PIT1_HUMAN
ID PIT1_HUMAN Reviewed; 291 AA.
AC P28069; O75757; Q15132; Q15133; Q9UD34; Q9UEL3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Pituitary-specific positive transcription factor 1;
DE Short=PIT-1;
DE AltName: Full=Growth hormone factor 1;
DE Short=GHF-1;
GN Name=POU1F1; Synonyms=GHF1, PIT1;
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 B).
RC TISSUE=Pituitary anterior lobe;
RX PubMed=1956794; DOI=10.1093/nar/19.22.6329;
RA Lew A.M., Elsholtz H.P.;
RT "Cloning of the human cDNA for transcription factor Pit-1.";
RL Nucleic Acids Res. 19:6329-6329(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM B).
RX PubMed=1370379; DOI=10.1016/0167-4781(92)90494-k;
RA Tatsumi K.I., Notomi T., Amino N., Miyai K.;
RT "Nucleotide sequence of the complementary DNA for human Pit-1/GHF-1.";
RL Biochim. Biophys. Acta 1129:231-234(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RA Tatsumi K., Notomi T., Irie Y., Endo Y., Onogi S., Amino N., Miyai K.;
RT "The structure and the chromosomal location of the human PIT1 gene.";
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71, AND ALTERNATIVE SPLICING
RP (ISOFORM A).
RC TISSUE=Placenta;
RX PubMed=7721104; DOI=10.1016/0378-1119(94)00757-j;
RA Delhase M., Vila V., Hooghe-Peters E.L., Castrillo J.-L.;
RT "A novel pituitary transcription factor is produced by alternative splicing
RT of the human GHF-1/PIT-1 gene.";
RL Gene 155:273-275(1995).
RN [5]
RP SEQUENCE REVISION.
RA Delhase M.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RX PubMed=1487156; DOI=10.1016/0378-1119(92)90234-g;
RA Ohta K., Nobukuni Y., Mitsubuchi H., Ohta T., Tohma T., Jinno Y., Endo F.,
RA Matsuda I.;
RT "Characterization of the gene encoding human pituitary-specific
RT transcription factor, Pit-1.";
RL Gene 122:387-388(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-273, VARIANT CPHD1 TRP-271, AND
RP INVOLVEMENT IN CPHD1.
RX PubMed=7852536; DOI=10.1210/jcem.80.2.7852536;
RA Cohen L.E., Wondisford F.E., Salvatoni A., Maghnie M., Brucker-Davis F.,
RA Weintraub B.D., Radovick S.;
RT "A 'hot spot' in the Pit-1 gene responsible for combined pituitary hormone
RT deficiency: clinical and molecular correlates.";
RL J. Clin. Endocrinol. Metab. 80:679-684(1995).
RN [8]
RP 9AATAD MOTIF.
RX PubMed=34342803; DOI=10.1007/s12015-021-10225-8;
RA Piskacek M., Otasevic T., Repko M., Knight A.;
RT "The 9aaTAD Activation Domains in the Yamanaka Transcription Factors Oct4,
RT Sox2, Myc, and Klf4.";
RL Stem. Cell. Rev. Rep. 17:1934-1936(2021).
RN [9]
RP VARIANTS CPHD1 LEU-24; GLN-143 AND TRP-271.
RX PubMed=1472057; DOI=10.1016/0006-291x(92)92281-2;
RA Ohta K., Nobukuni Y., Mitsubuchi H., Fujimoto S., Matsuo N., Inagaki H.,
RA Endo F., Matsuda I.;
RT "Mutations in the Pit-1 gene in children with combined pituitary hormone
RT deficiency.";
RL Biochem. Biophys. Res. Commun. 189:851-855(1992).
RN [10]
RP VARIANT CPHD1 TRP-271.
RX PubMed=1509262; DOI=10.1126/science.257.5073.1115;
RA Radovick S., Nations M., Du Y., Berg L.A., Weintraub B.D., Wondisford F.E.;
RT "A mutation in the POU-homeodomain of Pit-1 responsible for combined
RT pituitary hormone deficiency.";
RL Science 257:1115-1118(1992).
RN [11]
RP VARIANT CPHD1 PRO-158.
RX PubMed=1509263; DOI=10.1126/science.257.5073.1118;
RA Pfaeffle R.W., DiMattia G.E., Parks J.S., Brown M.R., Wit J.M., Jansen M.,
RA van der Nat H., van den Brande J.L., Rosenfeld M.G., Ingraham H.A.;
RT "Mutation of the POU-specific domain of Pit-1 and hypopituitarism without
RT pituitary hypoplasia.";
RL Science 257:1118-1121(1992).
RN [12]
RP VARIANTS ARG-4 AND TYR-227.
RC TISSUE=Pituitary;
RX PubMed=8346040; DOI=10.1093/nar/21.15.3584;
RA Pernasetti F.M., Wera S., Belayew A., Martial J.A.;
RT "Cloning of a human GHF-1/Pit-1 cDNA variant.";
RL Nucleic Acids Res. 21:3584-3584(1993).
RN [13]
RP VARIANT CPHD1 CYS-135.
RX PubMed=8768831; DOI=10.1210/jcem.81.8.8768831;
RA Pellegrini-Bouiller I., Belicar P., Barlier A., Gunz G., Charvet J.P.,
RA Jaquet P., Brue T., Vialettes B., Enjalbert A.;
RT "A new mutation of the gene encoding the transcription factor Pit-1 is
RT responsible for combined pituitary hormone deficiency.";
RL J. Clin. Endocrinol. Metab. 81:2790-2796(1996).
RN [14]
RP VARIANT CPHD1 GLY-174.
RX PubMed=9485179; DOI=10.1159/000023134;
RA Brown M.R., Parks J.S., Adess M.E., Rich B.H., Rosenthal I.M., Voss T.C.,
RA VanderHeyden T.C., Hurley D.L.;
RT "Central hypothyroidism reveals compound heterozygous mutations in the Pit-
RT 1 gene.";
RL Horm. Res. 49:98-102(1998).
RN [15]
RP VARIANT CPHD1 SER-239.
RX PubMed=9626142; DOI=10.1210/jcem.83.6.4901;
RA Pernasetti F.M., Milner R.D.G., Al-Ashwal A.A.Z., de Zegher F.,
RA Chavez V.M., Muller M., Martial J.A.;
RT "Pro239Ser: a novel recessive mutation of the Pit-1 gene in seven Middle
RT Eastern children with growth hormone, prolactin, and thyrotropin
RT deficiency.";
RL J. Clin. Endocrinol. Metab. 83:2079-2083(1998).
RN [16]
RP VARIANT CPHD1 ARG-193.
RX PubMed=11297581; DOI=10.1210/jcem.86.4.7371;
RA Hendriks-Stegeman B.I., Augustijn K.D., Bakker B., Holthuizen P.,
RA van der Vliet P.C., Jansen M.;
RT "Combined pituitary hormone deficiency caused by compound heterozygosity
RT for two novel mutations in the POU domain of the PIT1/POU1F1 gene.";
RL J. Clin. Endocrinol. Metab. 86:1545-1550(2001).
RN [17]
RP VARIANTS CPHD1 GLN-172; LYS-230 AND TRP-271, AND CHARACTERIZATION OF
RP VARIANTS CPHD1 GLN-172 AND LYS-230.
RX PubMed=15928241; DOI=10.1210/jc.2005-0570;
RA Turton J.P.G., Reynaud R., Mehta A., Torpiano J., Saveanu A., Woods K.S.,
RA Tiulpakov A., Zdravkovic V., Hamilton J., Attard-Montalto S.,
RA Parascandalo R., Vella C., Clayton P.E., Shalet S., Barton J., Brue T.,
RA Dattani M.T.;
RT "Novel mutations within the POU1F1 gene associated with variable combined
RT pituitary hormone deficiency.";
RL J. Clin. Endocrinol. Metab. 90:4762-4770(2005).
RN [18]
RP VARIANT CPHD1 ARG-179, AND CHARACTERIZATION OF VARIANT CPHD1 ARG-179.
RX PubMed=16968807; DOI=10.1210/jc.2005-2289;
RA Miyata I., Vallette-Kasic S., Saveanu A., Takeuchi M., Yoshikawa H.,
RA Tajima A., Tojo K., Reynaud R., Gueydan M., Enjalbert A., Tajima N.,
RA Eto Y., Brue T.;
RT "Identification and functional analysis of the novel S179R POU1F1 mutation
RT associated with combined pituitary hormone deficiency.";
RL J. Clin. Endocrinol. Metab. 91:4981-4987(2006).
RN [19]
RP VARIANT CPHD1 TRP-265, CHARACTERIZATION OF VARIANT CPHD1 TRP-265, AND
RP FUNCTION.
RX PubMed=22010633; DOI=10.1111/j.1365-2265.2011.04236.x;
RA Turton J.P., Strom M., Langham S., Dattani M.T., Le Tissier P.;
RT "Two novel mutations in the POU1F1 gene generate null alleles through
RT different mechanisms leading to c ombined pituitary hormone deficiency.";
RL Clin. Endocrinol. (Oxf.) 76:387-393(2012).
RN [20]
RP VARIANT CPHD1 LEU-76, CHARACTERIZATION OF VARIANT CPHD1 LEU-76, FUNCTION,
RP INTERACTION WITH ELK1; LHX3 AND PITX1, DNA-BINDING, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF LEU-74; THR-75; PRO-76; CYS-77 AND LEU-78.
RX PubMed=26612202; DOI=10.1093/hmg/ddv486;
RA Sobrier M.L., Tsai Y.C., Perez C., Leheup B., Bouceba T., Duquesnoy P.,
RA Copin B., Sizova D., Penzo A., Stanger B.Z., Cooke N.E., Liebhaber S.A.,
RA Amselem S.;
RT "Functional characterization of a human POU1F1 mutation associated with
RT isolated growth hormone deficiency: a novel etiology for IGHD.";
RL Hum. Mol. Genet. 25:472-483(2016).
CC -!- FUNCTION: Transcription factor involved in the specification of the
CC lactotrope, somatotrope, and thyrotrope phenotypes in the developing
CC anterior pituitary. Specifically binds to the consensus sequence 5'-
CC TAAAT-3'. Activates growth hormone and prolactin genes
CC (PubMed:22010633, PubMed:26612202). {ECO:0000269|PubMed:22010633,
CC ECO:0000269|PubMed:26612202}.
CC -!- SUBUNIT: Interacts with PITX1 (PubMed:26612202). Interacts with LHX3
CC (PubMed:26612202). Interacts with ELK1 (PubMed:26612202).
CC {ECO:0000269|PubMed:26612202}.
CC -!- INTERACTION:
CC P28069; Q03989: ARID5A; NbExp=3; IntAct=EBI-8673859, EBI-948603;
CC P28069; P15289: ARSA; NbExp=3; IntAct=EBI-8673859, EBI-2117357;
CC P28069; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-8673859, EBI-742054;
CC P28069; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8673859, EBI-10171774;
CC P28069; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-8673859, EBI-11992140;
CC P28069; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-8673859, EBI-12111050;
CC P28069; Q14847-2: LASP1; NbExp=5; IntAct=EBI-8673859, EBI-9088686;
CC P28069; Q969G2: LHX4; NbExp=3; IntAct=EBI-8673859, EBI-2865388;
CC P28069; P35548: MSX2; NbExp=3; IntAct=EBI-8673859, EBI-6447480;
CC P28069; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-8673859, EBI-948156;
CC P28069; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-8673859, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26612202}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Pit-1B, GHF-1;
CC IsoId=P28069-1; Sequence=Displayed;
CC Name=A; Synonyms=Pit-1A, GHF-2;
CC IsoId=P28069-2; Sequence=VSP_002314;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:34342803}.
CC -!- DISEASE: Pituitary hormone deficiency, combined, 1 (CPHD1)
CC [MIM:613038]: Combined pituitary hormone deficiency is defined as the
CC impaired production of growth hormone and one or more of the other five
CC anterior pituitary hormones. CPHD1 is characterized by pleiotropic
CC deficiencies of growth hormone, prolactin and thyroid-stimulating
CC hormone, while the production of adrenocorticotropic hormone,
CC luteinizing hormone, and follicle-stimulating hormone are preserved. In
CC infancy severe growth deficiency from birth as well as distinctive
CC facial features with prominent forehead, marked midfacial hypoplasia
CC with depressed nasal bridge, deep-set eyes, and a short nose with
CC anteverted nostrils and hypoplastic pituitary gland by MRI examination
CC can be seen. Some cases present with severe intellectual disability
CC along with short stature. {ECO:0000269|PubMed:11297581,
CC ECO:0000269|PubMed:1472057, ECO:0000269|PubMed:1509262,
CC ECO:0000269|PubMed:1509263, ECO:0000269|PubMed:15928241,
CC ECO:0000269|PubMed:16968807, ECO:0000269|PubMed:22010633,
CC ECO:0000269|PubMed:26612202, ECO:0000269|PubMed:7852536,
CC ECO:0000269|PubMed:8768831, ECO:0000269|PubMed:9485179,
CC ECO:0000269|PubMed:9626142}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform A]: Altered in its ability to trans-activate
CC compared to isoform B. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA54440.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L18781; AAA60093.1; -; mRNA.
DR EMBL; X62429; CAA44295.1; -; mRNA.
DR EMBL; D10216; BAA01068.1; -; mRNA.
DR EMBL; X72215; CAA51017.1; -; mRNA.
DR EMBL; D12892; BAA02291.1; -; Genomic_DNA.
DR EMBL; X77223; CAA54440.2; ALT_SEQ; Genomic_DNA.
DR EMBL; X77224; CAA54440.2; JOINED; Genomic_DNA.
DR EMBL; X77223; CAA54441.1; -; Genomic_DNA.
DR EMBL; X77224; CAA54441.1; JOINED; Genomic_DNA.
DR EMBL; D11333; BAA34536.1; -; Genomic_DNA.
DR CCDS; CCDS2919.1; -. [P28069-1]
DR CCDS; CCDS46873.1; -. [P28069-2]
DR PIR; S18718; S18718.
DR RefSeq; NP_000297.1; NM_000306.3. [P28069-1]
DR RefSeq; NP_001116229.1; NM_001122757.2. [P28069-2]
DR PDB; 5WC9; X-ray; 3.15 A; A/B/E/F=124-273.
DR PDBsum; 5WC9; -.
DR AlphaFoldDB; P28069; -.
DR SMR; P28069; -.
DR BioGRID; 111445; 31.
DR IntAct; P28069; 13.
DR MINT; P28069; -.
DR STRING; 9606.ENSP00000342931; -.
DR iPTMnet; P28069; -.
DR PhosphoSitePlus; P28069; -.
DR BioMuta; POU1F1; -.
DR DMDM; 123408; -.
DR jPOST; P28069; -.
DR MassIVE; P28069; -.
DR PeptideAtlas; P28069; -.
DR PRIDE; P28069; -.
DR ProteomicsDB; 54444; -. [P28069-1]
DR ProteomicsDB; 54445; -. [P28069-2]
DR Antibodypedia; 15685; 89 antibodies from 19 providers.
DR DNASU; 5449; -.
DR Ensembl; ENST00000344265.8; ENSP00000342931.3; ENSG00000064835.12. [P28069-2]
DR Ensembl; ENST00000350375.7; ENSP00000263781.2; ENSG00000064835.12. [P28069-1]
DR GeneID; 5449; -.
DR KEGG; hsa:5449; -.
DR MANE-Select; ENST00000350375.7; ENSP00000263781.2; NM_000306.4; NP_000297.1.
DR UCSC; uc003dqq.2; human. [P28069-1]
DR CTD; 5449; -.
DR DisGeNET; 5449; -.
DR GeneCards; POU1F1; -.
DR HGNC; HGNC:9210; POU1F1.
DR HPA; ENSG00000064835; Tissue enriched (pituitary).
DR MalaCards; POU1F1; -.
DR MIM; 173110; gene.
DR MIM; 613038; phenotype.
DR neXtProt; NX_P28069; -.
DR OpenTargets; ENSG00000064835; -.
DR Orphanet; 95494; Combined pituitary hormone deficiencies, genetic forms.
DR Orphanet; 226307; Hypothyroidism due to deficient transcription factors involved in pituitary development or function.
DR Orphanet; 231679; Isolated growth hormone deficiency type II.
DR PharmGKB; PA33534; -.
DR VEuPathDB; HostDB:ENSG00000064835; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000158913; -.
DR HOGENOM; CLU_882684_0_0_1; -.
DR InParanoid; P28069; -.
DR OMA; ATYGMMT; -.
DR OrthoDB; 797288at2759; -.
DR PhylomeDB; P28069; -.
DR TreeFam; TF316413; -.
DR PathwayCommons; P28069; -.
DR SignaLink; P28069; -.
DR SIGNOR; P28069; -.
DR BioGRID-ORCS; 5449; 14 hits in 1091 CRISPR screens.
DR GeneWiki; Pituitary-specific_positive_transcription_factor_1; -.
DR GenomeRNAi; 5449; -.
DR Pharos; P28069; Tbio.
DR PRO; PR:P28069; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P28069; protein.
DR Bgee; ENSG00000064835; Expressed in pituitary gland and 48 other tissues.
DR ExpressionAtlas; P28069; baseline and differential.
DR Genevisible; P28069; 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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0021984; P:adenohypophysis development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR015586; Pit_1.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR PANTHER; PTHR11636:SF84; PTHR11636:SF84; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Disease variant;
KW DNA-binding; Dwarfism; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..291
FT /note="Pituitary-specific positive transcription factor 1"
FT /id="PRO_0000100697"
FT DOMAIN 124..198
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 214..273
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT MOTIF 5..13
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:34342803"
FT VAR_SEQ 47
FT /note="T -> TVPSILSLIQTPKCLCTHFSVTTLGNT (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_002314"
FT VARIANT 4
FT /note="Q -> R (in dbSNP:rs1051612)"
FT /evidence="ECO:0000269|PubMed:8346040"
FT /id="VAR_003776"
FT VARIANT 19
FT /note="A -> V (in dbSNP:rs35182189)"
FT /id="VAR_049361"
FT VARIANT 24
FT /note="P -> L (in CPHD1; dbSNP:rs104893757)"
FT /evidence="ECO:0000269|PubMed:1472057"
FT /id="VAR_003777"
FT VARIANT 76
FT /note="P -> L (in CPHD1; reduces transactivation capacity
FT on the GH1 gene; increases the functional binding on the
FT GH1 promoter; increases the interaction with ELK1, LHX3 and
FT PITX1)"
FT /evidence="ECO:0000269|PubMed:26612202"
FT /id="VAR_075530"
FT VARIANT 135
FT /note="F -> C (in CPHD1; dbSNP:rs104893761)"
FT /evidence="ECO:0000269|PubMed:8768831"
FT /id="VAR_010574"
FT VARIANT 143
FT /note="R -> Q (in CPHD1; dbSNP:rs104893759)"
FT /evidence="ECO:0000269|PubMed:1472057"
FT /id="VAR_003778"
FT VARIANT 158
FT /note="A -> P (in CPHD1; dbSNP:rs104893756)"
FT /evidence="ECO:0000269|PubMed:1509263"
FT /id="VAR_003779"
FT VARIANT 172
FT /note="R -> Q (in CPHD1; associated with severe impairment
FT of transactivation; has a greatly reduced DNA-binding
FT affinity as the wild-type protein; dbSNP:rs104893765)"
FT /evidence="ECO:0000269|PubMed:15928241"
FT /id="VAR_063425"
FT VARIANT 174
FT /note="E -> G (in CPHD1; dbSNP:rs1207179169)"
FT /evidence="ECO:0000269|PubMed:9485179"
FT /id="VAR_010575"
FT VARIANT 179
FT /note="S -> R (in CPHD1; transactivation capacity of this
FT mutant is markedly decreased on the GH1; PRL, TSHB and
FT POU1F1 genes; abolishes the functional interaction of
FT POU1F1 on the PRL promoter with the coactivator CREBBP but
FT not with the transcription factor LHX3; displays normal
FT nuclear accumulation but a markedly decreased binding to a
FT DNA response element; dbSNP:rs104893766)"
FT /evidence="ECO:0000269|PubMed:16968807"
FT /id="VAR_063426"
FT VARIANT 193
FT /note="W -> R (in CPHD1; dbSNP:rs104893758)"
FT /evidence="ECO:0000269|PubMed:11297581"
FT /id="VAR_015260"
FT VARIANT 227
FT /note="D -> Y (in dbSNP:rs1131815)"
FT /evidence="ECO:0000269|PubMed:8346040"
FT /id="VAR_003780"
FT VARIANT 230
FT /note="E -> K (in CPHD1; associated with less severe
FT impairment of transactivation; has a similar DNA-binding
FT affinity as the wild-type protein; dbSNP:rs104893764)"
FT /evidence="ECO:0000269|PubMed:15928241"
FT /id="VAR_063427"
FT VARIANT 239
FT /note="P -> S (in CPHD1; loss of function;
FT dbSNP:rs104893762)"
FT /evidence="ECO:0000269|PubMed:9626142"
FT /id="VAR_010576"
FT VARIANT 265
FT /note="R -> W (in CPHD1; reduces transactivation capacity
FT on the PRL gene; increases instability of the protein;
FT dbSNP:rs780359925)"
FT /evidence="ECO:0000269|PubMed:22010633"
FT /id="VAR_075531"
FT VARIANT 271
FT /note="R -> W (in CPHD1; dbSNP:rs104893755)"
FT /evidence="ECO:0000269|PubMed:1472057,
FT ECO:0000269|PubMed:1509262, ECO:0000269|PubMed:15928241,
FT ECO:0000269|PubMed:7852536"
FT /id="VAR_003781"
FT MUTAGEN 74
FT /note="L->A: No effect on the interaction with ELK1, LHX3
FT and PITX1."
FT /evidence="ECO:0000269|PubMed:26612202"
FT MUTAGEN 75
FT /note="T->A: Increases the interaction with LHX3. No effect
FT on the interaction with ELK1."
FT /evidence="ECO:0000269|PubMed:26612202"
FT MUTAGEN 76
FT /note="P->A: Increases the interaction with LHX3 and PITX1.
FT No effect on the interaction with ELK1."
FT /evidence="ECO:0000269|PubMed:26612202"
FT MUTAGEN 77
FT /note="C->A: Increases the interaction with LHX3 and PITX1.
FT No effect on the interaction with ELK1."
FT /evidence="ECO:0000269|PubMed:26612202"
FT MUTAGEN 78
FT /note="L->A: Increases the interaction with LHX3 and PITX1.
FT No effect on the interaction with ELK1."
FT /evidence="ECO:0000269|PubMed:26612202"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:5WC9"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:5WC9"
SQ SEQUENCE 291 AA; 32912 MW; 0866777E3E425873 CRC64;
MSCQAFTSAD TFIPLNSDAS ATLPLIMHHS AAECLPVSNH ATNVMSTATG LHYSVPSCHY
GNQPSTYGVM AGSLTPCLYK FPDHTLSHGF PPIHQPLLAE DPTAADFKQE LRRKSKLVEE
PIDMDSPEIR ELEKFANEFK VRRIKLGYTQ TNVGEALAAV HGSEFSQTTI CRFENLQLSF
KNACKLKAIL SKWLEEAEQV GALYNEKVGA NERKRKRRTT ISIAAKDALE RHFGEQNKPS
SQEIMRMAEE LNLEKEVVRV WFCNRRQREK RVKTSLNQSL FSISKEHLEC R
