Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O14497

- ARI1A_HUMAN

UniProt

O14497 - ARI1A_HUMAN

Protein

AT-rich interactive domain-containing protein 1A

Gene

ARID1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (30 Aug 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Binds DNA non-specifically. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. 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.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. ligand-dependent nuclear receptor binding Source: BHF-UCL
    3. protein binding Source: IntAct
    4. transcription coactivator activity Source: BHF-UCL

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. ATP-dependent chromatin remodeling Source: Ensembl
    3. cardiac chamber development Source: Ensembl
    4. chromatin-mediated maintenance of transcription Source: UniProtKB
    5. chromatin remodeling Source: BHF-UCL
    6. forebrain development Source: Ensembl
    7. glucocorticoid receptor signaling pathway Source: UniProtKB
    8. intracellular estrogen receptor signaling pathway Source: UniProtKB
    9. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    10. neural tube closure Source: Ensembl
    11. nucleosome disassembly Source: BHF-UCL
    12. nucleosome mobilization Source: UniProtKB
    13. optic cup formation involved in camera-type eye development Source: Ensembl
    14. placenta blood vessel development Source: Ensembl
    15. positive regulation of transcription, DNA-templated Source: UniProtKB
    16. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    17. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AT-rich interactive domain-containing protein 1A
    Short name:
    ARID domain-containing protein 1A
    Alternative name(s):
    B120
    BRG1-associated factor 250
    Short name:
    BAF250
    BRG1-associated factor 250a
    Short name:
    BAF250A
    Osa homolog 1
    Short name:
    hOSA1
    SWI-like protein
    SWI/SNF complex protein p270
    SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1
    hELD
    Gene namesi
    Name:ARID1A
    Synonyms:BAF250, BAF250A, C1orf4, OSA1, SMARCF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11110. ARID1A.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nBAF complex Source: UniProtKB
    2. npBAF complex Source: UniProtKB
    3. nuclear chromatin Source: BHF-UCL
    4. nucleus Source: UniProtKB
    5. SWI/SNF complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal dominant 14 (MRD14) [MIM:614607]: A disease characterized by multiple congenital anomalies and mental retardation. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD14 patients manifest developmental delay, abnormal corpus callosum, absent/hypoplastic fifth finger/toenails, sparse scalp hair, long eyelashes, and a coarse facial appearance with wide mouth, thick lips, and abnormal ears.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1073 – 10731W → A: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1096. 1 Publication
    Mutagenesisi1096 – 10961Y → A: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1073. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi614607. phenotype.
    Orphaneti1465. Coffin-Siris syndrome.
    PharmGKBiPA35960.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 22852284AT-rich interactive domain-containing protein 1APRO_0000200575Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei286 – 2861Phosphothreonine2 Publications
    Modified residuei301 – 3011Phosphoserine1 Publication
    Modified residuei363 – 3631Phosphoserine3 Publications
    Modified residuei604 – 6041Phosphoserine1 Publication
    Modified residuei696 – 6961Phosphoserine4 Publications
    Modified residuei698 – 6981Phosphoserine3 Publications
    Modified residuei702 – 7021Phosphoserine3 Publications
    Modified residuei764 – 7641Phosphoserine1 Publication
    Modified residuei772 – 7721Phosphoserine4 Publications
    Modified residuei1184 – 11841Phosphoserine1 Publication
    Modified residuei1604 – 16041Phosphoserine1 Publication
    Modified residuei1612 – 16121N6-acetyllysine1 Publication
    Modified residuei1905 – 19051N6-acetyllysine1 Publication
    Modified residuei1944 – 19441Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14497.
    PaxDbiO14497.
    PRIDEiO14497.

    PTM databases

    PhosphoSiteiO14497.

    Expressioni

    Tissue specificityi

    Highly expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, and PBL, and at a much lower level in heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas.3 Publications

    Gene expression databases

    ArrayExpressiO14497.
    BgeeiO14497.
    GenevestigatoriO14497.

    Organism-specific databases

    HPAiCAB016334.
    HPA005456.

    Interactioni

    Subunit structurei

    Component of SWI/SNF chromatin remodeling complexes, in some of which it can be mutually exclusive with ARID1B/BAF250B. 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 the SWI/SNF Brm complex, at least composed of SMARCA2/BRM/BAF190B, SMARCB1/BAF47, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, BAF60 (one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C), SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A, SIN3A, HDAC1, HDAC2, and RBAP4. Component of the SWI/SNF complex Brg1(I), at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, BAF60 (one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C), SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A, SIN3A, and probably HDAC2 and RBAP4. Component of the SWI/SNF Brg1(II), at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A and probably HDAC2 and RBAP4. Component of a SWI/SNF-like EPAFa complex, at least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCC1/BAF155, SMARCC2/BAF170, BAF250A and MLLT1/ENL. 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. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. 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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIC1Q145262EBI-637887,EBI-2507362
    SMARCA2P515313EBI-637887,EBI-679562
    SMARCA4P5153222EBI-637887,EBI-302489

    Protein-protein interaction databases

    BioGridi113894. 44 interactions.
    DIPiDIP-33016N.
    IntActiO14497. 12 interactions.
    MINTiMINT-2795087.

    Structurei

    Secondary structure

    1
    2285
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1010 – 10123
    Beta strandi1014 – 10163
    Helixi1018 – 103316
    Beta strandi1045 – 10484
    Helixi1051 – 106111
    Helixi1066 – 10683
    Helixi1072 – 10798
    Helixi1087 – 109913
    Turni1100 – 11078
    Turni1109 – 11113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RYUNMR-A1000-1119[»]
    ProteinModelPortaliO14497.
    SMRiO14497. Positions 1000-1119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14497.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1017 – 110892ARIDPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi295 – 2995LXXLL
    Motifi1709 – 17135LXXLL
    Motifi1967 – 19715LXXLL
    Motifi2085 – 20895LXXLL

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi479 – 4824Poly-Gln
    Compositional biasi561 – 5677Poly-Gln
    Compositional biasi998 – 10014Poly-Ser
    Compositional biasi1327 – 140478Gln-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ARID domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG058196.
    InParanoidiO14497.
    KOiK11653.
    OMAiGSQYGPQ.
    OrthoDBiEOG7M6D7M.
    PhylomeDBiO14497.
    TreeFamiTF320364.

    Family and domain databases

    Gene3Di1.10.150.60. 1 hit.
    InterProiIPR001606. ARID/BRIGHT_DNA-bd.
    IPR016024. ARM-type_fold.
    IPR021906. DUF3518.
    [Graphical view]
    PfamiPF01388. ARID. 1 hit.
    PF12031. DUF3518. 1 hit.
    [Graphical view]
    SMARTiSM00501. BRIGHT. 1 hit.
    [Graphical view]
    SUPFAMiSSF46774. SSF46774. 1 hit.
    SSF48371. SSF48371. 1 hit.
    PROSITEiPS51011. ARID. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14497-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM     50
    KAAAGQESEG PAVGPPQPLG KELQDGAESN GGGGGGGAGS GGGPGAEPDL 100
    KNSNGNAGPR PALNNNLTEP PGGGGGGSSD GVGAPPHSAA AALPPPAYGF 150
    GQPYGRSPSA VAAAAAAVFH QQHGGQQSPG LAALQSGGGG GLEPYAGPQQ 200
    NSHDHGFPNH QYNSYYPNRS AYPPPAPAYA LSSPRGGTPG SGAAAAAGSK 250
    PPPSSSASAS SSSSSFAQQR FGAMGGGGPS AAGGGTPQPT ATPTLNQLLT 300
    SPSSARGYQG YPGGDYSGGP QDGGAGKGPA DMASQCWGAA AAAAAAAAAS 350
    GGAQQRSHHA PMSPGSSGGG GQPLARTPQP SSPMDQMGKM RPQPYGGTNP 400
    YSQQQGPPSG PQQGHGYPGQ PYGSQTPQRY PMTMQGRAQS AMGGLSYTQQ 450
    IPPYGQQGPS GYGQQGQTPY YNQQSPHPQQ QQPPYSQQPP SQTPHAQPSY 500
    QQQPQSQPPQ LQSSQPPYSQ QPSQPPHQQS PAPYPSQQST TQQHPQSQPP 550
    YSQPQAQSPY QQQQPQQPAP STLSQQAAYP QPQSQQSQQT AYSQQRFPPP 600
    QELSQDSFGS QASSAPSMTS SKGGQEDMNL SLQSRPSSLP DLSGSIDDLP 650
    MGTEGALSPG VSTSGISSSQ GEQSNPAQSP FSPHTSPHLP GIRGPSPSPV 700
    GSPASVAQSR SGPLSPAAVP GNQMPPRPPS GQSDSIMHPS MNQSSIAQDR 750
    GYMQRNPQMP QYSSPQPGSA LSPRQPSGGQ IHTGMGSYQQ NSMGSYGPQG 800
    GQYGPQGGYP RQPNYNALPN ANYPSAGMAG GINPMGAGGQ MHGQPGIPPY 850
    GTLPPGRMSH ASMGNRPYGP NMANMPPQVG SGMCPPPGGM NRKTQETAVA 900
    MHVAANSIQN RPPGYPNMNQ GGMMGTGPPY GQGINSMAGM INPQGPPYSM 950
    GGTMANNSAG MAASPEMMGL GDVKLTPATK MNNKADGTPK TESKSKKSSS 1000
    STTTNEKITK LYELGGEPER KMWVDRYLAF TEEKAMGMTN LPAVGRKPLD 1050
    LYRLYVSVKE IGGLTQVNKN KKWRELATNL NVGTSSSAAS SLKKQYIQCL 1100
    YAFECKIERG EDPPPDIFAA ADSKKSQPKI QPPSPAGSGS MQGPQTPQST 1150
    SSSMAEGGDL KPPTPASTPH SQIPPLPGMS RSNSVGIQDA FNDGSDSTFQ 1200
    KRNSMTPNPG YQPSMNTSDM MGRMSYEPNK DPYGSMRKAP GSDPFMSSGQ 1250
    GPNGGMGDPY SRAAGPGLGN VAMGPRQHYP YGGPYDRVRT EPGIGPEGNM 1300
    STGAPQPNLM PSNPDSGMYS PSRYPPQQQQ QQQQRHDSYG NQFSTQGTPS 1350
    GSPFPSQQTT MYQQQQQNYK RPMDGTYGPP AKRHEGEMYS VPYSTGQGQP 1400
    QQQQLPPAQP QPASQQQAAQ PSPQQDVYNQ YGNAYPATAT AATERRPAGG 1450
    PQNQFPFQFG RDRVSAPPGT NAQQNMPPQM MGGPIQASAE VAQQGTMWQG 1500
    RNDMTYNYAN RQSTGSAPQG PAYHGVNRTD EMLHTDQRAN HEGSWPSHGT 1550
    RQPPYGPSAP VPPMTRPPPS NYQPPPSMQN HIPQVSSPAP LPRPMENRTS 1600
    PSKSPFLHSG MKMQKAGPPV PASHIAPAPV QPPMIRRDIT FPPGSVEATQ 1650
    PVLKQRRRLT MKDIGTPEAW RVMMSLKSGL LAESTWALDT INILLYDDNS 1700
    IMTFNLSQLP GLLELLVEYF RRCLIEIFGI LKEYEVGDPG QRTLLDPGRF 1750
    SKVSSPAPME GGEEEEELLG PKLEEEEEEE VVENDEEIAF SGKDKPASEN 1800
    SEEKLISKFD KLPVKIVQKN DPFVVDCSDK LGRVQEFDSG LLHWRIGGGD 1850
    TTEHIQTHFE SKTELLPSRP HAPCPPAPRK HVTTAEGTPG TTDQEGPPPD 1900
    GPPEKRITAT MDDMLSTRSS TLTEDGAKSS EAIKESSKFP FGISPAQSHR 1950
    NIKILEDEPH SKDETPLCTL LDWQDSLAKR CVCVSNTIRS LSFVPGNDFE 2000
    MSKHPGLLLI LGKLILLHHK HPERKQAPLT YEKEEEQDQG VSCNKVEWWW 2050
    DCLEMLRENT LVTLANISGQ LDLSPYPESI CLPVLDGLLH WAVCPSAEAQ 2100
    DPFSTLGPNA VLSPQRLVLE TLSKLSIQDN NVDLILATPP FSRLEKLYST 2150
    MVRFLSDRKN PVCREMAVVL LANLAQGDSL AARAIAVQKG SIGNLLGFLE 2200
    DSLAATQFQQ SQASLLHMQN PPFEPTSVDM MRRAARALLA LAKVDENHSE 2250
    FTLYESRLLD ISVSPLMNSL VSQVICDVLF LIGQS 2285
    Length:2,285
    Mass (Da):242,045
    Last modified:August 30, 2005 - v3
    Checksum:i85BC5B6061625D8E
    GO
    Isoform 2 (identifier: O14497-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1367-1583: Missing.

    Show »
    Length:2,068
    Mass (Da):218,335
    Checksum:iEF78398FE65F9E33
    GO
    Isoform 3 (identifier: O14497-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-383: Missing.

    Show »
    Length:1,902
    Mass (Da):205,921
    Checksum:i35B2A6F804208A19
    GO

    Sequence cautioni

    The sequence AAF75765.1 differs from that shown. Reason: Frameshift at position 374.
    The sequence AAG33967.1 differs from that shown. Reason: Frameshift at positions 872 and 885.
    The sequence BAA23269.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAA83073.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAA83073.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101G → D in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti410 – 4101G → D in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti410 – 4101G → D in BAA83073. 1 PublicationCurated
    Sequence conflicti434 – 4341M → V in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti434 – 4341M → V in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti434 – 4341M → V in BAA83073. 1 PublicationCurated
    Sequence conflicti636 – 6361P → T in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti732 – 7321Q → S in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti732 – 7321Q → S in AAG17549. (PubMed:11734557)Curated
    Sequence conflicti732 – 7321Q → S in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti750 – 7501R → RG in BAA83073. 1 PublicationCurated
    Sequence conflicti757 – 7571P → S in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti757 – 7571P → S in AAG17549. (PubMed:11734557)Curated
    Sequence conflicti757 – 7571P → S in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti776 – 7761P → L in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti776 – 7761P → L in AAG17549. (PubMed:11734557)Curated
    Sequence conflicti776 – 7761P → L in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti858 – 8581M → V in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti871 – 8711N → T in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti875 – 8751M → I in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti1017 – 10171E → G in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti1017 – 10171E → G in AAG17549. (PubMed:11734557)Curated
    Sequence conflicti1017 – 10171E → G in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti1180 – 11801Missing in BAD96995. 1 PublicationCurated
    Sequence conflicti1307 – 13071P → S in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti1307 – 13071P → S in AAG17549. (PubMed:11734557)Curated
    Sequence conflicti1307 – 13071P → S in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti1389 – 13891Y → F in AAG17549. (PubMed:11734557)Curated
    Sequence conflicti1399 – 13991Q → L in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti1399 – 13991Q → L in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti1416 – 14161Q → P in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti1416 – 14161Q → P in BAA23269. (PubMed:9434167)Curated
    Sequence conflicti1532 – 15321M → V in AAG33967. (PubMed:11073988)Curated
    Sequence conflicti1638 – 16381D → A in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti1789 – 17891A → T in BAD96995. 1 PublicationCurated
    Sequence conflicti1839 – 18391S → R in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti2131 – 21311N → D in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti2143 – 21431R → H in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti2159 – 21591K → E in AAK54505. (PubMed:11318604)Curated
    Sequence conflicti2182 – 21821A → T in BAD96995. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1020 – 10201R → K Found in a clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064695
    Natural varianti1658 – 16581R → W Found in a gastric cancer sample; somatic mutation. 1 Publication
    VAR_068021
    Natural varianti1907 – 19071I → F Found in a breast cancer sample; somatic mutation. 1 Publication
    Corresponds to variant rs139230162 [ dbSNP | Ensembl ].
    VAR_068022
    Natural varianti2087 – 20871G → R Found in a breast cancer sample; somatic mutation. 1 Publication
    VAR_068023
    Natural varianti2089 – 20891L → P Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
    VAR_064696

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 383383Missing in isoform 3. 1 PublicationVSP_037157Add
    BLAST
    Alternative sequencei1367 – 1583217Missing in isoform 2. 1 PublicationVSP_015225Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF231056 mRNA. Translation: AAG33967.1. Frameshift.
    AL512408, AL034380 Genomic DNA. Translation: CAI23482.1.
    AL512408, AL034380 Genomic DNA. Translation: CAI23483.1.
    AL512408, AL034380 Genomic DNA. Translation: CAI23484.1.
    AL034380, AL512408 Genomic DNA. Translation: CAI21621.1.
    AL034380, AL512408 Genomic DNA. Translation: CAI21622.1.
    AL034380, AL512408 Genomic DNA. Translation: CAI21623.1.
    CH471059 Genomic DNA. Translation: EAX07795.1.
    CH471059 Genomic DNA. Translation: EAX07796.1.
    AF521670 mRNA. Translation: AAN03446.1.
    AF219114 mRNA. Translation: AAG17549.2.
    AF265208 mRNA. Translation: AAF75765.1. Frameshift.
    AB001895 mRNA. Translation: BAA23269.1. Frameshift.
    AB024075 Genomic DNA. Translation: BAA83073.1. Sequence problems.
    AF268913 mRNA. Translation: AAK54505.1.
    AK223275 mRNA. Translation: BAD96995.1.
    CCDSiCCDS285.1. [O14497-1]
    CCDS44091.1. [O14497-2]
    PIRiT00022.
    RefSeqiNP_006006.3. NM_006015.4. [O14497-1]
    NP_624361.1. NM_139135.2. [O14497-2]
    UniGeneiHs.468972.

    Genome annotation databases

    EnsembliENST00000324856; ENSP00000320485; ENSG00000117713. [O14497-1]
    ENST00000374152; ENSP00000363267; ENSG00000117713. [O14497-3]
    ENST00000457599; ENSP00000387636; ENSG00000117713. [O14497-2]
    GeneIDi8289.
    KEGGihsa:8289.
    UCSCiuc001bmt.1. human. [O14497-1]
    uc001bmu.1. human. [O14497-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF231056 mRNA. Translation: AAG33967.1 . Frameshift.
    AL512408 , AL034380 Genomic DNA. Translation: CAI23482.1 .
    AL512408 , AL034380 Genomic DNA. Translation: CAI23483.1 .
    AL512408 , AL034380 Genomic DNA. Translation: CAI23484.1 .
    AL034380 , AL512408 Genomic DNA. Translation: CAI21621.1 .
    AL034380 , AL512408 Genomic DNA. Translation: CAI21622.1 .
    AL034380 , AL512408 Genomic DNA. Translation: CAI21623.1 .
    CH471059 Genomic DNA. Translation: EAX07795.1 .
    CH471059 Genomic DNA. Translation: EAX07796.1 .
    AF521670 mRNA. Translation: AAN03446.1 .
    AF219114 mRNA. Translation: AAG17549.2 .
    AF265208 mRNA. Translation: AAF75765.1 . Frameshift.
    AB001895 mRNA. Translation: BAA23269.1 . Frameshift.
    AB024075 Genomic DNA. Translation: BAA83073.1 . Sequence problems.
    AF268913 mRNA. Translation: AAK54505.1 .
    AK223275 mRNA. Translation: BAD96995.1 .
    CCDSi CCDS285.1. [O14497-1 ]
    CCDS44091.1. [O14497-2 ]
    PIRi T00022.
    RefSeqi NP_006006.3. NM_006015.4. [O14497-1 ]
    NP_624361.1. NM_139135.2. [O14497-2 ]
    UniGenei Hs.468972.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RYU NMR - A 1000-1119 [» ]
    ProteinModelPortali O14497.
    SMRi O14497. Positions 1000-1119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113894. 44 interactions.
    DIPi DIP-33016N.
    IntActi O14497. 12 interactions.
    MINTi MINT-2795087.

    PTM databases

    PhosphoSitei O14497.

    Proteomic databases

    MaxQBi O14497.
    PaxDbi O14497.
    PRIDEi O14497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324856 ; ENSP00000320485 ; ENSG00000117713 . [O14497-1 ]
    ENST00000374152 ; ENSP00000363267 ; ENSG00000117713 . [O14497-3 ]
    ENST00000457599 ; ENSP00000387636 ; ENSG00000117713 . [O14497-2 ]
    GeneIDi 8289.
    KEGGi hsa:8289.
    UCSCi uc001bmt.1. human. [O14497-1 ]
    uc001bmu.1. human. [O14497-2 ]

    Organism-specific databases

    CTDi 8289.
    GeneCardsi GC01P027022.
    GeneReviewsi ARID1A.
    HGNCi HGNC:11110. ARID1A.
    HPAi CAB016334.
    HPA005456.
    MIMi 603024. gene.
    614607. phenotype.
    neXtProti NX_O14497.
    Orphaneti 1465. Coffin-Siris syndrome.
    PharmGKBi PA35960.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG058196.
    InParanoidi O14497.
    KOi K11653.
    OMAi GSQYGPQ.
    OrthoDBi EOG7M6D7M.
    PhylomeDBi O14497.
    TreeFami TF320364.

    Miscellaneous databases

    ChiTaRSi ARID1A. human.
    EvolutionaryTracei O14497.
    GeneWikii ARID1A.
    GenomeRNAii 8289.
    NextBioi 31061.
    PROi O14497.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14497.
    Bgeei O14497.
    Genevestigatori O14497.

    Family and domain databases

    Gene3Di 1.10.150.60. 1 hit.
    InterProi IPR001606. ARID/BRIGHT_DNA-bd.
    IPR016024. ARM-type_fold.
    IPR021906. DUF3518.
    [Graphical view ]
    Pfami PF01388. ARID. 1 hit.
    PF12031. DUF3518. 1 hit.
    [Graphical view ]
    SMARTi SM00501. BRIGHT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46774. SSF46774. 1 hit.
    SSF48371. SSF48371. 1 hit.
    PROSITEi PS51011. ARID. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A specificity and targeting subunit of a human SWI/SNF family-related chromatin-remodeling complex."
      Nie Z., Xue Y., Yang D., Zhou S., Deroo B.J., Archer T.K., Wang W.
      Mol. Cell. Biol. 20:8879-8888(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, IDENTIFICATION IN THE BAF COMPLEX.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 287-2285 (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH SMARCA2 AND SMARCA4, IDENTIFICATION IN A SWI/SNF COMPLEX WITH ARID1B.
    5. "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] OF 347-2285 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BAF COMPLEX.
      Tissue: Brain.
    6. "The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity."
      Dallas P.B., Pacchione S., Wilsker D., Bowrin V., Kobayashi R., Moran E.
      Mol. Cell. Biol. 20:3137-3146(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 358-2285 (ISOFORM 1), MUTAGENESIS OF TRP-1073 AND TYR-1096.
    7. "Molecular cloning and expression of a novel human cDNA containing CAG repeats."
      Takeuchi T., Chen B.-K., Qiu Y., Sonobe H., Ohtsuki Y.
      Gene 204:71-77(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1585 (ISOFORM 3).
    8. Takeuchi T., Misaki A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-1515.
    9. "Characterization of mammalian orthologues of the Drosophila osa gene: cDNA cloning, expression, chromosomal localization, and direct physical interaction with Brahma chromatin-remodeling complex."
      Kozmik Z., Machon O., Kralova J., Kreslova J., Paces J., Vlcek C.
      Genomics 73:140-148(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 384-2285 (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1104-2285 (ISOFORM 1).
      Tissue: Gastric mucosa.
    11. "Diversity and specialization of mammalian SWI/SNF complexes."
      Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.
      Genes Dev. 10:2117-2130(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN SWI/SNF COMPLEXES.
    12. "Selectivity of chromatin-remodelling cofactors for ligand-activated transcription."
      Lemon B., Inouye C., King D.S., Tjian R.
      Nature 414:924-928(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A SWI/SNF COMPLEX.
    13. "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: IDENTIFICATION IN A SWI/SNF-LIKE COMPLEX WITH ARID1A.
    14. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
      Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
      Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-698 AND SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-301; SER-696; SER-698; SER-764; SER-772 AND SER-1944, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "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].
    21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; THR-286; SER-363; SER-604; SER-696; SER-698; SER-702; SER-772 AND SER-1184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "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-1612 AND LYS-1905, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-772, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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-363; SER-696; SER-702 AND SER-1604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: INVOLVEMENT IN MRD14.
    27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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.
    29. "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: IDENTIFICATION IN A SWI/SNF-LIKE EPAFA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    30. "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: IDENTIFICATION IN SWI/SNF COMPLEXES, INTERACTION WITH SMARCA2; SMARCA4 AND SMARCC1.
    31. "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.
    32. "Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition."
      Kim S., Zhang Z., Upchurch S., Isern N., Chen Y.
      J. Biol. Chem. 279:16670-16676(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1000-1159.
    33. Cited for: VARIANTS LYS-1020 AND PRO-2089.
    34. Cited for: VARIANTS TRP-1658; PHE-1907 AND ARG-2087.

    Entry informationi

    Entry nameiARI1A_HUMAN
    AccessioniPrimary (citable) accession number: O14497
    Secondary accession number(s): D3DPL1
    , Q53FK9, Q5T0W1, Q5T0W2, Q5T0W3, Q8NFD6, Q96T89, Q9BY33, Q9HBJ5, Q9UPZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3