PROP1_HUMAN
ID PROP1_HUMAN Reviewed; 226 AA.
AC O75360;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Homeobox protein prophet of Pit-1;
DE Short=PROP-1;
DE AltName: Full=Pituitary-specific homeodomain factor;
GN Name=PROP1;
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 [GENOMIC DNA / MRNA], AND VARIANTS SER-20 AND CPHD
RP CYS-73.
RX PubMed=9824293; DOI=10.1016/s0014-5793(98)01234-4;
RA Duquesnoy P., Roy A., Dastot F., Ghali I., Teinturier C., Netchine I.,
RA Cacheux V., Hafez M., Salah N., Chaussain J.-L., Goossens M., Bougneres P.,
RA Amselem S.;
RT "Human Prop-1: cloning, mapping, genomic structure. Mutations in familial
RT combined pituitary hormone deficiency.";
RL FEBS Lett. 437:216-220(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-20; CPHD2 ILE-117 AND
RP CYS-120.
RX PubMed=9462743; DOI=10.1038/ng0298-147;
RA Wu W., Cogan J.D., Pfaeffle R.W., Dasen J.S., Frisch H., O'Connell S.M.,
RA Flynn S.E., Brown M.R., Mullis P.E., Parks J.S., Phillips J.A. III,
RA Rosenfeld M.G.;
RT "Mutations in PROP1 cause familial combined pituitary hormone deficiency.";
RL Nat. Genet. 18:147-149(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-20.
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 [5]
RP VARIANT CPHD2 CYS-120.
RX PubMed=9768691; DOI=10.1210/jcem.83.10.5172;
RA Fluck C., Deladoey J., Rutishauser K., Eble A., Marti U., Wu W.,
RA Mullis P.E.;
RT "Phenotypic variability in familial combined pituitary hormone deficiency
RT caused by a PROP1 gene mutation resulting in the substitution of Arg-->Cys
RT at codon 120 (R120C).";
RL J. Clin. Endocrinol. Metab. 83:3727-3734(1998).
RN [6]
RP VARIANT CPHD2 SER-88, AND CHARACTERIZATION OF VARIANT CPHD2 SER-88.
RX PubMed=10946881; DOI=10.1210/jcem.85.8.6744;
RA Osorio M.G., Kopp P., Marui S., Latronico A.C., Mendonca B.B.,
RA Arnhold I.J.;
RT "Combined pituitary hormone deficiency caused by a novel mutation of a
RT highly conserved residue (F88S) in the homeodomain of PROP-1.";
RL J. Clin. Endocrinol. Metab. 85:2779-2785(2000).
RN [7]
RP VARIANTS CPHD2 CYS-73 AND HIS-73.
RX PubMed=11549703; DOI=10.1210/jcem.86.9.7811;
RA Vallette-Kasic S., Barlier A., Teinturier C., Diaz A., Manavela M.,
RA Berthezene F., Bouchard P., Chaussain J.-L., Brauner R.,
RA Pellegrini-Bouiller I., Jaquet P., Enjalbert A., Brue T.;
RT "PROP1 gene screening in patients with multiple pituitary hormone
RT deficiency reveals two sites of hypermutability and a high incidence of
RT corticotroph deficiency.";
RL J. Clin. Endocrinol. Metab. 86:4529-4535(2001).
RN [8]
RP VARIANT CPHD2 GLN-99.
RX PubMed=12519826; DOI=10.1210/jc.2001-011872;
RA Vieira T.C., Dias da Silva M.R., Cerutti J.M., Brunner E., Borges M.,
RA Arnaldi L.T., Kopp P., Abucham J.;
RT "Familial combined pituitary hormone deficiency due to a novel mutation
RT R99Q in the hot spot region of Prophet of Pit-1 presenting as
RT constitutional growth delay.";
RL J. Clin. Endocrinol. Metab. 88:38-44(2003).
RN [9]
RP VARIANT CPHD2 CYS-73, AND CHARACTERIZATION OF VARIANT CPHD2 CYS-73.
RX PubMed=15531542; DOI=10.1210/jc.2003-032124;
RA Reynaud R., Chadli-Chaieb M., Vallette-Kasic S., Barlier A., Sarles J.,
RA Pellegrini-Bouiller I., Enjalbert A., Chaieb L., Brue T.;
RT "A familial form of congenital hypopituitarism due to a PROP1 mutation in a
RT large kindred: phenotypic and in vitro functional studies.";
RL J. Clin. Endocrinol. Metab. 89:5779-5786(2004).
RN [10]
RP VARIANT CPHD2 TRP-125.
RX PubMed=19128366; DOI=10.1111/j.1365-2265.2008.03326.x;
RA Kelberman D., Turton J.P., Woods K.S., Mehta A., Al-Khawari M.,
RA Greening J., Swift P.G., Otonkoski T., Rhodes S.J., Dattani M.T.;
RT "Molecular analysis of novel PROP1 mutations associated with combined
RT pituitary hormone deficiency (CPHD).";
RL Clin. Endocrinol. (Oxf.) 70:96-103(2009).
CC -!- FUNCTION: Possibly involved in the ontogenesis of pituitary
CC gonadotropes, as well as somatotropes, lactotropes and caudomedial
CC thyrotropes.
CC -!- INTERACTION:
CC O75360; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-9027467, EBI-12318443;
CC O75360; P15289: ARSA; NbExp=3; IntAct=EBI-9027467, EBI-2117357;
CC O75360; Q8N1L9: BATF2; NbExp=3; IntAct=EBI-9027467, EBI-742695;
CC O75360; Q9H5F2: C11orf1; NbExp=5; IntAct=EBI-9027467, EBI-718615;
CC O75360; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-9027467, EBI-11976299;
CC O75360; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-9027467, EBI-946029;
CC O75360; Q6UXA7: C6orf15; NbExp=3; IntAct=EBI-9027467, EBI-11990870;
CC O75360; Q6YFQ2: COX6B2; NbExp=3; IntAct=EBI-9027467, EBI-10291911;
CC O75360; P05813: CRYBA1; NbExp=3; IntAct=EBI-9027467, EBI-7043337;
CC O75360; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9027467, EBI-3867333;
CC O75360; Q15038: DAZAP2; NbExp=3; IntAct=EBI-9027467, EBI-724310;
CC O75360; O95967: EFEMP2; NbExp=3; IntAct=EBI-9027467, EBI-743414;
CC O75360; Q6J272: FAM166A; NbExp=3; IntAct=EBI-9027467, EBI-12811067;
CC O75360; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-9027467, EBI-11978259;
CC O75360; Q9BSH5: HDHD3; NbExp=3; IntAct=EBI-9027467, EBI-745201;
CC O75360; P52597: HNRNPF; NbExp=3; IntAct=EBI-9027467, EBI-352986;
CC O75360; P49639: HOXA1; NbExp=3; IntAct=EBI-9027467, EBI-740785;
CC O75360; Q5TA45: INTS11; NbExp=3; IntAct=EBI-9027467, EBI-748258;
CC O75360; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-9027467, EBI-12811111;
CC O75360; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-9027467, EBI-12805508;
CC O75360; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-9027467, EBI-10241353;
CC O75360; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-9027467, EBI-10261141;
CC O75360; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-9027467, EBI-716006;
CC O75360; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-9027467, EBI-10174029;
CC O75360; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-9027467, EBI-8487781;
CC O75360; Q6NSM0: NR1D2; NbExp=3; IntAct=EBI-9027467, EBI-10250949;
CC O75360; Q7RTU3: OLIG3; NbExp=3; IntAct=EBI-9027467, EBI-10225049;
CC O75360; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-9027467, EBI-12813389;
CC O75360; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-9027467, EBI-10181968;
CC O75360; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-9027467, EBI-373552;
CC O75360; P78424: POU6F2; NbExp=3; IntAct=EBI-9027467, EBI-12029004;
CC O75360; A5LHX3: PSMB11; NbExp=5; IntAct=EBI-9027467, EBI-19951687;
CC O75360; P28070: PSMB4; NbExp=3; IntAct=EBI-9027467, EBI-603350;
CC O75360; P78317: RNF4; NbExp=3; IntAct=EBI-9027467, EBI-2340927;
CC O75360; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-9027467, EBI-10269322;
CC O75360; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-9027467, EBI-12275818;
CC O75360; P63165: SUMO1; NbExp=3; IntAct=EBI-9027467, EBI-80140;
CC O75360; Q9Y458: TBX22; NbExp=3; IntAct=EBI-9027467, EBI-6427217;
CC O75360; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-9027467, EBI-750487;
CC O75360; Q96M29: TEKT5; NbExp=3; IntAct=EBI-9027467, EBI-10239812;
CC O75360; Q96A09: TENT5B; NbExp=3; IntAct=EBI-9027467, EBI-752030;
CC O75360; Q9GZM7: TINAGL1; NbExp=3; IntAct=EBI-9027467, EBI-715869;
CC O75360; Q08117: TLE5; NbExp=4; IntAct=EBI-9027467, EBI-717810;
CC O75360; Q08117-2: TLE5; NbExp=3; IntAct=EBI-9027467, EBI-11741437;
CC O75360; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-9027467, EBI-12038591;
CC O75360; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-9027467, EBI-5235829;
CC O75360; Q7KZS0: UBE2I; NbExp=5; IntAct=EBI-9027467, EBI-10180829;
CC O75360; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-9027467, EBI-12068150;
CC O75360; Q96F45: ZNF503; NbExp=3; IntAct=EBI-9027467, EBI-8832437;
CC O75360; P0DTC6: 6; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25475897;
CC O75360; P0DTC4: E; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25475850;
CC O75360; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25492388;
CC O75360; PRO_0000449630 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25475888;
CC O75360; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25475920;
CC O75360; PRO_0000449632 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25475891;
CC O75360; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-9027467, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in embryonic pituitary.
CC -!- DISEASE: Pituitary hormone deficiency, combined, 2 (CPHD2)
CC [MIM:262600]: 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. CPHD2 is characterized by pleiotropic
CC deficiencies of growth hormone, thyroid-stimulating hormone, follicle-
CC stimulating hormone, luteinizing hormone, prolactin and
CC adrenocorticotropic hormone. {ECO:0000269|PubMed:10946881,
CC ECO:0000269|PubMed:11549703, ECO:0000269|PubMed:12519826,
CC ECO:0000269|PubMed:15531542, ECO:0000269|PubMed:19128366,
CC ECO:0000269|PubMed:9462743, ECO:0000269|PubMed:9768691}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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DR EMBL; AF076214; AAC77453.1; -; Genomic_DNA.
DR EMBL; AF076215; AAC77454.1; -; mRNA.
DR EMBL; AF041141; AAC27900.1; -; Genomic_DNA.
DR EMBL; AF041139; AAC27900.1; JOINED; Genomic_DNA.
DR EMBL; AF041140; AAC27900.1; JOINED; Genomic_DNA.
DR EMBL; AC136940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069076; AAH69076.1; -; mRNA.
DR CCDS; CCDS4430.1; -.
DR RefSeq; NP_006252.3; NM_006261.4.
DR AlphaFoldDB; O75360; -.
DR SMR; O75360; -.
DR BioGRID; 111610; 61.
DR IntAct; O75360; 60.
DR STRING; 9606.ENSP00000311290; -.
DR iPTMnet; O75360; -.
DR PhosphoSitePlus; O75360; -.
DR BioMuta; PROP1; -.
DR EPD; O75360; -.
DR MassIVE; O75360; -.
DR PaxDb; O75360; -.
DR PeptideAtlas; O75360; -.
DR PRIDE; O75360; -.
DR ProteomicsDB; 49924; -.
DR Antibodypedia; 29400; 113 antibodies from 24 providers.
DR DNASU; 5626; -.
DR Ensembl; ENST00000308304.2; ENSP00000311290.2; ENSG00000175325.2.
DR GeneID; 5626; -.
DR KEGG; hsa:5626; -.
DR MANE-Select; ENST00000308304.2; ENSP00000311290.2; NM_006261.5; NP_006252.4.
DR UCSC; uc003mif.1; human.
DR CTD; 5626; -.
DR DisGeNET; 5626; -.
DR GeneCards; PROP1; -.
DR GeneReviews; PROP1; -.
DR HGNC; HGNC:9455; PROP1.
DR HPA; ENSG00000175325; Tissue enhanced (pituitary).
DR MalaCards; PROP1; -.
DR MIM; 262600; phenotype.
DR MIM; 601538; gene.
DR neXtProt; NX_O75360; -.
DR OpenTargets; ENSG00000175325; -.
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; 90695; Non-acquired panhypopituitarism.
DR PharmGKB; PA33808; -.
DR VEuPathDB; HostDB:ENSG00000175325; -.
DR eggNOG; KOG0490; Eukaryota.
DR GeneTree; ENSGT00940000162292; -.
DR HOGENOM; CLU_044912_1_0_1; -.
DR InParanoid; O75360; -.
DR OMA; EPPKSWN; -.
DR OrthoDB; 1351285at2759; -.
DR PhylomeDB; O75360; -.
DR TreeFam; TF315976; -.
DR PathwayCommons; O75360; -.
DR SignaLink; O75360; -.
DR BioGRID-ORCS; 5626; 6 hits in 1090 CRISPR screens.
DR GeneWiki; PROP1; -.
DR GenomeRNAi; 5626; -.
DR Pharos; O75360; Tbio.
DR PRO; PR:O75360; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O75360; protein.
DR Bgee; ENSG00000175325; Expressed in pituitary gland and 1 other tissue.
DR Genevisible; O75360; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
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:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR GO; GO:0048850; P:hypophysis morphogenesis; IEA:Ensembl.
DR GO; GO:0021979; P:hypothalamus cell differentiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060126; P:somatotropin secreting cell differentiation; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR000047; HTH_motif.
DR InterPro; IPR042412; PROP1.
DR PANTHER; PTHR47409; PTHR47409; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00031; HTHREPRESSR.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Disease variant; DNA-binding; Dwarfism; Homeobox; Nucleus;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Homeobox protein prophet of Pit-1"
FT /id="PRO_0000049271"
FT DNA_BIND 69..128
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 20
FT /note="N -> S (in dbSNP:rs7445271)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9462743, ECO:0000269|PubMed:9824293"
FT /id="VAR_054972"
FT VARIANT 73
FT /note="R -> C (in CPHD2; familial; no detectable DNA
FT binding observed with the mutant protein in electromobility
FT shift assays; whereas in vitro translated PROP1 and the
FT mutant proteins were similar in their expression and
FT electrophoretic properties; dbSNP:rs121917843)"
FT /evidence="ECO:0000269|PubMed:11549703,
FT ECO:0000269|PubMed:15531542, ECO:0000269|PubMed:9824293"
FT /id="VAR_003768"
FT VARIANT 73
FT /note="R -> H (in CPHD2; familial; dbSNP:rs121917842)"
FT /evidence="ECO:0000269|PubMed:11549703"
FT /id="VAR_012746"
FT VARIANT 88
FT /note="F -> S (in CPHD2; impairs binding of the mutated
FT protein to DNA target sequences; dbSNP:rs121917841)"
FT /evidence="ECO:0000269|PubMed:10946881"
FT /id="VAR_063235"
FT VARIANT 99
FT /note="R -> Q (in CPHD2; displays a significant decrease in
FT DNA binding on a paired-box response element (PRDQ9) and
FT trans-activation of a luciferase reporter gene;
FT dbSNP:rs137853100)"
FT /evidence="ECO:0000269|PubMed:12519826"
FT /id="VAR_063236"
FT VARIANT 117
FT /note="F -> I (in CPHD2; familial; dbSNP:rs121917840)"
FT /evidence="ECO:0000269|PubMed:9462743"
FT /id="VAR_003769"
FT VARIANT 120
FT /note="R -> C (in CPHD2; familial; dbSNP:rs121917839)"
FT /evidence="ECO:0000269|PubMed:9462743,
FT ECO:0000269|PubMed:9768691"
FT /id="VAR_003770"
FT VARIANT 125
FT /note="R -> W (in CPHD2; dbSNP:rs146918863)"
FT /evidence="ECO:0000269|PubMed:19128366"
FT /id="VAR_054973"
FT VARIANT 142
FT /note="A -> T (in dbSNP:rs1800197)"
FT /id="VAR_014531"
SQ SEQUENCE 226 AA; 24984 MW; CE6D59B3D295A86D CRC64;
MEAERRRQAE KPKKGRVGSN LLPERHPATG TPTTTVDSSA PPCRRLPGAG GGRSRFSPQG
GQRGRPHSRR RHRTTFSPVQ LEQLESAFGR NQYPDIWARE SLARDTGLSE ARIQVWFQNR
RAKQRKQERS LLQPLAHLSP AAFSSFLPES TACPYSYAAP PPPVTCFPHP YSHALPSQPS
TGGAFALSHQ SEDWYPTLHP APAGHLPCPP PPPMLPLSLE PSKSWN
