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Q8NFD5 (ARI1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AT-rich interactive domain-containing protein 1B

Short name=ARID domain-containing protein 1B
Alternative name(s):
BRG1-associated factor 250b
Short name=BAF250B
BRG1-binding protein hELD/OSA1
Osa homolog 2
Short name=hOsa2
p250R
Gene names
Name:ARID1B
Synonyms:BAF250B, DAN15, KIAA1235, OSA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Component of SWI/SNF chromatin remodeling complexes, in some of which it can be mutually exclusive with ARID1A/BAF250A. Component of the BAF (SWI/SNF-A) complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the SWI/SNF-B (PBAF) complex, at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PB1/BAF180, ARID2/BAF200, ARID1A/BAF250A or ARID1B/BAF250B and actin. Component of a SWI/SNF-like EPAFb complex, at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, SMARCC1/BAF155, SMARCC2/BAF170, ARID1B/BAF250B, MLLT1/ENL and actin. Component of a SWI/SNF-like complex containing ARID1A/BAF250A and ARID1B/BAF250B. Interacts through its C-terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A. Interacts with SMARCC1/BAF155. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin By similarity. Ref.1 Ref.5 Ref.6 Ref.7 Ref.19 Ref.21

Subcellular location

Nucleus Ref.7.

Tissue specificity

Widely expressed with high levels in heart, skeletal muscle and kidney. Ref.5 Ref.6 Ref.7

Polymorphism

The poly-Gln region is polymorphic and the number of Gln varies in the population (from 17 to 23).

Involvement in disease

Mental retardation, autosomal dominant 12 (MRD12) [MIM:614562]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD12 patients present with moderate to severe psychomotor retardation, and most show evidence of muscular hypotonia. In many patients, expressive speech is more severely affected than receptive function. Additional common findings include short stature, abnormal head shape and low-set, posteriorly rotated, and abnormally shaped ears, downslanting palpebral fissures, a bulbous nasal tip, a thin upper lip, minor teeth anomalies, and brachydactyly or single palmar creases. Autistic features are uncommon.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17

Sequence similarities

Contains 1 ARID domain.

Caution

It is uncertain whether Met-1 or Met-59 is the initiator.

Sequence caution

The sequence AAL76077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAN70985.1 differs from that shown. Reason: Frameshift at positions 857 and 863.

The sequence CAA69592.1 differs from that shown. Reason: Frameshift at position 132.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMARCA2P515313EBI-679921,EBI-679562
SMARCA4P515323EBI-679921,EBI-302489

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NFD5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8NFD5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     579-579: Q → QDSGDATWKETFWL
Isoform 3 (identifier: Q8NFD5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1032-1032: K → KDSYSSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGWPKTPSSP
Isoform 4 (identifier: Q8NFD5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-750: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 22362235AT-rich interactive domain-containing protein 1B
PRO_0000200576

Regions

Domain1053 – 114492ARID
Motif419 – 4235LXXLL
Motif2036 – 20405LXXLL
Compositional bias2 – 4746Ala-rich
Compositional bias35 – 5723Ser-rich
Compositional bias81 – 10424His-rich
Compositional bias107 – 13125Gln-rich
Compositional bias114 – 13118Poly-Gln
Compositional bias141 – 401261Gly-rich
Compositional bias329 – 493165Ala-rich
Compositional bias574 – 63360Gln-rich
Compositional bias684 – 77188Ser-rich
Compositional bias932 – 9354Poly-Ala
Compositional bias1034 – 10374Poly-Ser
Compositional bias1441 – 14444Poly-Ser
Compositional bias1459 – 1597139Pro-rich
Compositional bias1833 – 18364Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue5161Phosphoserine Ref.9
Modified residue15551Phosphoserine Ref.9 Ref.13 Ref.14
Modified residue15591Phosphoserine Ref.9 Ref.13
Modified residue17151Phosphoserine Ref.14
Modified residue17771N6-acetyllysine Ref.12

Natural variations

Alternative sequence1 – 750750Missing in isoform 4.
VSP_040800
Alternative sequence5791Q → QDSGDATWKETFWL in isoform 2.
VSP_015226
Alternative sequence10321K → KDSYSSQGISQPPTPGNLPV PSPMSPSSASISSFHGDESD SISSPGWPKTPSSP in isoform 3.
VSP_015227
Natural variant111A → AA. Ref.15
VAR_067662
Natural variant45 – 473Missing.
VAR_067663
Natural variant821Q → H. Ref.15
VAR_067664
Natural variant2461G → S. Ref.15
VAR_067665
Natural variant318 – 3192Missing.
VAR_067666
Natural variant3191Missing. Ref.15
VAR_067667
Natural variant327 – 3282Missing.
VAR_067668
Natural variant333 – 3375Missing.
VAR_067669
Natural variant3631A → V. Ref.15
VAR_067670
Natural variant3961G → A. Ref.15
VAR_067671
Natural variant4291M → V. Ref.15
VAR_067672
Natural variant4501P → PP. Ref.15
VAR_067673
Natural variant4971S → N. Ref.15
VAR_067674
Natural variant5311M → T. Ref.15
VAR_067675
Natural variant8141G → A in a breast cancer sample; somatic mutation. Ref.23
VAR_036257
Natural variant8761Q → E. Ref.15
VAR_067676
Natural variant9801Q → L. Ref.15
VAR_067677
Natural variant10921V → I. Ref.15
VAR_067678
Natural variant12491Q → P. Ref.15
VAR_067679
Natural variant12711G → E. Ref.15
VAR_067680
Natural variant13031G → R. Ref.15
VAR_067681
Natural variant13211S → N. Ref.15
VAR_067682
Natural variant14111P → S. Ref.15
VAR_067683
Natural variant14661Q → K. Ref.15
VAR_067684
Natural variant15061R → H. Ref.15
VAR_067685
Natural variant15731T → M. Ref.15
VAR_067686
Natural variant16591N → S. Ref.15
VAR_067687
Natural variant17331Missing. Ref.15
VAR_067688
Natural variant17731K → R. Ref.15
VAR_067689
Natural variant18511D → N. Ref.15
VAR_067690
Natural variant18981K → R. Ref.15
VAR_067691
Natural variant19541K → R. Ref.15
VAR_067692
Natural variant21631Q → R. Ref.15
VAR_067693

Experimental info

Sequence conflict334 – 3363AGA → SRS in AAN03447. Ref.5
Sequence conflict4461P → A in AAN70985. Ref.6
Sequence conflict6871V → A in AAL76077. Ref.7
Sequence conflict9041T → P in AAL76077. Ref.7
Sequence conflict12011T → I in AAG36928. Ref.1
Sequence conflict13391P → S in AAN70985. Ref.6
Sequence conflict14321P → L in BAA86549. Ref.8
Sequence conflict15341P → S in AAN70985. Ref.6
Sequence conflict17131D → N in AAL76077. Ref.7
Sequence conflict21961D → N in AAG36928. Ref.1

Secondary structure

............... 2236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 4538B4747606C918

FASTA2,236236,123
        10         20         30         40         50         60 
MAHNAGAAAA AGTHSAKSGG SEAALKEGGS AAALSSSSSS SAAAAAASSS SSSGPGSAME 

        70         80         90        100        110        120 
TGLLPNHKLK TVGEAPAAPP HQQHHHHHHA HHHHHHAHHL HHHHALQQQL NQFQQQQQQQ 

       130        140        150        160        170        180 
QQQQQQQQQQ QHPISNNNSL GGAGGGAPQP GPDMEQPQHG GAKDSAAGGQ ADPPGPPLLS 

       190        200        210        220        230        240 
KPGDEDDAPP KMGEPAGGRY EHPGLGALGT QQPPVAVPGG GGGPAAVPEF NNYYGSAAPA 

       250        260        270        280        290        300 
SGGPGGRAGP CFDQHGGQQS PGMGMMHSAS AAAAGAPGSM DPLQNSHEGY PNSQCNHYPG 

       310        320        330        340        350        360 
YSRPGAGGGG GGGGGGGGGS GGGGGGGGAG AGGAGAGAVA AAAAAAAAAA GGGGGGGYGG 

       370        380        390        400        410        420 
SSAGYGVLSS PRQQGGGMMM GPGGGGAASL SKAAAGSAAG GFQRFAGQNQ HPSGATPTLN 

       430        440        450        460        470        480 
QLLTSPSPMM RSYGGSYPEY SSPSAPPPPP SQPQSQAAAA GAAAGGQQAA AGMGLGKDMG 

       490        500        510        520        530        540 
AQYAAASPAW AAAQQRSHPA MSPGTPGPTM GRSQGSPMDP MVMKRPQLYG MGSNPHSQPQ 

       550        560        570        580        590        600 
QSSPYPGGSY GPPGPQRYPI GIQGRTPGAM AGMQYPQQQM PPQYGQQGVS GYCQQGQQPY 

       610        620        630        640        650        660 
YSQQPQPPHL PPQAQYLPSQ SQQRYQPQQD MSQEGYGTRS QPPLAPGKPN HEDLNLIQQE 

       670        680        690        700        710        720 
RPSSLPDLSG SIDDLPTGTE ATLSSAVSAS GSTSSQGDQS NPAQSPFSPH ASPHLSSIPG 

       730        740        750        760        770        780 
GPSPSPVGSP VGSNQSRSGP ISPASIPGSQ MPPQPPGSQS ESSSHPALSQ SPMPQERGFM 

       790        800        810        820        830        840 
AGTQRNPQMA QYGPQQTGPS MSPHPSPGGQ MHAGISSFQQ SNSSGTYGPQ MSQYGPQGNY 

       850        860        870        880        890        900 
SRPPAYSGVP SASYSGPGPG MGISANNQMH GQGPSQPCGA VPLGRMPSAG MQNRPFPGNM 

       910        920        930        940        950        960 
SSMTPSSPGM SQQGGPGMGP PMPTVNRKAQ EAAAAVMQAA ANSAQSRQGS FPGMNQSGLM 

       970        980        990       1000       1010       1020 
ASSSPYSQPM NNSSSLMNTQ APPYSMAPAM VNSSAASVGL ADMMSPGESK LPLPLKADGK 

      1030       1040       1050       1060       1070       1080 
EEGTPQPESK SKKSSSSTTT GEKITKVYEL GNEPERKLWV DRYLTFMEER GSPVSSLPAV 

      1090       1100       1110       1120       1130       1140 
GKKPLDLFRL YVCVKEIGGL AQVNKNKKWR ELATNLNVGT SSSAASSLKK QYIQYLFAFE 

      1150       1160       1170       1180       1190       1200 
CKIERGEEPP PEVFSTGDTK KQPKLQPPSP ANSGSLQGPQ TPQSTGSNSM AEVPGDLKPP 

      1210       1220       1230       1240       1250       1260 
TPASTPHGQM TPMQGGRSST ISVHDPFSDV SDSSFPKRNS MTPNAPYQQG MSMPDVMGRM 

      1270       1280       1290       1300       1310       1320 
PYEPNKDPFG GMRKVPGSSE PFMTQGQMPN SSMQDMYNQS PSGAMSNLGM GQRQQFPYGA 

      1330       1340       1350       1360       1370       1380 
SYDRRHEPYG QQYPGQGPPS GQPPYGGHQP GLYPQQPNYK RHMDGMYGPP AKRHEGDMYN 

      1390       1400       1410       1420       1430       1440 
MQYSSQQQEM YNQYGGSYSG PDRRPIQGQY PYPYSRERMQ GPGQIQTHGI PPQMMGGPLQ 

      1450       1460       1470       1480       1490       1500 
SSSSEGPQQN MWAARNDMPY PYQNRQGPGG PTQAPPYPGM NRTDDMMVPD QRINHESQWP 

      1510       1520       1530       1540       1550       1560 
SHVSQRQPYM SSSASMQPIT RPPQPSYQTP PSLPNHISRA PSPASFQRSL ENRMSPSKSP 

      1570       1580       1590       1600       1610       1620 
FLPSMKMQKV MPTVPTSQVT GPPPQPPPIR REITFPPGSV EASQPVLKQR RKITSKDIVT 

      1630       1640       1650       1660       1670       1680 
PEAWRVMMSL KSGLLAESTW ALDTINILLY DDSTVATFNL SQLSGFLELL VEYFRKCLID 

      1690       1700       1710       1720       1730       1740 
IFGILMEYEV GDPSQKALDH NAARKDDSQS LADDSGKEEE DAECIDDDEE DEEDEEEDSE 

      1750       1760       1770       1780       1790       1800 
KTESDEKSSI ALTAPDAAAD PKEKPKQASK FDKLPIKIVK KNNLFVVDRS DKLGRVQEFN 

      1810       1820       1830       1840       1850       1860 
SGLLHWQLGG GDTTEHIQTH FESKMEIPPR RRPPPPLSSA GRKKEQEGKG DSEEQQEKSI 

      1870       1880       1890       1900       1910       1920 
IATIDDVLSA RPGALPEDAN PGPQTESSKF PFGIQQAKSH RNIKLLEDEP RSRDETPLCT 

      1930       1940       1950       1960       1970       1980 
IAHWQDSLAK RCICVSNIVR SLSFVPGNDA EMSKHPGLVL ILGKLILLHH EHPERKRAPQ 

      1990       2000       2010       2020       2030       2040 
TYEKEEDEDK GVACSKDEWW WDCLEVLRDN TLVTLANISG QLDLSAYTES ICLPILDGLL 

      2050       2060       2070       2080       2090       2100 
HWMVCPSAEA QDPFPTVGPN SVLSPQRLVL ETLCKLSIQD NNVDLILATP PFSRQEKFYA 

      2110       2120       2130       2140       2150       2160 
TLVRYVGDRK NPVCREMSMA LLSNLAQGDA LAARAIAVQK GSIGNLISFL EDGVTMAQYQ 

      2170       2180       2190       2200       2210       2220 
QSQHNLMHMQ PPPLEPPSVD MMCRAAKALL AMARVDENRS EFLLHEGRLL DISISAVLNS 

      2230 
LVASVICDVL FQIGQL 

« Hide

Isoform 2 [UniParc].

Checksum: C7E3990BF1FD9712
Show »

FASTA2,249237,661
Isoform 3 [UniParc].

Checksum: 1DD3E3DB4D4BD73E
Show »

FASTA2,289241,463
Isoform 4 [UniParc].

Checksum: D9BF024652EC0031
Show »

FASTA1,486162,470

References

« Hide 'large scale' references
[1]"SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones."
Kato H., Tjernberg A., Zhang W., Krutchinsky A.N., An W., Takeuchi T., Ohtsuki Y., Sugano S., de Bruijn D.R., Chait B.T., Roeder R.G.
J. Biol. Chem. 277:5498-5505(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), IDENTIFICATION IN THE EPAFB COMPLEX.
Tissue: Brain.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"New 5'-(CGG)-3' repeats in the human genome."
Mangel L., Ternes T., Schmitz B., Doerfler W.
J. Biol. Chem. 273:30466-30471(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-515.
[4]"Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats."
Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M., Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O., Stevanin G., Agid Y., Brice A.
Nat. Genet. 14:285-291(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-199.
[5]"Largest subunits of the human SWI/SNF chromatin-remodeling complex promote transcriptional activation by steroid hormone receptors."
Inoue H., Furukawa T., Giannakopoulos S., Zhou S., King D.S., Tanese N.
J. Biol. Chem. 277:41674-41685(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-2236 (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH SMARCA2 AND SMARCA4, IDENTIFICATION IN A SWI/SNF-LIKE COMPLEX WITH ARID1A.
[6]"Novel SWI/SNF chromatin-remodeling complexes contain a mixed-lineage leukemia chromosomal translocation partner."
Nie Z., Yan Z., Chen E.H., Sechi S., Ling C., Zhou S., Xue Y., Yang D., Murray D., Kanakubo E., Cleary M.L., Wang W.
Mol. Cell. Biol. 23:2942-2952(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 272-2236 (ISOFORM 1), TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A SWI/SNF-LIKE EPAFB COMPLEX.
[7]"Cloning and characterization of hELD/OSA1, a novel BRG1 interacting protein."
Hurlstone A.F., Olave I.A., Barker N., van Noort M., Clevers H.
Biochem. J. 364:255-264(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 491-2236 (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SMARCA4, IDENTIFICATION IN A COMPLEX WITH SMARCA4 AND SMARCD1, IDENTIFICATION IN A SWI/SNF-LIKE COMPLEX WITH ARID1A.
[8]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-2236 (ISOFORM 3).
Tissue: Brain.
[9]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516; SER-1555 AND SER-1559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555 AND SER-1559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1555 AND SER-1715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Haploinsufficiency of ARID1B, a member of the SWI/SNF-a chromatin-remodeling complex, is a frequent cause of intellectual disability."
Hoyer J., Ekici A.B., Endele S., Popp B., Zweier C., Wiesener A., Wohlleber E., Dufke A., Rossier E., Petsch C., Zweier M., Gohring I., Zink A.M., Rappold G., Schrock E., Wieczorek D., Riess O., Engels H., Rauch A., Reis A.
Am. J. Hum. Genet. 90:565-572(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRD12, VARIANTS ALA-11 INS; 45-ALA--ALA-47 DEL; HIS-82; SER-246; 318-GLY-GLY-319 DEL; GLY-319 DEL; 327-GLY-GLY-328 DEL; 333-GLY--GLY-337 DEL; VAL-363; ALA-396; VAL-429; PRO-450 INS; ASN-497; THR-531; GLU-876; LEU-980; ILE-1092; PRO-1249; GLU-1271; ARG-1303; ASN-1321; SER-1411; LYS-1466; HIS-1506; MET-1573; SER-1659; GLU-1733 DEL; ARG-1773; ASN-1851; ARG-1898; ARG-1954 AND ARG-2163.
[16]"Mutations affecting components of the SWI/SNF complex cause Coffin-Siris syndrome."
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S. expand/collapse author list , Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.
Nat. Genet. 44:376-378(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRD12.
[17]"Mutations in SWI/SNF chromatin remodeling complex gene ARID1B cause Coffin-Siris syndrome."
Santen G.W., Aten E., Sun Y., Almomani R., Gilissen C., Nielsen M., Kant S.G., Snoeck I.N., Peeters E.A., Hilhorst-Hofstee Y., Wessels M.W., den Hollander N.S., Ruivenkamp C.A., van Ommen G.J., Breuning M.H., den Dunnen J.T., van Haeringen A., Kriek M.
Nat. Genet. 44:379-380(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRD12.
[18]"Recent advances in understanding chromatin remodeling by SWI/SNF complexes."
Martens J.A., Winston F.
Curr. Opin. Genet. Dev. 13:136-142(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
[19]"Two related ARID family proteins are alternative subunits of human SWI/SNF complexes."
Wang X., Nagl N.G., Wilsker D., Van Scoy M., Pacchione S., Yaciuk P., Dallas P.B., Moran E.
Biochem. J. 383:319-325(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, IDENTIFICATION IN SWI/SNF COMPLEXES, INTERACTION WITH SMARCA2; SMARCA4 AND SMARCC1.
[20]"The DNA-binding properties of the ARID-containing subunits of yeast and mammalian SWI/SNF complexes."
Wilsker D., Patsialou A., Zumbrun S.D., Kim S., Chen Y., Dallas P.B., Moran E.
Nucleic Acids Res. 32:1345-1353(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[21]"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[22]"Crystal structure of the HBAF250B AT-rich interaction domain (ARID)."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1041-1159.
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-814.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF259792 mRNA. Translation: AAG36928.1.
AL355297 expand/collapse EMBL AC list , AL049820, AL162578, AL591545 Genomic DNA. Translation: CAH71534.1.
AL049820 expand/collapse EMBL AC list , AL162578, AL355297, AL591545 Genomic DNA. Translation: CAI42308.1.
AL162578 expand/collapse EMBL AC list , AL049820, AL355297, AL591545 Genomic DNA. Translation: CAI40014.1.
AL591545 expand/collapse EMBL AC list , AL049820, AL162578, AL355297 Genomic DNA. Translation: CAI40666.1.
AL049820, AL591545 Genomic DNA. Translation: CAI42305.1.
AL591545, AL049820 Genomic DNA. Translation: CAI40664.1.
AJ001216 Genomic DNA. No translation available.
Y08266 mRNA. Translation: CAA69592.1. Frameshift.
AF521671 mRNA. Translation: AAN03447.1.
AF253515 mRNA. Translation: AAN70985.1. Sequence problems.
AF468300 mRNA. Translation: AAL76077.1. Different initiation.
AB033061 mRNA. Translation: BAA86549.1.
RefSeqNP_059989.2. NM_017519.2.
NP_065783.3. NM_020732.3.
UniGeneHs.291587.
Hs.744461.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CXYX-ray1.60A1041-1159[»]
2EH9X-ray2.00A1041-1159[»]
ProteinModelPortalQ8NFD5.
SMRQ8NFD5. Positions 1041-1154, 1620-1654, 1934-1966, 2066-2130, 2178-2205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121559. 25 interactions.
IntActQ8NFD5. 9 interactions.
MINTMINT-1153351.
STRING9606.ENSP00000275248.

PTM databases

PhosphoSiteQ8NFD5.

Polymorphism databases

DMDM73921720.

Proteomic databases

PaxDbQ8NFD5.
PRIDEQ8NFD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346085; ENSP00000344546; ENSG00000049618. [Q8NFD5-2]
ENST00000350026; ENSP00000055163; ENSG00000049618. [Q8NFD5-1]
ENST00000367148; ENSP00000356116; ENSG00000049618. [Q8NFD5-3]
GeneID57492.
KEGGhsa:57492.
UCSCuc003qqn.3. human. [Q8NFD5-3]
uc003qqo.3. human. [Q8NFD5-2]
uc003qqp.3. human. [Q8NFD5-1]

Organism-specific databases

CTD57492.
GeneCardsGC06P157191.
H-InvDBHIX0006320.
HIX0165033.
HGNCHGNC:18040. ARID1B.
HPAHPA016511.
MIM614556. gene.
614562. phenotype.
neXtProtNX_Q8NFD5.
Orphanet251056. 6q25 microdeletion syndrome.
1465. Coffin-Siris syndrome.
3051. Intellectual deficit - sparse hair - brachydactyly.
PharmGKBPA134909463.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG058196.
KOK11653.
OMAPIGIQGR.
OrthoDBEOG7M6D7M.
PhylomeDBQ8NFD5.
TreeFamTF320364.

Gene expression databases

ArrayExpressQ8NFD5.
BgeeQ8NFD5.
CleanExHS_ARID1B.
GenevestigatorQ8NFD5.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
1.25.10.10. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR011989. ARM-like.
IPR021906. DUF3518.
[Graphical view]
PfamPF01388. ARID. 1 hit.
PF12031. DUF3518. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
PROSITEPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8NFD5.
GeneWikiARID1B.
GenomeRNAi57492.
NextBio63782.
PROQ8NFD5.
SOURCESearch...

Entry information

Entry nameARI1B_HUMAN
AccessionPrimary (citable) accession number: Q8NFD5
Secondary accession number(s): Q5JRD1 expand/collapse secondary AC list , Q5VYC4, Q8IZY8, Q8TEV0, Q8TF02, Q99491, Q9ULI5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM