I2BPL_MOUSE - dbPTM
I2BPL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I2BPL_MOUSE
UniProt AC Q8K3X4
Protein Name Interferon regulatory factor 2-binding protein-like
Gene Name Irf2bpl
Organism Mus musculus (Mouse).
Sequence Length 775
Subcellular Localization Nucleus.
Protein Description May contribute to the control of female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity)..
Protein Sequence MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAQQQQQQQQQQQQQLNHVDGSTKPAVLAAPSGLERYGLSAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHAARLPNGLGGPNGFPKPAPEEGPPELNRQSPNSSSAATSVASRRGTHSGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPHGLGGSRGPPTPAPPGAPGGPACLGGPPGVSATVSSAPSSTSSTVAEVGVGAAGKRPGSVSSTDQERELKEKQRNAEALAELSESLRNRAEEWANKPKMVRDTLLTLAGCTPYEVRFKKDHSLLGRVFAFDAVSKPGMDYELKLFIEYPTGSGNVYSSASGVAKQMYQDCMKDFGRGLSSGFKYLEYEKKHGSGDWRLLGDLLPEAVRFFKEGVPGADMLPQPYLDASCPMLPTALVSLSRAPSAPPGTGALPPAAPTGRGAASSLRKRKASPEPPDSAESALKLGEEQQRQQWMANQSEALKLTMSAGGFAAPGHSAGGPPPPPPPLGPHSNRTTPPESAPQNGPSPMAALMSVADTLGTAHSPKDGSSVHSTTASARRNSSSPVSPASVPGQRRLASRNGDLNLQVAPPPPSAHPGMDQVHPQNIPDSPMANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP
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
13PhosphorylationVSSSRRQSCYLCDLP
HCCCCCCCEEECCCC		11.6926239621
15PhosphorylationSSRRQSCYLCDLPRM
CCCCCCEEECCCCCC		18.6625162660
69PhosphorylationGCFQDGRSPGPPPPV
CCCCCCCCCCCCCCC		39.4727087446
79AcetylationPPPPVGVKTVALSAK
CCCCCCCEEEEECHH		31.2122826441
79UbiquitinationPPPPVGVKTVALSAK
CCCCCCCEEEEECHH		31.2122790023
159O-linked_GlycosylationEYPPPPVSLGSSSHA
CCCCCCCCCCCCCCH		32.5555411795
195PhosphorylationPPELNRQSPNSSSAA
CCCCCCCCCCCCCHH		23.8627087446
198PhosphorylationLNRQSPNSSSAATSV
CCCCCCCCCCHHHHH		29.1123684622
199PhosphorylationNRQSPNSSSAATSVA
CCCCCCCCCHHHHHH		30.5422942356
200PhosphorylationRQSPNSSSAATSVAS
CCCCCCCCHHHHHHH		23.0325619855
203PhosphorylationPNSSSAATSVASRRG
CCCCCHHHHHHHHCC		24.3725619855
204PhosphorylationNSSSAATSVASRRGT
CCCCHHHHHHHHCCC		15.8025619855
207PhosphorylationSAATSVASRRGTHSG
CHHHHHHHHCCCCCC		21.9825168779
265PhosphorylationGGSRGPPTPAPPGAP
CCCCCCCCCCCCCCC		34.9028973931
313PhosphorylationAAGKRPGSVSSTDQE
CCCCCCCCCCCHHHH		22.8525521595
315PhosphorylationGKRPGSVSSTDQERE
CCCCCCCCCHHHHHH		29.2627742792
316PhosphorylationKRPGSVSSTDQEREL
CCCCCCCCHHHHHHH		33.5725521595
317PhosphorylationRPGSVSSTDQERELK
CCCCCCCHHHHHHHH		33.9125521595
339PhosphorylationALAELSESLRNRAEE
HHHHHHHHHHHHHHH		29.2922324799
376PhosphorylationVRFKKDHSLLGRVFA
EEECCCCHHHHHEEE		35.11-
402PhosphorylationELKLFIEYPTGSGNV
EEEEEEECCCCCCCC		10.9822817900
411PhosphorylationTGSGNVYSSASGVAK
CCCCCCCCCHHHHHH		18.3621183079
412PhosphorylationGSGNVYSSASGVAKQ
CCCCCCCCHHHHHHH		14.5721183079
437UbiquitinationRGLSSGFKYLEYEKK
CHHHHHCEEEEEEHH		53.0722790023
498PhosphorylationVSLSRAPSAPPGTGA
HHHHCCCCCCCCCCC		53.0425521595
503PhosphorylationAPSAPPGTGALPPAA
CCCCCCCCCCCCCCC		25.6725619855
526PhosphorylationSLRKRKASPEPPDSA
HHHHHCCCCCCCCCH		32.6027087446
532PhosphorylationASPEPPDSAESALKL
CCCCCCCCHHHHHHH		39.4425521595
535PhosphorylationEPPDSAESALKLGEE
CCCCCHHHHHHHCHH		38.3225619855
589PhosphorylationLGPHSNRTTPPESAP
CCCCCCCCCCCCCCC		48.1520139300
590PhosphorylationGPHSNRTTPPESAPQ
CCCCCCCCCCCCCCC		33.3420139300
594PhosphorylationNRTTPPESAPQNGPS
CCCCCCCCCCCCCCC		51.5323649490
601PhosphorylationSAPQNGPSPMAALMS
CCCCCCCCHHHHHHH		28.8021659605
608PhosphorylationSPMAALMSVADTLGT
CHHHHHHHHHHHHCC		18.2726745281
612PhosphorylationALMSVADTLGTAHSP
HHHHHHHHHCCCCCC		19.8326745281
615PhosphorylationSVADTLGTAHSPKDG
HHHHHHCCCCCCCCC		25.0621082442
618PhosphorylationDTLGTAHSPKDGSSV
HHHCCCCCCCCCCCC		31.0525177544
623PhosphorylationAHSPKDGSSVHSTTA
CCCCCCCCCCCCCCC		39.0426160508
624PhosphorylationHSPKDGSSVHSTTAS
CCCCCCCCCCCCCCC		29.4026160508
627PhosphorylationKDGSSVHSTTASARR
CCCCCCCCCCCCCCC		25.8726160508
628PhosphorylationDGSSVHSTTASARRN
CCCCCCCCCCCCCCC		16.1126160508
629PhosphorylationGSSVHSTTASARRNS
CCCCCCCCCCCCCCC		22.9426160508
631PhosphorylationSVHSTTASARRNSSS
CCCCCCCCCCCCCCC		21.8822668510
636PhosphorylationTASARRNSSSPVSPA
CCCCCCCCCCCCCCC		30.3127087446
637PhosphorylationASARRNSSSPVSPAS
CCCCCCCCCCCCCCC		42.0627087446
638PhosphorylationSARRNSSSPVSPASV
CCCCCCCCCCCCCCC		29.1927087446
641PhosphorylationRNSSSPVSPASVPGQ
CCCCCCCCCCCCCCC		20.3827087446
644PhosphorylationSSPVSPASVPGQRRL
CCCCCCCCCCCCHHH		32.0327087446
716AcetylationCPSVPSHKFCFPCSR
CCCCCCCCCEEECCH		48.4422826441
727UbiquitinationPCSRESIKAQGATGE
ECCHHHHHHCCCCCE		43.89-
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I2BPL_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of I2BPL_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of I2BPL_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND SER-526, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-636; SER-637;SER-638 AND SER-641, AND MASS SPECTROMETRY.

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