TFCP2_MOUSE
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 03-AUG-2022, entry version 143.
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 -!- INTERACTION:
CC Q9ERA0; Q3UNW5: Tfcp2l1; NbExp=3; IntAct=EBI-5717242, EBI-5691372;
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; 5.
DR IntAct; Q9ERA0; 2.
DR STRING; 10090.ENSMUSP00000009877; -.
DR PhosphoSitePlus; Q9ERA0; -.
DR EPD; Q9ERA0; -.
DR MaxQB; Q9ERA0; -.
DR PaxDb; Q9ERA0; -.
DR PeptideAtlas; Q9ERA0; -.
DR PRIDE; Q9ERA0; -.
DR ProteomicsDB; 262883; -. [Q9ERA0-1]
DR ProteomicsDB; 262884; -. [Q9ERA0-2]
DR ProteomicsDB; 262885; -. [Q9ERA0-3]
DR Antibodypedia; 26338; 213 antibodies from 31 providers.
DR DNASU; 21422; -.
DR Ensembl; ENSMUST00000009877; ENSMUSP00000009877; ENSMUSG00000009733. [Q9ERA0-3]
DR Ensembl; ENSMUST00000229696; ENSMUSP00000155683; ENSMUSG00000009733. [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 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; MILPFQY; -.
DR OrthoDB; 386296at2759; -.
DR PhylomeDB; Q9ERA0; -.
DR TreeFam; TF314132; -.
DR BioGRID-ORCS; 21422; 2 hits in 71 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 247 other tissues.
DR ExpressionAtlas; Q9ERA0; baseline and differential.
DR Genevisible; Q9ERA0; MM.
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:0008022; F:protein C-terminus binding; ISO:MGI.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:MGI.
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; -; 1.
DR InterPro; IPR007604; CP2.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041418; SAM_3.
DR InterPro; IPR037599; TFCP2_SAM.
DR Pfam; PF04516; CP2; 1.
DR Pfam; PF18016; SAM_3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51968; GRH_CP2_DB; 1.
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
