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Q00422

- GABPA_MOUSE

UniProt

Q00422 - GABPA_MOUSE

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Protein

GA-binding protein alpha chain

Gene
Gabpa, E4tf1a
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription factor capable of interacting with purine rich repeats (GA repeats).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi320 – 40081ETSAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: MGI
  3. protein heterodimerization activity Source: MGI
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  5. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  6. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
  7. transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  1. in utero embryonic development Source: MGI
  2. negative regulation of megakaryocyte differentiation Source: MGI
  3. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  4. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  5. regulation of transcription from RNA polymerase II promoter Source: MGI
  6. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_205251. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
GA-binding protein alpha chain
Short name:
GABP subunit alpha
Gene namesi
Name:Gabpa
Synonyms:E4tf1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:95610. Gabpa.

Subcellular locationi

GO - Cellular componenti

  1. nuclear chromatin Source: Ensembl
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454GA-binding protein alpha chainPRO_0000204128Add
BLAST

Proteomic databases

MaxQBiQ00422.
PaxDbiQ00422.
PRIDEiQ00422.

PTM databases

PhosphoSiteiQ00422.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ00422.
BgeeiQ00422.
CleanExiMM_GABPA.
GenevestigatoriQ00422.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.

Protein-protein interaction databases

DIPiDIP-156N.
IntActiQ00422. 1 interaction.
MINTiMINT-1531786.

Structurei

Secondary structure

1
454
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 4712
Helixi48 – 503
Helixi51 – 544
Helixi56 – 594
Beta strandi67 – 704
Turni81 – 833
Beta strandi90 – 9910
Beta strandi107 – 1159
Helixi168 – 17710
Turni178 – 1803
Helixi186 – 1883
Helixi191 – 20414
Helixi213 – 2153
Helixi219 – 2246
Helixi227 – 2337
Helixi238 – 24912
Turni250 – 2523
Helixi322 – 3309
Turni333 – 3386
Beta strandi339 – 3413
Beta strandi343 – 3497
Helixi353 – 36412
Helixi371 – 3799
Helixi380 – 3834
Beta strandi384 – 3896
Beta strandi396 – 3994
Helixi403 – 4064
Helixi411 – 42818

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWCX-ray2.15A320-429[»]
1SXDNMR-A168-254[»]
2JUONMR-A35-121[»]
ProteinModelPortaliQ00422.
SMRiQ00422. Positions 35-121, 168-254, 320-429.

Miscellaneous databases

EvolutionaryTraceiQ00422.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 25184PNTAdd
BLAST

Sequence similaritiesi

Belongs to the ETS family.

Phylogenomic databases

eggNOGiNOG252121.
GeneTreeiENSGT00750000117307.
HOGENOMiHOG000285952.
HOVERGENiHBG051687.
InParanoidiQ7TT22.
KOiK09441.
OMAiGIPYDPV.
OrthoDBiEOG7TXKGT.
TreeFamiTF350537.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProiIPR000418. Ets_dom.
IPR024668. GABP_asu_N.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016312. TF_GA-bd_asu.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00178. Ets. 1 hit.
PF11620. GABP-alpha. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]
PIRSFiPIRSF001703. GABP_alpha. 1 hit.
PRINTSiPR00454. ETSDOMAIN.
SMARTiSM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00422-1 [UniParc]FASTAAdd to Basket

« Hide

MTKREAEELI EIEIDGTEKA ECTEESIVEQ TYTPAECVSQ AIDINEPIGN    50
LKKLLEPRLQ CSLDAHEICL QDIQLDPDRS LFDQGVKTDG TVQLSVQVIS 100
YQGMEPKLNI LEIVKTAETV EVVIDPDAHH AEAEAHLVEE AQVITLDGTK 150
HITTISDETS EQVTRWAAAL EGYRKEQERL GIPYDPIHWS TDQVLHWVVW 200
VMKEFSMTDI DLTTLNISGR ELCSLNQEDF FQRVPRGEIL WSHLELLRKY 250
VLASQEQQMN EIVTIDQPVQ IIPASVPPAT PTTIKVINSS AKAAKVQRSP 300
RISGEDRSSP GNRTGNNGQI QLWQFLLELL TDKDARDCIS WVGDEGEFKL 350
NQPELVAQKW GQRKNKPTMN YEKLSRALRY YYDGDMICKV QGKRFVYKFV 400
CDLKTLIGYS AAELNRLVIE CEQKKLARMQ LHGIAQPVTA VALAATSLQA 450
DKEI 454
Length:454
Mass (Da):51,344
Last modified:July 27, 2011 - v2
Checksum:i2CBC40B895563685
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881H → R in AAA53030. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74515 mRNA. Translation: AAA53030.1.
AK139916 mRNA. Translation: BAE24181.1.
AK145446 mRNA. Translation: BAE26442.1.
AK145838 mRNA. Translation: BAE26687.1.
AK148087 mRNA. Translation: BAE28337.1.
AK150455 mRNA. Translation: BAE29575.1.
CH466521 Genomic DNA. Translation: EDK98317.1.
BC052448 mRNA. Translation: AAH52448.1.
CCDSiCCDS28284.1.
PIRiA40858.
RefSeqiNP_032091.2. NM_008065.2.
XP_006522970.1. XM_006522907.1.
UniGeneiMm.18974.

Genome annotation databases

EnsembliENSMUST00000009120; ENSMUSP00000009120; ENSMUSG00000008976.
ENSMUST00000114184; ENSMUSP00000109822; ENSMUSG00000008976.
GeneIDi14390.
KEGGimmu:14390.
UCSCiuc007ztj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74515 mRNA. Translation: AAA53030.1 .
AK139916 mRNA. Translation: BAE24181.1 .
AK145446 mRNA. Translation: BAE26442.1 .
AK145838 mRNA. Translation: BAE26687.1 .
AK148087 mRNA. Translation: BAE28337.1 .
AK150455 mRNA. Translation: BAE29575.1 .
CH466521 Genomic DNA. Translation: EDK98317.1 .
BC052448 mRNA. Translation: AAH52448.1 .
CCDSi CCDS28284.1.
PIRi A40858.
RefSeqi NP_032091.2. NM_008065.2.
XP_006522970.1. XM_006522907.1.
UniGenei Mm.18974.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AWC X-ray 2.15 A 320-429 [» ]
1SXD NMR - A 168-254 [» ]
2JUO NMR - A 35-121 [» ]
ProteinModelPortali Q00422.
SMRi Q00422. Positions 35-121, 168-254, 320-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-156N.
IntActi Q00422. 1 interaction.
MINTi MINT-1531786.

PTM databases

PhosphoSitei Q00422.

Proteomic databases

MaxQBi Q00422.
PaxDbi Q00422.
PRIDEi Q00422.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000009120 ; ENSMUSP00000009120 ; ENSMUSG00000008976 .
ENSMUST00000114184 ; ENSMUSP00000109822 ; ENSMUSG00000008976 .
GeneIDi 14390.
KEGGi mmu:14390.
UCSCi uc007ztj.1. mouse.

Organism-specific databases

CTDi 2551.
MGIi MGI:95610. Gabpa.

Phylogenomic databases

eggNOGi NOG252121.
GeneTreei ENSGT00750000117307.
HOGENOMi HOG000285952.
HOVERGENi HBG051687.
InParanoidi Q7TT22.
KOi K09441.
OMAi GIPYDPV.
OrthoDBi EOG7TXKGT.
TreeFami TF350537.

Enzyme and pathway databases

Reactomei REACT_205251. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

ChiTaRSi GABPA. mouse.
EvolutionaryTracei Q00422.
NextBioi 285913.
PROi Q00422.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00422.
Bgeei Q00422.
CleanExi MM_GABPA.
Genevestigatori Q00422.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProi IPR000418. Ets_dom.
IPR024668. GABP_asu_N.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016312. TF_GA-bd_asu.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00178. Ets. 1 hit.
PF11620. GABP-alpha. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view ]
PIRSFi PIRSF001703. GABP_alpha. 1 hit.
PRINTSi PR00454. ETSDOMAIN.
SMARTi SM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of Ets- and notch-related subunits in GA binding protein."
    Lamarco K., Thompson C.C., Byers B.P., Walton E.M., McKnight S.L.
    Science 253:789-792(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Egg and Liver.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., 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].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "The structure of GABPalpha/beta: an ETS domain-ankyrin repeat heterodimer bound to DNA."
    Batchelor A.H., Piper D.E., de la Brousse F.C., McKnight S.L., Wolberger C.
    Science 279:1037-1041(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 320-320.

Entry informationi

Entry nameiGABPA_MOUSE
AccessioniPrimary (citable) accession number: Q00422
Secondary accession number(s): Q7TT22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 137 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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