CP131_HUMAN
ID CP131_HUMAN Reviewed; 1083 AA.
AC Q9UPN4; A6NHI8; B2RN11; Q96F50;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Centrosomal protein of 131 kDa;
DE AltName: Full=5-azacytidine-induced protein 1;
DE AltName: Full=Pre-acrosome localization protein 1;
GN Name=CEP131; Synonyms=AZI1, KIAA1118;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-272;
RP ALA-397 AND ALA-473.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ALA-272;
RP ALA-397 AND ALA-473.
RC TISSUE=Lung;
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION IN CILIOGENESIS.
RX PubMed=17954613; DOI=10.1083/jcb.200707181;
RA Graser S., Stierhof Y.-D., Lavoie S.B., Gassner O.S., Lamla S.,
RA Le Clech M., Nigg E.A.;
RT "Cep164, a novel centriole appendage protein required for primary cilium
RT formation.";
RL J. Cell Biol. 179:321-330(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-105 AND SER-150, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 (ISOFORMS 2 AND 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-89; SER-105 AND
RP SER-798, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 AND SER-496
RP (ISOFORMS 2 AND 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-78 AND SER-453, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-47; SER-114; SER-146;
RP SER-381; THR-383 AND SER-798, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP INTERACTION WITH MAP1LC3B.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
RT satellites.";
RL Nature 502:254-257(2013).
RN [15]
RP FUNCTION IN GENOMIC STABILITY, INTERACTION WITH CEP290; DCTN1; PCM1 AND
RP PCNT, AND SUBCELLULAR LOCATION.
RX PubMed=22797915; DOI=10.1242/jcs.104059;
RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Lee A.J., Swanton C.,
RA Howell M., Boulton S.J., Collis S.J.;
RT "The centriolar satellite protein Cep131 is important for genome
RT stability.";
RL J. Cell Sci. 125:4770-4779(2012).
RN [16]
RP REVIEW, AND FUNCTION.
RX PubMed=24185901; DOI=10.1038/emboj.2013.241;
RA Chavali P.L., Gergely F.;
RT "Cilia born out of shock and stress.";
RL EMBO J. 32:3011-3013(2013).
RN [17]
RP FUNCTION IN CILIOGENESIS, UBIQUITINATION BY MIB1, INTERACTION WITH MIB1 AND
RP PCM1, ASSOCIATION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=24121310; DOI=10.1038/emboj.2013.223;
RA Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B., Merdes A.,
RA Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N.,
RA Bekker-Jensen S.;
RT "A new cellular stress response that triggers centriolar satellite
RT reorganization and ciliogenesis.";
RL EMBO J. 32:3029-3040(2013).
RN [18]
RP INDUCTION.
RX PubMed=23137637; DOI=10.1016/j.gene.2012.10.074;
RA Huong P.T., Soung N.K., Jang J.H., Cha-Molstad H.J., Sakchaisri K.,
RA Kim S.O., Jang J.M., Kim K.E., Lee K.S., Kwon Y.T., Erikson R.L., Ahn J.S.,
RA Kim B.Y.;
RT "Regulation of CEP131 gene expression by SP1.";
RL Gene 513:75-81(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP FUNCTION IN CILIARY TRAFFICKING, SUBUNIT, INTERACTION WITH BBS4, AND
RP ASSOCIATION WITH THE BBSOME COMPLEX.
RX PubMed=24550735; DOI=10.1371/journal.pgen.1004083;
RA Chamling X., Seo S., Searby C.C., Kim G., Slusarski D.C., Sheffield V.C.;
RT "The centriolar satellite protein AZI1 interacts with BBS4 and regulates
RT ciliary trafficking of the BBSome.";
RL PLoS Genet. 10:E1004083-E1004083(2014).
RN [21]
RP FUNCTION, INTERACTION WITH 14-3-3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-47; SER-78 AND SER-731, AND MUTAGENESIS OF SER-47; SER-78 AND SER-731.
RX PubMed=26616734; DOI=10.1038/ncomms10075;
RA Tollenaere M.A., Villumsen B.H., Blasius M., Nielsen J.C., Wagner S.A.,
RA Bartek J., Beli P., Mailand N., Bekker-Jensen S.;
RT "p38- and MK2-dependent signalling promotes stress-induced centriolar
RT satellite remodelling via 14-3-3-dependent sequestration of CEP131/AZI1.";
RL Nat. Commun. 6:10075-10075(2015).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP152 AND PCM1.
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 [23]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SDCCAG8.
RX PubMed=27224062; DOI=10.1371/journal.pone.0156081;
RA Airik R., Schueler M., Airik M., Cho J., Ulanowicz K.A., Porath J.D.,
RA Hurd T.W., Bekker-Jensen S., Schroeder J.M., Andersen J.S., Hildebrandt F.;
RT "SDCCAG8 interacts with RAB effector proteins RABEP2 and ERC1 and is
RT required for Hedgehog Signaling.";
RL PLoS ONE 11:E0156081-E0156081(2016).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-78, MUTAGENESIS OF
RP SER-78, AND INTERACTION WITH PLK4.
RX PubMed=30804208; DOI=10.1074/jbc.ra118.004867;
RA Denu R.A., Sass M.M., Johnson J.M., Potts G.K., Choudhary A., Coon J.J.,
RA Burkard M.E.;
RT "Polo-like kinase 4 maintains centriolar satellite integrity by
RT phosphorylation of centrosomal protein 131 (CEP131).";
RL J. Biol. Chem. 294:6531-6549(2019).
RN [25]
RP SUBCELLULAR LOCATION.
RX PubMed=30538148; DOI=10.1261/rna.069773.118;
RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D.,
RA Pellman D., Kennedy S., Slack F.J.;
RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing
RT factor.";
RL RNA 25:352-363(2019).
RN [26]
RP INTERACTION WITH CCDC61, AND SUBCELLULAR LOCATION.
RX PubMed=31789463; DOI=10.1111/boc.201900038;
RA Pizon V., Gaudin N., Poteau M., Cifuentes-Diaz C., Demdou R., Heyer V.,
RA Reina San Martin B., Azimzadeh J.;
RT "hVFL3/CCDC61 is a component of mother centriole subdistal appendages
RT required for centrosome cohesion and positioning.";
RL Biol. Cell 112:22-37(2020).
CC -!- FUNCTION: Component of centriolar satellites contributing to the
CC building of a complex and dynamic network required to regulate
CC cilia/flagellum formation (PubMed:17954613, PubMed:24185901). In
CC proliferating cells, MIB1-mediated ubiquitination induces its
CC sequestration within centriolar satellites, precluding untimely cilia
CC formation initiation (PubMed:24121310). In contrast, during normal and
CC ultraviolet or heat shock cellular stress-induced ciliogenesis, its
CC non-ubiquitinated form is rapidly displaced from centriolar satellites
CC and recruited to centrosome/basal bodies in a microtubule- and p38
CC MAPK-dependent manner (PubMed:24121310, PubMed:26616734). Acts also as
CC a negative regulator of BBSome ciliary trafficking (PubMed:24550735).
CC Plays a role in sperm flagellar formation; may be involved in the
CC regulation of intraflagellar transport (IFT) and/or intramanchette
CC (IMT) trafficking, which are important for axoneme extension and/or
CC cargo delivery to the nascent sperm tail (By similarity). Required for
CC optimal cell proliferation and cell cycle progression; may play a role
CC in the regulation of genome stability in non-ciliogenic cells
CC (PubMed:22797915, PubMed:26297806). Involved in centriole duplication
CC (By similarity). Required for CEP152, WDR62 and CEP63 centrosomal
CC localization and promotes the centrosomal localization of CDK2
CC (PubMed:26297806). Essential for maintaining proper centriolar
CC satellite integrity (PubMed:30804208). {ECO:0000250|UniProtKB:Q62036,
CC ECO:0000269|PubMed:17954613, ECO:0000269|PubMed:22797915,
CC ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:24185901,
CC ECO:0000269|PubMed:24550735, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:26616734, ECO:0000269|PubMed:30804208}.
CC -!- SUBUNIT: Self-associates. Associates with the centriolar satellite
CC BBSome protein complex. Interacts with BBS4; the interaction limits
CC BBS4 availability for association with the BBSome complex, and hence
CC negatively regulates ciliary localization of the BBSome complex
CC (PubMed:24550735). Interacts with MIB1 (PubMed:24121310). Interacts
CC with PCM1; the interaction increases in response to ultraviolet light
CC (UV) radiation (PubMed:22797915, PubMed:24121310). Associates with
CC microtubules; association with microtubules is reduced in response to
CC cellular stress, such as UV stimulation, in a process that requires p38
CC MAP kinase signaling (PubMed:24121310). Interacts with CEP290, DCTN1,
CC PCNT, PCM1 and CEP152. Interacts with 14-3-3 proteins following UV-
CC induced phosphorylation by MAPKAPK2; this inhibits formation of novel
CC centriolar satellites (PubMed:26616734). Interacts with SDCCAG8
CC (PubMed:27224062). Interacts with CCDC61 (PubMed:31789463). Interacts
CC with PLK4 (PubMed:30804208). {ECO:0000269|PubMed:22797915,
CC ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24121310,
CC ECO:0000269|PubMed:24550735, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:26616734, ECO:0000269|PubMed:27224062,
CC ECO:0000269|PubMed:30804208, ECO:0000269|PubMed:31789463}.
CC -!- INTERACTION:
CC Q9UPN4; O94986: CEP152; NbExp=3; IntAct=EBI-2558372, EBI-311012;
CC Q9UPN4; O15078: CEP290; NbExp=9; IntAct=EBI-2558372, EBI-1811944;
CC Q9UPN4; Q15154: PCM1; NbExp=5; IntAct=EBI-2558372, EBI-741421;
CC Q9UPN4; Q86SQ7: SDCCAG8; NbExp=3; IntAct=EBI-2558372, EBI-1047850;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:27224062, ECO:0000269|PubMed:30538148,
CC ECO:0000269|PubMed:30804208}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26616734,
CC ECO:0000269|PubMed:30804208, ECO:0000269|PubMed:31789463}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:30804208}. Cytoplasm, cytoskeleton, cilium basal
CC body. Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q62036}. Note=Colocalized with pericentriolar
CC material protein PCM1 at centriolar satellites. During spermiogenesis,
CC becomes enriched with nephrocystin NPHP1 at the transition zone, a
CC structure at the base of the ciliary axoneme important for regulating
CC traffic into the ciliary compartment. Traffics towards and away from
CC the centrosome/basal body and the transition zone of the ciliary
CC axoneme in a microtubule-dependent manner. Localized at the Golgi-
CC derived acrosome and the centrosome-containing head-tail coupling
CC apparatus (HTCA) (By similarity). Ubiquitinated form is sequestered and
CC colocalized with BBS4, CEP290, PCM1 and PCNT at centriolar satellites
CC in proliferating cells. Colocalized with the pericentriolar material
CC protein PCM1 at centrosome. Traffics towards and away from centriolar
CC satellites and centrosome in a microtubule- and dynein-dependent manner
CC in interphase cells. Displaced from centriolar satellites but still
CC remains associated with the centrosome in response to cellular stress,
CC such as ultraviolet light (UV) radiation or heat shock, in a process
CC that requires p38 MAPK signaling (PubMed:26616734). {ECO:0000250,
CC ECO:0000269|PubMed:26616734}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPN4-2; Sequence=VSP_015823;
CC Name=3;
CC IsoId=Q9UPN4-3; Sequence=VSP_015823, VSP_040204;
CC -!- INDUCTION: Up-regulated by the transcription factor SP1.
CC {ECO:0000269|PubMed:23137637}.
CC -!- PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3
CC ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia
CC formation. Monoubiquitination by MIB1 is inhibited in response to
CC cellular stress, such as ultraviolet light (UV) radiation or heat
CC shock, resulting in cilia formation initiation.
CC {ECO:0000269|PubMed:24121310}.
CC -!- PTM: MAPKAPK2-dependent phosphorylation at Ser-47 and Ser-78 occurs in
CC response to cellular stress such as exposure to ultraviolet irradiation
CC and promotes binding to 14-3-3 proteins which leads to cytoplasmic
CC sequestration of CEP131 and blocks formation of new centriolar
CC satellites (PubMed:26616734). Phosphorylation at Ser-78 mediated by
CC PLK4 is essential for proper organization and integrity of centriolar
CC satellites but is dispensable for its localization to centrioles and
CC its function in ciliogenesis (PubMed:30804208).
CC {ECO:0000269|PubMed:26616734, ECO:0000269|PubMed:30804208}.
CC -!- MISCELLANEOUS: Transient cell cultured-based knock-down (by RNAi) of
CC CEP131 leads to a reduction in ciliogenesis (PubMed:17954613,
CC PubMed:24121310). However, analysis of mice with chronic absence of
CC CEP131 following genetic deletion (knockout) shows that cilia develop
CC and function normally in vivo. This suggests that CEP131 is not
CC essential for ciliogenesis, except for the modified cilia of the
CC developing sperm flagella, and that there is an alternative mechanism
CC to compensate for the lack of CEP131. {ECO:0000305|PubMed:17954613,
CC ECO:0000305|PubMed:24121310}.
CC -!- SIMILARITY: Belongs to the CEP131 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83070.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB029041; BAA83070.1; ALT_INIT; mRNA.
DR EMBL; AC027601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011615; AAH11615.2; -; mRNA.
DR EMBL; BC136580; AAI36581.1; -; mRNA.
DR CCDS; CCDS32764.1; -. [Q9UPN4-3]
DR CCDS; CCDS45808.1; -. [Q9UPN4-2]
DR CCDS; CCDS82215.1; -. [Q9UPN4-1]
DR RefSeq; NP_001009811.2; NM_001009811.3. [Q9UPN4-3]
DR RefSeq; NP_001306157.1; NM_001319228.1. [Q9UPN4-1]
DR RefSeq; NP_055799.2; NM_014984.3. [Q9UPN4-2]
DR AlphaFoldDB; Q9UPN4; -.
DR SMR; Q9UPN4; -.
DR BioGRID; 116641; 217.
DR CORUM; Q9UPN4; -.
DR DIP; DIP-56658N; -.
DR IntAct; Q9UPN4; 120.
DR MINT; Q9UPN4; -.
DR STRING; 9606.ENSP00000393583; -.
DR iPTMnet; Q9UPN4; -.
DR MetOSite; Q9UPN4; -.
DR PhosphoSitePlus; Q9UPN4; -.
DR BioMuta; CEP131; -.
DR DMDM; 313104247; -.
DR EPD; Q9UPN4; -.
DR jPOST; Q9UPN4; -.
DR MassIVE; Q9UPN4; -.
DR MaxQB; Q9UPN4; -.
DR PaxDb; Q9UPN4; -.
DR PeptideAtlas; Q9UPN4; -.
DR PRIDE; Q9UPN4; -.
DR ProteomicsDB; 85387; -. [Q9UPN4-1]
DR ProteomicsDB; 85388; -. [Q9UPN4-2]
DR ProteomicsDB; 85389; -. [Q9UPN4-3]
DR Antibodypedia; 19799; 126 antibodies from 24 providers.
DR DNASU; 22994; -.
DR Ensembl; ENST00000269392.8; ENSP00000269392.4; ENSG00000141577.14. [Q9UPN4-1]
DR Ensembl; ENST00000374782.7; ENSP00000363914.3; ENSG00000141577.14. [Q9UPN4-3]
DR Ensembl; ENST00000450824.7; ENSP00000393583.2; ENSG00000141577.14. [Q9UPN4-2]
DR GeneID; 22994; -.
DR KEGG; hsa:22994; -.
DR MANE-Select; ENST00000450824.7; ENSP00000393583.2; NM_014984.4; NP_055799.2. [Q9UPN4-2]
DR UCSC; uc002jzn.2; human. [Q9UPN4-1]
DR CTD; 22994; -.
DR DisGeNET; 22994; -.
DR GeneCards; CEP131; -.
DR HGNC; HGNC:29511; CEP131.
DR HPA; ENSG00000141577; Low tissue specificity.
DR MIM; 613479; gene.
DR neXtProt; NX_Q9UPN4; -.
DR OpenTargets; ENSG00000141577; -.
DR PharmGKB; PA128394595; -.
DR PharmGKB; PA134920867; -.
DR VEuPathDB; HostDB:ENSG00000141577; -.
DR eggNOG; ENOG502RZME; Eukaryota.
DR GeneTree; ENSGT00390000001758; -.
DR HOGENOM; CLU_010690_0_0_1; -.
DR InParanoid; Q9UPN4; -.
DR OMA; RKECTLA; -.
DR OrthoDB; 918776at2759; -.
DR PhylomeDB; Q9UPN4; -.
DR TreeFam; TF328914; -.
DR PathwayCommons; Q9UPN4; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9UPN4; -.
DR BioGRID-ORCS; 22994; 348 hits in 1068 CRISPR screens.
DR ChiTaRS; CEP131; human.
DR GeneWiki; AZI1; -.
DR GenomeRNAi; 22994; -.
DR Pharos; Q9UPN4; Tbio.
DR PRO; PR:Q9UPN4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UPN4; protein.
DR Bgee; ENSG00000141577; Expressed in sural nerve and 95 other tissues.
DR ExpressionAtlas; Q9UPN4; baseline and differential.
DR Genevisible; Q9UPN4; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0002177; C:manchette; IEA:GOC.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0120212; C:sperm head-tail coupling apparatus; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
DR GO; GO:1990953; P:intramanchette transport; IEA:Ensembl.
DR GO; GO:1905198; P:manchette assembly; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
DR InterPro; IPR030465; CEP131.
DR PANTHER; PTHR31540; PTHR31540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Developmental protein; Differentiation; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Transport; Ubl conjugation.
FT CHAIN 1..1083
FT /note="Centrosomal protein of 131 kDa"
FT /id="PRO_0000064781"
FT DOMAIN 269..289
FT /note="IQ"
FT REGION 1..250
FT /note="Interaction with PLK4"
FT /evidence="ECO:0000269|PubMed:30804208"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62036"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 47
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine; by MAPKAPK2 and PLK4"
FT /evidence="ECO:0000269|PubMed:30804208,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62036"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26616734"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 491..493
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015823"
FT VAR_SEQ 777..812
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040204"
FT VARIANT 43
FT /note="V -> I (in dbSNP:rs8067409)"
FT /id="VAR_056740"
FT VARIANT 70
FT /note="I -> V (in dbSNP:rs752612451)"
FT /id="VAR_060226"
FT VARIANT 272
FT /note="T -> A (in dbSNP:rs2466773)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060227"
FT VARIANT 397
FT /note="T -> A (in dbSNP:rs2659015)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060228"
FT VARIANT 473
FT /note="V -> A (in dbSNP:rs2659016)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060229"
FT MUTAGEN 47
FT /note="S->A: Partially reduces in vitro phosphorylation by
FT MAPKAPK2 and decreases binding to 14-3-3. Abolishes in
FT vitro phosphorylation by MAPKAPK2, interaction with 14-3-3
FT and stress-induced centriolar satellite remodeling; when
FT associated with A-78."
FT /evidence="ECO:0000269|PubMed:26616734"
FT MUTAGEN 78
FT /note="S->A: Partially reduces in vitro phosphorylation by
FT MAPKAPK2 and decreases binding to 14-3-3. Abolishes in
FT vitro phosphorylation by MAPKAPK2, interaction with 14-3-3
FT and stress-induced centriolar satellite remodeling; when
FT associated with A-47. Loss of PLK4-mediated
FT phosphorylation. No effect on its localization to centriole
FT and centriolar satellite or on its function in
FT ciliogenesis. Cannot rescue centriolar satellite dispersion
FT defect mediated by deletion of CEP131."
FT /evidence="ECO:0000269|PubMed:26616734,
FT ECO:0000269|PubMed:30804208"
FT MUTAGEN 78
FT /note="S->D: Phosphomimetic mutant. No effect on its
FT localization to centriole and centriolar satellite or on
FT its function in ciliogenesis. Can rescue centriolar
FT satellite dispersion defect mediated by deletion of
FT CEP131."
FT /evidence="ECO:0000269|PubMed:30804208"
FT MUTAGEN 731
FT /note="S->A: No effect on interaction with 14-3-3."
FT /evidence="ECO:0000269|PubMed:26616734"
FT MOD_RES Q9UPN4-2:489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES Q9UPN4-2:496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9UPN4-3:489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES Q9UPN4-3:496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
SQ SEQUENCE 1083 AA; 122149 MW; 31C8CA426569CCAC CRC64;
MKGTRAIGSV PERSPAGVDL SLTGLPPPVS RRPGSAATTK PIVRSVSVVT GSEQKRKVLE
ATGPGGSQAI NNLRRSNSTT QVSQPRSGSP RPTEPTDFLM LFEGSPSGKK RPASLSTAPS
EKGATWNVLD DQPRGFTLPS NARSSSALDS PAGPRRKECT VALAPNFTAN NRSNKGAVGN
CVTTMVHNRY TPSERAPPLK SSNQTAPSLN NIIKAATCEG SESSGFGKLP KNVSSATHSA
RNNTGGSTGL PRRKEVTEEE AERFIHQVNQ ATVTIQRWYR HQVQRRGAGA ARLEHLLQAK
REEQRQRSGE GTLLDLHQQK EAARRKAREE KARQARRAAI QELQQKRALR AQKASTAERG
PPENPRETRV PGMRQPAQEL SPTPGGTAHQ ALKANNTGGG LPAAGPGDRC LPTSDSSPEP
QQPPEDRTQD VLAQDAAGDN LEMMAPSRGS AKSRGPLEEL LHTLQLLEKE PDVLPRPRTH
HRGRYAWASE VTTEDDASSL TADNLEKFGK LSAFPEPPED GTLLSEAKLQ SIMSFLDEME
KSGQDQLDSQ QEGWVPEAGP GPLELGSEVS TSVMRLKLEV EEKKQAMLLL QRALAQQRDL
TARRVKETEK ALSRQLQRQR EHYEATIQRH LAFIDQLIED KKVLSEKCEA VVAELKQEDQ
RCTERVAQAQ AQHELEIKKL KELMSATEKA RREKWISEKT KKIKEVTVRG LEPEIQKLIA
RHKQEVRRLK SLHEAELLQS DERASQRCLR QAEELREQLE REKEALGQQE RERARQRFQQ
HLEQEQWALQ QQRQRLYSEV AEERERLGQQ AARQRAELEE LRQQLEESSS ALTRALRAEF
EKGREEQERR HQMELNTLKQ QLELERQAWE AGRTRKEEAW LLNREQELRE EIRKGRDKEI
ELVIHRLEAD MALAKEESEK AAESRIKRLR DKYEAELSEL EQSERKLQER CSELKGQLGE
AEGENLRLQG LVRQKERALE DAQAVNEQLS SERSNLAQVI RQEFEDRLAA SEEETRQAKA
ELATLQARQQ LELEEVHRRV KTALARKEEA VSSLRTQHEA AVKRADHLEE LLEQHRRPTP
STK
