Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8VHR5 (P66B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-beta
Alternative name(s):
GATA zinc finger domain-containing protein 2B
p66/p68
Gene names
Name:Gatad2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

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

Domain

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

Sequence similarities

Contains 1 GATA-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsequence-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 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VHR5-1)

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: Q8VHR5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     475-485: EIEQRLQQQAA → VRTLTPTCTVI
     486-594: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Transcriptional repressor p66-beta
PRO_0000083503

Regions

Zinc finger415 – 46854GATA-type
Region166 – 19126CR1
Region341 – 481141CR2
Coiled coil141 – 19555 Potential
Coiled coil450 – 48334 Potential

Amino acid modifications

Modified residue1211Phosphothreonine Ref.4 Ref.5 Ref.6
Modified residue1231Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue1301Phosphoserine Ref.4
Modified residue1351Phosphoserine By similarity
Modified residue1361Phosphoserine Ref.4
Modified residue3341Phosphoserine By similarity
Modified residue3391Phosphoserine By similarity
Modified residue4871Phosphoserine Ref.3

Natural variations

Alternative sequence475 – 48511EIEQRLQQQAA → VRTLTPTCTVI in isoform 2.
VSP_010930
Alternative sequence486 – 594109Missing in isoform 2.
VSP_010931

Sequences

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

Last modified March 1, 2002. Version 1.
Checksum: C57330259EADAAE6

FASTA59465,411
        10         20         30         40         50         60 
MDRMTEDALR LNLLKRSLDP ADERDDVLAK RLKMEGHEAM ERLKMLALLK RKDLANLEVP 

        70         80         90        100        110        120 
HELPTKQDGS GVKGYEEKLN GNLRPHGDNN RTAGRPGKEN INDEPVDMSA RRSEPDRGRL 

       130        140        150        160        170        180 
TPSPDIIVLS DNEASSPRSS SRMEERLKAA NLEMFKGKGM EERQQLIKQL RDELRLEEAR 

       190        200        210        220        230        240 
LVLLKKLRQS QLQKENVVQK TPVVQNAASI VQPSPAHVGQ QGLSKLPSRP GAQGIEPQNM 

       250        260        270        280        290        300 
RTLQGHSVIR SATNTTLPHM LMSQRVIAPN PAQLQGQRGP PKPGIVRTTT PNMNPAISYQ 

       310        320        330        340        350        360 
PQSSSSVPCQ RTTSSAIYMN LASHIQPGTV NRVSSPLPSP SAMSDAANSQ AAAKLALRKQ 

       370        380        390        400        410        420 
LEKTLLEIPP PKPPAPLLHF LPSAANSEFI YMVGLEEVVQ SVIDSQGKNC ASLLRVEPFV 

       430        440        450        460        470        480 
CAQCRTDFTP HWKQEKNGKI LCEQCMTSNQ KKALKAEHTN RLKNAFVKAL QQEQEIEQRL 

       490        500        510        520        530        540 
QQQAALSPTT APAVSSVSKQ ETIMRHHTLR QAPQPQSSLQ RGIPTSARSM LSNFAQAPQL 

       550        560        570        580        590 
SVPGGLLGMP GVNIAYLNTG IGGHKAPSLA DRQREYLLDM IPPRSISQSI SGQK 

« Hide

Isoform 2 [UniParc].

Checksum: 319D9E907558D734
Show »

FASTA48553,734

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, MASS SPECTROMETRY.
Tissue: Embryonic brain.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123; SER-130 AND SER-136, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121 AND SER-123, MASS SPECTROMETRY.
Tissue: Melanoma.
[6]"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 AND SER-123, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF411837 mRNA. Translation: AAL39081.1.
AK041594 mRNA. Translation: BAC30997.1.
IPIIPI00128615.
IPI00453989.
RefSeqNP_647465.1. NM_139304.1.
UniGeneMm.270999.

3D structure databases

ProteinModelPortalQ8VHR5.
SMRQ8VHR5. Positions 161-200.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8VHR5. 1 interaction.
STRING10090.ENSMUSP00000041370.

PTM databases

PhosphoSiteQ8VHR5.

Proteomic databases

PaxDbQ8VHR5.
PRIDEQ8VHR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049382; ENSMUSP00000041370; ENSMUSG00000042390.
GeneID229542.
KEGGmmu:229542.
UCSCuc008qca.1. mouse.
uc008qcb.1. mouse.

Organism-specific databases

CTD57459.
MGIMGI:2443225. Gatad2b.

Phylogenomic databases

eggNOGNOG293566.
GeneTreeENSGT00390000004097.
HOGENOMHOG000074070.
HOVERGENHBG053401.
InParanoidQ8VHR5.
OMAPCQRTTS.
OrthoDBEOG4CVG6R.

Gene expression databases

ArrayExpressQ8VHR5.
BgeeQ8VHR5.
CleanExMM_GATAD2B.
GenevestigatorQ8VHR5.
GermOnlineENSMUSG00000042390. Mus musculus.

Family and domain databases

Gene3D3.30.50.10. 1 hit.
InterProIPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00320. GATA. 1 hit.
[Graphical view]
PROSITEPS00344. GATA_ZN_FINGER_1. False negative.
PS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGATAD2B. mouse.
NextBio379495.
SOURCESearch...

Entry information

Entry nameP66B_MOUSE
AccessionPrimary (citable) accession number: Q8VHR5
Secondary accession number(s): Q8C9Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families