ID   TFCP2_MOUSE             Reviewed;         502 AA.
AC   Q9ERA0; Q3UGJ4; Q8VC13;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Alpha-globin transcription factor CP2;
GN   Name=Tfcp2; Synonyms=Tcfcp2;
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=1732747; DOI=10.1128/mcb.12.2.828-835.1992;
RA   Lim L.C., Swendeman S.L., Sheffery M.;
RT   "Molecular cloning of the alpha-globin transcription factor CP2.";
RL   Mol. Cell. Biol. 12:828-835(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Heart, Melanocyte, and Visual cortex;
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 3).
RC   STRAIN=FVB/N; TISSUE=Liver;
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 UBP1 AND PIAS1.
RC   STRAIN=DBA/2J; TISSUE=Erythroleukemia;
RX   PubMed=15988015; DOI=10.1128/mcb.25.14.6005-6020.2005;
RA   Kang H.C., Chae J.H., Lee Y.H., Park M.-A., Shin J.H., Kim S.-H., Ye S.-K.,
RA   Cho Y.S., Fiering S., Kim C.G.;
RT   "Erythroid cell-specific alpha-globin gene regulation by the CP2
RT   transcription factor family.";
RL   Mol. Cell. Biol. 25:6005-6020(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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: Binds a variety of cellular promoters including fibrinogen,
CC       alpha-globin promoters. Activation of the alpha-globin promoter in
CC       erythroid cells is via synergistic interaction with UBP1 (By
CC       similarity). Functions as part of the SSP (stage selector protein)
CC       complex. Facilitates the interaction of the gamma-globin genes with
CC       enhancer elements contained in the locus control region in fetal
CC       erythroid cells. Interacts by binding to the stage selector element
CC       (SSE) in the proximal gamma-globin promoter (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds to DNA as a dimer. Interacts with UBP1 and PIAS1, and is
CC       probably part of a complex containing TFCP2, UBP1 and PIAS1. Component
CC       of the SSP (stage selector protein) complex, which appears to be a
CC       heteromer of TFCP2 and 2 copies of NFE4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9ERA0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ERA0-2; Sequence=VSP_017650;
CC       Name=3;
CC         IsoId=Q9ERA0-3; Sequence=VSP_017649;
CC   -!- SIMILARITY: Belongs to the grh/CP2 family. CP2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M84809; AAF99390.1; -; mRNA.
DR   EMBL; AK146503; BAE27218.1; -; mRNA.
DR   EMBL; AK147898; BAE28214.1; -; mRNA.
DR   EMBL; AK158682; BAE34609.1; -; mRNA.
DR   EMBL; BC022131; AAH22131.1; -; mRNA.
DR   CCDS; CCDS27840.1; -. [Q9ERA0-1]
DR   CCDS; CCDS88846.1; -. [Q9ERA0-3]
DR   PIR; B42030; B42030.
DR   RefSeq; NP_001276532.1; NM_001289603.1. [Q9ERA0-3]
DR   RefSeq; NP_258437.1; NM_033476.3. [Q9ERA0-1]
DR   AlphaFoldDB; Q9ERA0; -.
DR   SMR; Q9ERA0; -.
DR   BioGRID; 204014; 9.
DR   IntAct; Q9ERA0; 3.
DR   STRING; 10090.ENSMUSP00000155683; -.
DR   iPTMnet; Q9ERA0; -.
DR   PhosphoSitePlus; Q9ERA0; -.
DR   EPD; Q9ERA0; -.
DR   MaxQB; Q9ERA0; -.
DR   PaxDb; 10090-ENSMUSP00000009877; -.
DR   PeptideAtlas; Q9ERA0; -.
DR   ProteomicsDB; 262883; -. [Q9ERA0-1]
DR   ProteomicsDB; 262884; -. [Q9ERA0-2]
DR   ProteomicsDB; 262885; -. [Q9ERA0-3]
DR   Pumba; Q9ERA0; -.
DR   Antibodypedia; 26338; 229 antibodies from 31 providers.
DR   DNASU; 21422; -.
DR   Ensembl; ENSMUST00000009877.8; ENSMUSP00000009877.8; ENSMUSG00000009733.10. [Q9ERA0-3]
DR   Ensembl; ENSMUST00000229696.2; ENSMUSP00000155683.2; ENSMUSG00000009733.10. [Q9ERA0-1]
DR   GeneID; 21422; -.
DR   KEGG; mmu:21422; -.
DR   UCSC; uc007xrl.2; mouse. [Q9ERA0-1]
DR   UCSC; uc007xrm.1; mouse. [Q9ERA0-2]
DR   UCSC; uc011zzo.2; mouse. [Q9ERA0-3]
DR   AGR; MGI:98509; -.
DR   CTD; 7024; -.
DR   MGI; MGI:98509; Tfcp2.
DR   VEuPathDB; HostDB:ENSMUSG00000009733; -.
DR   eggNOG; KOG4091; Eukaryota.
DR   GeneTree; ENSGT00940000157629; -.
DR   HOGENOM; CLU_015127_2_0_1; -.
DR   InParanoid; Q9ERA0; -.
DR   OMA; GFNSAHS; -.
DR   OrthoDB; 1363858at2759; -.
DR   PhylomeDB; Q9ERA0; -.
DR   TreeFam; TF314132; -.
DR   BioGRID-ORCS; 21422; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Tfcp2; mouse.
DR   PRO; PR:Q9ERA0; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9ERA0; Protein.
DR   Bgee; ENSMUSG00000009733; Expressed in embryonic brain and 251 other cell types or tissues.
DR   ExpressionAtlas; Q9ERA0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; TAS:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; TAS:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   CDD; cd09589; SAM_TFCP2; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR007604; CP2.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR040167; TF_CP2-like.
DR   InterPro; IPR037599; TFCP2_SAM.
DR   PANTHER; PTHR11037:SF11; ALPHA-GLOBIN TRANSCRIPTION FACTOR CP2; 1.
DR   PANTHER; PTHR11037; TRANSCRIPTION FACTOR CP2; 1.
DR   Pfam; PF04516; CP2; 1.
DR   Pfam; PF18016; SAM_3; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS51968; GRH_CP2_DB; 1.
DR   Genevisible; Q9ERA0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..502
FT                   /note="Alpha-globin transcription factor CP2"
FT                   /id="PRO_0000228002"
FT   DOMAIN          63..300
FT                   /note="Grh/CP2 DB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT   REGION          133..386
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          241..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12800"
FT   VAR_SEQ         354..355
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017649"
FT   VAR_SEQ         474..502
FT                   /note="MVQNFQEEACFILDTMEAETSDSYHVILK -> VVLSCLILPGTELWSSGRT
FT                   AGTLNCLALPFL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017650"
SQ   SEQUENCE   502 AA;  57031 MW;  02D43CAA95CDF495 CRC64;
     MAWALKLPLA DEVIESGLVQ DFDASLSGIG QELGAGAYSM SDVLALPIFK QEESSLPPDN
     ENEILPFQYV LCAATSPAVK LHDETLTYLN QGQSYEIRML DNRKLGELPE LNGKLVKSIF
     RVVFHDRRLQ YTEHQQLEGW RWNRPGDRIL DIDIPMSVGV IDPRANPTQL NTVEFLWDPS
     KRTSVFIQVH CISTEFTMRK HGGEKGVPFR VQIDTFKENG NGEYTEHLHS ASCQIKVFKP
     KGADRKQKID REKMEKRTPH EKEKYQPSYE TTILTECSPW PEITYVNNSP SPGFNSSHSS
     FSLGEGNGSP NHQPEPPPPV TDNLLPTTTP QEAQQWLHRN RFSTFTRLFT NFSGADLLKL
     TRDDVIQICG PADGIRLFNA LKGRMVRPRL TIYVCQESLQ LREQQPQPQP QPQKQEDGDS
     NGTFFVYHAI YLEELTAVEL TEKIAQLFSI SPHQISQIYK QGPTGIHVVI SDEMVQNFQE
     EACFILDTME AETSDSYHVI LK
//