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Q62431 (ARI3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AT-rich interactive domain-containing protein 3A

Short name=ARID domain-containing protein 3A
Alternative name(s):
B-cell regulator of IgH transcription
Short name=Bright
Dead ringer-like protein 1
Gene names
Name:Arid3a
Synonyms:Dri1, Dril1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence 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 REKLES domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601AT-rich interactive domain-containing protein 3A
PRO_0000200579

Regions

Domain243 – 33593ARID
Domain449 – 54698REKLES
Region128 – 16538Acidic
Region450 – 49344Important for nuclear localization
Region495 – 51824Homodimerization By similarity
Region542 – 56221Important for cytoplasmic localization
Compositional bias27 – 348Poly-Pro
Compositional bias68 – 714Poly-Ala
Compositional bias128 – 1314Poly-Asp
Compositional bias146 – 1549Poly-Glu
Compositional bias158 – 1658Poly-Glu
Compositional bias437 – 44610Poly-Ala
Compositional bias543 – 5464Poly-Pro

Amino acid modifications

Modified residue781Phosphoserine By similarity
Modified residue821Phosphoserine By similarity
Modified residue891Phosphoserine By similarity
Modified residue991Phosphothreonine By similarity
Modified residue1021Phosphoserine By similarity
Modified residue1271Phosphoserine Ref.11

Experimental info

Mutagenesis2681P → A: Impairs DNA-binding. Ref.7
Mutagenesis2991W → A: Impairs DNA-binding. Ref.7
Mutagenesis3171F → A: Impairs DNA-binding. Ref.7
Mutagenesis3301Y → A: Impairs DNA-binding. Ref.7
Mutagenesis4571K → A: No effect on cellular location. Ref.8
Mutagenesis4631P → A: Abolishes nuclear localization. Ref.8
Mutagenesis4661K → A: Abolishes nuclear localization. Ref.8
Mutagenesis4671K → A: Abolishes nuclear localization. Ref.8
Mutagenesis5321G → A: Abolishes cytosolic localization. Ref.8
Mutagenesis5351Y → A: Abolishes cytosolic localization. Ref.8
Mutagenesis5351Y → F: No effect on cellular location. Ref.8
Mutagenesis5371G → A: Abolishes cytosolic localization. Ref.8
Mutagenesis5391L → A: Abolishes cytosolic localization. Ref.8
Sequence conflict405 – 4062Missing in AAH50925. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q62431 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 66994C01E1FB68CD

FASTA60164,173
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS23999.1.
RefSeqNP_001275554.1. NM_001288625.1.
NP_001275555.1. NM_001288626.1.
NP_031906.1. NM_007880.4.
XP_006513264.1. XM_006513201.1.
XP_006513265.1. XM_006513202.1.
UniGeneMm.301282.

3D structure databases

ProteinModelPortalQ62431.
SMRQ62431. Positions 223-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199312. 2 interactions.
IntActQ62431. 1 interaction.
MINTMINT-4088325.
STRING10090.ENSMUSP00000019708.

PTM databases

PhosphoSiteQ62431.

Proteomic databases

PaxDbQ62431.
PRIDEQ62431.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019708; ENSMUSP00000019708; ENSMUSG00000019564.
ENSMUST00000105376; ENSMUSP00000101015; ENSMUSG00000019564.
ENSMUST00000105377; ENSMUSP00000101016; ENSMUSG00000019564.
GeneID13496.
KEGGmmu:13496.
UCSCuc007gap.1. mouse.

Organism-specific databases

CTD1820.
MGIMGI:1328360. Arid3a.

Phylogenomic databases

eggNOGNOG327790.
GeneTreeENSGT00550000074575.
HOGENOMHOG000236281.
HOVERGENHBG050574.
InParanoidQ62431.
OMALFAYSPG.
OrthoDBEOG77DJ6W.
PhylomeDBQ62431.
TreeFamTF320364.

Gene expression databases

ArrayExpressQ62431.
BgeeQ62431.
CleanExMM_ARID3A.
GenevestigatorQ62431.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR023334. REKLES_domain.
[Graphical view]
PfamPF01388. ARID. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
PROSITEPS51011. ARID. 1 hit.
PS51486. REKLES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARID3A. mouse.
NextBio284025.
PROQ62431.
SOURCESearch...

Entry information

Entry nameARI3A_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot