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O14497 (ARI1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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 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 names
Name:ARID1A
Synonyms:BAF250, BAF250A, C1orf4, OSA1, SMARCF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2285 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). 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. Ref.14

Subunit structure

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. Ref.1 Ref.4 Ref.5 Ref.11 Ref.12 Ref.13 Ref.14 Ref.29 Ref.30 Ref.31

Subcellular location

Nucleus Ref.9.

Tissue specificity

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. Ref.1 Ref.4 Ref.9

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

Sequence similarities

Contains 1 ARID domain.

Sequence caution

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: Erroneous gene model prediction.

The sequence BAA83073.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processNeurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   LigandDNA-binding
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from electronic annotation. Source: Ensembl

androgen receptor signaling pathway

Inferred from direct assay Ref.4. Source: UniProtKB

cardiac chamber development

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Inferred from direct assay PubMed 11726552. Source: BHF-UCL

chromatin-mediated maintenance of transcription

Traceable author statement Ref.4. Source: UniProtKB

forebrain development

Inferred from electronic annotation. Source: Ensembl

glucocorticoid receptor signaling pathway

Inferred from direct assay Ref.4. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Inferred from direct assay Ref.4. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

nucleosome disassembly

Inferred from direct assay PubMed 8895581. Source: BHF-UCL

nucleosome mobilization

Traceable author statement Ref.4. Source: UniProtKB

optic cup formation involved in camera-type eye development

Inferred from electronic annotation. Source: Ensembl

placenta blood vessel development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.4. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Non-traceable author statement Ref.11. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSWI/SNF complex

Inferred from direct assay PubMed 11078522Ref.4. Source: UniProtKB

nBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

npBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 17363140. Source: BHF-UCL

nucleus

Traceable author statement Ref.4. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.6. Source: UniProtKB

ligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 17363140. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.12Ref.13Ref.4PubMed 12368262PubMed 15985610PubMed 19486893PubMed 23540691. Source: IntAct

transcription coactivator activity

Non-traceable author statement Ref.11. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14497-1)

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: O14497-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1367-1583: Missing.
Isoform 3 (identifier: O14497-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.20
Chain2 – 22852284AT-rich interactive domain-containing protein 1A
PRO_0000200575

Regions

Domain1017 – 110892ARID
Motif295 – 2995LXXLL
Motif1709 – 17135LXXLL
Motif1967 – 19715LXXLL
Motif2085 – 20895LXXLL
Compositional bias479 – 4824Poly-Gln
Compositional bias561 – 5677Poly-Gln
Compositional bias998 – 10014Poly-Ser
Compositional bias1327 – 140478Gln-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.20 Ref.27
Modified residue791Phosphoserine Ref.21
Modified residue2861Phosphothreonine Ref.19 Ref.21
Modified residue3011Phosphoserine Ref.19
Modified residue3631Phosphoserine Ref.15 Ref.21 Ref.25
Modified residue6041Phosphoserine Ref.21
Modified residue6961Phosphoserine Ref.16 Ref.19 Ref.21 Ref.25
Modified residue6981Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue7021Phosphoserine Ref.16 Ref.21 Ref.25
Modified residue7641Phosphoserine Ref.19
Modified residue7721Phosphoserine Ref.18 Ref.19 Ref.21 Ref.23
Modified residue11841Phosphoserine Ref.21
Modified residue16041Phosphoserine Ref.25
Modified residue16121N6-acetyllysine Ref.22
Modified residue19051N6-acetyllysine Ref.22
Modified residue19441Phosphoserine Ref.19

Natural variations

Alternative sequence1 – 383383Missing in isoform 3.
VSP_037157
Alternative sequence1367 – 1583217Missing in isoform 2.
VSP_015225
Natural variant10201R → K Found in a clear cell renal carcinoma; somatic mutation. Ref.33
VAR_064695
Natural variant16581R → W Found in a gastric cancer sample; somatic mutation. Ref.34
VAR_068021
Natural variant19071I → F Found in a breast cancer sample; somatic mutation. Ref.34
Corresponds to variant rs139230162 [ dbSNP | Ensembl ].
VAR_068022
Natural variant20871G → R Found in a breast cancer sample; somatic mutation. Ref.34
VAR_068023
Natural variant20891L → P Found in a clear cell renal carcinoma case; somatic mutation. Ref.33
VAR_064696

Experimental info

Mutagenesis10731W → A: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1096. Ref.6
Mutagenesis10961Y → A: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1073. Ref.6
Sequence conflict4101G → D in AAG33967. Ref.1
Sequence conflict4101G → D in BAA23269. Ref.7
Sequence conflict4101G → D in BAA83073. Ref.8
Sequence conflict4341M → V in AAG33967. Ref.1
Sequence conflict4341M → V in BAA23269. Ref.7
Sequence conflict4341M → V in BAA83073. Ref.8
Sequence conflict6361P → T in AAK54505. Ref.9
Sequence conflict7321Q → S in AAG33967. Ref.1
Sequence conflict7321Q → S in AAG17549. Ref.5
Sequence conflict7321Q → S in BAA23269. Ref.7
Sequence conflict7501R → RG in BAA83073. Ref.8
Sequence conflict7571P → S in AAG33967. Ref.1
Sequence conflict7571P → S in AAG17549. Ref.5
Sequence conflict7571P → S in BAA23269. Ref.7
Sequence conflict7761P → L in AAG33967. Ref.1
Sequence conflict7761P → L in AAG17549. Ref.5
Sequence conflict7761P → L in BAA23269. Ref.7
Sequence conflict8581M → V in AAK54505. Ref.9
Sequence conflict8711N → T in BAA23269. Ref.7
Sequence conflict8751M → I in AAK54505. Ref.9
Sequence conflict10171E → G in AAG33967. Ref.1
Sequence conflict10171E → G in AAG17549. Ref.5
Sequence conflict10171E → G in BAA23269. Ref.7
Sequence conflict11801Missing in BAD96995. Ref.10
Sequence conflict13071P → S in AAG33967. Ref.1
Sequence conflict13071P → S in AAG17549. Ref.5
Sequence conflict13071P → S in BAA23269. Ref.7
Sequence conflict13891Y → F in AAG17549. Ref.5
Sequence conflict13991Q → L in AAG33967. Ref.1
Sequence conflict13991Q → L in BAA23269. Ref.7
Sequence conflict14161Q → P in AAG33967. Ref.1
Sequence conflict14161Q → P in BAA23269. Ref.7
Sequence conflict15321M → V in AAG33967. Ref.1
Sequence conflict16381D → A in AAK54505. Ref.9
Sequence conflict17891A → T in BAD96995. Ref.10
Sequence conflict18391S → R in AAK54505. Ref.9
Sequence conflict21311N → D in AAK54505. Ref.9
Sequence conflict21431R → H in AAK54505. Ref.9
Sequence conflict21591K → E in AAK54505. Ref.9
Sequence conflict21821A → T in BAD96995. Ref.10

Secondary structure

.................... 2285
Helix Strand Turn

Details...

Sequences

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

Last modified August 30, 2005. Version 3.
Checksum: 85BC5B6061625D8E

FASTA2,285242,045
        10         20         30         40         50         60 
MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM KAAAGQESEG 

        70         80         90        100        110        120 
PAVGPPQPLG KELQDGAESN GGGGGGGAGS GGGPGAEPDL KNSNGNAGPR PALNNNLTEP 

       130        140        150        160        170        180 
PGGGGGGSSD GVGAPPHSAA AALPPPAYGF GQPYGRSPSA VAAAAAAVFH QQHGGQQSPG 

       190        200        210        220        230        240 
LAALQSGGGG GLEPYAGPQQ NSHDHGFPNH QYNSYYPNRS AYPPPAPAYA LSSPRGGTPG 

       250        260        270        280        290        300 
SGAAAAAGSK PPPSSSASAS SSSSSFAQQR FGAMGGGGPS AAGGGTPQPT ATPTLNQLLT 

       310        320        330        340        350        360 
SPSSARGYQG YPGGDYSGGP QDGGAGKGPA DMASQCWGAA AAAAAAAAAS GGAQQRSHHA 

       370        380        390        400        410        420 
PMSPGSSGGG GQPLARTPQP SSPMDQMGKM RPQPYGGTNP YSQQQGPPSG PQQGHGYPGQ 

       430        440        450        460        470        480 
PYGSQTPQRY PMTMQGRAQS AMGGLSYTQQ IPPYGQQGPS GYGQQGQTPY YNQQSPHPQQ 

       490        500        510        520        530        540 
QQPPYSQQPP SQTPHAQPSY QQQPQSQPPQ LQSSQPPYSQ QPSQPPHQQS PAPYPSQQST 

       550        560        570        580        590        600 
TQQHPQSQPP YSQPQAQSPY QQQQPQQPAP STLSQQAAYP QPQSQQSQQT AYSQQRFPPP 

       610        620        630        640        650        660 
QELSQDSFGS QASSAPSMTS SKGGQEDMNL SLQSRPSSLP DLSGSIDDLP MGTEGALSPG 

       670        680        690        700        710        720 
VSTSGISSSQ GEQSNPAQSP FSPHTSPHLP GIRGPSPSPV GSPASVAQSR SGPLSPAAVP 

       730        740        750        760        770        780 
GNQMPPRPPS GQSDSIMHPS MNQSSIAQDR GYMQRNPQMP QYSSPQPGSA LSPRQPSGGQ 

       790        800        810        820        830        840 
IHTGMGSYQQ NSMGSYGPQG GQYGPQGGYP RQPNYNALPN ANYPSAGMAG GINPMGAGGQ 

       850        860        870        880        890        900 
MHGQPGIPPY GTLPPGRMSH ASMGNRPYGP NMANMPPQVG SGMCPPPGGM NRKTQETAVA 

       910        920        930        940        950        960 
MHVAANSIQN RPPGYPNMNQ GGMMGTGPPY GQGINSMAGM INPQGPPYSM GGTMANNSAG 

       970        980        990       1000       1010       1020 
MAASPEMMGL GDVKLTPATK MNNKADGTPK TESKSKKSSS STTTNEKITK LYELGGEPER 

      1030       1040       1050       1060       1070       1080 
KMWVDRYLAF TEEKAMGMTN LPAVGRKPLD LYRLYVSVKE IGGLTQVNKN KKWRELATNL 

      1090       1100       1110       1120       1130       1140 
NVGTSSSAAS SLKKQYIQCL YAFECKIERG EDPPPDIFAA ADSKKSQPKI QPPSPAGSGS 

      1150       1160       1170       1180       1190       1200 
MQGPQTPQST SSSMAEGGDL KPPTPASTPH SQIPPLPGMS RSNSVGIQDA FNDGSDSTFQ 

      1210       1220       1230       1240       1250       1260 
KRNSMTPNPG YQPSMNTSDM MGRMSYEPNK DPYGSMRKAP GSDPFMSSGQ GPNGGMGDPY 

      1270       1280       1290       1300       1310       1320 
SRAAGPGLGN VAMGPRQHYP YGGPYDRVRT EPGIGPEGNM STGAPQPNLM PSNPDSGMYS 

      1330       1340       1350       1360       1370       1380 
PSRYPPQQQQ QQQQRHDSYG NQFSTQGTPS GSPFPSQQTT MYQQQQQNYK RPMDGTYGPP 

      1390       1400       1410       1420       1430       1440 
AKRHEGEMYS VPYSTGQGQP QQQQLPPAQP QPASQQQAAQ PSPQQDVYNQ YGNAYPATAT 

      1450       1460       1470       1480       1490       1500 
AATERRPAGG PQNQFPFQFG RDRVSAPPGT NAQQNMPPQM MGGPIQASAE VAQQGTMWQG 

      1510       1520       1530       1540       1550       1560 
RNDMTYNYAN RQSTGSAPQG PAYHGVNRTD EMLHTDQRAN HEGSWPSHGT RQPPYGPSAP 

      1570       1580       1590       1600       1610       1620 
VPPMTRPPPS NYQPPPSMQN HIPQVSSPAP LPRPMENRTS PSKSPFLHSG MKMQKAGPPV 

      1630       1640       1650       1660       1670       1680 
PASHIAPAPV QPPMIRRDIT FPPGSVEATQ PVLKQRRRLT MKDIGTPEAW RVMMSLKSGL 

      1690       1700       1710       1720       1730       1740 
LAESTWALDT INILLYDDNS IMTFNLSQLP GLLELLVEYF RRCLIEIFGI LKEYEVGDPG 

      1750       1760       1770       1780       1790       1800 
QRTLLDPGRF SKVSSPAPME GGEEEEELLG PKLEEEEEEE VVENDEEIAF SGKDKPASEN 

      1810       1820       1830       1840       1850       1860 
SEEKLISKFD KLPVKIVQKN DPFVVDCSDK LGRVQEFDSG LLHWRIGGGD TTEHIQTHFE 

      1870       1880       1890       1900       1910       1920 
SKTELLPSRP HAPCPPAPRK HVTTAEGTPG TTDQEGPPPD GPPEKRITAT MDDMLSTRSS 

      1930       1940       1950       1960       1970       1980 
TLTEDGAKSS EAIKESSKFP FGISPAQSHR NIKILEDEPH SKDETPLCTL LDWQDSLAKR 

      1990       2000       2010       2020       2030       2040 
CVCVSNTIRS LSFVPGNDFE MSKHPGLLLI LGKLILLHHK HPERKQAPLT YEKEEEQDQG 

      2050       2060       2070       2080       2090       2100 
VSCNKVEWWW DCLEMLRENT LVTLANISGQ LDLSPYPESI CLPVLDGLLH WAVCPSAEAQ 

      2110       2120       2130       2140       2150       2160 
DPFSTLGPNA VLSPQRLVLE TLSKLSIQDN NVDLILATPP FSRLEKLYST MVRFLSDRKN 

      2170       2180       2190       2200       2210       2220 
PVCREMAVVL LANLAQGDSL AARAIAVQKG SIGNLLGFLE DSLAATQFQQ SQASLLHMQN 

      2230       2240       2250       2260       2270       2280 
PPFEPTSVDM MRRAARALLA LAKVDENHSE FTLYESRLLD ISVSPLMNSL VSQVICDVLF 


LIGQS 

« Hide

Isoform 2 [UniParc].

Checksum: EF78398FE65F9E33
Show »

FASTA2,068218,335
Isoform 3 [UniParc].

Checksum: 35B2A6F804208A19
Show »

FASTA1,902205,921

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"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 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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 MRD14.
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-1020 AND PRO-2089.
[34]"Somatic mutations in the chromatin remodeling gene ARID1A occur in several tumor types."
Jones S., Li M., Parsons D.W., Zhang X., Wesseling J., Kristel P., Schmidt M.K., Markowitz S., Yan H., Bigner D., Hruban R.H., Eshleman J.R., Iacobuzio-Donahue C.A., Goggins M., Maitra A., Malek S.N., Powell S., Vogelstein B. expand/collapse author list , Kinzler K.W., Velculescu V.E., Papadopoulos N.
Hum. Mutat. 33:100-103(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TRP-1658; PHE-1907 AND ARG-2087.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS285.1. [O14497-1]
CCDS44091.1. [O14497-2]
PIRT00022.
RefSeqNP_006006.3. NM_006015.4. [O14497-1]
NP_624361.1. NM_139135.2. [O14497-2]
UniGeneHs.468972.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RYUNMR-A1000-1119[»]
ProteinModelPortalO14497.
SMRO14497. Positions 1000-1119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113894. 44 interactions.
DIPDIP-33016N.
IntActO14497. 12 interactions.
MINTMINT-2795087.

PTM databases

PhosphoSiteO14497.

Proteomic databases

MaxQBO14497.
PaxDbO14497.
PRIDEO14497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324856; ENSP00000320485; ENSG00000117713. [O14497-1]
ENST00000374152; ENSP00000363267; ENSG00000117713. [O14497-3]
ENST00000457599; ENSP00000387636; ENSG00000117713. [O14497-2]
GeneID8289.
KEGGhsa:8289.
UCSCuc001bmt.1. human. [O14497-1]
uc001bmu.1. human. [O14497-2]

Organism-specific databases

CTD8289.
GeneCardsGC01P027022.
GeneReviewsARID1A.
HGNCHGNC:11110. ARID1A.
HPACAB016334.
HPA005456.
MIM603024. gene.
614607. phenotype.
neXtProtNX_O14497.
Orphanet1465. Coffin-Siris syndrome.
PharmGKBPA35960.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG058196.
InParanoidO14497.
KOK11653.
OMAGSQYGPQ.
OrthoDBEOG7M6D7M.
PhylomeDBO14497.
TreeFamTF320364.

Gene expression databases

ArrayExpressO14497.
BgeeO14497.
GenevestigatorO14497.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR016024. ARM-type_fold.
IPR021906. DUF3518.
[Graphical view]
PfamPF01388. ARID. 1 hit.
PF12031. DUF3518. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
SSF48371. SSF48371. 1 hit.
PROSITEPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARID1A. human.
EvolutionaryTraceO14497.
GeneWikiARID1A.
GenomeRNAi8289.
NextBio31061.
PROO14497.
SOURCESearch...

Entry information

Entry nameARI1A_HUMAN
AccessionPrimary (citable) accession number: O14497
Secondary accession number(s): D3DPL1 expand/collapse secondary AC list , Q53FK9, Q5T0W1, Q5T0W2, Q5T0W3, Q8NFD6, Q96T89, Q9BY33, Q9HBJ5, Q9UPZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 148 of the entry and version 3 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 1

Human chromosome 1: entries, gene names and cross-references to MIM