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 24-JAN-2024, entry version 164. 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=7; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 217. DR DIP; DIP-56669N; -. DR IntAct; Q8WXW3; 68. 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; 9606-ENSP00000317144; -. DR PeptideAtlas; Q8WXW3; -. DR ProteomicsDB; 75105; -. [Q8WXW3-1] DR ProteomicsDB; 75106; -. [Q8WXW3-2] DR ProteomicsDB; 75107; -. [Q8WXW3-3] DR Pumba; Q8WXW3; -. DR Antibodypedia; 24415; 365 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 AGR; HGNC:23352; -. 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; KCERDTF; -. DR OrthoDB; 5395306at2759; -. DR PhylomeDB; Q8WXW3; -. DR TreeFam; TF329068; -. DR PathwayCommons; Q8WXW3; -. DR SignaLink; Q8WXW3; -. DR BioGRID-ORCS; 10464; 18 hits in 1152 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 186 other cell types or tissues. DR ExpressionAtlas; Q8WXW3; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. 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 chromosome alignment; 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; PROGESTERONE-INDUCED BLOCKING FACTOR 1; 1. DR PANTHER; PTHR18950:SF1; PROGESTERONE-INDUCED-BLOCKING FACTOR 1; 1. DR Genevisible; Q8WXW3; HS. 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 (found in patients with microcephaly and FT intellectual disability; likely pathogenic; disrupts FT interaction with CEP63; no effect on interaction with PCM1; FT 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 //