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Protein

Transcriptional repressor p66-beta

Gene

Gatad2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A (By similarity). Targets MBD3 to discrete loci in the nucleus (By similarity). Plays a role in synapse development (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri415 – 46854GATA-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor p66-beta
Alternative name(s):
GATA zinc finger domain-containing protein 2B
p66/p68
Gene namesi
Name:Gatad2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2443225. Gatad2b.

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 – 594594Transcriptional repressor p66-betaPRO_0000083503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphothreonineCombined sources
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei130 – 1301PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei334 – 3341PhosphoserineBy similarity
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei487 – 4871PhosphoserineBy similarity
Cross-linki499 – 499Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VHR5.
MaxQBiQ8VHR5.
PaxDbiQ8VHR5.
PRIDEiQ8VHR5.

PTM databases

iPTMnetiQ8VHR5.
PhosphoSiteiQ8VHR5.

Expressioni

Gene expression databases

BgeeiQ8VHR5.
CleanExiMM_GATAD2B.
ExpressionAtlasiQ8VHR5. baseline and differential.
GenevisibleiQ8VHR5. 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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Nr4a1P128132EBI-3043880,EBI-10896863

Protein-protein interaction databases

BioGridi230858. 7 interactions.
IntActiQ8VHR5. 4 interactions.
MINTiMINT-4106148.
STRINGi10090.ENSMUSP00000041370.

Structurei

3D structure databases

ProteinModelPortaliQ8VHR5.
SMRiQ8VHR5. Positions 161-200.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 19126CR1Add
BLAST
Regioni341 – 481141CR2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili141 – 19555Sequence analysisAdd
BLAST
Coiled coili450 – 48334Sequence analysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri415 – 46854GATA-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IQ4W. Eukaryota.
ENOG410ZCNE. LUCA.
GeneTreeiENSGT00390000004097.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
InParanoidiQ8VHR5.
OMAiNLEVSHE.
OrthoDBiEOG783MV0.
PhylomeDBiQ8VHR5.
TreeFamiTF321369.

Family and domain databases

Gene3Di3.30.50.10. 1 hit.
InterProiIPR032346. P66_CC.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00320. GATA. 1 hit.
PF16563. P66_CC. 1 hit.
[Graphical view]
PROSITEiPS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VHR5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDRMTEDALR LNLLKRSLDP ADERDDVLAK RLKMEGHEAM ERLKMLALLK
60 70 80 90 100
RKDLANLEVP HELPTKQDGS GVKGYEEKLN GNLRPHGDNN RTAGRPGKEN
110 120 130 140 150
INDEPVDMSA RRSEPDRGRL TPSPDIIVLS DNEASSPRSS SRMEERLKAA
160 170 180 190 200
NLEMFKGKGM EERQQLIKQL RDELRLEEAR LVLLKKLRQS QLQKENVVQK
210 220 230 240 250
TPVVQNAASI VQPSPAHVGQ QGLSKLPSRP GAQGIEPQNM RTLQGHSVIR
260 270 280 290 300
SATNTTLPHM LMSQRVIAPN PAQLQGQRGP PKPGIVRTTT PNMNPAISYQ
310 320 330 340 350
PQSSSSVPCQ RTTSSAIYMN LASHIQPGTV NRVSSPLPSP SAMSDAANSQ
360 370 380 390 400
AAAKLALRKQ LEKTLLEIPP PKPPAPLLHF LPSAANSEFI YMVGLEEVVQ
410 420 430 440 450
SVIDSQGKNC ASLLRVEPFV CAQCRTDFTP HWKQEKNGKI LCEQCMTSNQ
460 470 480 490 500
KKALKAEHTN RLKNAFVKAL QQEQEIEQRL QQQAALSPTT APAVSSVSKQ
510 520 530 540 550
ETIMRHHTLR QAPQPQSSLQ RGIPTSARSM LSNFAQAPQL SVPGGLLGMP
560 570 580 590
GVNIAYLNTG IGGHKAPSLA DRQREYLLDM IPPRSISQSI SGQK
Length:594
Mass (Da):65,411
Last modified:March 1, 2002 - v1
Checksum:iC57330259EADAAE6
GO
Isoform 2 (identifier: Q8VHR5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     475-485: EIEQRLQQQAA → VRTLTPTCTVI
     486-594: Missing.

Note: May be due to intron retention. No experimental confirmation available.
Show »
Length:485
Mass (Da):53,734
Checksum:i319D9E907558D734
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei475 – 48511EIEQRLQQQAA → VRTLTPTCTVI in isoform 2. 1 PublicationVSP_010930Add
BLAST
Alternative sequencei486 – 594109Missing in isoform 2. 1 PublicationVSP_010931Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411837 mRNA. Translation: AAL39081.1.
AK041594 mRNA. Translation: BAC30997.1.
CCDSiCCDS17526.1. [Q8VHR5-1]
RefSeqiNP_647465.1. NM_139304.1. [Q8VHR5-1]
XP_006501422.2. XM_006501359.2. [Q8VHR5-1]
XP_006501424.1. XM_006501361.1. [Q8VHR5-1]
UniGeneiMm.270999.

Genome annotation databases

EnsembliENSMUST00000049382; ENSMUSP00000041370; ENSMUSG00000042390. [Q8VHR5-1]
ENSMUST00000199607; ENSMUSP00000142617; ENSMUSG00000042390. [Q8VHR5-1]
ENSMUST00000199754; ENSMUSP00000142514; ENSMUSG00000042390. [Q8VHR5-1]
GeneIDi229542.
KEGGimmu:229542.
UCSCiuc008qca.1. mouse. [Q8VHR5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411837 mRNA. Translation: AAL39081.1.
AK041594 mRNA. Translation: BAC30997.1.
CCDSiCCDS17526.1. [Q8VHR5-1]
RefSeqiNP_647465.1. NM_139304.1. [Q8VHR5-1]
XP_006501422.2. XM_006501359.2. [Q8VHR5-1]
XP_006501424.1. XM_006501361.1. [Q8VHR5-1]
UniGeneiMm.270999.

3D structure databases

ProteinModelPortaliQ8VHR5.
SMRiQ8VHR5. Positions 161-200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230858. 7 interactions.
IntActiQ8VHR5. 4 interactions.
MINTiMINT-4106148.
STRINGi10090.ENSMUSP00000041370.

PTM databases

iPTMnetiQ8VHR5.
PhosphoSiteiQ8VHR5.

Proteomic databases

EPDiQ8VHR5.
MaxQBiQ8VHR5.
PaxDbiQ8VHR5.
PRIDEiQ8VHR5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049382; ENSMUSP00000041370; ENSMUSG00000042390. [Q8VHR5-1]
ENSMUST00000199607; ENSMUSP00000142617; ENSMUSG00000042390. [Q8VHR5-1]
ENSMUST00000199754; ENSMUSP00000142514; ENSMUSG00000042390. [Q8VHR5-1]
GeneIDi229542.
KEGGimmu:229542.
UCSCiuc008qca.1. mouse. [Q8VHR5-1]

Organism-specific databases

CTDi57459.
MGIiMGI:2443225. Gatad2b.

Phylogenomic databases

eggNOGiENOG410IQ4W. Eukaryota.
ENOG410ZCNE. LUCA.
GeneTreeiENSGT00390000004097.
HOGENOMiHOG000074070.
HOVERGENiHBG053401.
InParanoidiQ8VHR5.
OMAiNLEVSHE.
OrthoDBiEOG783MV0.
PhylomeDBiQ8VHR5.
TreeFamiTF321369.

Enzyme and pathway databases

ReactomeiR-MMU-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

NextBioi379495.
PROiQ8VHR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHR5.
CleanExiMM_GATAD2B.
ExpressionAtlasiQ8VHR5. baseline and differential.
GenevisibleiQ8VHR5. MM.

Family and domain databases

Gene3Di3.30.50.10. 1 hit.
InterProiIPR032346. P66_CC.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00320. GATA. 1 hit.
PF16563. P66_CC. 1 hit.
[Graphical view]
PROSITEiPS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and functional characterization of the p66/p68 components of the MeCP1 complex."
    Feng Q., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Zhang Y.
    Mol. Cell. Biol. 22:536-546(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123; SER-130 AND SER-136, 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 THR-121; SER-123 AND SER-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123; SER-130; SER-135; SER-136; SER-339 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiP66B_MOUSE
AccessioniPrimary (citable) accession number: Q8VHR5
Secondary accession number(s): Q8C9Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 111 of the entry and version 1 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.