PIBF1_HUMAN
ID PIBF1_HUMAN Reviewed; 757 AA.
AC Q8WXW3; O95664; Q6U9V2; Q6UG50; Q86V07; Q96SF4;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Progesterone-induced-blocking factor 1;
DE Short=PIBF;
DE AltName: Full=Centrosomal protein of 90 kDa;
DE Short=CEP90 {ECO:0000303|PubMed:21224392};
GN Name=PIBF1; Synonyms=C13orf24, PIBF;
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 1), AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=11935316; DOI=10.1007/s00439-001-0646-6;
RA Rozenblum E., Vahteristo P., Sandberg T., Bergthorsson J.T., Syrjakoski K.,
RA Weaver D., Haraldsson K., Johannsdottir H.K., Vehmanen P., Nigam S.,
RA Golberger N., Robbins C., Pak E., Dutra A., Gillander E., Stephan D.A.,
RA Bailey-Wilson J., Juo S.-H.H., Kainu T., Arason A., Barkardottir R.B.,
RA Nevanlinna H., Borg A., Kallioniemi O.-P.;
RT "A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer
RT development: identification and characterization of candidate genes.";
RL Hum. Genet. 110:111-121(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RX PubMed=15305375; DOI=10.1002/ijc.20326;
RA Lachmann M., Gelbmann D., Kalman E., Polgar B., Buschle M., Von Gabain A.,
RA Szekeres-Bartho J., Nagy E.;
RT "PIBF (progesterone induced blocking factor) is overexpressed in highly
RT proliferating cells and associated with the centrosome.";
RL Int. J. Cancer 112:51-60(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Szekeres-Bartho J.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION (ISOFORM 4).
RX PubMed=14634107; DOI=10.4049/jimmunol.171.11.5956;
RA Polgar B., Kispal G., Lachmann M., Paar C., Nagy E., Csere P., Miko E.,
RA Szereday L., Varga P., Szekeres-Bartho J., Paar G.;
RT "Molecular cloning and immunologic characterization of a novel cDNA coding
RT for progesterone-induced blocking factor.";
RL J. Immunol. 171:5956-5963(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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, INDUCTION BY PROGESTERONE, AND SUBCELLULAR LOCATION (ISOFORM 4).
RX PubMed=3863495; DOI=10.1111/j.1600-0897.1985.tb00334.x;
RA Szekeres-Bartho J., Kilar F., Falkay G., Csernus V., Toeroek A.,
RA Pacsa A.S.;
RT "The mechanism of the inhibitory effect of progesterone on lymphocyte
RT cytotoxicity: I. Progesterone-treated lymphocytes release a substance
RT inhibiting cytotoxicity and prostaglandin synthesis.";
RL Am. J. Reprod. Immunol. 9:15-18(1985).
RN [8]
RP REVIEW.
RX PubMed=11407300; DOI=10.1016/s1567-5769(01)00035-2;
RA Szekeres-Bartho J., Barakonyi A., Par G., Polgar B., Palkovics T.,
RA Szereday L.;
RT "Progesterone as an immunomodulatory molecule.";
RL Int. Immunopharmacol. 1:1037-1048(2001).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12516630; DOI=10.1034/j.1600-0897.2002.01133.x;
RA Laskarin G., Tokmadzic V.S., Strbo N., Bogovic T., Szekeres-Bartho J.,
RA Randic L., Podack E.R., Rukavina D.;
RT "Progesterone induced blocking factor (PIBF) mediates progesterone induced
RT suppression of decidual lymphocyte cytotoxicity.";
RL Am. J. Reprod. Immunol. 48:201-209(2002).
RN [10]
RP FUNCTION.
RX PubMed=12733588; DOI=10.1034/j.1600-0897.2003.01149.x;
RA Par G., Geli J., Kozma N., Varga P., Szekeres-Bartho J.;
RT "Progesterone regulates IL12 expression in pregnancy lymphocytes by
RT inhibiting phospholipase A2.";
RL Am. J. Reprod. Immunol. 49:1-5(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP INVOLVEMENT IN PREMATURE PREGNANCY.
RX PubMed=15269099; DOI=10.1095/biolreprod.104.030437;
RA Polgar B., Nagy E., Miko E., Varga P., Szekeres-Bartho J.;
RT "Urinary progesterone-induced blocking factor concentration is related to
RT pregnancy outcome.";
RL Biol. Reprod. 71:1699-1705(2004).
RN [13]
RP FUNCTION.
RX PubMed=16393965; DOI=10.4049/jimmunol.176.2.819;
RA Kozma N., Halasz M., Polgar B., Poehlmann T.G., Markert U.R., Palkovics T.,
RA Keszei M., Par G., Kiss K., Szeberenyi J., Grama L., Szekeres-Bartho J.;
RT "Progesterone-induced blocking factor activates STAT6 via binding to a
RT novel IL-4 receptor.";
RL J. Immunol. 176:819-826(2006).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=18817979; DOI=10.1016/j.jri.2008.06.002;
RA Anderle C., Hammer A., Polgar B., Hartmann M., Wintersteiger R.,
RA Blaschitz A., Dohr G., Desoye G., Szekeres-Bartho J., Sedlmayr P.;
RT "Human trophoblast cells express the immunomodulator progesterone-induced
RT blocking factor.";
RL J. Reprod. Immunol. 79:26-36(2008).
RN [15]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND INTERACTION
RP WITH PCM1 AND BBS4.
RX PubMed=21224392; DOI=10.1242/jcs.078329;
RA Kim K., Rhee K.;
RT "The pericentriolar satellite protein CEP90 is crucial for integrity of the
RT mitotic spindle pole.";
RL J. Cell Sci. 124:338-347(2011).
RN [16]
RP FUNCTION (ISOFORM 1), AND INTERACTION WITH PCM1.
RX PubMed=23110211; DOI=10.1371/journal.pone.0048196;
RA Kim K., Lee K., Rhee K.;
RT "CEP90 is required for the assembly and centrosomal accumulation of
RT centriolar satellites, which is essential for primary cilia formation.";
RL PLoS ONE 7:E48196-E48196(2012).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP IL4R.
RX PubMed=25218441; DOI=10.1016/j.jsbmb.2014.09.007;
RA Gonzalez-Arenas A., Valadez-Cosmes P., Jimenez-Arellano C.,
RA Lopez-Sanchez M., Camacho-Arroyo I.;
RT "Progesterone-induced blocking factor is hormonally regulated in human
RT astrocytoma cells, and increases their growth through the IL-4R/JAK1/STAT6
RT pathway.";
RL J. Steroid Biochem. Mol. Biol. 144:463-470(2014).
RN [18]
RP INTERACTION WITH PCM1 AND CEP63, SUBCELLULAR LOCATION, VARIANT GLN-89,
RP CHARACTERIZATION OF VARIANT GLN-89, POSSIBLE INVOLVEMENT IN MICROCEPHALY,
RP AND FUNCTION (ISOFORM 1).
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [19]
RP FUNCTION, INVOLVEMENT IN JBTS33, VARIANTS JBTS33 GLN-405 AND ALA-637, AND
RP CHARACTERIZATION OF VARIANTS JBTS33 GLN-405 AND ALA-637.
RX PubMed=26167768; DOI=10.1038/ncb3201;
RG UK10K Consortium;
RG University of Washington Center for Mendelian Genomics;
RA Wheway G., Schmidts M., Mans D.A., Szymanska K., Nguyen T.M., Racher H.,
RA Phelps I.G., Toedt G., Kennedy J., Wunderlich K.A., Sorusch N.,
RA Abdelhamed Z.A., Natarajan S., Herridge W., van Reeuwijk J., Horn N.,
RA Boldt K., Parry D.A., Letteboer S.J., Roosing S., Adams M., Bell S.M.,
RA Bond J., Higgins J., Morrison E.E., Tomlinson D.C., Slaats G.G.,
RA van Dam T.J., Huang L., Kessler K., Giessl A., Logan C.V., Boyle E.A.,
RA Shendure J., Anazi S., Aldahmesh M., Al Hazzaa S., Hegele R.A., Ober C.,
RA Frosk P., Mhanni A.A., Chodirker B.N., Chudley A.E., Lamont R.,
RA Bernier F.P., Beaulieu C.L., Gordon P., Pon R.T., Donahue C.,
RA Barkovich A.J., Wolf L., Toomes C., Thiel C.T., Boycott K.M., McKibbin M.,
RA Inglehearn C.F., Stewart F., Omran H., Huynen M.A., Sergouniotis P.I.,
RA Alkuraya F.S., Parboosingh J.S., Innes A.M., Willoughby C.E., Giles R.H.,
RA Webster A.R., Ueffing M., Blacque O., Gleeson J.G., Wolfrum U.,
RA Beales P.L., Gibson T., Doherty D., Mitchison H.M., Roepman R.,
RA Johnson C.A.;
RT "An siRNA-based functional genomics screen for the identification of
RT regulators of ciliogenesis and ciliopathy genes.";
RL Nat. Cell Biol. 17:1074-1087(2015).
CC -!- FUNCTION: Plays a role in ciliogenesis. {ECO:0000269|PubMed:26167768}.
CC -!- FUNCTION: [Isoform 1]: Pericentriolar protein required to maintain
CC mitotic spindle pole integrity (PubMed:21224392). Required for the
CC centrosomal accumulation of PCM1 and the recruitment of centriolar
CC satellite proteins such as BBS4. Via association with PCM1 may be
CC involved in primary cilia formation (PubMed:23110211). Required for
CC CEP63 centrosomal localization and its interaction with WDR62. Together
CC with CEP63 promotes centriole duplication. Promotes the centrosomal
CC localization of CDK2 (PubMed:26297806). {ECO:0000269|PubMed:21224392,
CC ECO:0000269|PubMed:23110211, ECO:0000269|PubMed:26297806}.
CC -!- FUNCTION: [Isoform 4]: The secreted form is a mediator of progesterone
CC that by acting on the phospholipase A2 enzyme interferes with
CC arachidonic acid metabolism, induces a Th2 biased immune response, and
CC by controlling decidual naturakl killer cells (NK) activity exerts an
CC anti-abortive effect (PubMed:14634107, PubMed:3863495,
CC PubMed:12516630). Increases the production of Th2-type cytokines by
CC signaling via the JAK/STAT pathway. Activates STAT6 and inhibits STAT4
CC phosphorylation. Signaling via a not identified receptor seems to
CC implicate IL4R and a GPI-anchored protein (PubMed:16393965,
CC PubMed:25218441). {ECO:0000269|PubMed:12516630,
CC ECO:0000269|PubMed:14634107, ECO:0000269|PubMed:16393965,
CC ECO:0000269|PubMed:25218441, ECO:0000269|PubMed:3863495,
CC ECO:0000305|PubMed:11407300}.
CC -!- SUBUNIT: Isoform 1 interacts with PCM1, BBS4 and CEP63
CC (PubMed:21224392, PubMed:23110211, PubMed:26297806). Interacts with
CC IL4R (PubMed:25218441). {ECO:0000269|PubMed:21224392,
CC ECO:0000269|PubMed:23110211, ECO:0000269|PubMed:25218441,
CC ECO:0000269|PubMed:26297806}.
CC -!- INTERACTION:
CC Q8WXW3; Q96MT8: CEP63; NbExp=6; IntAct=EBI-2558770, EBI-741977;
CC Q8WXW3; P42858: HTT; NbExp=3; IntAct=EBI-2558770, EBI-466029;
CC Q8WXW3; Q15154: PCM1; NbExp=7; IntAct=EBI-2558770, EBI-741421;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm
CC {ECO:0000269|PubMed:25218441}. Secreted {ECO:0000269|PubMed:25218441}.
CC Note=In progesterone-treated astrocytoma cells a 57 kDa protein and
CC isoform 1 (90 kDa) have been described, both being located in the
CC intracellular medium and secreted. Respective predominant forms are
CC isoform 1 in the intracellular and the 57 kDa protein in the
CC extracellular medium (PubMed:25218441). {ECO:0000269|PubMed:25218441}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:14634107, ECO:0000269|PubMed:25218441}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:15305375}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:21224392, ECO:0000269|PubMed:26297806}. Secreted
CC {ECO:0000269|PubMed:25218441}. Note=Localizes to centriolar satellites
CC throughout the cell cycle. {ECO:0000269|PubMed:26297806}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted
CC {ECO:0000269|PubMed:14634107, ECO:0000269|PubMed:3863495}.
CC Note=Secreted by progesterone-treated lymphocytes (PubMed:14634107).
CC {ECO:0000269|PubMed:14634107}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=90 kDa form;
CC IsoId=Q8WXW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXW3-2; Sequence=VSP_015302;
CC Name=3;
CC IsoId=Q8WXW3-3; Sequence=VSP_015303, VSP_015304;
CC Name=4; Synonyms=34/35 kDa form;
CC IsoId=Q8WXW3-4; Sequence=VSP_057956;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in testis. Moderate
CC expression is detected in spleen, thymus, prostate, ovary, small
CC intestine, and colon (PubMed:11935316). Expressed in the first
CC trimester pregnancy decidua (PubMed:12516630). Localized to
CC extravillous cytotrophoblast (at protein level). Also found in
CC syncytiotrophoblast and part of the villous cytotrophoblast. Isoform 1
CC is expressed in first trimester and term villous trophoblast;
CC trophoblast cells can additionally express other isoforms
CC (PubMed:18817979). Overexpressed in solid tumors from stomach and
CC uterus and in cells from ovary, cervical, breast, lymphoma and leukemia
CC cancer (PubMed:25218441). {ECO:0000269|PubMed:11935316,
CC ECO:0000269|PubMed:12516630, ECO:0000269|PubMed:18817979,
CC ECO:0000305|PubMed:25218441}.
CC -!- INDUCTION: By progesterone. {ECO:0000269|PubMed:3863495}.
CC -!- DISEASE: Note=May be associated with microcephaly.
CC {ECO:0000305|PubMed:26297806}.
CC -!- DISEASE: Joubert syndrome 33 (JBTS33) [MIM:617767]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. JBTS33 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:26167768}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: During normal pregnancy, the production is continuously
CC increasing until the 37th gestational week and is followed by a sharp
CC decrease after the 41st week of gestation. In pathological pregnancies,
CC urinary levels fail to increase. Candidate for the diagnosis of
CC threatened premature pregnancy termination.
CC {ECO:0000305|PubMed:15269099}.
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DR EMBL; AF330046; AAL37481.1; -; mRNA.
DR EMBL; AY375528; AAQ67659.1; -; mRNA.
DR EMBL; AY370776; AAQ73282.1; -; mRNA.
DR EMBL; Y09631; CAA70844.1; -; Genomic_DNA.
DR EMBL; AL354720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051911; AAH51911.1; -; mRNA.
DR CCDS; CCDS31991.1; -. [Q8WXW3-1]
DR RefSeq; NP_006337.2; NM_006346.2. [Q8WXW3-1]
DR AlphaFoldDB; Q8WXW3; -.
DR SMR; Q8WXW3; -.
DR BioGRID; 115727; 211.
DR DIP; DIP-56669N; -.
DR IntAct; Q8WXW3; 64.
DR MINT; Q8WXW3; -.
DR STRING; 9606.ENSP00000317144; -.
DR iPTMnet; Q8WXW3; -.
DR PhosphoSitePlus; Q8WXW3; -.
DR BioMuta; PIBF1; -.
DR DMDM; 73920251; -.
DR EPD; Q8WXW3; -.
DR jPOST; Q8WXW3; -.
DR MassIVE; Q8WXW3; -.
DR MaxQB; Q8WXW3; -.
DR PaxDb; Q8WXW3; -.
DR PeptideAtlas; Q8WXW3; -.
DR PRIDE; Q8WXW3; -.
DR ProteomicsDB; 75105; -. [Q8WXW3-1]
DR ProteomicsDB; 75106; -. [Q8WXW3-2]
DR ProteomicsDB; 75107; -. [Q8WXW3-3]
DR Antibodypedia; 24415; 317 antibodies from 32 providers.
DR DNASU; 10464; -.
DR Ensembl; ENST00000326291.11; ENSP00000317144.6; ENSG00000083535.16. [Q8WXW3-1]
DR Ensembl; ENST00000615625.1; ENSP00000483286.1; ENSG00000083535.16. [Q8WXW3-2]
DR GeneID; 10464; -.
DR KEGG; hsa:10464; -.
DR MANE-Select; ENST00000326291.11; ENSP00000317144.6; NM_006346.4; NP_006337.2.
DR UCSC; uc001vjc.4; human. [Q8WXW3-1]
DR CTD; 10464; -.
DR DisGeNET; 10464; -.
DR GeneCards; PIBF1; -.
DR HGNC; HGNC:23352; PIBF1.
DR HPA; ENSG00000083535; Low tissue specificity.
DR MalaCards; PIBF1; -.
DR MIM; 607532; gene.
DR MIM; 617767; phenotype.
DR neXtProt; NX_Q8WXW3; -.
DR OpenTargets; ENSG00000083535; -.
DR Orphanet; 475; Joubert syndrome.
DR PharmGKB; PA162399421; -.
DR VEuPathDB; HostDB:ENSG00000083535; -.
DR eggNOG; ENOG502QRKC; Eukaryota.
DR GeneTree; ENSGT00390000015293; -.
DR HOGENOM; CLU_1277225_0_0_1; -.
DR InParanoid; Q8WXW3; -.
DR OMA; MMKQVLI; -.
DR OrthoDB; 421171at2759; -.
DR PhylomeDB; Q8WXW3; -.
DR TreeFam; TF329068; -.
DR PathwayCommons; Q8WXW3; -.
DR SignaLink; Q8WXW3; -.
DR BioGRID-ORCS; 10464; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; PIBF1; human.
DR GeneWiki; C13orf24; -.
DR GenomeRNAi; 10464; -.
DR Pharos; Q8WXW3; Tbio.
DR PRO; PR:Q8WXW3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8WXW3; protein.
DR Bgee; ENSG00000083535; Expressed in calcaneal tendon and 184 other tissues.
DR ExpressionAtlas; Q8WXW3; baseline and differential.
DR Genevisible; Q8WXW3; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005136; F:interleukin-4 receptor binding; IDA:UniProtKB.
DR GO; GO:0042976; P:activation of Janus kinase activity; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:0032815; P:negative regulation of natural killer cell activation; IDA:UniProtKB.
DR GO; GO:0031393; P:negative regulation of prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
DR InterPro; IPR026205; PIBF1.
DR PANTHER; PTHR18950; PTHR18950; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ciliopathy; Cytoplasm; Cytoskeleton; Disease variant;
KW Immunity; Joubert syndrome; Nucleus; Reference proteome; Secreted.
FT CHAIN 1..757
FT /note="Progesterone-induced-blocking factor 1"
FT /id="PRO_0000058426"
FT REGION 1..419
FT /note="Mediates modulation of Th2 dominant cytokine
FT production"
FT /evidence="ECO:0000269|PubMed:14634107"
FT REGION 1..184
FT /note="Sufficient for NK inhibitory function"
FT /evidence="ECO:0000269|PubMed:14634107"
FT REGION 271..363
FT /note="Required for interaction with PCM1"
FT /evidence="ECO:0000269|PubMed:23110211"
FT REGION 712..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..541
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15305375"
FT /id="VSP_015302"
FT VAR_SEQ 101..103
FT /note="LLT -> QTF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15305375"
FT /id="VSP_015303"
FT VAR_SEQ 104..757
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15305375"
FT /id="VSP_015304"
FT VAR_SEQ 225..683
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305|PubMed:15305375"
FT /id="VSP_057956"
FT VARIANT 89
FT /note="E -> Q (probable disease-associated variant found in
FT patients with microcephaly and intellectual disability;
FT disrupts interaction with CEP63; no effect on interaction
FT with PCM1; dbSNP:rs865883692)"
FT /evidence="ECO:0000269|PubMed:26297806"
FT /id="VAR_073952"
FT VARIANT 167
FT /note="I -> V (in dbSNP:rs1372000)"
FT /id="VAR_051279"
FT VARIANT 405
FT /note="R -> Q (in JBTS33; loss of function in ciliogenesis;
FT dbSNP:rs17089782)"
FT /evidence="ECO:0000269|PubMed:26167768"
FT /id="VAR_051280"
FT VARIANT 630
FT /note="I -> V (in dbSNP:rs11544631)"
FT /id="VAR_051281"
FT VARIANT 637
FT /note="D -> A (in JBTS33; loss of function in ciliogenesis;
FT dbSNP:rs987735817)"
FT /evidence="ECO:0000269|PubMed:26167768"
FT /id="VAR_080441"
FT CONFLICT 155
FT /note="N -> S (in Ref. 3; CAA70844)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> C (in Ref. 3; CAA70844)"
FT /evidence="ECO:0000305"
FT CONFLICT 597..614
FT /note="DLEHRKDQVTQLSQELDR -> RSGTSKGPSNTAFTRSLTE (in Ref.
FT 3; AAQ67659)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="Q -> P (in Ref. 1; AAL37481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 89805 MW; B469FB3BCC7E80FD CRC64;
MSRKISKESK KVNISSSLES EDISLETTVP TDDISSSEER EGKVRITRQL IERKELLHNI
QLLKIELSQK TMMIDNLKVD YLTKIEELEE KLNDALHQKQ LLTLRLDNQL AFQQKDASKY
QELMKQEMET ILLRQKQLEE TNLQLREKAG DVRRNLRDFE LTEEQYIKLK AFPEDQLSIP
EYVSVRFYEL VNPLRKEICE LQVKKNILAE ELSTNKNQLK QLTETYEEDR KNYSEVQIRC
QRLALELADT KQLIQQGDYR QENYDKVKSE RDALEQEVIE LRRKHEILEA SHMIQTKERS
ELSKEVVTLE QTVTLLQKDK EYLNRQNMEL SVRCAHEEDR LERLQAQLEE SKKAREEMYE
KYVASRDHYK TEYENKLHDE LEQIRLKTNQ EIDQLRNASR EMYERENRNL REARDNAVAE
KERAVMAEKD ALEKHDQLLD RYRELQLSTE SKVTEFLHQS KLKSFESERV QLLQEETARN
LTQCQLECEK YQKKLEVLTK EFYSLQASSE KRITELQAQN SEHQARLDIY EKLEKELDEI
IMQTAEIENE DEAERVLFSY GYGANVPTTA KRRLKQSVHL ARRVLQLEKQ NSLILKDLEH
RKDQVTQLSQ ELDRANSLLN QTQQPYRYLI ESVRQRDSKI DSLTESIAQL EKDVSNLNKE
KSALLQTKNQ MALDLEQLLN HREELAAMKQ ILVKMHSKHS ENSLLLTKTE PKHVTENQKS
KTLNVPKEHE DNIFTPKPTL FTKKEAPEWS KKQKMKT
