CBY1_HUMAN
ID CBY1_HUMAN Reviewed; 126 AA.
AC Q9Y3M2; B2R4S2; Q66GT6; Q9UIK9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein chibby homolog 1;
DE AltName: Full=ARPP-binding protein;
DE AltName: Full=Cytosolic leucine-rich protein;
DE AltName: Full=PIGEA-14;
DE AltName: Full=PKD2 interactor, Golgi and endoplasmic reticulum-associated 1;
GN Name=CBY1; Synonyms=ARB1, C22orf2, CBY, PGEA1; ORFNames=HRIHFB2025;
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].
RA Huang C.-H.;
RT "A novel cytosolic leucine-rich protein.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Moriyama M., Nakada C., Tsukamoto Y., Baba T., Kondo G., Ishiguro N.,
RA Horiuchi M., Sekine C., Maeda A.;
RT "Human ARPP-binding protein, arb1.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-126.
RC TISSUE=Fetal brain;
RA Ueki N.;
RT "HRI NTT human fetal brain cDNA project.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP CTNNB1.
RX PubMed=12712206; DOI=10.1038/nature01570;
RA Takemaru K., Yamaguchi S., Lee Y.S., Zhang Y., Carthew R.W., Moon R.T.;
RT "Chibby, a nuclear beta-catenin-associated antagonist of the Wnt/Wingless
RT pathway.";
RL Nature 422:905-909(2003).
RN [12]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PKD2
RP AND GM130.
RX PubMed=15194699; DOI=10.1074/jbc.m314206200;
RA Hidaka S., Koenecke V., Osten L., Witzgall R.;
RT "PIGEA-14, a novel coiled-coil protein affecting the intracellular
RT distribution of polycystin-2.";
RL J. Biol. Chem. 279:35009-35016(2004).
RN [13]
RP INTERACTION WITH TCIM AND CTNNB1, AND SUBCELLULAR LOCATION.
RX PubMed=16424001; DOI=10.1158/0008-5472.can-05-3124;
RA Jung Y., Bang S., Choi K., Kim E., Kim Y., Kim J., Park J., Koo H.,
RA Moon R.T., Song K., Lee I.;
RT "TC1 (C8orf4) enhances the Wnt/beta-catenin pathway by relieving
RT antagonistic activity of Chibby.";
RL Cancer Res. 66:723-728(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INTERACTION WITH FAM92A AND CIBAR2, AND SUBCELLULAR LOCATION.
RX PubMed=27528616; DOI=10.1128/mcb.00160-16;
RA Li F.Q., Chen X., Fisher C., Siller S.S., Zelikman K., Kuriyama R.,
RA Takemaru K.I.;
RT "BAR domain-containing FAM92 proteins interact with chibby1 to facilitate
RT ciliogenesis.";
RL Mol. Cell. Biol. 36:2668-2680(2016).
RN [17]
RP INTERACTION WITH FAM92A, AND SUBCELLULAR LOCATION.
RX PubMed=30395363; DOI=10.1002/jbmr.3594;
RA Schrauwen I., Giese A.P., Aziz A., Lafont D.T., Chakchouk I.,
RA Santos-Cortez R.L.P., Lee K., Acharya A., Khan F.S., Ullah A.,
RA Nickerson D.A., Bamshad M.J., Ali G., Riazuddin S., Ansar M., Ahmad W.,
RA Ahmed Z.M., Leal S.M.;
RT "FAM92A underlies nonsyndromic postaxial polydactyly in humans and an
RT abnormal limb and digit skeletal phenotype in mice.";
RL J. Bone Miner. Res. 34:375-386(2019).
CC -!- FUNCTION: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-
CC catenin and inhibiting beta-catenin-mediated transcriptional activation
CC through competition with TCF/LEF transcription factors. Has also been
CC shown to play a role in regulating the intracellular trafficking of
CC polycystin-2/PKD2 and possibly of other intracellular proteins.
CC Promotes adipocyte and cardiomyocyte differentiation.
CC {ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:15194699}.
CC -!- SUBUNIT: Homodimer. Interacts with polycystin-2/PKD2 and GM130.
CC Interacts with the C-terminal region of CTNNB1 (PubMed:12712206,
CC PubMed:16424001). Interacts (C-terminus) with TCIM (C-terminus), TCIM
CC competes with CTNNB1 for the interaction with CBY1 (PubMed:16424001).
CC Interacts with FAM92A; this interaction facilitates targeting of FAM92A
CC to cilium basal body (PubMed:27528616, PubMed:30395363). Interacts with
CC CIBAR2 (PubMed:27528616). {ECO:0000269|PubMed:12712206,
CC ECO:0000269|PubMed:15194699, ECO:0000269|PubMed:16424001,
CC ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}.
CC -!- INTERACTION:
CC Q9Y3M2; Q96M91: CFAP53; NbExp=4; IntAct=EBI-947308, EBI-742422;
CC Q9Y3M2; Q8IYY4: DZIP1L; NbExp=3; IntAct=EBI-947308, EBI-10264440;
CC Q9Y3M2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-947308, EBI-744099;
CC Q9Y3M2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-947308, EBI-7225287;
CC Q9Y3M2; A1XBS5: FAM92A; NbExp=3; IntAct=EBI-947308, EBI-2349888;
CC Q9Y3M2; A1XBS5-3: FAM92A; NbExp=3; IntAct=EBI-947308, EBI-12348777;
CC Q9Y3M2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-947308, EBI-739467;
CC Q9Y3M2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-947308, EBI-739832;
CC Q9Y3M2; Q15311: RALBP1; NbExp=4; IntAct=EBI-947308, EBI-749285;
CC Q9Y3M2; A6NK89: RASSF10; NbExp=3; IntAct=EBI-947308, EBI-6912267;
CC Q9Y3M2; Q5GJ75: TNFAIP8L3; NbExp=3; IntAct=EBI-947308, EBI-14222571;
CC Q9Y3M2; Q99816: TSG101; NbExp=3; IntAct=EBI-947308, EBI-346882;
CC Q9Y3M2; Q6PF05-3: TTC23L; NbExp=3; IntAct=EBI-947308, EBI-10182647;
CC Q9Y3M2; P62258: YWHAE; NbExp=3; IntAct=EBI-947308, EBI-356498;
CC Q9Y3M2; P63104: YWHAZ; NbExp=3; IntAct=EBI-947308, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16424001}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:27528616}. Golgi apparatus. Golgi apparatus, trans-
CC Golgi network {ECO:0000269|PubMed:16424001}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in
CC heart, skeletal muscle, kidney and placenta. Also found in brain, lung,
CC liver and testis. Significantly down-regulated in thyroid and
CC metastatic uterine tumors. {ECO:0000269|PubMed:12712206}.
CC -!- MISCELLANEOUS: 'Chibby' is Japanese for 'small'; the gene was so named
CC for the RNAi phenotype seen in flies.
CC -!- SIMILARITY: Belongs to the chibby family. {ECO:0000305}.
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DR EMBL; AF331041; AAL56062.1; -; mRNA.
DR EMBL; AB111855; BAC78839.1; -; mRNA.
DR EMBL; AL136686; CAB66621.1; -; mRNA.
DR EMBL; AL050345; CAB43547.1; -; mRNA.
DR EMBL; CR456410; CAG30296.1; -; mRNA.
DR EMBL; AK311928; BAG34869.1; -; mRNA.
DR EMBL; AL021707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60254.1; -; Genomic_DNA.
DR EMBL; BC016139; AAH16139.1; -; mRNA.
DR EMBL; AB015347; BAA88119.1; -; mRNA.
DR EMBL; BK005534; DAA05582.1; -; Genomic_DNA.
DR CCDS; CCDS13974.1; -.
DR CCDS; CCDS74861.1; -.
DR RefSeq; NP_001002880.2; NM_001002880.1.
DR RefSeq; NP_056188.1; NM_015373.3.
DR PDB; 4WRQ; X-ray; 2.41 A; C/D=12-29.
DR PDBsum; 4WRQ; -.
DR AlphaFoldDB; Q9Y3M2; -.
DR SMR; Q9Y3M2; -.
DR BioGRID; 117311; 176.
DR DIP; DIP-29651N; -.
DR ELM; Q9Y3M2; -.
DR IntAct; Q9Y3M2; 45.
DR MINT; Q9Y3M2; -.
DR STRING; 9606.ENSP00000478962; -.
DR iPTMnet; Q9Y3M2; -.
DR PhosphoSitePlus; Q9Y3M2; -.
DR BioMuta; CBY1; -.
DR DMDM; 20454882; -.
DR EPD; Q9Y3M2; -.
DR jPOST; Q9Y3M2; -.
DR MassIVE; Q9Y3M2; -.
DR MaxQB; Q9Y3M2; -.
DR PaxDb; Q9Y3M2; -.
DR PeptideAtlas; Q9Y3M2; -.
DR PRIDE; Q9Y3M2; -.
DR ProteomicsDB; 86044; -.
DR Antibodypedia; 26394; 169 antibodies from 26 providers.
DR DNASU; 25776; -.
DR Ensembl; ENST00000216029.8; ENSP00000216029.3; ENSG00000100211.11.
DR Ensembl; ENST00000396811.6; ENSP00000380026.2; ENSG00000100211.11.
DR GeneID; 25776; -.
DR KEGG; hsa:25776; -.
DR MANE-Select; ENST00000216029.8; ENSP00000216029.3; NM_015373.4; NP_056188.1.
DR UCSC; uc003awc.5; human.
DR CTD; 25776; -.
DR DisGeNET; 25776; -.
DR GeneCards; CBY1; -.
DR HGNC; HGNC:1307; CBY1.
DR HPA; ENSG00000100211; Low tissue specificity.
DR MalaCards; CBY1; -.
DR MIM; 607757; gene.
DR neXtProt; NX_Q9Y3M2; -.
DR OpenTargets; ENSG00000100211; -.
DR Orphanet; 475; Joubert syndrome.
DR PharmGKB; PA25886; -.
DR VEuPathDB; HostDB:ENSG00000100211; -.
DR eggNOG; ENOG502S6C8; Eukaryota.
DR GeneTree; ENSGT00940000153137; -.
DR InParanoid; Q9Y3M2; -.
DR OrthoDB; 1492677at2759; -.
DR PhylomeDB; Q9Y3M2; -.
DR TreeFam; TF324419; -.
DR PathwayCommons; Q9Y3M2; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q9Y3M2; -.
DR SIGNOR; Q9Y3M2; -.
DR BioGRID-ORCS; 25776; 15 hits in 1073 CRISPR screens.
DR ChiTaRS; CBY1; human.
DR GeneWiki; CBY1; -.
DR GenomeRNAi; 25776; -.
DR Pharos; Q9Y3M2; Tbio.
DR PRO; PR:Q9Y3M2; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y3M2; protein.
DR Bgee; ENSG00000100211; Expressed in oocyte and 190 other tissues.
DR ExpressionAtlas; Q9Y3M2; baseline and differential.
DR Genevisible; Q9Y3M2; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0033504; P:floor plate development; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR CDD; cd07429; Cby_like; 1.
DR DisProt; DP00709; -.
DR InterPro; IPR028118; Chibby_fam.
DR Pfam; PF14645; Chibby; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Differentiation; Golgi apparatus; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..126
FT /note="Protein chibby homolog 1"
FT /id="PRO_0000058354"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..112
FT /note="Minimal region for the interaction with PKD2"
FT /evidence="ECO:0000269|PubMed:15194699"
FT COILED 67..125
FT /evidence="ECO:0000255"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4I6"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 73
FT /note="E -> K (in Ref. 1; AAL56062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 14470 MW; 0D243AD2CC436E55 CRC64;
MPFFGNTFSP KKTPPRKSAS LSNLHSLDRS TREVELGLEY GSPTMNLAGQ SLKFENGQWI
AETGVSGGVD RREVQRLRRR NQQLEEENNL LRLKVDILLD MLSESTAESH LMEKELDELR
ISRKRK
