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Q86YP4 (P66A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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:
Transcriptional repressor p66-alpha

Short name=Hp66alpha
Alternative name(s):
GATA zinc finger domain-containing protein 2A
Gene names
Name:GATAD2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B. Ref.1 Ref.9

Subunit structure

Binds MBD2 and MBD3. Interaction with MBD2 is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin. Component of the MeCP1 histone deacetylase complex. Interacts with histone tails, including that of histones H2A, H2B, H3 and H4. This interaction is reduced by histone acetylation. Ref.1 Ref.9 Ref.18

Subcellular location

Nucleus speckle. Note: Speckled nuclear localization requires both CR1 and CR2 regions. Ref.1 Ref.9

Tissue specificity

Ubiquitous, both in fetal and adult tissues. Ref.1

Domain

Both CR1 and CR2 regions are required for speckled nuclear localization.

Sequence similarities

Contains 1 GATA-type zinc finger.

Sequence caution

The sequence AAH11684.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA90939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Traceable author statement Ref.1. Source: UniProtKB

anterior neuropore closure

Inferred from electronic annotation. Source: Ensembl

blood vessel development

Inferred from electronic annotation. Source: Ensembl

embryonic body morphogenesis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

neural fold formation

Inferred from electronic annotation. Source: Ensembl

programmed cell death

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from direct assay Ref.1. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

protein binding, bridging

Inferred from direct assay Ref.1. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86YP4-1)

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 2 (identifier: Q86YP4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     500-524: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86YP4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     401-401: Q → QA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633Transcriptional repressor p66-alpha
PRO_0000083500

Regions

Zinc finger411 – 46454GATA-type
Region144 – 17835CR1; MBD2-binding
Region340 – 480141CR2; histone tail-binding
Coiled coil139 – 17436 Potential

Amino acid modifications

Modified residue491Phosphothreonine Ref.10 Ref.12 Ref.14 Ref.15 Ref.17
Modified residue1001Phosphoserine Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17
Modified residue1071Phosphoserine Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17
Modified residue1141Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue1891Phosphothreonine Ref.14
Modified residue3401Phosphoserine Ref.14
Modified residue3431Phosphoserine Ref.17
Modified residue5461Phosphoserine Ref.12 Ref.15
Modified residue5481Phosphoserine Ref.12 Ref.15
Modified residue5981Phosphoserine Ref.12

Natural variations

Alternative sequence4011Q → QA in isoform 3.
VSP_053410
Alternative sequence500 – 52425Missing in isoform 2.
VSP_010929
Natural variant171R → Q.
Corresponds to variant rs10426883 [ dbSNP | Ensembl ].
VAR_059308
Natural variant2961N → S.
Corresponds to variant rs2288851 [ dbSNP | Ensembl ].
VAR_059309

Experimental info

Mutagenesis1491K → R: Disruption of MBD2-binding, loss of enhancement of MBD2-mediated repression and loss of speckled nuclear localization. Ref.9
Sequence conflict4321K → E in BAA90939. Ref.5

Secondary structure

... 633
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 64F0066B4BEFCB39

FASTA63368,063
        10         20         30         40         50         60 
MTEEACRTRS QKRALERDPT EDDVESKKIK MERGLLASDL NTDGDMRVTP EPGAGPTQGL 

        70         80         90        100        110        120 
LRATEATAMA MGRGEGLVGD GPVDMRTSHS DMKSERRPPS PDVIVLSDNE QPSSPRVNGL 

       130        140        150        160        170        180 
TTVALKETST EALMKSSPEE RERMIKQLKE ELRLEEAKLV LLKKLRQSQI QKEATAQKPT 

       190        200        210        220        230        240 
GSVGSTVTTP PPLVRGTQNI PAGKPSLQTS SARMPGSVIP PPLVRGGQQA SSKLGPQASS 

       250        260        270        280        290        300 
QVVMPPLVRG AQQIHSIRQH SSTGPPPLLL APRASVPSVQ IQGQRIIQQG LIRVANVPNT 

       310        320        330        340        350        360 
SLLVNIPQPT PASLKGTTAT SAQANSTPTS VASVVTSAES PASRQAAAKL ALRKQLEKTL 

       370        380        390        400        410        420 
LEIPPPKPPA PEMNFLPSAA NNEFIYLVGL EEVVQNLLET QGRMSAATVL SREPYMCAQC 

       430        440        450        460        470        480 
KTDFTCRWRE EKSGAIMCEN CMTTNQKKAL KVEHTSRLKA AFVKALQQEQ EIEQRLLQQG 

       490        500        510        520        530        540 
TAPAQAKAEP TAAPHPVLKQ VIKPRRKLAF RSGEARDWSN GAVLQASSQL SRGSATTPRG 

       550        560        570        580        590        600 
VLHTFSPSPK LQNSASATAL VSRTGRHSER TVSAGKGSAT SNWKKTPLST GGTLAFVSPS 

       610        620        630 
LAVHKSSSAV DRQREYLLDM IPPRSIPQSA TWK 

« Hide

Isoform 2 [UniParc].

Checksum: 751DB0FC42DA3BC8
Show »

FASTA60865,225
Isoform 3 [UniParc].

Checksum: 4C5D2B9CD5FE719E
Show »

FASTA63468,134

References

« Hide 'large scale' references
[1]"Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3."
Brackertz M., Boeke J., Zhang R., Renkawitz R.
J. Biol. Chem. 277:40958-40966(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MBD2 AND MBD3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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].
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 3).
Tissue: Ovary and Skin.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 417-633 (ISOFORM 1).
Tissue: Colon.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-633 (ISOFORM 2).
Tissue: Brain.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-107 AND SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction."
Brackertz M., Gong Z., Leers J., Renkawitz R.
Nucleic Acids Res. 34:397-406(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MBD2 AND HISTONE TAILS, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-149.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107; SER-114; SER-546; SER-548 AND SER-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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 THR-49; SER-100; SER-107; SER-114; THR-189 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107; SER-546 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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 THR-49; SER-100; SER-107 AND SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex."
Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A., Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.
Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 137-178 IN COMPLEX WITH MBD2, SUBUNIT, INTERACTION WITH MBD2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY186731 mRNA. Translation: AAO31797.1.
AC003030 Genomic DNA. No translation available.
AC011448 Genomic DNA. No translation available.
AC092067 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84819.1.
BC011684 mRNA. Translation: AAH11684.1. Different initiation.
BC012902 mRNA. Translation: AAH12902.2.
AK000092 mRNA. Translation: BAA90939.1. Different initiation.
AL390164 mRNA. Translation: CAB99095.1.
CCDSCCDS12402.2. [Q86YP4-1]
PIRT51878.
RefSeqNP_060130.3. NM_017660.3. [Q86YP4-1]
XP_005260015.1. XM_005259958.1. [Q86YP4-3]
XP_005260016.1. XM_005259959.2. [Q86YP4-3]
XP_005260017.1. XM_005259960.2. [Q86YP4-3]
XP_005260018.1. XM_005259961.1. [Q86YP4-3]
UniGeneHs.118964.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2LNMR-A137-178[»]
ProteinModelPortalQ86YP4.
SMRQ86YP4. Positions 137-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120172. 22 interactions.
IntActQ86YP4. 15 interactions.
MINTMINT-1387810.
STRING9606.ENSP00000351552.

PTM databases

PhosphoSiteQ86YP4.

Polymorphism databases

DMDM50401012.

Proteomic databases

MaxQBQ86YP4.
PaxDbQ86YP4.
PRIDEQ86YP4.

Protocols and materials databases

DNASU54815.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252577; ENSP00000252577; ENSG00000167491. [Q86YP4-2]
ENST00000358713; ENSP00000351552; ENSG00000167491. [Q86YP4-1]
ENST00000360315; ENSP00000353463; ENSG00000167491. [Q86YP4-1]
ENST00000404158; ENSP00000384899; ENSG00000167491. [Q86YP4-3]
GeneID54815.
KEGGhsa:54815.
UCSCuc010xqt.2. human. [Q86YP4-1]

Organism-specific databases

CTD54815.
GeneCardsGC19P019496.
H-InvDBHIX0014940.
HGNCHGNC:29989. GATAD2A.
HPAHPA006759.
HPA024373.
MIM614997. gene.
neXtProtNX_Q86YP4.
PharmGKBPA142671746.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252421.
HOGENOMHOG000074070.
HOVERGENHBG053401.
OMALVNIPQP.
PhylomeDBQ86YP4.
TreeFamTF321369.

Gene expression databases

ArrayExpressQ86YP4.
BgeeQ86YP4.
CleanExHS_GATAD2A.
GenevestigatorQ86YP4.

Family and domain databases

Gene3D3.30.50.10. 1 hit.
InterProIPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PROSITEPS00344. GATA_ZN_FINGER_1. 1 hit.
PS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi54815.
NextBio35478060.
PMAP-CutDBQ86YP4.
PROQ86YP4.
SOURCESearch...

Entry information

Entry nameP66A_HUMAN
AccessionPrimary (citable) accession number: Q86YP4
Secondary accession number(s): B5MC40 expand/collapse secondary AC list , Q7L3J2, Q96F28, Q9NPU2, Q9NXS1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 113 of the entry and version 1 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