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Protein

Transcriptional repressor p66 alpha

Gene

Gatad2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor (By similarity). Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri410 – 46253GATA-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • anterior neuropore closure Source: MGI
  • blood vessel development Source: MGI
  • embryonic body morphogenesis Source: MGI
  • in utero embryonic development Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • neural fold formation Source: MGI
  • programmed cell death Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-6804758. Regulation of TP53 Activity through Acetylation.
R-MMU-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor p66 alpha
Alternative name(s):
GATA zinc finger domain-containing protein 2A
Gene namesi
Name:Gatad2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2384585. Gatad2a.

Subcellular locationi

  • Nucleus speckle By similarity

  • Note: Speckled nuclear localization requires both CR1 and CR2 regions.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 629629Transcriptional repressor p66 alphaPRO_0000083501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei109 – 1091PhosphoserineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei185 – 1851PhosphothreonineBy similarity
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei338 – 3381PhosphoserineBy similarity
Cross-linki485 – 485Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei543 – 5431PhosphoserineBy similarity
Modified residuei545 – 5451PhosphoserineBy similarity
Cross-linki547 – 547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei594 – 5941PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8CHY6.
MaxQBiQ8CHY6.
PaxDbiQ8CHY6.
PRIDEiQ8CHY6.

PTM databases

iPTMnetiQ8CHY6.
PhosphoSiteiQ8CHY6.

Expressioni

Gene expression databases

BgeeiQ8CHY6.
CleanExiMM_GATAD2A.
ExpressionAtlasiQ8CHY6. baseline and differential.
GenevisibleiQ8CHY6. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi231518. 8 interactions.
IntActiQ8CHY6. 7 interactions.
MINTiMINT-4106129.
STRINGi10090.ENSMUSP00000070229.

Structurei

3D structure databases

ProteinModelPortaliQ8CHY6.
SMRiQ8CHY6. Positions 133-174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 17435CR1; MBD2-bindingBy similarityAdd
BLAST
Regioni335 – 478144CR2; histone tail-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili135 – 17036Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi402 – 4076Poly-Ala

Sequence similaritiesi

Contains 1 GATA-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri410 – 46253GATA-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG3740. Eukaryota.
ENOG410XRVM. LUCA.
GeneTreeiENSGT00390000004097.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
InParanoidiQ8CHY6.
PhylomeDBiQ8CHY6.

Family and domain databases

InterProiIPR032346. P66_CC.
[Graphical view]
PfamiPF16563. P66_CC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CHY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEACRTRS QKRTLEPDLT EDDVENKKMK MEKGSSELTV DGDSRVMPEP
60 70 80 90 100
SAGSAQGLLR TTEAMGTGSG EGLLGDGPVD MRTSHSDMKS EKRPPSPDVI
110 120 130 140 150
VLSDSEQPSS PRVNGLTTVA LKDTSTEALL KSSPEERERM IKQLKEELRL
160 170 180 190 200
EEAKLVLLKK LRQSQIQKEA TAQKPTASSG STVTTPPPLV RGTQNIPAGK
210 220 230 240 250
TSLQTSSTRI PGSIIPPPLV RGGQQVSAKL GPQASSQVVM PPLVRGAQIH
260 270 280 290 300
NIRQHSSTGP PPLLLAPRAS VPSMQIQGQR IIQQGLIRVA NVPNTSLLVN
310 320 330 340 350
IPQPTAASMK GTAVASAQAN STPTSVASVV ASAESPASRQ AAAKLALRKQ
360 370 380 390 400
LEKTLLEIPP PKPPAPEMNF LPSAANNEFI YLVGLEEVVQ NLLETQAGRI
410 420 430 440 450
SATAAAAVLS REPYMCVQCK TDFTCRWREK GGAVMCENCM TSNQKKALKV
460 470 480 490 500
EHTSRLKAAF VKALQQEQEM EQRLLQQGVG TASIKAEPAA PHPTLKQVIK
510 520 530 540 550
PRRKLAFRSG EARVWNNGSS LQASSQLSRG SATAPRGVLH TFSQSPKLQN
560 570 580 590 600
AASATALVSR TGRHSERVVG TGKGTASNWK KTPLSTGGTL AFVSPSLAVH
610 620
KTSSAVDRQR EYLLDMIPPR SIPQSATWK
Length:629
Mass (Da):67,334
Last modified:July 19, 2004 - v2
Checksum:i5EA79CC71C9E29A4
GO

Sequence cautioni

The sequence AAH19178.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH31407.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC40736.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481Q → QQ in BAC40736 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK089074 mRNA. Translation: BAC40736.1. Different initiation.
BC019178 mRNA. Translation: AAH19178.1. Different initiation.
BC031407 mRNA. Translation: AAH31407.1. Different initiation.
BC038221 mRNA. Translation: AAH38221.2.
CCDSiCCDS52567.1.
RefSeqiNP_001106817.1. NM_001113346.1.
XP_011240597.1. XM_011242295.1.
UniGeneiMm.270044.

Genome annotation databases

EnsembliENSMUST00000116463; ENSMUSP00000112164; ENSMUSG00000036180.
ENSMUST00000177851; ENSMUSP00000137386; ENSMUSG00000036180.
GeneIDi234366.
KEGGimmu:234366.
UCSCiuc009lyf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK089074 mRNA. Translation: BAC40736.1. Different initiation.
BC019178 mRNA. Translation: AAH19178.1. Different initiation.
BC031407 mRNA. Translation: AAH31407.1. Different initiation.
BC038221 mRNA. Translation: AAH38221.2.
CCDSiCCDS52567.1.
RefSeqiNP_001106817.1. NM_001113346.1.
XP_011240597.1. XM_011242295.1.
UniGeneiMm.270044.

3D structure databases

ProteinModelPortaliQ8CHY6.
SMRiQ8CHY6. Positions 133-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231518. 8 interactions.
IntActiQ8CHY6. 7 interactions.
MINTiMINT-4106129.
STRINGi10090.ENSMUSP00000070229.

PTM databases

iPTMnetiQ8CHY6.
PhosphoSiteiQ8CHY6.

Proteomic databases

EPDiQ8CHY6.
MaxQBiQ8CHY6.
PaxDbiQ8CHY6.
PRIDEiQ8CHY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000116463; ENSMUSP00000112164; ENSMUSG00000036180.
ENSMUST00000177851; ENSMUSP00000137386; ENSMUSG00000036180.
GeneIDi234366.
KEGGimmu:234366.
UCSCiuc009lyf.2. mouse.

Organism-specific databases

CTDi54815.
MGIiMGI:2384585. Gatad2a.

Phylogenomic databases

eggNOGiKOG3740. Eukaryota.
ENOG410XRVM. LUCA.
GeneTreeiENSGT00390000004097.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
InParanoidiQ8CHY6.
PhylomeDBiQ8CHY6.

Enzyme and pathway databases

ReactomeiR-MMU-6804758. Regulation of TP53 Activity through Acetylation.
R-MMU-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiGatad2a. mouse.
PROiQ8CHY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHY6.
CleanExiMM_GATAD2A.
ExpressionAtlasiQ8CHY6. baseline and differential.
GenevisibleiQ8CHY6. MM.

Family and domain databases

InterProiIPR032346. P66_CC.
[Graphical view]
PfamiPF16563. P66_CC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
    , 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: NOD.
    Tissue: Thymus.
  2. "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: FVB/N and FVB/N-3.
    Tissue: Mammary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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-96; SER-103 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103; SER-109 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiP66A_MOUSE
AccessioniPrimary (citable) accession number: Q8CHY6
Secondary accession number(s): Q8BTQ2, Q8VEC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: June 8, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.