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Q99856 (ARI3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
E2F-binding protein 1
Gene names
Name:ARID3A
Synonyms:DRIL1, DRIL3, DRX, E2FBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation. Ref.6 Ref.7

Subunit structure

Homodimer. Heterodimer with ARID3B. Interacts with E2F1. Interacts with GTF2I and BTK. Ref.2 Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between nucleus and cytoplasm. Ref.10

Tissue specificity

Widely expressed, with highest expression in skeletal muscle, thalamus, and colon.

Induction

By p53/TP53 following DNA damage. Ref.7

Sequence similarities

Contains 1 ARID domain.

Contains 1 REKLES domain.

Sequence caution

The sequence AAW30734.1 differs from that shown. Reason: Frameshift at position 498.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BTKQ061873EBI-5458244,EBI-624835

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593AT-rich interactive domain-containing protein 3A
PRO_0000200578

Regions

Domain238 – 33093ARID
Domain444 – 54198REKLES
Region119 – 15638Acidic
Region445 – 48844Important for nuclear localization By similarity
Region490 – 51324Homodimerization
Region537 – 55721Important for cytoplasmic localization By similarity
Compositional bias67 – 704Poly-Ala
Compositional bias89 – 15769Glu-rich
Compositional bias424 – 44522Ala-rich
Compositional bias550 – 57930Gly-rich

Amino acid modifications

Modified residue771Phosphoserine Ref.8 Ref.13 Ref.15
Modified residue811Phosphoserine Ref.8 Ref.13
Modified residue881Phosphoserine Ref.8 Ref.13 Ref.15
Modified residue981Phosphothreonine Ref.15
Modified residue1011Phosphoserine Ref.15
Modified residue1191Phosphoserine Ref.15

Natural variations

Natural variant361P → H. Ref.5
Corresponds to variant rs17857499 [ dbSNP | Ensembl ].
VAR_033203
Natural variant3201K → E. Ref.5
Corresponds to variant rs17857501 [ dbSNP | Ensembl ].
VAR_033204
Natural variant5561G → S. Ref.2 Ref.5
Corresponds to variant rs1051505 [ dbSNP | Ensembl ].
VAR_033205

Experimental info

Mutagenesis3251Y → A: Abolishes DNA-binding. Ref.9
Mutagenesis4611K → A: Abolishes nuclear targeting. Ref.10
Mutagenesis5271G → A or P: Impairs DNA-binding but not self-association. Ref.10
Mutagenesis5301Y → A: Impairs DNA-binding but not self-association. Ref.10
Mutagenesis5301Y → F: No effect on DNA-binding. Ref.10
Mutagenesis5321G → A: Impairs DNA-binding. Ref.10
Mutagenesis5341L → A: Impairs DNA-binding. Ref.10
Sequence conflict4231V → S in AAN74028. Ref.2

Secondary structure

................... 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99856 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 4D09131E168A2880

FASTA59362,889
        10         20         30         40         50         60 
MKLQAVMETL LQRQQRARQE LEARQQLPPD PPAAPPGRAR AAPDEDREPE SARMQRAQMA 

        70         80         90        100        110        120 
ALAAMRAAAA GLGHPASPGG SEDGPPGSEE EDAAREGTPG SPGRGREGPG EEHFEDMASD 

       130        140        150        160        170        180 
EDMKPKWEEE EMEEDLGEDE EEEEEDYEDE EEEEDEEGLG PPGPASLGTT ALFPRKAQPP 

       190        200        210        220        230        240 
QAFRGDGVPR VLGGQERPGP GPAHPGGAAH VAPQLQPPDH GDWTYEEQFK QLYELDGDPK 

       250        260        270        280        290        300 
RKEFLDDLFS FMQKRGTPVN RIPIMAKQVL DLFMLYVLVT EKGGLVEVIN KKLWREITKG 

       310        320        330        340        350        360 
LNLPTSITSA AFTLRTQYMK YLYPYECEKR GLSNPNELQA AIDSNRREGR RQSFGGSLFA 

       370        380        390        400        410        420 
YSPGGAHGML SSPKLPVSSL GLAASTNGSS ITPAPKIKKE EDSAIPITVP GRLPVSLAGH 

       430        440        450        460        470        480 
PVVAAQAAAV QAAAAQAAVA AQAAALEQLR EKLESAEPPE KKMALVADEQ QRLMQRALQQ 

       490        500        510        520        530        540 
NFLAMAAQLP MSIRINSQAS ESRQDSAVNL TGTNGSNSIS MSVEINGIMY TGVLFAQPPA 

       550        560        570        580        590 
PTPTSAPNKG GGGGGGSSSN AGGRGGNTGT SGGQAGPAGL STPSTSTSNN SLP 

« Hide

References

« Hide 'large scale' references
[1]"The human dead ringer/bright homolog, DRIL1: cDNA cloning, gene structure, and mapping to D19S886, a marker on 19p13.3 that is strictly linked to the Peutz-Jeghers syndrome."
Kortschak R.D., Reimann H., Zimmer M., Eyre H.J., Saint R., Jenne D.E.
Genomics 51:288-292(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer."
Suzuki M., Okuyama S., Okamoto S., Shirasuna K., Nakajima T., Hachiya T., Nojima H., Sekiya S., Oda K.
Oncogene 17:853-865(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH E2F1, VARIANT SER-556.
[3]"Molecular cloning and immunologic characterization of DRIL3, a new bright-like ARID protein expressed in both myeloid and lymphoid cells, shares homology to E2FBP1/pRB family complexes."
Paulin Y.G., Frank R.T., Davy E.J.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANTS HIS-36; GLU-320 AND SER-556.
Tissue: Placenta.
[6]"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence."
Peeper D.S., Shvarts A., Brummelkamp T., Douma S., Koh E.Y., Daley G.Q., Bernards R.
Nat. Cell Biol. 4:148-153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53."
Ma K., Araki K., Ichwan S.J.A., Suganuma T., Tamamori-Adachi M., Ikeda M.-A.
Mol. Cancer Res. 1:438-444(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"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-77; SER-81 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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, SUBUNIT, DNA-BINDING, MUTAGENESIS OF TYR-325.
[10]"REKLES is an ARID3-restricted multifunctional domain."
Kim D., Probst L., Das C., Tucker P.W.
J. Biol. Chem. 282:15768-15777(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARID3B, DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-461; GLY-527; TYR-530; GLY-532 AND LEU-534.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-77; SER-81 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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].
[15]"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-77; SER-88; THR-98; SER-101 AND SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution NMR structure of the ARID domain of human AT-rich interactive domain-containing protein 3A: a human cancer protein interaction network target."
Liu G., Huang Y.J., Xiao R., Wang D., Acton T.B., Montelione G.T.
Proteins 78:2170-2175(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 218-351.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U88047 mRNA. Translation: AAC32888.1.
AF039850 expand/collapse EMBL AC list , AF039844, AF039845, AF039846, AF039847, AF039848, AF039849 Genomic DNA. Translation: AAC69994.1.
AY152547 mRNA. Translation: AAN74028.1.
AY845638 mRNA. Translation: AAW30734.1. Frameshift.
AC005391 Genomic DNA. Translation: AAC28918.1.
AC005379 Genomic DNA. Translation: AAC28499.1.
BC033163 mRNA. Translation: AAH33163.1.
BC060828 mRNA. Translation: AAH60828.1.
CCDSCCDS12050.1.
RefSeqNP_005215.1. NM_005224.2.
XP_005259569.1. XM_005259512.1.
XP_005259570.1. XM_005259513.2.
XP_005259571.1. XM_005259514.2.
UniGeneHs.501296.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KK0NMR-A218-351[»]
4LJXX-ray2.21A/B216-351[»]
ProteinModelPortalQ99856.
SMRQ99856. Positions 218-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108154. 15 interactions.
IntActQ99856. 6 interactions.
MINTMINT-4537882.
STRING9606.ENSP00000263620.

PTM databases

PhosphoSiteQ99856.

Polymorphism databases

DMDM12230034.

Proteomic databases

MaxQBQ99856.
PaxDbQ99856.
PRIDEQ99856.

Protocols and materials databases

DNASU1820.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263620; ENSP00000263620; ENSG00000116017.
GeneID1820.
KEGGhsa:1820.
UCSCuc002lql.3. human.

Organism-specific databases

CTD1820.
GeneCardsGC19P000926.
HGNCHGNC:3031. ARID3A.
HPAHPA004793.
MIM603265. gene.
neXtProtNX_Q99856.
PharmGKBPA27485.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327790.
HOGENOMHOG000236281.
HOVERGENHBG050574.
InParanoidQ99856.
OMALFAYSPG.
OrthoDBEOG77DJ6W.
PhylomeDBQ99856.
TreeFamTF320364.

Gene expression databases

ArrayExpressQ99856.
BgeeQ99856.
CleanExHS_ARID3A.
GenevestigatorQ99856.

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

EvolutionaryTraceQ99856.
GeneWikiARID3A.
GenomeRNAi1820.
NextBio7417.
PROQ99856.
SOURCESearch...

Entry information

Entry nameARI3A_HUMAN
AccessionPrimary (citable) accession number: Q99856
Secondary accession number(s): Q5I858 expand/collapse secondary AC list , Q6P9C6, Q8IZA7, Q8N4Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM