Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O14497

- ARI1A_HUMAN

UniProt

O14497 - ARI1A_HUMAN

(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)

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

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. 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
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_228108. RMTs methylate histone arginines.

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
Complete GO annotation...

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

BgeeiO14497.
ExpressionAtlasiO14497. baseline and differential.
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. 46 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 – 10123Combined sources
Beta strandi1014 – 10163Combined sources
Helixi1018 – 103316Combined sources
Beta strandi1045 – 10484Combined sources
Helixi1051 – 106111Combined sources
Helixi1066 – 10683Combined sources
Helixi1072 – 10798Combined sources
Helixi1087 – 109913Combined sources
Turni1100 – 11078Combined sources
Turni1109 – 11113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RYUNMR-A1000-1119[»]
ProteinModelPortaliO14497.
SMRiO14497. Positions 1000-1119, 1672-1720, 2117-2199.
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.
GeneTreeiENSGT00550000074575.
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

        10         20         30         40         50
MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM
60 70 80 90 100
KAAAGQESEG PAVGPPQPLG KELQDGAESN GGGGGGGAGS GGGPGAEPDL
110 120 130 140 150
KNSNGNAGPR PALNNNLTEP PGGGGGGSSD GVGAPPHSAA AALPPPAYGF
160 170 180 190 200
GQPYGRSPSA VAAAAAAVFH QQHGGQQSPG LAALQSGGGG GLEPYAGPQQ
210 220 230 240 250
NSHDHGFPNH QYNSYYPNRS AYPPPAPAYA LSSPRGGTPG SGAAAAAGSK
260 270 280 290 300
PPPSSSASAS SSSSSFAQQR FGAMGGGGPS AAGGGTPQPT ATPTLNQLLT
310 320 330 340 350
SPSSARGYQG YPGGDYSGGP QDGGAGKGPA DMASQCWGAA AAAAAAAAAS
360 370 380 390 400
GGAQQRSHHA PMSPGSSGGG GQPLARTPQP SSPMDQMGKM RPQPYGGTNP
410 420 430 440 450
YSQQQGPPSG PQQGHGYPGQ PYGSQTPQRY PMTMQGRAQS AMGGLSYTQQ
460 470 480 490 500
IPPYGQQGPS GYGQQGQTPY YNQQSPHPQQ QQPPYSQQPP SQTPHAQPSY
510 520 530 540 550
QQQPQSQPPQ LQSSQPPYSQ QPSQPPHQQS PAPYPSQQST TQQHPQSQPP
560 570 580 590 600
YSQPQAQSPY QQQQPQQPAP STLSQQAAYP QPQSQQSQQT AYSQQRFPPP
610 620 630 640 650
QELSQDSFGS QASSAPSMTS SKGGQEDMNL SLQSRPSSLP DLSGSIDDLP
660 670 680 690 700
MGTEGALSPG VSTSGISSSQ GEQSNPAQSP FSPHTSPHLP GIRGPSPSPV
710 720 730 740 750
GSPASVAQSR SGPLSPAAVP GNQMPPRPPS GQSDSIMHPS MNQSSIAQDR
760 770 780 790 800
GYMQRNPQMP QYSSPQPGSA LSPRQPSGGQ IHTGMGSYQQ NSMGSYGPQG
810 820 830 840 850
GQYGPQGGYP RQPNYNALPN ANYPSAGMAG GINPMGAGGQ MHGQPGIPPY
860 870 880 890 900
GTLPPGRMSH ASMGNRPYGP NMANMPPQVG SGMCPPPGGM NRKTQETAVA
910 920 930 940 950
MHVAANSIQN RPPGYPNMNQ GGMMGTGPPY GQGINSMAGM INPQGPPYSM
960 970 980 990 1000
GGTMANNSAG MAASPEMMGL GDVKLTPATK MNNKADGTPK TESKSKKSSS
1010 1020 1030 1040 1050
STTTNEKITK LYELGGEPER KMWVDRYLAF TEEKAMGMTN LPAVGRKPLD
1060 1070 1080 1090 1100
LYRLYVSVKE IGGLTQVNKN KKWRELATNL NVGTSSSAAS SLKKQYIQCL
1110 1120 1130 1140 1150
YAFECKIERG EDPPPDIFAA ADSKKSQPKI QPPSPAGSGS MQGPQTPQST
1160 1170 1180 1190 1200
SSSMAEGGDL KPPTPASTPH SQIPPLPGMS RSNSVGIQDA FNDGSDSTFQ
1210 1220 1230 1240 1250
KRNSMTPNPG YQPSMNTSDM MGRMSYEPNK DPYGSMRKAP GSDPFMSSGQ
1260 1270 1280 1290 1300
GPNGGMGDPY SRAAGPGLGN VAMGPRQHYP YGGPYDRVRT EPGIGPEGNM
1310 1320 1330 1340 1350
STGAPQPNLM PSNPDSGMYS PSRYPPQQQQ QQQQRHDSYG NQFSTQGTPS
1360 1370 1380 1390 1400
GSPFPSQQTT MYQQQQQNYK RPMDGTYGPP AKRHEGEMYS VPYSTGQGQP
1410 1420 1430 1440 1450
QQQQLPPAQP QPASQQQAAQ PSPQQDVYNQ YGNAYPATAT AATERRPAGG
1460 1470 1480 1490 1500
PQNQFPFQFG RDRVSAPPGT NAQQNMPPQM MGGPIQASAE VAQQGTMWQG
1510 1520 1530 1540 1550
RNDMTYNYAN RQSTGSAPQG PAYHGVNRTD EMLHTDQRAN HEGSWPSHGT
1560 1570 1580 1590 1600
RQPPYGPSAP VPPMTRPPPS NYQPPPSMQN HIPQVSSPAP LPRPMENRTS
1610 1620 1630 1640 1650
PSKSPFLHSG MKMQKAGPPV PASHIAPAPV QPPMIRRDIT FPPGSVEATQ
1660 1670 1680 1690 1700
PVLKQRRRLT MKDIGTPEAW RVMMSLKSGL LAESTWALDT INILLYDDNS
1710 1720 1730 1740 1750
IMTFNLSQLP GLLELLVEYF RRCLIEIFGI LKEYEVGDPG QRTLLDPGRF
1760 1770 1780 1790 1800
SKVSSPAPME GGEEEEELLG PKLEEEEEEE VVENDEEIAF SGKDKPASEN
1810 1820 1830 1840 1850
SEEKLISKFD KLPVKIVQKN DPFVVDCSDK LGRVQEFDSG LLHWRIGGGD
1860 1870 1880 1890 1900
TTEHIQTHFE SKTELLPSRP HAPCPPAPRK HVTTAEGTPG TTDQEGPPPD
1910 1920 1930 1940 1950
GPPEKRITAT MDDMLSTRSS TLTEDGAKSS EAIKESSKFP FGISPAQSHR
1960 1970 1980 1990 2000
NIKILEDEPH SKDETPLCTL LDWQDSLAKR CVCVSNTIRS LSFVPGNDFE
2010 2020 2030 2040 2050
MSKHPGLLLI LGKLILLHHK HPERKQAPLT YEKEEEQDQG VSCNKVEWWW
2060 2070 2080 2090 2100
DCLEMLRENT LVTLANISGQ LDLSPYPESI CLPVLDGLLH WAVCPSAEAQ
2110 2120 2130 2140 2150
DPFSTLGPNA VLSPQRLVLE TLSKLSIQDN NVDLILATPP FSRLEKLYST
2160 2170 2180 2190 2200
MVRFLSDRKN PVCREMAVVL LANLAQGDSL AARAIAVQKG SIGNLLGFLE
2210 2220 2230 2240 2250
DSLAATQFQQ SQASLLHMQN PPFEPTSVDM MRRAARALLA LAKVDENHSE
2260 2270 2280
FTLYESRLLD ISVSPLMNSL VSQVICDVLF LIGQS
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. Curated
The sequence AAG33967.1 differs from that shown. Reason: Frameshift at positions 872 and 885. Curated
The sequence BAA23269.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence BAA83073.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence BAA83073.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RYU NMR - A 1000-1119 [» ]
ProteinModelPortali O14497.
SMRi O14497. Positions 1000-1119, 1672-1720, 2117-2199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113894. 46 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.
GeneTreei ENSGT00550000074575.
HOVERGENi HBG058196.
InParanoidi O14497.
KOi K11653.
OMAi GSQYGPQ.
OrthoDBi EOG7M6D7M.
PhylomeDBi O14497.
TreeFami TF320364.

Enzyme and pathway databases

Reactomei REACT_228108. RMTs methylate histone arginines.

Miscellaneous databases

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

Gene expression databases

Bgeei O14497.
ExpressionAtlasi O14497. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 151 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