GABP2_MOUSE
ID GABP2_MOUSE Reviewed; 414 AA.
AC P81069; A7E218; Q8CDA6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=GA-binding protein subunit beta-2;
DE Short=GABP subunit beta-2;
DE Short=GABPB-2;
DE AltName: Full=GA-binding protein beta-2-1;
DE Short=GABP subunit beta-2-1;
DE Short=GABPB2-1;
GN Name=Gabpb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7958862; DOI=10.1101/gad.8.15.1853;
RA de la Brousse F.C., Birkenmeier E.H., King D.S., Rowe L.B., McKnight S.L.;
RT "Molecular and genetic characterization of GABP beta.";
RL Genes Dev. 8:1853-1865(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH ADGRB2.
RX PubMed=16412436; DOI=10.1016/j.febslet.2005.12.086;
RA Jeong B.C., Kim M.Y., Lee J.H., Kee H.J., Kho D.H., Han K.E., Qian Y.R.,
RA Kim J.K., Kim K.K.;
RT "Brain-specific angiogenesis inhibitor 2 regulates VEGF through GABP that
RT acts as a transcriptional repressor.";
RL FEBS Lett. 580:669-676(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor capable of interacting with purine rich
CC repeats (GA repeats). Must associate with GABP-alpha to bind DNA.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. The C-
CC terminal is necessary for the formation of a heterotetrameric GABP-
CC alpha-2/beta-2 complex, and also facilitates homotypic dimerization.
CC Interacts with ADGRB2 (PubMed:16412436). {ECO:0000269|PubMed:16412436}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P81069-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P81069-2; Sequence=VSP_032473;
CC -!- TISSUE SPECIFICITY: High levels in thymus, spleen, kidney and
CC intestine.
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DR EMBL; AK030849; BAC27157.1; -; mRNA.
DR EMBL; AK141382; BAE24666.1; -; mRNA.
DR EMBL; BC150160; AAI50161.1; -; mRNA.
DR EMBL; BC150482; AAI50483.1; -; mRNA.
DR CCDS; CCDS17605.1; -. [P81069-1]
DR PIR; A53950; A53950.
DR RefSeq; NP_084161.1; NM_029885.1. [P81069-1]
DR RefSeq; NP_766100.1; NM_172512.2. [P81069-1]
DR RefSeq; XP_006501313.1; XM_006501250.3. [P81069-1]
DR RefSeq; XP_006501314.1; XM_006501251.3. [P81069-1]
DR RefSeq; XP_006501315.1; XM_006501252.3. [P81069-1]
DR RefSeq; XP_011238360.1; XM_011240058.2. [P81069-1]
DR RefSeq; XP_011238361.1; XM_011240059.2. [P81069-1]
DR RefSeq; XP_011238362.1; XM_011240060.2. [P81069-1]
DR RefSeq; XP_011238363.1; XM_011240061.2. [P81069-1]
DR RefSeq; XP_017175004.1; XM_017319515.1. [P81069-2]
DR AlphaFoldDB; P81069; -.
DR SMR; P81069; -.
DR STRING; 10090.ENSMUSP00000121283; -.
DR iPTMnet; P81069; -.
DR PhosphoSitePlus; P81069; -.
DR EPD; P81069; -.
DR jPOST; P81069; -.
DR MaxQB; P81069; -.
DR PaxDb; P81069; -.
DR PeptideAtlas; P81069; -.
DR PRIDE; P81069; -.
DR ProteomicsDB; 268835; -. [P81069-1]
DR ProteomicsDB; 268836; -. [P81069-2]
DR Antibodypedia; 34049; 257 antibodies from 26 providers.
DR DNASU; 213054; -.
DR Ensembl; ENSMUST00000098873; ENSMUSP00000096470; ENSMUSG00000038766. [P81069-1]
DR Ensembl; ENSMUST00000107209; ENSMUSP00000102827; ENSMUSG00000038766. [P81069-1]
DR Ensembl; ENSMUST00000136139; ENSMUSP00000121283; ENSMUSG00000038766. [P81069-1]
DR GeneID; 213054; -.
DR KEGG; mmu:213054; -.
DR UCSC; uc008qin.2; mouse. [P81069-1]
DR UCSC; uc008qip.2; mouse. [P81069-2]
DR CTD; 126626; -.
DR MGI; MGI:95612; Gabpb2.
DR VEuPathDB; HostDB:ENSMUSG00000038766; -.
DR eggNOG; ENOG502QRTX; Eukaryota.
DR GeneTree; ENSGT00940000156794; -.
DR HOGENOM; CLU_000134_12_0_1; -.
DR InParanoid; P81069; -.
DR OMA; MTEEPQP; -.
DR OrthoDB; 1514706at2759; -.
DR PhylomeDB; P81069; -.
DR TreeFam; TF326036; -.
DR BioGRID-ORCS; 213054; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Gabpb2; mouse.
DR PRO; PR:P81069; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P81069; protein.
DR Bgee; ENSMUSG00000038766; Expressed in manus and 216 other tissues.
DR ExpressionAtlas; P81069; baseline and differential.
DR Genevisible; P81069; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..414
FT /note="GA-binding protein subunit beta-2"
FT /id="PRO_0000066995"
FT REPEAT 5..34
FT /note="ANK 1"
FT REPEAT 37..66
FT /note="ANK 2"
FT REPEAT 70..99
FT /note="ANK 3"
FT REPEAT 103..132
FT /note="ANK 4"
FT REPEAT 136..166
FT /note="ANK 5"
FT COILED 310..362
FT /evidence="ECO:0000255"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 208..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032473"
FT CONFLICT 24
FT /note="T -> I (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="D -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Missing (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="E -> EC (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="T -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="D -> Q (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..373
FT /note="EE -> QQ (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45658 MW; 7F601EF08DB6C5A2 CRC64;
MSLVDLGKRL LEAARKGQDD EVRTLMANGA PFTTDWLGTS PLHLAAQYGH YSTAEVLLRA
GVSRDARTKV DRTPLHMAAA DGHVHIVELL VRSGADVNAK DMLQMTALHW ATEHHHRDVV
ELLIKYGADV YAFSKFDKSA FDIAMEKNNT EILVMLQEAM QNQVNTNHER ANPVANPVTV
TAPFIFTSGE VINLASFVSS ANTKATSAHL EEMEEGNSLD SSTQQVVGSG GQRVITIVTD
GVPLGNIQTS LPAGGIGQPF IVTMQDGQQV LTVPAGQVAE ETIIEDEEEE EEKLPLVKRP
RMAEMTNRVE EMKEGSEREL LQQQLQEANR RAQEYRHQLL KKEQEAEQYR LRLEAMAQQQ
TNGVEVDVTV VEEVAEVDAV VVTEGDEVER ATQVMKSGRT TEPHTNVSIE TISS
