC		19.8330278072
636PhosphorylationSVADTLGTAHSPKDG
HHHHHHCCCCCCCCC		25.0622115753
639PhosphorylationDTLGTAHSPKDGSSV
HHHCCCCCCCCCCCC		31.0530278072
644PhosphorylationAHSPKDGSSVHSTTA
CCCCCCCCCCCCCCC		39.0425404012
645PhosphorylationHSPKDGSSVHSTTAS
CCCCCCCCCCCCCCC		29.4025404012
648PhosphorylationKDGSSVHSTTASARR
CCCCCCCCCCCCCCC		25.8730576142
649PhosphorylationDGSSVHSTTASARRN
CCCCCCCCCCCCCCC		16.1129449344
650PhosphorylationGSSVHSTTASARRNS
CCCCCCCCCCCCCCC		22.9429449344
652PhosphorylationSVHSTTASARRNSSS
CCCCCCCCCCCCCCC		21.8825404012
657PhosphorylationTASARRNSSSPVSPA
CCCCCCCCCCCCCCC		30.3129255136
658PhosphorylationASARRNSSSPVSPAS
CCCCCCCCCCCCCCC		42.0629255136
659PhosphorylationSARRNSSSPVSPASV
CCCCCCCCCCCCCCC		29.1919664994
662PhosphorylationRNSSSPVSPASVPGQ
CCCCCCCCCCCCCCC		20.3829255136
665PhosphorylationSSPVSPASVPGQRRL
CCCCCCCCCCCCHHH		32.0322167270
674PhosphorylationPGQRRLASRNGDLNL
CCCHHHHHCCCCCCE		30.7625332170
689PhosphorylationQVAPPPPSAHPGMDQ
EECCCCCCCCCCCCC		45.0122210691
705PhosphorylationHPQNIPDSPMANSGP
CCCCCCCCCCCCCCC		15.9526074081
710PhosphorylationPDSPMANSGPLCCTI
CCCCCCCCCCEEEEE		32.0526074081
716PhosphorylationNSGPLCCTICHERLE
CCCCEEEEEEHHHCC		26.1626074081
748UbiquitinationPCSRESIKAQGATGE
ECCHHHHHHCCCCCE		43.8932015554
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 I2BPL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I2BPL_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 I2BPL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSF_HUMANNSFphysical
22939629
HIBCH_HUMANHIBCHphysical
22939629
ETFB_HUMANETFBphysical
22939629
NPM3_HUMANNPM3physical
22863883
I2BP2_HUMANIRF2BP2physical
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 I2BPL_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-69; SER-547; SER-657;SER-659 AND SER-662, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547; SER-659; SER-662AND SER-665, 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-69; SER-547; SER-657;SER-658; SER-659 AND SER-662, 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-657; SER-658; SER-659AND SER-662, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-659, ANDMASS SPECTROMETRY.
"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-547, 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-547, AND MASSSPECTROMETRY.
"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-657; SER-659 ANDSER-662, AND MASS SPECTROMETRY.

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