Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  AT-rich interactive domain-containing protein 1B  

UniProtKB / Swiss-Prot ID :  ARI1B_HUMAN

Gene Name (Synonyms) : 
ARID1B, BAF250B, DAN15, KIAA1235, OSA2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Binds DNA non-specifically. 

Protein Sequence MAHNAGAAAAAGTHSAKSGGSEAALKEGGSAAALSSSSSSSAAAAAASSSSSSGPGSAMETGLLPNHKLK...
Predicted Secondary Structure CCCCCCCCHHCCCCCCCCCCCHHHHHCCCCCCEECCCCCCHHHHHHCCCCCCCCCCHHHHHCCCCCCHHC...
Protein Variant
LocationDescription
11A -> AA. VAR_067662
45Missing. VAR_067663
82Q -> H. VAR_067664
246G -> S. VAR_067665
318Missing. VAR_067666
319Missing. VAR_067667
327Missing. VAR_067668
333Missing. VAR_067669
363A -> V. VAR_067670
396G -> A. VAR_067671
429M -> V. VAR_067672
450P -> PP. VAR_067673
497S -> N. VAR_067674
531M -> T. VAR_067675
814G -> A (in a breast cancer sample;somatic mutation).
876Q -> E. VAR_067676
980Q -> L. VAR_067677
1092V -> I. VAR_067678
1249Q -> P. VAR_067679
1271G -> E. VAR_067680
1303G -> R. VAR_067681
1321S -> N. VAR_067682
1411P -> S. VAR_067683
1466Q -> K. VAR_067684
1506R -> H. VAR_067685
1573T -> M. VAR_067686
1659N -> S. VAR_067687
1733Missing. VAR_067688
1773K -> R. VAR_067689
1851D -> N. VAR_067690
1898K -> R. VAR_067691
1954K -> R. VAR_067692
2163Q -> R. VAR_067693
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAHNAG
---CCCCCC
18.88UniProtKB
Link-
502PhosphoserineHPAMSPGTP
CCCCCCCCC
23.45Phosphositeplus
Link-
516PhosphoserineRSQGSPMDP
CCCCCCCCC
14.93PhosphoELM
Link-
516PhosphoserineRSQGSPMDP
CCCCCCCCC
14.93Phosphositeplus
Link-
516PhosphoserineRSQGSPMDP
CCCCCCCCC
14.93SysPTM
Link-
516Phosphoserine.RSQGSPMDP
CCCCCCCCC
14.93UniProtKB
Link-
632PhosphoserineQQDMSQEGY
CCCCCCCCC
33.11Phosphositeplus
Link-
1189PhosphoserineTGSNSMAEV
CCCCHHHHC
22.52HPRD
Link-
1240PhosphoserinePKRNSMTPN
CCCCCCCCC
28.24Phosphositeplus
Link-
1242PhosphothreonineRNSMTPNAP
CCCCCCCCC
17.14Phosphositeplus
Link-
1497PhosphoserineINHESQWPS
CCCCCCCCC
29.96HPRD
Link-
1497PhosphoserineINHESQWPS
CCCCCCCCC
29.96HPRD
Link-
1501PhosphoserineSQWPSHVSQ
CCCCCCCCC
33.30HPRD
Link-
1542PhosphoserineSRAPSPASF
CCCCCCCCC
31.92Phosphositeplus
Link-
1555PhosphoserineENRMSPSKS
CCCCCCCCC
23.84PhosphoELM
Link-
1555PhosphoserineENRMSPSKS
CCCCCCCCC
23.84Phosphositeplus
Link-
1555PhosphoserineENRMSPSKS
CCCCCCCCC
23.84SysPTM
Link-
1555Phosphoserine.ENRMSPSKS
CCCCCCCCC
23.84UniProtKB
Link-
1557PhosphoserineRMSPSKSPF
CCCCCCCCC
38.16Phosphositeplus
Link-
1559PhosphoserineSPSKSPFLP
CCCCCCCCC
25.81PhosphoELM
Link-
1559PhosphoserineSPSKSPFLP
CCCCCCCCC
25.81Phosphositeplus
Link-
1559PhosphoserineSPSKSPFLP
CCCCCCCCC
25.81SysPTM
Link-
1559Phosphoserine.SPSKSPFLP
CCCCCCCCC
25.81UniProtKB
Link-
1564PhosphoserinePFLPSMKMQ
CCCCCCCCH
32.93Phosphositeplus
Link-
1566N6-acetyllysineLPSMKMQKV
CCCCCCHHC
42.38Phosphositeplus
Link-
1566N6-acetyllysine.LPSMKMQKV
CCCCCCHHC
42.38UniProtKB
Link-
1710PhosphoserineDDSQSLADD
HHHCCCCCC
29.49HPRD
Link-
1715PhosphoserineLADDSGKEE
CCCCCCCCC
52.92Phosphositeplus
Link-
1777N6-acetyllysineKLPIKIVKK
CCCEEEEEC
39.24Phosphositeplus
Link-
1777N6-acetyllysine.KLPIKIVKK
CCCEEEEEC
39.24UniProtKB
Link-
2097Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SRQEKFYAT
HHHHHHHHH
35.02Phosphositeplus
Link-
2187Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CRAAKALLA
HHHHHHHHH
38.28Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RELB_HUMANphysical interactionMINT-49019MINT14743216
SMCA4_HUMANphysical interaction
physical interaction
physical interaction
EBI-684569
EBI-680030
EBI-679
intact12200431
12200431
12200431
SMCA2_HUMANin vitro
in vivo
HPRD:10660HPRD12200431
SMCA4_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:10660HPRD11988099
12200431
ARI1B_HUMANin vitroHPRD:10660HPRD11078522
SMAD9_HUMANyeast 2-hybridHPRD:10660HPRD15231748
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Disease Reference
Kegg disease
OMIM disease
614562Mental retardation, autosomal dominant 12 (MRD12)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1566 AND LYS-1777, 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, 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-1555, 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-516; SER-1555 ANDSER-1559, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures