O14497 (ARI1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ARID1A
Synonyms:	BAF250, BAF250A, C1orf4, OSA1, SMARCF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2285 AA.
Sequence status	Complete.
Protein existence	Evidence 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.27 Ref.28 Ref.29
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 adaptative 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.25
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 process	Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Mental retardation
Ligand	DNA-binding
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Inferred from direct assay Ref.4. Source: UniProtKB chromatin-mediated maintenance of transcription Traceable author statement Ref.4. Source: UniProtKB 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 nervous system development Inferred from electronic annotation. Source: UniProtKB-KW nucleosome disassembly Inferred from direct assay PubMed 8895581. Source: BHF-UCL nucleosome mobilization Traceable author statement Ref.4. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Non-traceable author statement Ref.11. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SWI/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
Molecular_function	DNA binding Non-traceable author statement Ref.6. Source: UniProtKB transcription coactivator activity Non-traceable author statement Ref.11. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIC1	Q14526	2	EBI-637887,EBI-2507362
SMARCA2	P51531	3	EBI-637887,EBI-679562
SMARCA4	P51532	11	EBI-637887,EBI-302489

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2285

2285

AT-rich interactive domain-containing protein 1A

PRO_0000200575

Regions

Domain

1017 – 1108

92

ARID

Motif

295 – 299

5

LXXLL

Motif

1709 – 1713

5

LXXLL

Motif

1967 – 1971

5

LXXLL

Motif

2085 – 2089

5

LXXLL

Compositional bias

479 – 482

4

Poly-Gln

Compositional bias

561 – 567

7

Poly-Gln

Compositional bias

998 – 1001

4

Poly-Ser

Compositional bias

1327 – 1404

78

Gln-rich

Amino acid modifications

Modified residue

79

1

Phosphoserine Ref.20

Modified residue

286

1

Phosphothreonine Ref.19 Ref.20

Modified residue

301

1

Phosphoserine Ref.19

Modified residue

363

1

Phosphoserine Ref.15 Ref.20 Ref.24

Modified residue

604

1

Phosphoserine Ref.20

Modified residue

696

1

Phosphoserine Ref.16 Ref.19 Ref.20 Ref.24

Modified residue

698

1

Phosphoserine Ref.16 Ref.19 Ref.20

Modified residue

702

1

Phosphoserine Ref.16 Ref.20 Ref.24

Modified residue

764

1

Phosphoserine Ref.19

Modified residue

772

1

Phosphoserine Ref.18 Ref.19 Ref.20 Ref.22

Modified residue

1184

1

Phosphoserine Ref.20

Modified residue

1604

1

Phosphoserine Ref.24

Modified residue

1612

1

N6-acetyllysine Ref.21

Modified residue

1905

1

N6-acetyllysine Ref.21

Modified residue

1944

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

1 – 383

383

Missing in isoform 3.

VSP_037157

Alternative sequence

1367 – 1583

217

Missing in isoform 2.

VSP_015225

Natural variant

1020

1

R → K Found in a clear cell renal carcinoma; somatic mutation. Ref.31

VAR_064695

Natural variant

1658

1

R → W Found in a gastric cancer sample; somatic mutation. Ref.32

VAR_068021

Natural variant

1907

1

I → F Found in a breast cancer sample; somatic mutation. Ref.32
Corresponds to variant rs139230162 [ dbSNP | Ensembl ].

VAR_068022

Natural variant

2087

1

G → R Found in a breast cancer sample; somatic mutation. Ref.32

VAR_068023

Natural variant

2089

1

L → P Found in a clear cell renal carcinoma case; somatic mutation. Ref.31

VAR_064696

Experimental info

Mutagenesis

1073

1

W → A: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1096. Ref.6

Mutagenesis

1096

1

Y → A: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1073. Ref.6

Sequence conflict

410

1

G → D in AAG33967. Ref.1

Sequence conflict

410

1

G → D in BAA23269. Ref.7

Sequence conflict

410

1

G → D in BAA83073. Ref.8

Sequence conflict

434

1

M → V in AAG33967. Ref.1

Sequence conflict

434

1

M → V in BAA23269. Ref.7

Sequence conflict

434

1

M → V in BAA83073. Ref.8

Sequence conflict

636

1

P → T in AAK54505. Ref.9

Sequence conflict

732

1

Q → S in AAG33967. Ref.1

Sequence conflict

732

1

Q → S in AAG17549. Ref.5

Sequence conflict

732

1

Q → S in BAA23269. Ref.7

Sequence conflict

750

1

R → RG in BAA83073. Ref.8

Sequence conflict

757

1

P → S in AAG33967. Ref.1

Sequence conflict

757

1

P → S in AAG17549. Ref.5

Sequence conflict

757

1

P → S in BAA23269. Ref.7

Sequence conflict

776

1

P → L in AAG33967. Ref.1

Sequence conflict

776

1

P → L in AAG17549. Ref.5

Sequence conflict

776

1

P → L in BAA23269. Ref.7

Sequence conflict

858

1

M → V in AAK54505. Ref.9

Sequence conflict

871

1

N → T in BAA23269. Ref.7

Sequence conflict

875

1

M → I in AAK54505. Ref.9

Sequence conflict

1017

1

E → G in AAG33967. Ref.1

Sequence conflict

1017

1

E → G in AAG17549. Ref.5

Sequence conflict

1017

1

E → G in BAA23269. Ref.7

Sequence conflict

1180

1

Missing in BAD96995. Ref.10

Sequence conflict

1307

1

P → S in AAG33967. Ref.1

Sequence conflict

1307

1

P → S in AAG17549. Ref.5

Sequence conflict

1307

1

P → S in BAA23269. Ref.7

Sequence conflict

1389

1

Y → F in AAG17549. Ref.5

Sequence conflict

1399

1

Q → L in AAG33967. Ref.1

Sequence conflict

1399

1

Q → L in BAA23269. Ref.7

Sequence conflict

1416

1

Q → P in AAG33967. Ref.1

Sequence conflict

1416

1

Q → P in BAA23269. Ref.7

Sequence conflict

1532

1

M → V in AAG33967. Ref.1

Sequence conflict

1638

1

D → A in AAK54505. Ref.9

Sequence conflict

1789

1

A → T in BAD96995. Ref.10

Sequence conflict

1839

1

S → R in AAK54505. Ref.9

Sequence conflict

2131

1

N → D in AAK54505. Ref.9

Sequence conflict

2143

1

R → H in AAK54505. Ref.9

Sequence conflict

2159

1

K → E in AAK54505. Ref.9

Sequence conflict

2182

1

A → T in BAD96995. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2285

Helix Strand Turn

Details...

Helix

1010 – 1012

3

Beta strand

1014 – 1016

3

Helix

1018 – 1033

16

Beta strand

1045 – 1048

4

Helix

1051 – 1061

11

Helix

1066 – 1068

3

Helix

1072 – 1079

8

Helix

1087 – 1099

13

Turn

1100 – 1107

8

Turn

1109 – 1111

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2005. Version 3. Checksum: 85BC5B6061625D8E	FASTA	2,285	242,045
	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
	Isoform 2 [UniParc]. Checksum: EF78398FE65F9E33	FASTA	2,068	218,335
	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 MYQQQQQVSS PAPLPRPMEN 1390 1400 1410 1420 1430 1440 RTSPSKSPFL HSGMKMQKAG PPVPASHIAP APVQPPMIRR DITFPPGSVE ATQPVLKQRR 1450 1460 1470 1480 1490 1500 RLTMKDIGTP EAWRVMMSLK SGLLAESTWA LDTINILLYD DNSIMTFNLS QLPGLLELLV 1510 1520 1530 1540 1550 1560 EYFRRCLIEI FGILKEYEVG DPGQRTLLDP GRFSKVSSPA PMEGGEEEEE LLGPKLEEEE 1570 1580 1590 1600 1610 1620 EEEVVENDEE IAFSGKDKPA SENSEEKLIS KFDKLPVKIV QKNDPFVVDC SDKLGRVQEF 1630 1640 1650 1660 1670 1680 DSGLLHWRIG GGDTTEHIQT HFESKTELLP SRPHAPCPPA PRKHVTTAEG TPGTTDQEGP 1690 1700 1710 1720 1730 1740 PPDGPPEKRI TATMDDMLST RSSTLTEDGA KSSEAIKESS KFPFGISPAQ SHRNIKILED 1750 1760 1770 1780 1790 1800 EPHSKDETPL CTLLDWQDSL AKRCVCVSNT IRSLSFVPGN DFEMSKHPGL LLILGKLILL 1810 1820 1830 1840 1850 1860 HHKHPERKQA PLTYEKEEEQ DQGVSCNKVE WWWDCLEMLR ENTLVTLANI SGQLDLSPYP 1870 1880 1890 1900 1910 1920 ESICLPVLDG LLHWAVCPSA EAQDPFSTLG PNAVLSPQRL VLETLSKLSI QDNNVDLILA 1930 1940 1950 1960 1970 1980 TPPFSRLEKL YSTMVRFLSD RKNPVCREMA VVLLANLAQG DSLAARAIAV QKGSIGNLLG 1990 2000 2010 2020 2030 2040 FLEDSLAATQ FQQSQASLLH MQNPPFEPTS VDMMRRAARA LLALAKVDEN HSEFTLYESR 2050 2060 LLDISVSPLM NSLVSQVICD VLFLIGQS
	Isoform 3 [UniParc]. Checksum: 35B2A6F804208A19	FASTA	1,902	205,921
	10 20 30 40 50 60 MDQMGKMRPQ PYGGTNPYSQ QQGPPSGPQQ GHGYPGQPYG SQTPQRYPMT MQGRAQSAMG 70 80 90 100 110 120 GLSYTQQIPP YGQQGPSGYG QQGQTPYYNQ QSPHPQQQQP PYSQQPPSQT PHAQPSYQQQ 130 140 150 160 170 180 PQSQPPQLQS SQPPYSQQPS QPPHQQSPAP YPSQQSTTQQ HPQSQPPYSQ PQAQSPYQQQ 190 200 210 220 230 240 QPQQPAPSTL SQQAAYPQPQ SQQSQQTAYS QQRFPPPQEL SQDSFGSQAS SAPSMTSSKG 250 260 270 280 290 300 GQEDMNLSLQ SRPSSLPDLS GSIDDLPMGT EGALSPGVST SGISSSQGEQ SNPAQSPFSP 310 320 330 340 350 360 HTSPHLPGIR GPSPSPVGSP ASVAQSRSGP LSPAAVPGNQ MPPRPPSGQS DSIMHPSMNQ 370 380 390 400 410 420 SSIAQDRGYM QRNPQMPQYS SPQPGSALSP RQPSGGQIHT GMGSYQQNSM GSYGPQGGQY 430 440 450 460 470 480 GPQGGYPRQP NYNALPNANY PSAGMAGGIN PMGAGGQMHG QPGIPPYGTL PPGRMSHASM 490 500 510 520 530 540 GNRPYGPNMA NMPPQVGSGM CPPPGGMNRK TQETAVAMHV AANSIQNRPP GYPNMNQGGM 550 560 570 580 590 600 MGTGPPYGQG INSMAGMINP QGPPYSMGGT MANNSAGMAA SPEMMGLGDV KLTPATKMNN 610 620 630 640 650 660 KADGTPKTES KSKKSSSSTT TNEKITKLYE LGGEPERKMW VDRYLAFTEE KAMGMTNLPA 670 680 690 700 710 720 VGRKPLDLYR LYVSVKEIGG LTQVNKNKKW RELATNLNVG TSSSAASSLK KQYIQCLYAF 730 740 750 760 770 780 ECKIERGEDP PPDIFAAADS KKSQPKIQPP SPAGSGSMQG PQTPQSTSSS MAEGGDLKPP 790 800 810 820 830 840 TPASTPHSQI PPLPGMSRSN SVGIQDAFND GSDSTFQKRN SMTPNPGYQP SMNTSDMMGR 850 860 870 880 890 900 MSYEPNKDPY GSMRKAPGSD PFMSSGQGPN GGMGDPYSRA AGPGLGNVAM GPRQHYPYGG 910 920 930 940 950 960 PYDRVRTEPG IGPEGNMSTG APQPNLMPSN PDSGMYSPSR YPPQQQQQQQ QRHDSYGNQF 970 980 990 1000 1010 1020 STQGTPSGSP FPSQQTTMYQ QQQQNYKRPM DGTYGPPAKR HEGEMYSVPY STGQGQPQQQ 1030 1040 1050 1060 1070 1080 QLPPAQPQPA SQQQAAQPSP QQDVYNQYGN AYPATATAAT ERRPAGGPQN QFPFQFGRDR 1090 1100 1110 1120 1130 1140 VSAPPGTNAQ QNMPPQMMGG PIQASAEVAQ QGTMWQGRND MTYNYANRQS TGSAPQGPAY 1150 1160 1170 1180 1190 1200 HGVNRTDEML HTDQRANHEG SWPSHGTRQP PYGPSAPVPP MTRPPPSNYQ PPPSMQNHIP 1210 1220 1230 1240 1250 1260 QVSSPAPLPR PMENRTSPSK SPFLHSGMKM QKAGPPVPAS HIAPAPVQPP MIRRDITFPP 1270 1280 1290 1300 1310 1320 GSVEATQPVL KQRRRLTMKD IGTPEAWRVM MSLKSGLLAE STWALDTINI LLYDDNSIMT 1330 1340 1350 1360 1370 1380 FNLSQLPGLL ELLVEYFRRC LIEIFGILKE YEVGDPGQRT LLDPGRFSKV SSPAPMEGGE 1390 1400 1410 1420 1430 1440 EEEELLGPKL EEEEEEEVVE NDEEIAFSGK DKPASENSEE KLISKFDKLP VKIVQKNDPF 1450 1460 1470 1480 1490 1500 VVDCSDKLGR VQEFDSGLLH WRIGGGDTTE HIQTHFESKT ELLPSRPHAP CPPAPRKHVT 1510 1520 1530 1540 1550 1560 TAEGTPGTTD QEGPPPDGPP EKRITATMDD MLSTRSSTLT EDGAKSSEAI KESSKFPFGI 1570 1580 1590 1600 1610 1620 SPAQSHRNIK ILEDEPHSKD ETPLCTLLDW QDSLAKRCVC VSNTIRSLSF VPGNDFEMSK 1630 1640 1650 1660 1670 1680 HPGLLLILGK LILLHHKHPE RKQAPLTYEK EEEQDQGVSC NKVEWWWDCL EMLRENTLVT 1690 1700 1710 1720 1730 1740 LANISGQLDL SPYPESICLP VLDGLLHWAV CPSAEAQDPF STLGPNAVLS PQRLVLETLS 1750 1760 1770 1780 1790 1800 KLSIQDNNVD LILATPPFSR LEKLYSTMVR FLSDRKNPVC REMAVVLLAN LAQGDSLAAR 1810 1820 1830 1840 1850 1860 AIAVQKGSIG NLLGFLEDSL AATQFQQSQA SLLHMQNPPF EPTSVDMMRR AARALLALAK 1870 1880 1890 1900 VDENHSEFTL YESRLLDISV SPLMNSLVSQ VICDVLFLIG QS

References

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[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. , 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), 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.
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[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.
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[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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, MASS SPECTROMETRY.
[22]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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. , 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.
[26]	"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.
[27]	"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: MASS SPECTROMETRY, IDENTIFICATION IN A SWI/SNF-LIKE EPAFA COMPLEX.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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. , 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.
[32]	"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. , 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.

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.

IPI

IPI00642705.
IPI00643722.
IPI00929427.

PIR

T00022.

RefSeq

NP_006006.3. NM_006015.4.
NP_624361.1. NM_139135.2.

UniGene

Hs.468972.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RYU	NMR	-	A	1000-1119	[»]

ProteinModelPortal

O14497.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33016N.

IntAct

O14497. 7 interactions.

PTM databases

PhosphoSite

O14497.

Proteomic databases

PaxDb

O14497.

PRIDE

O14497.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324856; ENSP00000320485; ENSG00000117713.
ENST00000374152; ENSP00000363267; ENSG00000117713.
ENST00000457599; ENSP00000387636; ENSG00000117713.

GeneID

8289.

KEGG

hsa:8289.

UCSC

uc001bmt.1. human.
uc001bmu.1. human.
uc001bmx.1. human.

Organism-specific databases

CTD

8289.

GeneCards

GC01P027022.

HGNC

HGNC:11110. ARID1A.

HPA

CAB016334.
HPA005456.

MIM

603024. gene.
614607. phenotype.

neXtProt

NX_O14497.

Orphanet

1465. Coffin-Siris syndrome.

PharmGKB

PA35960.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG058196.

InParanoid

O14497.

KO

K11653.

OMA

GSQYGPQ.

OrthoDB

EOG437RD2.

PhylomeDB

O14497.

Gene expression databases

ArrayExpress

O14497.

Bgee

O14497.

Genevestigator

O14497.

GermOnline

ENSG00000117713. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.60. 1 hit.

InterPro

IPR001606. ARID/BRIGHT_DNA-bd.
IPR021906. DUF3518.
[Graphical view]

Pfam

PF01388. ARID. 1 hit.
PF12031. DUF3518. 1 hit.
[Graphical view]

SMART

SM00501. BRIGHT. 1 hit.
[Graphical view]

SUPFAM

SSF46774. ARID. 1 hit.

PROSITE

PS51011. ARID. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARID1A. human.

EvolutionaryTrace

O14497.

GenomeRNAi

8289.

NextBio

31061.

SOURCE

Search...

Entry information

Entry name

ARI1A_HUMAN

Accession

Primary (citable) accession number: O14497
Secondary accession number(s): D3DPL1 , 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:	May 1, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.