TFCP2_HUMAN
ID TFCP2_HUMAN Reviewed; 502 AA.
AC Q12800; A8K5E9; Q12801; Q9UD75; Q9UD77;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Alpha-globin transcription factor CP2;
DE AltName: Full=SAA3 enhancer factor;
DE AltName: Full=Transcription factor LSF;
GN Name=TFCP2; Synonyms=LSF, SEF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 129-140;
RP 165-176; 348-358 AND 390-397, FUNCTION, AND SUBCELLULAR LOCATION.
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 [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 61-502 (ISOFORM 3), DNA-BINDING, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP SPLICING.
RX PubMed=8114710; DOI=10.1128/mcb.14.3.1776-1785.1994;
RA Yoon J.-B., Li G., Roeder R.G.;
RT "Characterization of a family of related cellular transcription factors
RT which can modulate human immunodeficiency virus type 1 transcription in
RT vitro.";
RL Mol. Cell. Biol. 14:1776-1785(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 7-21;
RP 81-98; 149-164; 165-179; 348-359 AND 363-376, FUNCTION, ALTERNATIVE
RP SPLICING, AND MUTAGENESIS OF VAL-211; ILE-213; GLN-234 AND LYS-236.
RX PubMed=8035790; DOI=10.1128/mcb.14.8.5076-5087.1994;
RA Shirra M.K., Zhu Q., Huang H.-C., Pallas D., Hansen U.;
RT "One exon of the human LSF gene includes conserved regions involved in
RT novel DNA-binding and dimerization motifs.";
RL Mol. Cell. Biol. 14:5076-5087(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8157699; DOI=10.1016/s0021-9258(19)78176-9;
RA Swendeman S.L., Spielholz C., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA Sheffery M.;
RT "Characterization of the genomic structure, chromosomal location, promoter,
RT and development expression of the alpha-globin transcription factor CP2.";
RL J. Biol. Chem. 269:11663-11671(1994).
RN [8]
RP IDENTIFICATION IN THE SSP COMPLEX, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=7828600; DOI=10.1002/j.1460-2075.1995.tb06979.x;
RA Jane S.M., Nienhuis A.W., Cunningham J.M.;
RT "Hemoglobin switching in man and chicken is mediated by a heteromeric
RT complex between the ubiquitous transcription factor CP2 and a
RT developmentally specific protein.";
RL EMBO J. 14:97-105(1995).
RN [9]
RP ERRATUM OF PUBMED:7828600.
RA Jane S.M., Nienhuis A.W., Cunningham J.M.;
RL EMBO J. 15:854-855(1995).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10455131; DOI=10.1074/jbc.274.35.24649;
RA Bing Z., Reddy S.A., Ren Y., Qin J., Liao W.S.-L.;
RT "Purification and characterization of the serum amyloid A3 enhancer
RT factor.";
RL J. Biol. Chem. 274:24649-24656(1999).
RN [11]
RP INTERACTION WITH NFE4.
RX PubMed=11003662; DOI=10.1128/mcb.20.20.7662-7672.2000;
RA Zhou W., Clouston D.R., Wang X., Cerruti L., Cunningham J.M., Jane S.M.;
RT "Induction of human fetal globin gene expression by a novel erythroid
RT factor, NF-E4.";
RL Mol. Cell. Biol. 20:7662-7672(2000).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Binds a variety of cellular and viral promoters including
CC fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the
CC alpha-globin promoter in erythroid cells is via synergistic interaction
CC with UBP1 (By similarity). Functions as part of the SSP (stage selector
CC protein) complex. Facilitates the interaction of the gamma-globin genes
CC with 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. {ECO:0000250,
CC ECO:0000269|PubMed:10455131, ECO:0000269|PubMed:1732747,
CC ECO:0000269|PubMed:8035790, ECO:0000269|PubMed:8157699}.
CC -!- SUBUNIT: Binds to DNA as a dimer, isoform 3 does not bind to DNA or
CC affect the binding of isoform 1 to DNA. Interacts with UBP1 and PIAS1,
CC and is probably part of a complex containing TFCP2, UBP1 and PIAS1 (By
CC similarity). Component of the SSP (stage selector protein) complex,
CC which appears to be a heteromer of TFCP2 and 2 copies of NFE4.
CC {ECO:0000250, ECO:0000269|PubMed:11003662, ECO:0000269|PubMed:7828600}.
CC -!- INTERACTION:
CC Q12800; P09110: ACAA1; NbExp=3; IntAct=EBI-717422, EBI-3926709;
CC Q12800; P54922: ADPRH; NbExp=3; IntAct=EBI-717422, EBI-6657604;
CC Q12800; Q8TDY4: ASAP3; NbExp=3; IntAct=EBI-717422, EBI-2609717;
CC Q12800; P46379: BAG6; NbExp=3; IntAct=EBI-717422, EBI-347552;
CC Q12800; Q9NVV2: C19orf73; NbExp=3; IntAct=EBI-717422, EBI-2859285;
CC Q12800; P00915: CA1; NbExp=6; IntAct=EBI-717422, EBI-3912102;
CC Q12800; A0A0S2Z3E6: CAPN3; NbExp=3; IntAct=EBI-717422, EBI-16430532;
CC Q12800; P20807-2: CAPN3; NbExp=3; IntAct=EBI-717422, EBI-16433991;
CC Q12800; Q9HC52: CBX8; NbExp=6; IntAct=EBI-717422, EBI-712912;
CC Q12800; Q6P1J9: CDC73; NbExp=8; IntAct=EBI-717422, EBI-930143;
CC Q12800; Q9NZQ0: DNAJC27; NbExp=6; IntAct=EBI-717422, EBI-10317544;
CC Q12800; Q9UF47: DNAJC5B; NbExp=3; IntAct=EBI-717422, EBI-10320535;
CC Q12800; Q9BZG8: DPH1; NbExp=3; IntAct=EBI-717422, EBI-10303200;
CC Q12800; A0AVK6: E2F8; NbExp=3; IntAct=EBI-717422, EBI-7779316;
CC Q12800; Q96JC9: EAF1; NbExp=3; IntAct=EBI-717422, EBI-769261;
CC Q12800; Q8N5A0: EIF5B; NbExp=3; IntAct=EBI-717422, EBI-6137508;
CC Q12800; Q5JZY3-3: EPHA10; NbExp=3; IntAct=EBI-717422, EBI-10244652;
CC Q12800; Q92731-3: ESR2; NbExp=3; IntAct=EBI-717422, EBI-12259414;
CC Q12800; Q9NW38: FANCL; NbExp=3; IntAct=EBI-717422, EBI-2339898;
CC Q12800; O95363: FARS2; NbExp=3; IntAct=EBI-717422, EBI-2513774;
CC Q12800; Q96D16: FBXL18; NbExp=3; IntAct=EBI-717422, EBI-744419;
CC Q12800; O95872: GPANK1; NbExp=3; IntAct=EBI-717422, EBI-751540;
CC Q12800; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-717422, EBI-11956675;
CC Q12800; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-717422, EBI-9658404;
CC Q12800; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-717422, EBI-9679267;
CC Q12800; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-717422, EBI-399246;
CC Q12800; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-717422, EBI-10288852;
CC Q12800; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-717422, EBI-5453723;
CC Q12800; Q9NQ50: MRPL40; NbExp=3; IntAct=EBI-717422, EBI-1053902;
CC Q12800; Q96AH0: NABP1; NbExp=3; IntAct=EBI-717422, EBI-2889252;
CC Q12800; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-717422, EBI-2859639;
CC Q12800; Q8NDH3-4: NPEPL1; NbExp=3; IntAct=EBI-717422, EBI-10269715;
CC Q12800; O43189: PHF1; NbExp=4; IntAct=EBI-717422, EBI-530034;
CC Q12800; A0A0S2Z615: PHF21B; NbExp=3; IntAct=EBI-717422, EBI-16434035;
CC Q12800; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-717422, EBI-2568609;
CC Q12800; O00562: PITPNM1; NbExp=3; IntAct=EBI-717422, EBI-2861268;
CC Q12800; Q9NQ66: PLCB1; NbExp=3; IntAct=EBI-717422, EBI-3396023;
CC Q12800; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-717422, EBI-10320765;
CC Q12800; Q9BT43: POLR3GL; NbExp=3; IntAct=EBI-717422, EBI-2855862;
CC Q12800; Q13427: PPIG; NbExp=3; IntAct=EBI-717422, EBI-396072;
CC Q12800; Q9UD71: PPP1R1B; NbExp=3; IntAct=EBI-717422, EBI-722119;
CC Q12800; Q96LZ3: PPP3R2; NbExp=3; IntAct=EBI-717422, EBI-3906025;
CC Q12800; Q16401: PSMD5; NbExp=3; IntAct=EBI-717422, EBI-752143;
CC Q12800; P29558: RBMS1; NbExp=3; IntAct=EBI-717422, EBI-5462600;
CC Q12800; P28702-3: RXRB; NbExp=3; IntAct=EBI-717422, EBI-16429492;
CC Q12800; O00560: SDCBP; NbExp=3; IntAct=EBI-717422, EBI-727004;
CC Q12800; A0MZ66-7: SHTN1; NbExp=3; IntAct=EBI-717422, EBI-10171490;
CC Q12800; Q93045: STMN2; NbExp=3; IntAct=EBI-717422, EBI-714194;
CC Q12800; P63165: SUMO1; NbExp=3; IntAct=EBI-717422, EBI-80140;
CC Q12800; Q15560: TCEA2; NbExp=3; IntAct=EBI-717422, EBI-710310;
CC Q12800; Q9BXT4-2: TDRD1; NbExp=3; IntAct=EBI-717422, EBI-10301451;
CC Q12800; Q9UKI8: TLK1; NbExp=3; IntAct=EBI-717422, EBI-740492;
CC Q12800; Q53QD4: TRAPPC12; NbExp=3; IntAct=EBI-717422, EBI-10242701;
CC Q12800; O95859: TSPAN12; NbExp=3; IntAct=EBI-717422, EBI-2466403;
CC Q12800; P63279: UBE2I; NbExp=4; IntAct=EBI-717422, EBI-80168;
CC Q12800; Q9BW85: YJU2; NbExp=6; IntAct=EBI-717422, EBI-10300345;
CC Q12800; Q8TBK6: ZCCHC10; NbExp=4; IntAct=EBI-717422, EBI-597063;
CC Q12800; Q6PEW1: ZCCHC12; NbExp=6; IntAct=EBI-717422, EBI-748373;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1732747,
CC ECO:0000269|PubMed:7828600, ECO:0000269|PubMed:8114710}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=LBP-1c;
CC IsoId=Q12800-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12800-2; Sequence=VSP_017647, VSP_017648;
CC Name=3; Synonyms=LBP-1d;
CC IsoId=Q12800-3; Sequence=VSP_017647;
CC Name=4;
CC IsoId=Q12800-4; Sequence=VSP_017648;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in brain, ovary, kidney,
CC thymus, spleen, liver, adrenal, heart and lung (at protein level).
CC {ECO:0000269|PubMed:10455131, ECO:0000269|PubMed:7828600,
CC ECO:0000269|PubMed:8157699}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal erythroid tissue.
CC {ECO:0000269|PubMed:7828600, ECO:0000269|PubMed:8157699}.
CC -!- MISCELLANEOUS: In PubMed:8114710 authors noted that a 10-fold molar
CC excess of isoform 3 over isoform 1 inhibited DNA-binding.
CC -!- SIMILARITY: Belongs to the grh/CP2 family. CP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; M84810; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U03494; AAA21324.1; -; mRNA.
DR EMBL; U03495; AAA21325.1; -; mRNA.
DR EMBL; AK291264; BAF83953.1; -; mRNA.
DR EMBL; CH471111; EAW58178.1; -; Genomic_DNA.
DR EMBL; BC003634; AAH03634.1; -; mRNA.
DR CCDS; CCDS55827.1; -. [Q12800-2]
DR CCDS; CCDS8808.1; -. [Q12800-1]
DR PIR; A42030; A42030.
DR PIR; A53771; A53771.
DR PIR; C56205; C56205.
DR RefSeq; NP_001166923.1; NM_001173452.1. [Q12800-4]
DR RefSeq; NP_001166924.1; NM_001173453.1. [Q12800-2]
DR RefSeq; NP_005644.2; NM_005653.4. [Q12800-1]
DR AlphaFoldDB; Q12800; -.
DR SMR; Q12800; -.
DR BioGRID; 112882; 435.
DR IntAct; Q12800; 126.
DR MINT; Q12800; -.
DR STRING; 9606.ENSP00000257915; -.
DR GlyGen; Q12800; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12800; -.
DR PhosphoSitePlus; Q12800; -.
DR BioMuta; TFCP2; -.
DR DMDM; 90101767; -.
DR EPD; Q12800; -.
DR jPOST; Q12800; -.
DR MassIVE; Q12800; -.
DR MaxQB; Q12800; -.
DR PaxDb; Q12800; -.
DR PeptideAtlas; Q12800; -.
DR PRIDE; Q12800; -.
DR ProteomicsDB; 58951; -. [Q12800-1]
DR ProteomicsDB; 58952; -. [Q12800-2]
DR ProteomicsDB; 58953; -. [Q12800-3]
DR ProteomicsDB; 58954; -. [Q12800-4]
DR Antibodypedia; 26338; 213 antibodies from 31 providers.
DR DNASU; 7024; -.
DR Ensembl; ENST00000257915.10; ENSP00000257915.5; ENSG00000135457.11. [Q12800-1]
DR Ensembl; ENST00000548115.5; ENSP00000447991.1; ENSG00000135457.11. [Q12800-2]
DR GeneID; 7024; -.
DR KEGG; hsa:7024; -.
DR MANE-Select; ENST00000257915.10; ENSP00000257915.5; NM_005653.5; NP_005644.2.
DR UCSC; uc001rxw.4; human. [Q12800-1]
DR CTD; 7024; -.
DR DisGeNET; 7024; -.
DR GeneCards; TFCP2; -.
DR HGNC; HGNC:11748; TFCP2.
DR HPA; ENSG00000135457; Low tissue specificity.
DR MIM; 189889; gene.
DR neXtProt; NX_Q12800; -.
DR OpenTargets; ENSG00000135457; -.
DR PharmGKB; PA36463; -.
DR VEuPathDB; HostDB:ENSG00000135457; -.
DR eggNOG; KOG4091; Eukaryota.
DR GeneTree; ENSGT00940000157629; -.
DR InParanoid; Q12800; -.
DR OMA; MILPFQY; -.
DR PhylomeDB; Q12800; -.
DR TreeFam; TF314132; -.
DR PathwayCommons; Q12800; -.
DR SignaLink; Q12800; -.
DR SIGNOR; Q12800; -.
DR BioGRID-ORCS; 7024; 10 hits in 1102 CRISPR screens.
DR ChiTaRS; TFCP2; human.
DR GeneWiki; TFCP2; -.
DR GenomeRNAi; 7024; -.
DR Pharos; Q12800; Tbio.
DR PRO; PR:Q12800; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q12800; protein.
DR Bgee; ENSG00000135457; Expressed in mucosa of paranasal sinus and 200 other tissues.
DR ExpressionAtlas; Q12800; baseline and differential.
DR Genevisible; Q12800; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008134; F:transcription factor binding; IPI:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
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; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..502
FT /note="Alpha-globin transcription factor CP2"
FT /id="PRO_0000228001"
FT DOMAIN 61..300
FT /note="Grh/CP2 DB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT REGION 133..395
FT /note="DNA-binding"
FT REGION 238..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..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:0007744|PubMed:24275569"
FT VAR_SEQ 189..239
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8035790,
FT ECO:0000303|PubMed:8114710"
FT /id="VSP_017647"
FT VAR_SEQ 491
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1732747, ECO:0000303|PubMed:8035790"
FT /id="VSP_017648"
FT MUTAGEN 211
FT /note="V->E: Does not affect DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:8035790"
FT MUTAGEN 213
FT /note="I->R: Does not affect DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:8035790"
FT MUTAGEN 234
FT /note="Q->L: Significant reduction of DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:8035790"
FT MUTAGEN 236
FT /note="K->E: Significant reduction of DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:8035790"
FT CONFLICT 92
FT /note="G -> A (in Ref. 1; M84810/AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> M (in Ref. 1; M84810/AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> Q (in Ref. 3; AAA21324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 57256 MW; B93825C2687F89FF CRC64;
MAWALKLPLA DEVIESGLVQ DFDASLSGIG QELGAGAYSM SDVLALPIFK QEESSLPPDN
ENKILPFQYV LCAATSPAVK LHDETLTYLN QGQSYEIRML DNRKLGELPE INGKLVKSIF
RVVFHDRRLQ YTEHQQLEGW RWNRPGDRIL DIDIPMSVGI IDPRANPTQL NTVEFLWDPA
KRTSVFIQVH CISTEFTMRK HGGEKGVPFR VQIDTFKENE NGEYTEHLHS ASCQIKVFKP
KGADRKQKTD REKMEKRTPH EKEKYQPSYE TTILTECSPW PEITYVNNSP SPGFNSSHSS
FSLGEGNGSP NHQPEPPPPV TDNLLPTTTP QEAQQWLHRN RFSTFTRLFT NFSGADLLKL
TRDDVIQICG PADGIRLFNA LKGRMVRPRL TIYVCQESLQ LREQQQQQQQ QQQKHEDGDS
NGTFFVYHAI YLEELTAVEL TEKIAQLFSI SPCQISQIYK QGPTGIHVLI SDEMIQNFQE
EACFILDTMK AETNDSYHII LK
