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P29374 (ARI4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 127. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AT-rich interactive domain-containing protein 4A

Short name=ARID domain-containing protein 4A
Alternative name(s):
Retinoblastoma-binding protein 1
Short name=RBBP-1
Gene names
Name:ARID4A
Synonyms:RBBP1, RBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with the viral protein-binding domain of the retinoblastoma protein.

Subunit structure

Interacts with BRMS1. Identified in mSin3A corepressor complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1, HDAC1 and HDAC2. Ref.5

Subcellular location

Nucleus Ref.3.

Sequence similarities

Contains 1 ARID domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform I (identifier: P29374-1)

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 II (identifier: P29374-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1121-1174: Missing.
Isoform III (identifier: P29374-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1106-1174: Missing.
     1175-1175: N → D

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12571257AT-rich interactive domain-containing protein 4A
PRO_0000200580

Regions

Domain309 – 40193ARID
Region951 – 96414Retinoblastoma protein binding Potential

Amino acid modifications

Modified residue5381Phosphoserine Ref.10
Modified residue5421Phosphoserine Ref.10
Modified residue6761Phosphoserine Ref.7
Modified residue11091Phosphoserine Ref.7

Natural variations

Alternative sequence1106 – 117469Missing in isoform III.
VSP_004371
Alternative sequence1121 – 117454Missing in isoform II.
VSP_004373
Alternative sequence11751N → D in isoform III.
VSP_004372
Natural variant4121H → P.
Corresponds to variant rs34982206 [ dbSNP | Ensembl ].
VAR_031566
Natural variant7241N → S.
Corresponds to variant rs2230098 [ dbSNP | Ensembl ].
VAR_031567
Natural variant7791T → A. Ref.1
Corresponds to variant rs1051858 [ dbSNP | Ensembl ].
VAR_031568

Experimental info

Sequence conflict3851V → L in AAB28543. Ref.1
Sequence conflict6181R → S in AAB28543. Ref.1
Sequence conflict6531K → V in AAB25833. Ref.3
Sequence conflict6531K → V in AAB25834. Ref.3
Sequence conflict6531K → V in AAB25835. Ref.3
Sequence conflict11781D → S no nucleotide entry Ref.4
Sequence conflict1196 – 12016IRKYYM → SENIICL no nucleotide entry Ref.4

Secondary structure

............................ 1257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform I [UniParc].

Last modified September 23, 2008. Version 3.
Checksum: 5B3F6A5AFB7588CF

FASTA1,257142,752
        10         20         30         40         50         60 
MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL VQDDQVKGPL 

        70         80         90        100        110        120 
RVGAIVETRT SDGSFQEAII SKLTDASWYT VVFDDGDERT LRRTSLCLKG ERHFAESETL 

       130        140        150        160        170        180 
DQLPLTNPEH FGTPVIAKKT NRGRRSSLPV TEDEKEEESS EEEDEDKRRL NDELLGKVVS 

       190        200        210        220        230        240 
VVSATERTEW YPALVISPSC NDDITVKKDQ CLVRSFIDSK FYSIARKDIK EVDILNLPES 

       250        260        270        280        290        300 
ELSTKPGLQK ASIFLKTRVV PDNWKMDISE ILESSSSDDE DGPAEENDEE KEKEAKKTEE 

       310        320        330        340        350        360 
EVPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV YHQGGCDNID 

       370        380        390        400        410        420 
SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC RSANIQFRTV HHHEPKVKEE 

       430        440        450        460        470        480 
KKDLEESMEE ALKLDQEMPL TEVKSEPEEN IDSNSESERE EIELKSPRGR RRIARDVNSI 

       490        500        510        520        530        540 
KKEIEEEKTE DKLKDNDTEN KDVDDDYETA EKKENELLLG RKNTPKQKEK KIKKQEDSDK 

       550        560        570        580        590        600 
DSDEEEEKSQ EREETESKCD SEGEEDEEDM EPCLTGTKVK VKYGRGKTQK IYEASIKSTE 

       610        620        630        640        650        660 
IDDGEVLYLV HYYGWNVRYD EWVKADRIIW PLDKGGPKKK QKKKAKNKED SEKDEKRDEE 

       670        680        690        700        710        720 
RQKSKRGRPP LKSTLSSNMP YGLSKTANSE GKSDSCSSDS ETEDALEKNL INEELSLKDE 

       730        740        750        760        770        780 
LEKNENLNDD KLDEENPKIS AHILKENDRT QMQPLETLKL EVGENEQIVQ IFGNKMEKTE 

       790        800        810        820        830        840 
EVKKEAEKSP KGKGRRSKTK DLSLEIIKIS SFGQNEAGSE PHIEAHSLEL SSLDNKNFSS 

       850        860        870        880        890        900 
ATEDEIDQCV KEKKLKRKIL GQSSPEKKIR IENGMEMTNT VSQERTSDCI GSEGMKNLNF 

       910        920        930        940        950        960 
EQHFERENEG MPSLIAESNQ CIQQLTSERF DSPAEETVNI PLKEDEDAMP LIGPETLVCH 

       970        980        990       1000       1010       1020 
EVDLDDLDEK DKTSIEDVAV ESSESNSLVS IPPALPPVVQ HNFSVASPLT LSQDESRSVK 

      1030       1040       1050       1060       1070       1080 
SESDITIEVD SIAEESQEGL CERESANGFE TNVASGTCSI IVQERESREK GQKRPSDGNS 

      1090       1100       1110       1120       1130       1140 
GLMAKKQKRT PKRTSAAAKN EKNGTGQSSD SEDLPVLDNS SKCTPVKHLN VSKPQKLARS 

      1150       1160       1170       1180       1190       1200 
PARISPHIKD GEKDKHREKH PNSSPRTYKW SFQLNELDNM NSTERISFLQ EKLQEIRKYY 

      1210       1220       1230       1240       1250 
MSLKSEVATI DRRRKRLKKK DREVSHAGAS MSSASSDTGM SPSSSSPPQN VLAVECR 

« Hide

Isoform II [UniParc].

Checksum: B2A06AA7071AAAE2
Show »

FASTA1,203136,495
Isoform III [UniParc].

Checksum: 0576FA849F761B54
Show »

FASTA1,188134,951

References

« Hide 'large scale' references
[1]"Characterization of the retinoblastoma binding proteins RBP1 and RBP2."
Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.
Oncogene 8:3149-3156(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), VARIANT ALA-779.
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites."
Otterson G.A., Kratzke R.A., Lin A.Y., Johnston P.G., Kaye F.J.
Oncogene 8:949-957(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 338-1257 (ISOFORMS I; II AND III), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
[4]"Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product."
Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A., Hanobik M.G., Huber H.E., Oliff A.
Nature 352:251-254(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 855-1203 (ISOFORM I).
[5]"Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription."
Meehan W.J., Samant R.S., Hopper J.E., Carrozza M.J., Shevde L.A., Workman J.L., Eckert K.A., Verderame M.F., Welch D.R.
J. Biol. Chem. 279:1562-1569(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH WITH SIN3A; SIN3B; HDAC1; HDAC2; SAP30; BRMS1; RBBP4 AND RBBP7.
[6]"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.
[7]"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-676 AND SER-1109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-538 AND SER-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Solution structure of the RBB1NT domain of human RB(Retinoblastoma)-binding protein 1."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 170-277.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S66427 mRNA. Translation: AAB28543.1.
AL132989 Genomic DNA. No translation available.
AL139021 Genomic DNA. No translation available.
S57153 mRNA. Translation: AAB25833.1.
S57160 mRNA. Translation: AAB25834.1.
S57162 mRNA. Translation: AAB25835.2.
PIRI58383.
RefSeqNP_002883.3. NM_002892.3.
NP_075376.2. NM_023000.2.
NP_075377.2. NM_023001.2.
UniGeneHs.161000.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LCCNMR-A568-635[»]
2MAMNMR-A4-121[»]
2YRVNMR-A170-274[»]
ProteinModelPortalP29374.
SMRP29374. Positions 4-121, 170-277, 306-397, 568-635.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111861. 23 interactions.
DIPDIP-463N.
IntActP29374. 4 interactions.
MINTMINT-150005.
STRING9606.ENSP00000347602.

PTM databases

PhosphoSiteP29374.

Polymorphism databases

DMDM206729929.

Proteomic databases

PaxDbP29374.
PRIDEP29374.

Protocols and materials databases

DNASU5926.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348476; ENSP00000344556; ENSG00000032219. [P29374-3]
ENST00000355431; ENSP00000347602; ENSG00000032219. [P29374-1]
ENST00000395168; ENSP00000378597; ENSG00000032219. [P29374-2]
ENST00000431317; ENSP00000397368; ENSG00000032219. [P29374-3]
GeneID5926.
KEGGhsa:5926.
UCSCuc001xdo.3. human. [P29374-2]
uc001xdp.3. human. [P29374-1]
uc001xdq.3. human. [P29374-3]

Organism-specific databases

CTD5926.
GeneCardsGC14P058766.
H-InvDBHIX0037655.
HGNCHGNC:9885. ARID4A.
HPAHPA048899.
MIM180201. gene.
neXtProtNX_P29374.
PharmGKBPA34249.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248805.
HOGENOMHOG000015398.
HOVERGENHBG058247.
InParanoidP29374.
OMAISPSCND.
OrthoDBEOG7PVWNP.
PhylomeDBP29374.
TreeFamTF106427.

Gene expression databases

ArrayExpressP29374.
BgeeP29374.
CleanExHS_ARID4A.
HS_RBP1.
GenevestigatorP29374.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARID4A. human.
EvolutionaryTraceP29374.
GeneWikiARID4A.
GenomeRNAi5926.
NextBio23080.
PROP29374.
SOURCESearch...

Entry information

Entry nameARI4A_HUMAN
AccessionPrimary (citable) accession number: P29374
Secondary accession number(s): Q15991, Q15992, Q15993
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 23, 2008
Last modified: March 19, 2014
This is version 127 of the entry and version 3 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 14

Human chromosome 14: entries, gene names and cross-references to MIM