Reviewed, UniProtKB/Swiss-Prot Q62431 (ARI3A_MOUSE)

Names and origin

Protein names

Recommended name:
    AT-rich interactive domain-containing protein 3A
      Short name=ARID domain-containing protein 3A
Alternative name(s):
    Dead ringer-like protein 1
    B-cell regulator of IgH transcription
      Short name=Bright

Gene names

Name:	Arid3a
Synonyms:	Dri1, Dril1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	601 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transcription factor involved in B-cell differentiation. Binds a VH promoter proximal site necessary for induced mu-heavy-chain transcription. Binds the minor groove of a restricted ATC sequence that is sufficient for nuclear matrix association. This sequence motif is present in matrix-associating regions (MARS) proximal to the promoter and flanking E mu. Activates E mu-driven transcription by binding these sites. May be involved in the control of cell cycle progression by the RB1/E2F1 pathway. Ref.1 Ref.6 Ref.10
Subunit structure	Homodimer. Heterodimer with ARID3B. Interacts with E2F1 By similarity. Interacts with GTF2I and BTK. Ref.5 Ref.7 Ref.9
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between nucleus and cytoplasm. Ref.7 Ref.8
Tissue specificity	B-cell specific in the adult. Expressed in B-cell progenitors, down-regulated in the immature B-cell stage, and is up-regulated again at later stages of B-lymphocyte differentiation. Ref.4
Developmental stage	Expressed in lymphocytes from fetal liver. Expressed in fetal thymus and brain. Ref.4
Sequence similarities	Contains 1 ARID domain. Contains 1 NAP (nucleosome assembly protein) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Ref.7 Inferred from direct assay. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.7 Inferred from direct assay. Source: MGI
Molecular function	protein homodimerization activity Ref.7 Inferred from physical interaction. Source: MGI transcription factor activity Ref.7 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 601	601	AT-rich interactive domain-containing protein 3A		PRO_0000200579
Regions
	Domain	131 – 165	35	NAP
	Domain	243 – 335	93	ARID
	Region	450 – 493	44	Important for nuclear localization
	Region	495 – 518	24	Homodimerization By similarity
	Region	542 – 562	21	Important for cytoplasmic localization
	Compositional bias	27 – 34	8	Poly-Pro
	Compositional bias	68 – 71	4	Poly-Ala
	Compositional bias	128 – 131	4	Poly-Asp
	Compositional bias	146 – 154	9	Poly-Glu
	Compositional bias	158 – 165	8	Poly-Glu
	Compositional bias	437 – 446	10	Poly-Ala
	Compositional bias	543 – 546	4	Poly-Pro
Amino acid modifications
	Modified residue	78	1	Phosphoserine By similarity
	Modified residue	82	1	Phosphoserine By similarity
	Modified residue	89	1	Phosphoserine By similarity
	Modified residue	127	1	Phosphoserine Ref.11 Ref.12
Experimental info
	Mutagenesis	268	1	P → A: Impairs DNA-binding. Ref.7
	Mutagenesis	299	1	W → A: Impairs DNA-binding. Ref.7
	Mutagenesis	317	1	F → A: Impairs DNA-binding. Ref.7
	Mutagenesis	330	1	Y → A: Impairs DNA-binding. Ref.7
	Mutagenesis	457	1	K → A: No effect on cellular location. Ref.8
	Mutagenesis	463	1	P → A: Abolishes nuclear localization. Ref.8
	Mutagenesis	466	1	K → A: Abolishes nuclear localization. Ref.8
	Mutagenesis	467	1	K → A: Abolishes nuclear localization. Ref.8
	Mutagenesis	532	1	G → A: Abolishes cytosolic localization. Ref.8
	Mutagenesis	535	1	Y → A: Abolishes cytosolic localization. Ref.8
	Mutagenesis	535	1	Y → F: No effect on cellular location. Ref.8
	Mutagenesis	537	1	G → A: Abolishes cytosolic localization. Ref.8
	Mutagenesis	539	1	L → A: Abolishes cytosolic localization. Ref.8
	Sequence conflict	405 – 406	2	Missing in AAH50925. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q62431-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 66994C01E1FB68CD	FASTA	601	64,173
	10 20 30 40 50 60 MKLQAVMETL IQRQQRARQE LEARQAPPPP PPEPTGVRAR TTMTDEDREP ENARMHRTQM 70 80 90 100 110 120 AALAAMRAAA AGLGHPSSPG GSEDGPPISG DEDTAREGTL SSPALHGSVL EGAGHAEGDR 130 140 150 160 170 180 HLMDVGSDDD DTKSKWEEQE LEELGEEEEE EEEEDDFEEE EEEEEGLGPP ESASLGTAGL 190 200 210 220 230 240 FTRKAPPAQA FRGDGGPRML SGPERLGPGP AHPSHMASQM PPPDHGDWTF EEQFKQLYEL 250 260 270 280 290 300 DADPKRKEFL DDLFSFMQKR GTPVNRIPIM AKQVLDLFML YVLVTEKGGL VEVINKKLWR 310 320 330 340 350 360 EITKGLNLPT SITSAAFTLR TQYMKYLYPY ECERRGLSSP NELQAAIDSN RREGRRQSFG 370 380 390 400 410 420 GSLFAYSPSG AHSMLPSPKL PVTPLGLAAS TNGSSITPAP KIKKEEDSAI PITVPGRLPV 430 440 450 460 470 480 SLAGHPVVAA QAAAVQAAAA QAAVAAQAAA LEQLREKLES TEPPEKKMAL VADEQQRLMQ 490 500 510 520 530 540 RAVQQSFLAM TAQLPMNIRI NSQASESRQD SAVSLTSANG SNSISMSVEM NGIVYTGVLF 550 560 570 580 590 600 AQPPPPTAPS APGKGGVSSI GTNTTTGSRT GASGSTVSGG QVGLPGVSTP TMSSTSNNSL P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family." Herrscher R.F., Kaplan M.H., Lelsz D.L., Das C., Scheuermann R., Tucker P.W. Genes Dev. 9:3067-3082(1995) [PubMed: 8543152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"Expression of bright at two distinct stages of B lymphocyte development." Webb C.F., Smith E.A., Medina K.L., Buchanan K.L., Smithson G., Dou S. J. Immunol. 160:4747-4754(1998) [PubMed: 9590220] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]	"The transcription factor Bright associates with Bruton's tyrosine kinase, the defective protein in immunodeficiency disease." Webb C.F., Yamashita Y., Ayers N., Evetts S., Paulin Y., Conley M.E., Smith E.A. J. Immunol. 165:6956-6965(2000) [PubMed: 11120822] [Abstract] Cited for: INTERACTION WITH BTK.
[6]	"Transcriptional activation by a matrix associating region-binding protein. contextual requirements for the function of bright." Kaplan M.H., Zong R.-T., Herrscher R.F., Scheuermann R.H., Tucker P.W. J. Biol. Chem. 276:21325-21330(2001) [PubMed: 11294836] [Abstract] Cited for: FUNCTION.
[7]	"Mutations in the DNA-binding domain of the transcription factor Bright act as dominant negative proteins and interfere with immunoglobulin transactivation." Nixon J.C., Rajaiya J., Webb C.F. J. Biol. Chem. 279:52465-52472(2004) [PubMed: 15456761] [Abstract] Cited for: DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-268; TRP-299; PHE-317 AND TYR-330.
[8]	"A regulated nucleocytoplasmic shuttle contributes to Bright's function as a transcriptional activator of immunoglobulin genes." Kim D., Tucker P.W. Mol. Cell. Biol. 26:2187-2201(2006) [PubMed: 16507996] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-457; PRO-463; LYS-466; LYS-467; GLY-532; TYR-535; GLY-537 AND LEU-539.
[9]	"Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I." Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F. Mol. Cell. Biol. 26:4758-4768(2006) [PubMed: 16738337] [Abstract] Cited for: INTERACTION WITH GTF2I AND BTK.
[10]	"Anti-nuclear antibody production and autoimmunity in transgenic mice that overexpress the transcription factor Bright." Shankar M., Nixon J.C., Maier S., Workman J., Farris A.D., Webb C.F. J. Immunol. 178:2996-3006(2007) [PubMed: 17312145] [Abstract] Cited for: FUNCTION.
[11]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, MASS SPECTROMETRY.
[12]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U60335 mRNA. Translation: AAB03416.1. AK141283 mRNA. Translation: BAE24635.1. AK154956 mRNA. Translation: BAE32951.1. BC050925 mRNA. Translation: AAH50925.1.
IPI	IPI00125956.
RefSeq	NP_031906.1.
UniGene	Mm.301282
3D structure databases
SMR	Q62431. Positions 228-354.
ModBase	Search...
PTM databases
PhosphoSite	Q62431.
Proteomic databases
PRIDE	Q62431.
Genome annotation databases
Ensembl	ENSMUST00000019708; ENSMUSP00000019708; ENSMUSG00000019564; Mus musculus. [Genome view] ENSMUST00000105376; ENSMUSP00000101015; ENSMUSG00000019564; Mus musculus. [Genome view]
GeneID	13496.
KEGG	mmu:13496.
UCSC	uc007gap.1. mouse.
Organism-specific databases
CTD	13496.
MGI	MGI:1328360. Arid3a.
Phylogenomic databases
eggNOG	roNOG12276.
HOGENOM	HBG402789.
HOVERGEN	Q62431.
InParanoid	Q62431.
OMA	PKWEEEE.
OrthoDB	EOG9B2WH6.
PhylomeDB	Q62431.
Gene expression databases
ArrayExpress	Q62431.
Bgee	Q62431.
CleanEx	MM_ARID3A.
Genevestigator	Q62431.
GermOnline	ENSMUSG00000019564. Mus musculus.
Family and domain databases
InterPro	IPR001606. ARID/BRIGHT_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.150.60. ARID. 1 hit.
Pfam	PF01388. ARID. 1 hit. [Graphical view]
SMART	SM00501. BRIGHT. 1 hit. [Graphical view]
PROSITE	PS51011. ARID. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	284025.
SOURCE	Search...

Entry information

Entry name

ARI3A_MOUSE

Accession

Primary (citable) accession number: Q62431
Secondary accession number(s): Q3U338, Q80YP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)