P29374 (ARI4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1257 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 12724404. Source: GDB transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	transcriptional repressor complex Inferred from direct assay PubMed 11283269. Source: GDB
Molecular_function	DNA binding Inferred from direct assay PubMed 15640446. Source: GDB sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1257

1257

AT-rich interactive domain-containing protein 4A

PRO_0000200580

Regions

Domain

309 – 401

93

ARID

Region

951 – 964

14

Retinoblastoma protein binding Potential

Amino acid modifications

Modified residue

538

1

Phosphoserine Ref.10

Modified residue

542

1

Phosphoserine Ref.10

Modified residue

676

1

Phosphoserine Ref.7

Modified residue

1109

1

Phosphoserine Ref.7

Natural variations

Alternative sequence

1106 – 1174

69

Missing in isoform III.

VSP_004371

Alternative sequence

1121 – 1174

54

Missing in isoform II.

VSP_004373

Alternative sequence

1175

1

N → D in isoform III.

VSP_004372

Natural variant

412

1

H → P.
Corresponds to variant rs34982206 [ dbSNP | Ensembl ].

VAR_031566

Natural variant

724

1

N → S.
Corresponds to variant rs2230098 [ dbSNP | Ensembl ].

VAR_031567

Natural variant

779

1

T → A. Ref.1
Corresponds to variant rs1051858 [ dbSNP | Ensembl ].

VAR_031568

Experimental info

Sequence conflict

385

1

V → L in AAB28543. Ref.1

Sequence conflict

618

1

R → S in AAB28543. Ref.1

Sequence conflict

653

1

K → V in AAB25833. Ref.3

Sequence conflict

653

1

K → V in AAB25834. Ref.3

Sequence conflict

653

1

K → V in AAB25835. Ref.3

Sequence conflict

1178

1

D → S no nucleotide entry Ref.4

Sequence conflict

1196 – 1201

6

IRKYYM → SENIICL no nucleotide entry Ref.4

Secondary structure

1

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1257

Helix Strand Turn

Details...

Beta strand

15 – 20

6

Beta strand

23 – 32

10

Beta strand

36 – 42

7

Turn

43 – 45

3

Beta strand

48 – 52

5

Turn

53 – 55

3

Beta strand

56 – 58

3

Beta strand

65 – 69

5

Beta strand

75 – 85

11

Beta strand

89 – 92

4

Beta strand

98 – 101

4

Helix

103 – 105

3

Helix

107 – 109

3

Beta strand

177 – 182

6

Beta strand

190 – 196

7

Beta strand

211 – 218

8

Beta strand

221 – 224

4

Turn

226 – 228

3

Helix

239 – 244

6

Helix

246 – 256

11

Turn

262 – 264

3

Helix

269 – 272

4

Beta strand

578 – 585

8

Beta strand

588 – 602

15

Beta strand

605 – 612

8

Beta strand

621 – 624

4

Helix

625 – 627

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform I [UniParc]. Last modified September 23, 2008. Version 3. Checksum: 5B3F6A5AFB7588CF	FASTA	1,257	142,752
	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
	Isoform II [UniParc]. Checksum: B2A06AA7071AAAE2	FASTA	1,203	136,495
	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 NELDNMNSTE RISFLQEKLQ 1150 1160 1170 1180 1190 1200 EIRKYYMSLK SEVATIDRRR KRLKKKDREV SHAGASMSSA SSDTGMSPSS SSPPQNVLAV ECR
	Isoform III [UniParc]. Checksum: 0576FA849F761B54	FASTA	1,188	134,951
	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 EKNGTDELDN MNSTERISFL QEKLQEIRKY YMSLKSEVAT 1150 1160 1170 1180 IDRRRKRLKK KDREVSHAGA SMSSASSDTG MSPSSSSPPQ NVLAVECR

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00218648.
IPI00296069.
IPI00328418.

PIR

I58383.

RefSeq

NP_002883.3. NM_002892.3.
NP_075376.2. NM_023000.2.
NP_075377.2. NM_023001.2.

UniGene

Hs.161000.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LCC	NMR	-	A	568-635	[»]
2LCD	NMR	-	A	4-121	[»]
2YRV	NMR	-	A	170-274	[»]

ProteinModelPortal

P29374.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-463N.

IntAct

P29374. 3 interactions.

STRING

9606.ENSP00000347602.

PTM databases

PhosphoSite

P29374.

Polymorphism databases

DMDM

206729929.

Proteomic databases

PaxDb

P29374.

PRIDE

P29374.

Protocols and materials databases

DNASU

5926.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000348476; ENSP00000344556; ENSG00000032219.
ENST00000355431; ENSP00000347602; ENSG00000032219.
ENST00000395168; ENSP00000378597; ENSG00000032219.
ENST00000431317; ENSP00000397368; ENSG00000032219.

GeneID

5926.

KEGG

hsa:5926.

UCSC

uc001xdo.3. human.
uc001xdp.3. human.
uc001xdq.3. human.

Organism-specific databases

CTD

5926.

GeneCards

GC14P058766.

H-InvDB

HIX0037655.

HGNC

HGNC:9885. ARID4A.

HPA

HPA048899.

MIM

180201. gene.

neXtProt

NX_P29374.

PharmGKB

PA34249.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG248805.

HOGENOM

HOG000015398.

HOVERGEN

HBG058247.

InParanoid

P29374.

OMA

TCSIIVQ.

OrthoDB

EOG498V0C.

PhylomeDB

P29374.

Gene expression databases

ArrayExpress

P29374.

Bgee

P29374.

CleanEx

HS_ARID4A.
HS_RBP1.

Genevestigator

P29374.

GermOnline

ENSG00000032219. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.60. 1 hit.

InterPro

IPR001606. ARID/BRIGHT_DNA-bd.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view]

Pfam

PF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]

SMART

SM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 1 hit.
[Graphical view]

SUPFAM

SSF46774. ARID. 1 hit.
SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS51011. ARID. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARID4A. human.

EvolutionaryTrace

P29374.

GenomeRNAi

5926.

NextBio

23080.

SOURCE

Search...

Entry information

Entry name

ARI4A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 119 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.