ARI3B_HUMAN - dbPTM
ARI3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARI3B_HUMAN
UniProt AC Q8IVW6
Protein Name AT-rich interactive domain-containing protein 3B
Gene Name ARID3B
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Nucleus .
Protein Description Transcription factor which may be involved in neuroblastoma growth and malignant transformation. Favors nuclear targeting of ARID3A..
Protein Sequence MEPLQQQQQQQQQQQKQPHLAPLQMDAREKQGQQMREAQFLYAQKLVTQPTLLSATAGRPSGSTPLGPLARVPPTAAVAQVFERGNMNSEPEEEDGGLEDEDGDDEVAEVAEKETQAASKYFHVQKVARQDPRVAPMSNLLPAPGLPPHGQQAKEDHTKDASKASPSVSTAGQPNWNLDEQLKQNGGLAWSDDADGGRGREISRDFAKLYELDGDPERKEFLDDLFVFMQKRGTPINRIPIMAKQILDLYMLYKLVTEKGGLVEIINKKIWREITKGLNLPTSITSAAFTLRTQYMKYLYAYECEKKALSSPAELQAAIDGNRREGRRPSYSSSLFGYSPAAATAAAAAGAPALLSPPKIRFPILGLGSSSGTNTSSPRISPATTLRKGDGAPVTTVPVPNRLAVPVTLASQQAGTRTAALEQLRERLESGEPAEKKASRLSEEEQRLVQQAFQRNFFSMARQLPMKIRINGRAEDRAEASAAALNLTTSSIGSINMSVDIDGTTYAGVLFAQKPVVHLITGSAPQSLGSSASSSSSSHCSPSPTSSRGTPSAEPSTSWSL
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
1Acetylation-------MEPLQQQQ
-------CCHHHHHH		12.3519413330
61PhosphorylationSATAGRPSGSTPLGP
HHCCCCCCCCCCCCC		43.9728555341
75PhosphorylationPLARVPPTAAVAQVF
CCCCCCCCHHHHHHH		22.60-
89PhosphorylationFERGNMNSEPEEEDG
HHCCCCCCCCCCCCC		43.7022617229
89 (in isoform 4)Phosphorylation-43.70-
120AcetylationKETQAASKYFHVQKV
HHHHHHHHHHHHHHH		47.4030587025
121PhosphorylationETQAASKYFHVQKVA
HHHHHHHHHHHHHHH		9.0927642862
162PhosphorylationEDHTKDASKASPSVS
HHHCCCHHHCCCCCC		38.6028450419
165PhosphorylationTKDASKASPSVSTAG
CCCHHHCCCCCCCCC		22.8025159151
165O-linked_GlycosylationTKDASKASPSVSTAG
CCCHHHCCCCCCCCC		22.8023301498
165 (in isoform 4)Phosphorylation-22.8027251275
167PhosphorylationDASKASPSVSTAGQP
CHHHCCCCCCCCCCC		26.6330108239
169PhosphorylationSKASPSVSTAGQPNW
HHCCCCCCCCCCCCC		19.5130108239
170PhosphorylationKASPSVSTAGQPNWN
HCCCCCCCCCCCCCC		32.4328450419
208UbiquitinationEISRDFAKLYELDGD
EECHHHHHHHCCCCC		52.1529967540
210PhosphorylationSRDFAKLYELDGDPE
CHHHHHHHCCCCCHH		17.4627642862
234PhosphorylationVFMQKRGTPINRIPI
HHHHHCCCCCCHHHH		25.6526670566
286PhosphorylationNLPTSITSAAFTLRT
CCCCHHHHHHHHHHH		18.87-
290PhosphorylationSITSAAFTLRTQYMK
HHHHHHHHHHHHHHH		15.5924719451
310PhosphorylationECEKKALSSPAELQA
HHHHHHCCCHHHHHH		38.8530108239
311PhosphorylationCEKKALSSPAELQAA
HHHHHCCCHHHHHHH		29.0421815630
330PhosphorylationRREGRRPSYSSSLFG
CCCCCCCCCCCCHHC		35.5228450419
331PhosphorylationREGRRPSYSSSLFGY
CCCCCCCCCCCHHCC		18.4328450419
331 (in isoform 4)Phosphorylation-18.4324719451
332PhosphorylationEGRRPSYSSSLFGYS
CCCCCCCCCCHHCCC		20.1428450419
332 (in isoform 4)Phosphorylation-20.1427251275
333PhosphorylationGRRPSYSSSLFGYSP
CCCCCCCCCHHCCCH		23.8728450419
334PhosphorylationRRPSYSSSLFGYSPA
CCCCCCCCHHCCCHH		23.0630576142
338PhosphorylationYSSSLFGYSPAAATA
CCCCHHCCCHHHHHH		12.2630576142
339PhosphorylationSSSLFGYSPAAATAA
CCCHHCCCHHHHHHH		14.4028450419
344PhosphorylationGYSPAAATAAAAAGA
CCCHHHHHHHHHCCC		16.4728450419
356PhosphorylationAGAPALLSPPKIRFP
CCCCHHCCCCCCCCC		39.7530108239
361Asymmetric dimethylarginineLLSPPKIRFPILGLG
HCCCCCCCCCEECCC		37.10-
361MethylationLLSPPKIRFPILGLG
HCCCCCCCCCEECCC		37.10-
371PhosphorylationILGLGSSSGTNTSSP
EECCCCCCCCCCCCC		51.8629978859
373PhosphorylationGLGSSSGTNTSSPRI
CCCCCCCCCCCCCCC		36.9529978859
375PhosphorylationGSSSGTNTSSPRISP
CCCCCCCCCCCCCCC		30.3529978859
376PhosphorylationSSSGTNTSSPRISPA
CCCCCCCCCCCCCCC		40.1829978859
377PhosphorylationSSGTNTSSPRISPAT
CCCCCCCCCCCCCCC		19.0318669648
377 (in isoform 4)Phosphorylation-19.03-
381PhosphorylationNTSSPRISPATTLRK
CCCCCCCCCCCCCCC		15.1230108239
384 (in isoform 4)Phosphorylation-29.73-
384PhosphorylationSPRISPATTLRKGDG
CCCCCCCCCCCCCCC		29.7318669648
395PhosphorylationKGDGAPVTTVPVPNR
CCCCCCCEEEECCCC		22.4824129246
396PhosphorylationGDGAPVTTVPVPNRL
CCCCCCEEEECCCCE		24.0524129246
402MethylationTTVPVPNRLAVPVTL
EEEECCCCEEEECEE		20.25-
408O-linked_GlycosylationNRLAVPVTLASQQAG
CCEEEECEEECCCCC		15.5523301498
411O-linked_GlycosylationAVPVTLASQQAGTRT
EEECEEECCCCCCHH		26.4123301498
416O-linked_GlycosylationLASQQAGTRTAALEQ
EECCCCCCHHHHHHH		28.0623301498
439PhosphorylationEPAEKKASRLSEEEQ
CCHHHHHHHCCHHHH		42.51-
442PhosphorylationEKKASRLSEEEQRLV
HHHHHHCCHHHHHHH		41.6824905233
521PhosphorylationKPVVHLITGSAPQSL
CCEEEEEECCCCCHH		31.2929449344
523PhosphorylationVVHLITGSAPQSLGS
EEEEEECCCCCHHCC		28.2929449344
527PhosphorylationITGSAPQSLGSSASS
EECCCCCHHCCCCCC		33.3729449344
530PhosphorylationSAPQSLGSSASSSSS
CCCCHHCCCCCCCCC		28.2029449344
531PhosphorylationAPQSLGSSASSSSSS
CCCHHCCCCCCCCCC		30.3029449344
533PhosphorylationQSLGSSASSSSSSHC
CHHCCCCCCCCCCCC		32.4729449344
534PhosphorylationSLGSSASSSSSSHCS
HHCCCCCCCCCCCCC		33.6829449344
535PhosphorylationLGSSASSSSSSHCSP
HCCCCCCCCCCCCCC		31.5729449344
536PhosphorylationGSSASSSSSSHCSPS
CCCCCCCCCCCCCCC		37.5029449344
537PhosphorylationSSASSSSSSHCSPSP
CCCCCCCCCCCCCCC		26.5029449344
538PhosphorylationSASSSSSSHCSPSPT
CCCCCCCCCCCCCCC		30.3829449344
541PhosphorylationSSSSSHCSPSPTSSR
CCCCCCCCCCCCCCC		24.0029449344
543PhosphorylationSSSHCSPSPTSSRGT
CCCCCCCCCCCCCCC		25.2329449344
545PhosphorylationSHCSPSPTSSRGTPS
CCCCCCCCCCCCCCC		43.6129449344
546PhosphorylationHCSPSPTSSRGTPSA
CCCCCCCCCCCCCCC		22.7929449344
547PhosphorylationCSPSPTSSRGTPSAE
CCCCCCCCCCCCCCC		36.8929449344
556PhosphorylationGTPSAEPSTSWSL--
CCCCCCCCCCCCC--		26.9521406692
557PhosphorylationTPSAEPSTSWSL---
CCCCCCCCCCCC---		44.9521406692
558PhosphorylationPSAEPSTSWSL----
CCCCCCCCCCC----		21.0021406692
558O-linked_GlycosylationPSAEPSTSWSL----
CCCCCCCCCCC----		21.0023301498
560PhosphorylationAEPSTSWSL------
CCCCCCCCC------		24.7830108239
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 ARI3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARI3B_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 ARI3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 ARI3B_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-165, 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-89, 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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-165, 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-89, AND MASSSPECTROMETRY.

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