PCM1_MOUSE
ID PCM1_MOUSE Reviewed; 2025 AA.
AC Q9R0L6; E9QLK2; O70287; Q3URH6; Q7TMS7; Q8C9V2; Q91Y27; Q91Y28; Q91Y51;
AC Q923L0; Q9CRK8; Q9CT57;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Pericentriolar material 1 protein;
DE Short=PCM-1;
DE Short=mPCM-1;
GN Name=Pcm1 {ECO:0000312|MGI:MGI:1277958};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=10579718; DOI=10.1083/jcb.147.5.969;
RA Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N.;
RT "Centriolar satellites: molecular characterization, ATP-dependent movement
RT toward centrioles and possible involvement in ciliogenesis.";
RL J. Cell Biol. 147:969-980(1999).
RN [2]
RP ERRATUM OF PUBMED:10579718.
RA Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N.;
RL J. Cell Biol. 147:1585-1585(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-448 (ISOFORM 2).
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-443 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1978-2025 (ISOFORMS 1/2).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-78 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 41-2004 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1922-2025
RP (ISOFORMS 1/2), AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1193-2025.
RC STRAIN=129S6/SvEvTac, and C57BL/6J; TISSUE=Placenta;
RA van Geel M., Bolland D.J., Carim Todd L., Frants R.R., Hewitt J.E.,
RA de Jong P.J.;
RT "Comparative analysis of an evolutionary chromosomal breakpoint indicates a
RT recent origin for the human 4q telomere.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1722-1784.
RX PubMed=9680377; DOI=10.1007/s003359900829;
RA Grewal P.K., Bolland D.J., Todd L.C., Hewitt J.E.;
RT "High-resolution mapping of mouse chromosome 8 identifies an evolutionary
RT chromosomal breakpoint.";
RL Mamm. Genome 9:603-607(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1779-2005 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=12466851; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., Schriml L.M.,
RA Kanapin A., Matsuda H., Batalov S., Beisel K.W., Blake J.A., Bradt D.,
RA Brusic V., Chothia C., Corbani L.E., Cousins S., Dalla E., Dragani T.A.,
RA Fletcher C.F., Forrest A., Frazer K.S., Gaasterland T., Gariboldi M.,
RA Gissi C., Godzik A., Gough J., Grimmond S., Gustincich S., Hirokawa N.,
RA Jackson I.J., Jarvis E.D., Kanai A., Kawaji H., Kawasawa Y.,
RA Kedzierski R.M., King B.L., Konagaya A., Kurochkin I.V., Lee Y.,
RA Lenhard B., Lyons P.A., Maglott D.R., Maltais L., Marchionni L.,
RA McKenzie L., Miki H., Nagashima T., Numata K., Okido T., Pavan W.J.,
RA Pertea G., Pesole G., Petrovsky N., Pillai R., Pontius J.U., Qi D.,
RA Ramachandran S., Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z.,
RA Ringwald M., Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., Verardo R.,
RA Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., Wilming L.G.,
RA Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., Yuan Z., Zavolan M.,
RA Zhu Y., Zimmer A., Carninci P., Hayatsu N., Hirozane-Kishikawa T.,
RA Konno H., Nakamura M., Sakazume N., Sato K., Shiraki T., Waki K., Kawai J.,
RA Aizawa K., Arakawa T., Fukuda S., Hara A., Hashizume W., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Miyazaki A., Sakai K., Sasaki D., Shibata K.,
RA Shinagawa A., Yasunishi A., Yoshino M., Waterston R., Lander E.S.,
RA Rogers J., Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12112146; DOI=10.1002/cm.10043;
RA Balczon R., Simerly C., Takahashi D., Schatten G.;
RT "Arrest of cell cycle progression during first interphase in murine zygotes
RT microinjected with anti-PCM-1 antibodies.";
RL Cell Motil. Cytoskeleton 52:183-192(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12403812; DOI=10.1083/jcb.200204023;
RA Dammermann A., Merdes A.;
RT "Assembly of centrosomal proteins and microtubule organization depends on
RT PCM-1.";
RL J. Cell Biol. 159:255-266(2002).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12571289; DOI=10.1242/jcs.00282;
RA Kubo A., Tsukita S.;
RT "Non-membranous granular organelle consisting of PCM-1: subcellular
RT distribution and cell-cycle-dependent assembly/disassembly.";
RL J. Cell Sci. 116:919-928(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-1766 AND SER-1769,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=15107855; DOI=10.1038/ng1352;
RA Kim J.C., Badano J.L., Sibold S., Esmail M.A., Hill J., Hoskins B.E.,
RA Leitch C.C., Venner K., Ansley S.J., Ross A.J., Leroux M.R., Katsanis N.,
RA Beales P.L.;
RT "The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region
RT and is required for microtubule anchoring and cell cycle progression.";
RL Nat. Genet. 36:462-470(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-69; SER-644; SER-1766
RP AND SER-1769, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [15]
RP INTERACTION WITH CEP290.
RX PubMed=17705300; DOI=10.1002/humu.20614;
RA Frank V., den Hollander A.I., Bruechle N.O., Zonneveld M.N., Nuernberg G.,
RA Becker C., Du Bois G., Kendziorra H., Roosing S., Senderek J.,
RA Nuernberg P., Cremers F.P., Zerres K., Bergmann C.;
RT "Mutations of the CEP290 gene encoding a centrosomal protein cause Meckel-
RT Gruber syndrome.";
RL Hum. Mutat. 29:45-52(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69; SER-110;
RP SER-116; SER-119; SER-644; SER-859; SER-864; SER-867; SER-870; THR-875;
RP SER-1185; SER-1254; SER-1257; SER-1259; SER-1260; SER-1315; SER-1317;
RP SER-1571; SER-1729; SER-1766; SER-1769; SER-1777 AND SER-1783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP INTERACTION WITH SSX2IP.
RX PubMed=24356449; DOI=10.1091/mbc.e13-09-0526;
RA Klinger M., Wang W., Kuhns S., Baerenz F., Draeger-Meurer S., Pereira G.,
RA Gruss O.J.;
RT "The novel centriolar satellite protein SSX2IP targets Cep290 to the
RT ciliary transition zone.";
RL Mol. Biol. Cell 25:495-507(2014).
RN [20]
RP INTERACTION WITH C2CD3.
RX PubMed=24469809; DOI=10.1073/pnas.1318737111;
RA Ye X., Zeng H., Ning G., Reiter J.F., Liu A.;
RT "C2cd3 is critical for centriolar distal appendage assembly and ciliary
RT vesicle docking in mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2164-2169(2014).
RN [21]
RP INTERACTION WITH KIAA0753; CEP20 AND OFD1.
RX PubMed=26643951; DOI=10.1093/hmg/ddv488;
RA Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M., Lembo F.,
RA Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P., Kuentz P.,
RA Thevenon J., Burglen L., Faivre L., Riviere J.B., Huynen M.A., Birnbaum D.,
RA Rosnet O., Thauvin-Robinet C.;
RT "OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
RT satellites and centrosomes and is mutated in one individual with oral-
RT facial-digital syndrome.";
RL Hum. Mol. Genet. 25:497-513(2016).
RN [22]
RP FUNCTION, AND INTERACTION WITH DZIP1.
RX PubMed=27979967; DOI=10.1074/jbc.m116.765438;
RA Zhang B., Wang G., Xu X., Yang S., Zhuang T., Wang G., Ren H., Cheng S.Y.,
RA Jiang Q., Zhang C.;
RT "DAZ-interacting Protein 1 (Dzip1) Phosphorylation by Polo-like Kinase 1
RT (Plk1) Regulates the Centriolar Satellite Localization of the BBSome
RT Protein during the Cell Cycle.";
RL J. Biol. Chem. 292:1351-1360(2017).
CC -!- FUNCTION: Required for centrosome assembly and function
CC (PubMed:12112146). Essential for the correct localization of several
CC centrosomal proteins including CEP250, CETN3, PCNT and NEK2 (By
CC similarity). Required to anchor microtubules to the centrosome (By
CC similarity). Also involved in cilium biogenesis by recruiting the
CC BBSome, a ciliary protein complex involved in cilium biogenesis, to the
CC centriolar satellites (PubMed:27979967). Recruits the tubulin
CC polyglutamylase complex (TPGC) to centriolar satellites (By
CC similarity). {ECO:0000250|UniProtKB:Q15154,
CC ECO:0000269|PubMed:12112146, ECO:0000269|PubMed:27979967}.
CC -!- SUBUNIT: Self-associates. Interacts with BBS4, BBS8, CETN3, HAP1, NDE1,
CC NDEL1, MAP1LC3B, GABARAPAL2, and GABARAP. Interacts with CEP131; the
CC interaction increases in response to ultraviolet light (UV) radiation.
CC Associates with microtubule; association to microtubule is reduced in
CC response to cellular stress, such as ultraviolet light (UV) radiation
CC or heat shock, in a process that requires p38 MAP kinase signaling (By
CC similarity). Interacts with C2CD3 (PubMed:24469809). Interacts with
CC CCDC113 (By similarity). Interacts with SSX2IP (PubMed:24356449).
CC Interacts with CCDC13 (By similarity). Interacts with CEP290
CC (PubMed:17705300). Interacts with PARD6A (By similarity). Interacts
CC with KIAA0753/OFIP, CEP20/FOR20 and OFD1; the interaction with
CC CEP20/FOR20 and OFD1 may be mediated by KIAA0753/OFIP
CC (PubMed:26643951). Interacts with CCDC66 (By similarity). Interacts
CC with CCDC61 (By similarity). Interacts with DZIP1; localizes DZIP1 and
CC the associated BBSome to centriolar satellite (PubMed:27979967).
CC Interacts with CSTPP1, TTLL1, TPGS1 and LRRC49 (By similarity).
CC {ECO:0000250|UniProtKB:Q15154, ECO:0000269|PubMed:17705300,
CC ECO:0000269|PubMed:24356449, ECO:0000269|PubMed:24469809,
CC ECO:0000269|PubMed:26643951, ECO:0000269|PubMed:27979967}.
CC -!- INTERACTION:
CC Q9R0L6; Q6A078: Cep290; NbExp=4; IntAct=EBI-4284371, EBI-1811999;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8AV28}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:10579718,
CC ECO:0000269|PubMed:12112146, ECO:0000269|PubMed:12403812}. Cytoplasmic
CC granule {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:12571289}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000269|PubMed:10579718,
CC ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:12571289}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q15154}.
CC Note=Recruitment to the centrosome requires microtubules and dynein.
CC Displaced from centriolar satellites and centrosome in response to
CC cellular stress, such as ultraviolet light (UV) radiation or heat
CC shock, in a process that requires p38 MAP kinase signaling (By
CC similarity). The majority of the protein dissociates from the
CC centrosome during metaphase and subsequently localizes to the cleavage
CC site in telophase. {ECO:0000250|UniProtKB:Q15154}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9R0L6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R0L6-2; Sequence=VSP_022612;
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus and dentate gyrus, the
CC columnar epithelial cells of bronchioles, the olfactory epithelium, the
CC pericardium and the inner segment of the retina.
CC {ECO:0000269|PubMed:15107855}.
CC -!- DEVELOPMENTAL STAGE: Maternally derived during fertilization. Expressed
CC in the pericardium of the developing embryo and in the epidermal layer
CC surrounding the digits. {ECO:0000269|PubMed:12112146}.
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:0000250|UniProtKB:Q15154}.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues by DYRK3
CC during the G2-to-M transition, after the nuclear-envelope breakdown.
CC Phosphorylation by DYRK3 promotes disassembly of pericentriolar
CC material (By similarity). Phosphorylation at Ser-372 mediated by PLK4
CC is required to maintain the integrity of centriolar satellites (By
CC similarity). {ECO:0000250|UniProtKB:Q15154}.
CC -!- SIMILARITY: Belongs to the PCM1 family. {ECO:0000305}.
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DR EMBL; AB029291; BAA87861.1; -; mRNA.
DR EMBL; AC144926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053728; AAH53728.1; -; mRNA.
DR EMBL; AK011147; BAB27430.3; -; mRNA.
DR EMBL; AK040482; BAC30604.1; -; mRNA.
DR EMBL; AK141516; BAE24712.1; -; mRNA.
DR EMBL; AY028080; AAK21980.1; -; Genomic_DNA.
DR EMBL; AF352180; AAK39513.1; -; mRNA.
DR EMBL; AF369838; AAK39564.1; -; mRNA.
DR EMBL; AF369839; AAK39565.1; -; mRNA.
DR EMBL; AF039021; AAC96068.1; -; Genomic_DNA.
DR EMBL; AK020493; BAB32121.1; -; mRNA.
DR CCDS; CCDS22261.1; -. [Q9R0L6-1]
DR RefSeq; NP_076151.2; NM_023662.3. [Q9R0L6-1]
DR RefSeq; XP_006509361.1; XM_006509298.2. [Q9R0L6-2]
DR AlphaFoldDB; Q9R0L6; -.
DR SMR; Q9R0L6; -.
DR BioGRID; 202047; 35.
DR IntAct; Q9R0L6; 25.
DR MINT; Q9R0L6; -.
DR STRING; 10090.ENSMUSP00000039709; -.
DR iPTMnet; Q9R0L6; -.
DR PhosphoSitePlus; Q9R0L6; -.
DR SwissPalm; Q9R0L6; -.
DR EPD; Q9R0L6; -.
DR jPOST; Q9R0L6; -.
DR MaxQB; Q9R0L6; -.
DR PaxDb; Q9R0L6; -.
DR PeptideAtlas; Q9R0L6; -.
DR PRIDE; Q9R0L6; -.
DR ProteomicsDB; 287998; -. [Q9R0L6-1]
DR ProteomicsDB; 287999; -. [Q9R0L6-2]
DR Antibodypedia; 5155; 228 antibodies from 31 providers.
DR DNASU; 18536; -.
DR Ensembl; ENSMUST00000045218; ENSMUSP00000039709; ENSMUSG00000031592. [Q9R0L6-1]
DR Ensembl; ENSMUST00000211247; ENSMUSP00000147887; ENSMUSG00000031592. [Q9R0L6-2]
DR GeneID; 18536; -.
DR KEGG; mmu:18536; -.
DR UCSC; uc009lnr.2; mouse. [Q9R0L6-1]
DR UCSC; uc009lns.1; mouse. [Q9R0L6-2]
DR CTD; 5108; -.
DR MGI; MGI:1277958; Pcm1.
DR VEuPathDB; HostDB:ENSMUSG00000031592; -.
DR eggNOG; ENOG502QRMF; Eukaryota.
DR GeneTree; ENSGT00390000006641; -.
DR HOGENOM; CLU_002145_0_0_1; -.
DR InParanoid; Q9R0L6; -.
DR OMA; NEVCSHQ; -.
DR OrthoDB; 500021at2759; -.
DR TreeFam; TF328740; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 18536; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pcm1; mouse.
DR PRO; PR:Q9R0L6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R0L6; protein.
DR Bgee; ENSMUSG00000031592; Expressed in spermatocyte and 253 other tissues.
DR ExpressionAtlas; Q9R0L6; baseline and differential.
DR Genevisible; Q9R0L6; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:BHF-UCL.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; ISS:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IMP:BHF-UCL.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:BHF-UCL.
DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR InterPro; IPR031446; PCM1_C.
DR InterPro; IPR024138; Pericentriolar_Pcm1.
DR PANTHER; PTHR14164; PTHR14164; 1.
DR Pfam; PF15717; PCM1_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT CHAIN 2..2025
FT /note="Pericentriolar material 1 protein"
FT /id="PRO_0000274038"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..1458
FT /note="Mediates interaction with DZIP1"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..301
FT /evidence="ECO:0000255"
FT COILED 399..426
FT /evidence="ECO:0000255"
FT COILED 492..518
FT /evidence="ECO:0000255"
FT COILED 652..772
FT /evidence="ECO:0000255"
FT COILED 822..856
FT /evidence="ECO:0000255"
FT COILED 985..1017
FT /evidence="ECO:0000255"
FT COILED 1061..1086
FT /evidence="ECO:0000255"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1815
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 372
FT /note="Phosphoserine; by PLK4"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 857
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 875
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 1729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 1769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 1777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1959
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT MOD_RES 1978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15154"
FT VAR_SEQ 263
FT /note="R -> RENEEEDVRTVDSAVGSGSVAESTSLNADVQSEASDTTAR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.6"
FT /id="VSP_022612"
FT CONFLICT 305
FT /note="A -> T (in Ref. 4; AAH53728)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="Q -> R (in Ref. 4; AAH53728)"
FT /evidence="ECO:0000305"
FT CONFLICT 1216
FT /note="V -> I (in Ref. 6; AAK39513)"
FT /evidence="ECO:0000305"
FT CONFLICT 1329
FT /note="N -> S (in Ref. 6; AAK39513)"
FT /evidence="ECO:0000305"
FT CONFLICT 1819
FT /note="I -> V (in Ref. 1; BAA87861 and 6; AAK21980)"
FT /evidence="ECO:0000305"
FT CONFLICT 2018..2025
FT /note="ETVGAQSI -> GKSYQF (in Ref. 5; BAC30604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2025 AA; 228847 MW; 39D790997E6C5418 CRC64;
MATGGGPFEE VMHDQDLPNW SNDSVDDRLN NMEWGGQQKK ANRSSEKNKK KFGVASDKRV
TNAISPESSP GVGRRRTKIP HTFPHSRYMT QMSVPEQAEL EKLKQRINFS DLDQRSIGSD
SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDATASL PKREMTTSAQ CKELFASALS
NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT
HLIEHLKEQE KSYMKFLQKI LARDPQQEPM EETENLKKQH DLLKRMLQQQ EQLRALQGRQ
AALLALQHKA EQAIAVMDDS VVTETTGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA
VPDNRRQAES LSLTREISQS RNPSVSEHLP DEKVQLFSKM RVLQEKKQKM DKLLGELHNL
RDQHLNNSSF VPSTSLQRSG DKRSSTVALS APVGFASAVN GEANSLISSV PCPATSLVSQ
NESENEGHLN PAEKLQKLNE VQKRLNELRE LVHYYEQTSD MMTDAVNENT KDEETEESEY
DSEHENSEPV TNIRNPQVAS TWNEVNTNSN TQCGSNNRDG RPVNSNCEIN NRSAANIRAL
NMPPLDCRYN REGEQRLHVA HGEDEEEEVE EEGVSGASLS SRRSSLVDEA PEDEEFEQKI
SRLMAAKEKL KQLQDLVAMV QDDDATQVVV PAASNLDDFY AAEEDIKQNS NNARENSNKI
DTGVNEKTRE KFYEAKLQQQ QRELKQLQEE RKKLIEIQEK IQAVQKACPD LQLSATSISS
GPTKKYLPAI TSTPTVNEND SSTSKCVIDP EDSSVVDNEL WSDMRRHEML REELRQRRKQ
LEALMAEHQR RQGLAETSSP VAISLRSDGS ENLCTPQQSR TEKTMATWGG STQCALDEEG
DEDGYLSEGI VRTDEEEEEE QDASSNDNFP IYPPSMNQNS YNVKETKTRW KSNRPVSADG
NYRPLAKTRQ QNISMQRQEN LRWVSELSYI EEKEQWQEQI NQLKKQLDFS VNICQTLMQD
QQTLSCLLQT LLTGPYSVLP SNVASPQVHL IMHQLNQCYT QLTWQQNNVQ RLKQMLTELM
RQQNQHPEKP RSKERGSSAS HPSSPNLFCP FSFPTQPVNL FNLPGFTNFP SFAPGMNFSP
LFPSNFGDFS QNVSTPTEQQ QPLAQNPSGK TEYMAFPKPF ESSSSLGAEK QRNQKQPEEE
AENTKTPWLY DQEGGVEKPF FKTGFTESVE KATNSNRKNQ PDTSRRRRQF DEESLESFSS
MPDPIDPTTV TKTFKTRKAS AQASLASKDK TPKSKSKKRN STQLKSRVKN IGYESASVSS
TCEPCKNRNR HSAQTEEPVQ AKLFSRKNHE QLEKIIKYSR SAEISSETGS DFSMFEALRD
TIYSEVATLI SQNESRPHFL IELFHELQLL NTDYLRQRAL YALQDIVSRH ISESDEREGE
NVKPVNSGTW VASNSELTPS ESLVTTDDET FEKNFERETH KVSEQNDADN VSVMSVSSNF
EPFATDDLGN TVIHLDQALA RMREYERMKT ETESHSNMRC TCRVIEDEDG AAAAATVSNS
EETPIIENHN SPQPISDVSA VPCPRIDTQQ LDRQIKAIMK EVIPFLKEHM DEVCSSQLLT
SVRRMVLTLT QQNDESKEFV KFFHKQLGSI LQDSLAKFAG RKLKDCGEDL LVEISEVLFN
ELAFFKLMQD LDNNSIAVKQ RCKRKIEAAG VRQSYAKEAK RILEGDHGSP AGEIDDEDKD
KDETETVKQT QTSEVYDAKG PKNVRSDVSD QEEDEESERC PVSINLSKAE SQALTNYGSG
EDENEDEEME DFEESPVDIQ TSLQANTETT EENEHDSQIL QHDLEKTPES TNVPSDQEPT
SKNDQDSSPV KPCYLNILEN EQQLNSATHK DSLTTTDSSK QPEPLPLPLA ASETLVPRVK
EVKSAQETPE SSLAGSPDTE SPVLVNDYEA ESGNISQKSD EEDFVKVEDL PLKLTVYSEE
ELRKKMIEEE QKNHLSGEIC EMQTEELAGN SQILKEPETV GAQSI
