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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
 
 
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