PITX1_HUMAN
ID PITX1_HUMAN Reviewed; 314 AA.
AC P78337; A8K3M0; D3DQB0; O14677; O60425; Q9BTI5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Pituitary homeobox 1;
DE AltName: Full=Hindlimb-expressed homeobox protein backfoot;
DE AltName: Full=Homeobox protein PITX1;
DE AltName: Full=Paired-like homeodomain transcription factor 1;
GN Name=PITX1; Synonyms=BFT, PTX1;
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].
RX PubMed=9070926; DOI=10.1006/geno.1996.4558;
RA Shang J., Li X., Ring H.Z., Clayton D.A., Francke U.;
RT "Backfoot, a novel homeobox gene, maps to human chromosome 5 (BFT) and
RT mouse chromosome 13 (Bft).";
RL Genomics 40:108-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9337397; DOI=10.1007/s003359900589;
RA Crawford M.J., Lanctot C., Tremblay J.J., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Beatty B., Drouin J.;
RT "Human and murine PTX1/Ptx1 gene maps to the region for Treacher Collins
RT syndrome.";
RL Mamm. Genome 8:841-845(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-299.
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-299.
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-299.
RC TISSUE=Pancreas, and Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP INVOLVEMENT IN LBNBG.
RX PubMed=23022097; DOI=10.1016/j.ajhg.2012.08.014;
RA Spielmann M., Brancati F., Krawitz P.M., Robinson P.N., Ibrahim D.M.,
RA Franke M., Hecht J., Lohan S., Dathe K., Nardone A.M., Ferrari P.,
RA Landi A., Wittler L., Timmermann B., Chan D., Mennen U., Klopocki E.,
RA Mundlos S.;
RT "Homeotic arm-to-leg transformation associated with genomic rearrangements
RT at the PITX1 locus.";
RL Am. J. Hum. Genet. 91:629-635(2012).
RN [9]
RP INVOLVEMENT IN CCF.
RX PubMed=22258522; DOI=10.1038/ejhg.2011.264;
RA Klopocki E., Kahler C., Foulds N., Shah H., Joseph B., Vogel H.,
RA Luttgen S., Bald R., Besoke R., Held K., Mundlos S., Kurth I.;
RT "Deletions in PITX1 cause a spectrum of lower-limb malformations including
RT mirror-image polydactyly.";
RL Eur. J. Hum. Genet. 20:705-708(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP INTERACTION WITH POU1F1.
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).
RN [12]
RP VARIANT CCF LYS-130, AND CHARACTERIZATION OF VARIANT CCF LYS-130.
RX PubMed=18950742; DOI=10.1016/j.ajhg.2008.10.004;
RA Gurnett C.A., Alaee F., Kruse L.M., Desruisseau D.M., Hecht J.T.,
RA Wise C.A., Bowcock A.M., Dobbs M.B.;
RT "Asymmetric lower-limb malformations in individuals with homeobox PITX1
RT gene mutation.";
RL Am. J. Hum. Genet. 83:616-622(2008).
CC -!- FUNCTION: Sequence-specific transcription factor that binds gene
CC promoters and activates their transcription. May play a role in the
CC development of anterior structures, and in particular, the brain and
CC facies and in specifying the identity or structure of hindlimb.
CC {ECO:0000250|UniProtKB:P56673}.
CC -!- SUBUNIT: Interacts with POU1F1 (PubMed:26612202).
CC {ECO:0000269|PubMed:26612202}.
CC -!- INTERACTION:
CC P78337; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-748265, EBI-12318443;
CC P78337; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-748265, EBI-357530;
CC P78337; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-748265, EBI-12102070;
CC P78337; Q92870-2: APBB2; NbExp=3; IntAct=EBI-748265, EBI-21535880;
CC P78337; Q03989: ARID5A; NbExp=3; IntAct=EBI-748265, EBI-948603;
CC P78337; Q86V38: ATN1; NbExp=3; IntAct=EBI-748265, EBI-11954292;
CC P78337; Q9NP55: BPIFA1; NbExp=5; IntAct=EBI-748265, EBI-953896;
CC P78337; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-748265, EBI-12809220;
CC P78337; Q9H5F2: C11orf1; NbExp=5; IntAct=EBI-748265, EBI-718615;
CC P78337; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-748265, EBI-11976299;
CC P78337; Q5W0N0-2: C9orf57; NbExp=3; IntAct=EBI-748265, EBI-18101667;
CC P78337; P40199: CEACAM6; NbExp=3; IntAct=EBI-748265, EBI-4314501;
CC P78337; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-748265, EBI-3867333;
CC P78337; O75935-2: DCTN3; NbExp=3; IntAct=EBI-748265, EBI-12091947;
CC P78337; Q92997: DVL3; NbExp=4; IntAct=EBI-748265, EBI-739789;
CC P78337; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-748265, EBI-948630;
CC P78337; O95967: EFEMP2; NbExp=3; IntAct=EBI-748265, EBI-743414;
CC P78337; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-748265, EBI-11978259;
CC P78337; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-748265, EBI-12193763;
CC P78337; P15976-2: GATA1; NbExp=3; IntAct=EBI-748265, EBI-9090198;
CC P78337; Q08379: GOLGA2; NbExp=3; IntAct=EBI-748265, EBI-618309;
CC P78337; P49639: HOXA1; NbExp=5; IntAct=EBI-748265, EBI-740785;
CC P78337; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-748265, EBI-12056251;
CC P78337; Q6UWQ7-2: IGFL2; NbExp=3; IntAct=EBI-748265, EBI-18115692;
CC P78337; O94829: IPO13; NbExp=4; IntAct=EBI-748265, EBI-747310;
CC P78337; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-748265, EBI-724915;
CC P78337; O76011: KRT34; NbExp=3; IntAct=EBI-748265, EBI-1047093;
CC P78337; P78385: KRT83; NbExp=3; IntAct=EBI-748265, EBI-10221390;
CC P78337; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-748265, EBI-11953846;
CC P78337; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-748265, EBI-1048945;
CC P78337; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-748265, EBI-10241353;
CC P78337; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-748265, EBI-3957672;
CC P78337; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-748265, EBI-3957694;
CC P78337; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-748265, EBI-12111050;
CC P78337; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-748265, EBI-11962084;
CC P78337; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-748265, EBI-18394498;
CC P78337; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-748265, EBI-10261141;
CC P78337; Q14847-2: LASP1; NbExp=5; IntAct=EBI-748265, EBI-9088686;
CC P78337; Q9Y5V3: MAGED1; NbExp=4; IntAct=EBI-748265, EBI-716006;
CC P78337; Q99750: MDFI; NbExp=3; IntAct=EBI-748265, EBI-724076;
CC P78337; Q8N6F8: METTL27; NbExp=5; IntAct=EBI-748265, EBI-8487781;
CC P78337; P35548: MSX2; NbExp=3; IntAct=EBI-748265, EBI-6447480;
CC P78337; A7E2Y1-2: MYH7B; NbExp=3; IntAct=EBI-748265, EBI-12813813;
CC P78337; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-748265, EBI-5662487;
CC P78337; P0CG21: NHLRC4; NbExp=5; IntAct=EBI-748265, EBI-12868744;
CC P78337; Q8IV28: NID2; NbExp=3; IntAct=EBI-748265, EBI-10261509;
CC P78337; Q99471: PFDN5; NbExp=3; IntAct=EBI-748265, EBI-357275;
CC P78337; O15496: PLA2G10; NbExp=3; IntAct=EBI-748265, EBI-726466;
CC P78337; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-748265, EBI-373552;
CC P78337; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-748265, EBI-750734;
CC P78337; P86480: PRR20D; NbExp=3; IntAct=EBI-748265, EBI-12754095;
CC P78337; A5LHX3: PSMB11; NbExp=3; IntAct=EBI-748265, EBI-19951687;
CC P78337; Q13882: PTK6; NbExp=3; IntAct=EBI-748265, EBI-1383632;
CC P78337; Q93062: RBPMS; NbExp=6; IntAct=EBI-748265, EBI-740322;
CC P78337; Q93062-3: RBPMS; NbExp=4; IntAct=EBI-748265, EBI-740343;
CC P78337; Q01974: ROR2; NbExp=3; IntAct=EBI-748265, EBI-6422642;
CC P78337; Q9UGK8: SERGEF; NbExp=3; IntAct=EBI-748265, EBI-465368;
CC P78337; P05121: SERPINE1; NbExp=3; IntAct=EBI-748265, EBI-953978;
CC P78337; A0A0B4J2F2: SIK1B; NbExp=3; IntAct=EBI-748265, EBI-22345187;
CC P78337; Q16348: SLC15A2; NbExp=3; IntAct=EBI-748265, EBI-12806032;
CC P78337; Q99932-2: SPAG8; NbExp=4; IntAct=EBI-748265, EBI-11959123;
CC P78337; Q8IWL8: STH; NbExp=3; IntAct=EBI-748265, EBI-12843506;
CC P78337; O60806: TBX19; NbExp=3; IntAct=EBI-748265, EBI-12096770;
CC P78337; Q9Y458: TBX22; NbExp=3; IntAct=EBI-748265, EBI-6427217;
CC P78337; Q96M29: TEKT5; NbExp=5; IntAct=EBI-748265, EBI-10239812;
CC P78337; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-748265, EBI-11952651;
CC P78337; Q08117-2: TLE5; NbExp=8; IntAct=EBI-748265, EBI-11741437;
CC P78337; Q12888: TP53BP1; NbExp=3; IntAct=EBI-748265, EBI-396540;
CC P78337; Q13077: TRAF1; NbExp=3; IntAct=EBI-748265, EBI-359224;
CC P78337; P36406: TRIM23; NbExp=4; IntAct=EBI-748265, EBI-740098;
CC P78337; Q86WV8: TSC1; NbExp=3; IntAct=EBI-748265, EBI-12806590;
CC P78337; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-748265, EBI-12068150;
CC P78337; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-748265, EBI-11957216;
CC P78337; A0A0C4DGF1: ZBTB32; NbExp=6; IntAct=EBI-748265, EBI-10188476;
CC P78337; G4XUV3; NbExp=3; IntAct=EBI-748265, EBI-10177989;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DISEASE: Clubfoot, congenital, with or without deficiency of long bones
CC and/or mirror-image polydactyly (CCF) [MIM:119800]: A congenital limb
CC deformity defined as fixation of the foot in cavus, adductus, varus,
CC and equinus (i.e., inclined inwards, axially rotated outwards, and
CC pointing downwards) with concomitant soft tissue abnormalities.
CC Clubfoot may occur in isolation or as part of a syndrome. Some patients
CC present tibial hemimelia, bilateral patellar hypoplasia, and preaxial
CC mirror-image polydactyly. {ECO:0000269|PubMed:18950742,
CC ECO:0000269|PubMed:22258522}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Liebenberg syndrome (LBNBG) [MIM:186550]: An upper limb-
CC malformation syndrome characterized by the combination of dysplastic
CC elbow joints and the fusion of wrist bones with consequent radial
CC deviation. {ECO:0000269|PubMed:23022097}. Note=The gene represented in
CC this entry is involved in disease pathogenesis. A chromosomal
CC aberration involving the PITX1 locus results in LBNBG. Translocation
CC t(5;18)(q31.1;q12.3). Additionally, two chromosome 5 deletions located
CC 5'of PITX1 have been found in LBNBG patients. These structural
CC variations cause altered expression of PITX1 in the forelimb via the
CC activation of ectopic enhancers (PubMed:23022097).
CC {ECO:0000269|PubMed:23022097}.
CC -!- SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.
CC {ECO:0000305}.
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DR EMBL; U70370; AAC51126.1; -; mRNA.
DR EMBL; AF009650; AAB65251.1; -; Genomic_DNA.
DR EMBL; AF009648; AAB65251.1; JOINED; Genomic_DNA.
DR EMBL; AF009649; AAB65251.1; JOINED; Genomic_DNA.
DR EMBL; AK290635; BAF83324.1; -; mRNA.
DR EMBL; AC004764; AAC17733.1; -; Genomic_DNA.
DR EMBL; AC008406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62226.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62227.1; -; Genomic_DNA.
DR EMBL; BC009412; AAH09412.1; -; mRNA.
DR EMBL; BC003685; AAH03685.1; -; mRNA.
DR CCDS; CCDS4182.1; -.
DR RefSeq; NP_002644.4; NM_002653.4.
DR AlphaFoldDB; P78337; -.
DR SMR; P78337; -.
DR BioGRID; 111324; 115.
DR IntAct; P78337; 90.
DR STRING; 9606.ENSP00000265340; -.
DR GlyGen; P78337; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78337; -.
DR PhosphoSitePlus; P78337; -.
DR BioMuta; PITX1; -.
DR DMDM; 108935922; -.
DR EPD; P78337; -.
DR jPOST; P78337; -.
DR MassIVE; P78337; -.
DR PaxDb; P78337; -.
DR PeptideAtlas; P78337; -.
DR PRIDE; P78337; -.
DR ProteomicsDB; 57573; -.
DR ABCD; P78337; 1 sequenced antibody.
DR Antibodypedia; 14722; 236 antibodies from 33 providers.
DR DNASU; 5307; -.
DR Ensembl; ENST00000265340.12; ENSP00000265340.6; ENSG00000069011.16.
DR Ensembl; ENST00000506438.5; ENSP00000427542.1; ENSG00000069011.16.
DR GeneID; 5307; -.
DR KEGG; hsa:5307; -.
DR MANE-Select; ENST00000265340.12; ENSP00000265340.6; NM_002653.5; NP_002644.4.
DR CTD; 5307; -.
DR DisGeNET; 5307; -.
DR GeneCards; PITX1; -.
DR HGNC; HGNC:9004; PITX1.
DR HPA; ENSG00000069011; Tissue enhanced (esophagus, pituitary gland, vagina).
DR MalaCards; PITX1; -.
DR MIM; 119800; phenotype.
DR MIM; 186550; phenotype.
DR MIM; 602149; gene.
DR neXtProt; NX_P78337; -.
DR OpenTargets; ENSG00000069011; -.
DR Orphanet; 1275; Brachydactyly-elbow wrist dysplasia syndrome.
DR Orphanet; 293144; Familial clubfoot due to 5q31 microdeletion.
DR Orphanet; 293150; Familial clubfoot due to PITX1 point mutation.
DR Orphanet; 498494; Mirror-image polydactyly.
DR PharmGKB; PA33338; -.
DR VEuPathDB; HostDB:ENSG00000069011; -.
DR eggNOG; KOG0486; Eukaryota.
DR GeneTree; ENSGT00940000154518; -.
DR HOGENOM; CLU_030301_0_0_1; -.
DR InParanoid; P78337; -.
DR OMA; QASHDMA; -.
DR OrthoDB; 1432356at2759; -.
DR PhylomeDB; P78337; -.
DR TreeFam; TF351940; -.
DR PathwayCommons; P78337; -.
DR SignaLink; P78337; -.
DR SIGNOR; P78337; -.
DR BioGRID-ORCS; 5307; 13 hits in 1092 CRISPR screens.
DR ChiTaRS; PITX1; human.
DR GeneWiki; PITX1; -.
DR GenomeRNAi; 5307; -.
DR Pharos; P78337; Tbio.
DR PRO; PR:P78337; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P78337; protein.
DR Bgee; ENSG00000069011; Expressed in lower esophagus mucosa and 120 other tissues.
DR ExpressionAtlas; P78337; baseline and differential.
DR Genevisible; P78337; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0014707; P:branchiomeric skeletal muscle development; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0048625; P:myoblast fate commitment; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR016233; Homeobox_Pitx/unc30.
DR InterPro; IPR003654; OAR_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF03826; OAR; 1.
DR PIRSF; PIRSF000563; Homeobox_protein_Pitx/Unc30; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS50803; OAR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Developmental protein; Disease variant;
KW DNA-binding; Homeobox; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..314
FT /note="Pituitary homeobox 1"
FT /id="PRO_0000049218"
FT DNA_BIND 89..148
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..279
FT /note="Interaction with PIT-1"
FT /evidence="ECO:0000250"
FT MOTIF 280..293
FT /note="OAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00138"
FT MOTIF 286..290
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 15..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 130
FT /note="E -> K (in CCF; reduces the ability to transactivate
FT a luciferase reporter gene; suppresses wild-type activity
FT in a dose-dependent manner; dbSNP:rs121909109)"
FT /evidence="ECO:0000269|PubMed:18950742"
FT /id="VAR_058113"
FT VARIANT 299
FT /note="G -> A (in dbSNP:rs479632)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15372022, ECO:0000269|PubMed:15489334"
FT /id="VAR_049586"
FT CONFLICT 17
FT /note="L -> F (in Ref. 1; AAC51126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34128 MW; F0DFE45E14508A43 CRC64;
MDAFKGGMSL ERLPEGLRPP PPPPHDMGPA FHLARPADPR EPLENSASES SDTELPEKER
GGEPKGPEDS GAGGTGCGGA DDPAKKKKQR RQRTHFTSQQ LQELEATFQR NRYPDMSMRE
EIAVWTNLTE PRVRVWFKNR RAKWRKRERN QQLDLCKGGY VPQFSGLVQP YEDVYAAGYS
YNNWAAKSLA PAPLSTKSFT FFNSMSPLSS QSMFSAPSSI SSMTMPSSMG PGAVPGMPNS
GLNNINNLTG SSLNSAMSPG ACPYGTPASP YSVYRDTCNS SLASLRLKSK QHSSFGYGGL
QGPASGLNAC QYNS
