PCM1_HUMAN
ID PCM1_HUMAN Reviewed; 2024 AA.
AC Q15154; A6NNN6; B4DYD5; E7ETA6; E7EV56; Q58F13; Q6P1K7; Q8NB85; Q9BWC1;
AC Q9H4A2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 5.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Pericentriolar material 1 protein {ECO:0000305};
DE Short=PCM-1;
DE Short=hPCM-1;
GN Name=PCM1 {ECO:0000312|HGNC:HGNC:8727};
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), SUBCELLULAR LOCATION, AND VARIANTS
RP SER-159 AND VAL-597.
RC TISSUE=Liver;
RX PubMed=8120099; DOI=10.1083/jcb.124.5.783;
RA Balczon R., Bao L., Zimmer W.E.;
RT "PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle
RT distribution.";
RL J. Cell Biol. 124:783-793(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-404 (ISOFORMS 1/2), AND VARIANT SER-159.
RC TISSUE=Lung, Testis, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1244-2024 (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1527-1610 (ISOFORMS 1/2), SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH RET.
RX PubMed=10980597; DOI=10.1038/sj.onc.1203772;
RA Corvi R., Berger N., Balczon R., Romeo G.;
RT "RET/PCM-1: a novel fusion gene in papillary thyroid carcinoma.";
RL Oncogene 19:4236-4242(2000).
RN [6]
RP INTERACTION WITH HAP1.
RX PubMed=9361024; DOI=10.1093/hmg/6.13.2205;
RA Engelender S., Sharp A.H., Colomer V., Tokito M.K., Lanahan A., Worley P.,
RA Holzbaur E.L.F., Ross C.A.;
RT "Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued
RT subunit of dynactin.";
RL Hum. Mol. Genet. 6:2205-2212(1997).
RN [7]
RP FUNCTION, INTERACTION WITH CETN3, AND 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 [8]
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 [9]
RP INTERACTION WITH BBS8, AND SUBCELLULAR LOCATION.
RX PubMed=14520415; DOI=10.1038/nature02030;
RA Ansley S.J., Badano J.L., Blacque O.E., Hill J., Hoskins B.E., Leitch C.C.,
RA Kim J.C., Ross A.J., Eichers E.R., Teslovich T.M., Mah A.K., Johnsen R.C.,
RA Cavender J.C., Lewis R.A., Leroux M.R., Beales P.L., Katsanis N.;
RT "Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl
RT syndrome.";
RL Nature 425:628-633(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
RP INTERACTION WITH BBS4, AND SUBCELLULAR LOCATION.
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 [12]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15184884; DOI=10.1038/sj.onc.1207740;
RA Armes J.E., Hammet F., de Silva M., Ciciulla J., Ramus S.J., Soo W.-K.,
RA Mahoney A., Yarovaya N., Henderson M.A., Gish K., Hutchins A.-M.,
RA Price G.R., Venter D.J.;
RT "Candidate tumor-suppressor genes on chromosome arm 8p in early-onset and
RT high-grade breast cancers.";
RL Oncogene 23:5697-5702(2004).
RN [13]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16270321; DOI=10.1002/cncr.21538;
RA Pils D., Horak P., Gleiss A., Sax C., Fabjani G., Moebus V.J.,
RA Zielinski C., Reinthaller A., Zeillinger R., Krainer M.;
RT "Five genes from chromosomal band 8p22 are significantly down-regulated in
RT ovarian carcinoma: N33 and EFA6R have a potential impact on overall
RT survival.";
RL Cancer 104:2417-2429(2005).
RN [14]
RP CHROMOSOMAL TRANSLOCATION WITH JAK2.
RX PubMed=15805263; DOI=10.1158/0008-5472.can-04-4263;
RA Reiter A., Walz C., Watmore A., Schoch C., Blau I., Schlegelberger B.,
RA Berger U., Telford N., Aruliah S., Yin J.A., Vanstraelen D., Barker H.F.,
RA Taylor P.C., O'Driscoll A., Benedetti F., Rudolph C., Kolb H.-J.,
RA Hochhaus A., Hehlmann R., Chase A., Cross N.C.P.;
RT "The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute
RT leukemia that fuses PCM1 to JAK2.";
RL Cancer Res. 65:2662-2667(2005).
RN [15]
RP CHROMOSOMAL TRANSLOCATION WITH JAK2.
RX PubMed=16034466; DOI=10.1038/sj.leu.2403879;
RA Murati A., Gelsi-Boyer V., Adelaide J., Perot C., Talmant P., Giraudier S.,
RA Lode L., Letessier A., Delaval B., Brunel V., Imbert M., Garand R.,
RA Xerri L., Birnbaum D., Mozziconacci M.-J., Chaffanet M.;
RT "PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid
RT leukemia with t(8;9) translocation.";
RL Leukemia 19:1692-1696(2005).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15659651; DOI=10.1091/mbc.e04-08-0688;
RA Hames R.S., Crookes R.E., Straatman K.R., Merdes A., Hayes M.J.,
RA Faragher A.J., Fry A.M.;
RT "Dynamic recruitment of Nek2 kinase to the centrosome involves
RT microtubules, PCM-1, and localized proteasomal degradation.";
RL Mol. Biol. Cell 16:1711-1724(2005).
RN [17]
RP CHROMOSOMAL TRANSLOCATION WITH JAK2.
RX PubMed=16091753; DOI=10.1038/sj.onc.1208850;
RA Bousquet M., Quelen C., De Mas V., Duchayne E., Roquefeuil B., Delsol G.,
RA Laurent G., Dastugue N., Brousset P.;
RT "The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia
RT yields a new PCM1-JAK2 fusion gene.";
RL Oncogene 24:7248-7252(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-110 AND SER-1730, AND
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 [19]
RP CHROMOSOMAL TRANSLOCATION WITH JAK2.
RX PubMed=16769584;
RA Bacher U., Reiter A., Haferlach T., Mueller L., Schnittger S., Kern W.,
RA Schoch C.;
RT "A combination of cytomorphology, cytogenetic analysis, fluorescence in
RT situ hybridization and reverse transcriptase polymerase chain reaction for
RT establishing clonality in cases of persisting hypereosinophilia.";
RL Haematologica 91:817-820(2006).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16943179; DOI=10.1083/jcb.200606051;
RA Srsen V., Gnadt N., Dammermann A., Merdes A.;
RT "Inhibition of centrosome protein assembly leads to p53-dependent exit from
RT the cell cycle.";
RL J. Cell Biol. 174:625-630(2006).
RN [21]
RP TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH JAK2.
RX PubMed=16424865; DOI=10.1038/sj.leu.2404104;
RA Adelaide J., Perot C., Gelsi-Boyer V., Pautas C., Murati A.,
RA Copie-Bergman C., Imbert M., Chaffanet M., Birnbaum D., Mozziconacci M.-J.;
RT "A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell
RT lymphoma.";
RL Leukemia 20:536-537(2006).
RN [22]
RP INTERACTION WITH NDE1 AND NDEL1, AND SUBCELLULAR LOCATION.
RX PubMed=16291865; DOI=10.1091/mbc.e05-04-0360;
RA Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.;
RT "Nudel contributes to microtubule anchoring at the mother centriole and is
RT involved in both dynein-dependent and -independent centrosomal protein
RT assembly.";
RL Mol. Biol. Cell 17:680-689(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-69, AND
RP IDENTIFICATION BY 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69; SER-93;
RP SER-960; SER-1231; SER-1257; SER-1260; SER-1263; SER-1730; SER-1765;
RP SER-1768 AND SER-1776, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69; SER-93;
RP SER-1185; SER-1697; SER-1765; SER-1768; SER-1776 AND SER-1977, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [28]
RP FUNCTION.
RX PubMed=20551181; DOI=10.1242/jcs.065045;
RA Sedjai F., Acquaviva C., Chevrier V., Chauvin J.P., Coppin E., Aouane A.,
RA Coulier F., Tolun A., Pierres M., Birnbaum D., Rosnet O.;
RT "Control of ciliogenesis by FOR20, a novel centrosome and pericentriolar
RT satellite protein.";
RL J. Cell Sci. 123:2391-2401(2010).
RN [29]
RP INTERACTION WITH PARD6A, AND SUBCELLULAR LOCATION.
RX PubMed=20719959; DOI=10.1091/mbc.e10-05-0430;
RA Kodani A., Tonthat V., Wu B., Suetterlin C.;
RT "Par6 alpha interacts with the dynactin subunit p150 Glued and is a
RT critical regulator of centrosomal protein recruitment.";
RL Mol. Biol. Cell 21:3376-3385(2010).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69; SER-93;
RP SER-861; SER-960 AND SER-1730, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-1730;
RP SER-1765; SER-1768 AND SER-1958, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [34]
RP FUNCTION IN CILIOGENESIS, UBIQUITINATION BY MIB1, INTERACTION WITH CEP131,
RP ASSOCIATION WITH MICROTUBULE, 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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69; SER-93;
RP SER-110; SER-116; SER-119; SER-370; SER-372; SER-384; SER-588; THR-859;
RP SER-861; SER-960; SER-977; SER-988; SER-991; SER-1229; SER-1231; SER-1257;
RP SER-1697; SER-1730 AND SER-1977, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-159 (VARIANT SER-159), VARIANT [LARGE SCALE ANALYSIS] SER-159, AND
RP IDENTIFICATION BY 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 [36]
RP INTERACTION WITH MAP1LC3B; GABARAPAL2 AND GABARAP.
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 [37]
RP INTERACTION WITH CCDC13.
RX PubMed=24816561; DOI=10.1242/jcs.147785;
RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Howard A.E.,
RA Barone G., Lee A.J., Swanton C., Howell M., Maslen S., Skehel J.M.,
RA Boulton S.J., Collis S.J.;
RT "Ccdc13 is a novel human centriolar satellite protein required for
RT ciliogenesis and genome stability.";
RL J. Cell Sci. 127:2910-2919(2014).
RN [38]
RP INTERACTION WITH CCDC113.
RX PubMed=25074808; DOI=10.1242/jcs.157008;
RA Firat-Karalar E.N., Sante J., Elliott S., Stearns T.;
RT "Proteomic analysis of mammalian sperm cells identifies new components of
RT the centrosome.";
RL J. Cell Sci. 127:4128-4133(2014).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1468, AND IDENTIFICATION BY
RP 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 [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [41]
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 [42]
RP FUNCTION, INTERACTION WITH DZIP1, AND REGION.
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).
RN [43]
RP INTERACTION WITH CCDC66.
RX PubMed=28235840; DOI=10.1242/jcs.196832;
RA Conkar D., Culfa E., Odabasi E., Rauniyar N., Yates J.R. III,
RA Firat-Karalar E.N.;
RT "The centriolar satellite protein CCDC66 interacts with CEP290 and
RT functions in cilium formation and trafficking.";
RL J. Cell Sci. 130:1450-1462(2017).
RN [44]
RP PHOSPHORYLATION.
RX PubMed=29973724; DOI=10.1038/s41586-018-0279-8;
RA Rai A.K., Chen J.X., Selbach M., Pelkmans L.;
RT "Kinase-controlled phase transition of membraneless organelles in
RT mitosis.";
RL Nature 559:211-216(2018).
RN [45]
RP PHOSPHORYLATION AT SER-372, MUTAGENESIS OF SER-372, AND SUBCELLULAR
RP LOCATION.
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 [46]
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).
RN [47]
RP FUNCTION, INTERACTION WITH CSTPP1; TTLL1; TPGS1 AND LRRC49, AND SUBCELLULAR
RP LOCATION.
RX PubMed=34782749; DOI=10.1038/s41422-021-00584-9;
RA Wang L., Paudyal S.C., Kang Y., Owa M., Liang F.X., Spektor A., Knaut H.,
RA Sanchez I., Dynlacht B.D.;
RT "Regulators of tubulin polyglutamylation control nuclear shape and cilium
RT disassembly by balancing microtubule and actin assembly.";
RL Cell Res. 32:190-209(2022).
CC -!- FUNCTION: Required for centrosome assembly and function
CC (PubMed:12403812, PubMed:15659651, PubMed:16943179). Essential for the
CC correct localization of several centrosomal proteins including CEP250,
CC CETN3, PCNT and NEK2 (PubMed:12403812, PubMed:15659651). Required to
CC anchor microtubules to the centrosome (PubMed:12403812,
CC PubMed:15659651). Also involved in cilium biogenesis by recruiting the
CC BBSome, a ciliary protein complex involved in cilium biogenesis, to the
CC centriolar satellites (PubMed:20551181, PubMed:24121310,
CC PubMed:27979967). Recruits the tubulin polyglutamylase complex (TPGC)
CC to centriolar satellites (PubMed:34782749).
CC {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:15659651,
CC ECO:0000269|PubMed:16943179, ECO:0000269|PubMed:20551181,
CC ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:27979967,
CC ECO:0000269|PubMed:34782749}.
CC -!- SUBUNIT: Self-associates. Interacts with C2CD3 (By similarity).
CC Interacts with BBS4, BBS8, CETN3, HAP1, NDE1, NDEL1, MAP1LC3B,
CC GABARAPAL2, and GABARAP (PubMed:12403812, PubMed:14520415,
CC PubMed:15107855, PubMed:16291865, PubMed:24089205, PubMed:9361024).
CC Interacts with CEP131; the interaction increases in response to
CC ultraviolet light (UV) radiation (PubMed:24121310). Associates with
CC microtubule; association to microtubule is reduced 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
CC (PubMed:24121310). Interacts with CCDC113 (PubMed:25074808). Interacts
CC with SSX2IP (By similarity). Interacts with CCDC13 (PubMed:24816561).
CC Interacts with CEP290 (By similarity). Interacts with PARD6A
CC (PubMed:20719959). Interacts with KIAA0753/OFIP, CEP20/FOR20 and OFD1;
CC the interaction with CEP20/FOR20 and OFD1 may be mediated by
CC KIAA0753/OFIP (PubMed:26643951). Interacts with CCDC66
CC (PubMed:28235840). Interacts with CCDC61 (PubMed:31789463). Interacts
CC with DZIP1; localizes DZIP1 and the associated BBSome to centriolar
CC satellite (PubMed:27979967). Interacts with CSTPP1, TTLL1, TPGS1 and
CC LRRC49 (PubMed:34782749). {ECO:0000250|UniProtKB:Q9R0L6,
CC ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:14520415,
CC ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:16291865,
CC ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:24089205,
CC ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:24816561,
CC ECO:0000269|PubMed:25074808, ECO:0000269|PubMed:26643951,
CC ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:28235840,
CC ECO:0000269|PubMed:31789463, ECO:0000269|PubMed:34782749,
CC ECO:0000269|PubMed:9361024}.
CC -!- INTERACTION:
CC Q15154; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-741421, EBI-743598;
CC Q15154; Q8NFJ9: BBS1; NbExp=2; IntAct=EBI-741421, EBI-1805484;
CC Q15154; Q96RK4: BBS4; NbExp=17; IntAct=EBI-741421, EBI-1805814;
CC Q15154; Q49A88: CCDC14; NbExp=6; IntAct=EBI-741421, EBI-751035;
CC Q15154; Q9UPN4: CEP131; NbExp=5; IntAct=EBI-741421, EBI-2558372;
CC Q15154; Q9P209: CEP72; NbExp=7; IntAct=EBI-741421, EBI-739498;
CC Q15154; O95166: GABARAP; NbExp=8; IntAct=EBI-741421, EBI-712001;
CC Q15154; P60520: GABARAPL2; NbExp=2; IntAct=EBI-741421, EBI-720116;
CC Q15154; Q2KHM9: KIAA0753; NbExp=7; IntAct=EBI-741421, EBI-2805604;
CC Q15154; O75665: OFD1; NbExp=8; IntAct=EBI-741421, EBI-716327;
CC Q15154; O95613: PCNT; NbExp=8; IntAct=EBI-741421, EBI-530012;
CC Q15154; Q8WXW3: PIBF1; NbExp=7; IntAct=EBI-741421, EBI-2558770;
CC Q15154; Q96R06: SPAG5; NbExp=2; IntAct=EBI-741421, EBI-413317;
CC Q15154; Q9Y2D8: SSX2IP; NbExp=10; IntAct=EBI-741421, EBI-2212028;
CC Q15154; Q9Y3C0: WASHC3; NbExp=5; IntAct=EBI-741421, EBI-712969;
CC Q15154; P54256: Hap1; Xeno; NbExp=3; IntAct=EBI-741421, EBI-994539;
CC Q15154-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11742977, EBI-11096309;
CC Q15154-3; Q8TD31-3: CCHCR1; NbExp=5; IntAct=EBI-11742977, EBI-10175300;
CC Q15154-3; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-11742977, EBI-11521003;
CC Q15154-3; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-11742977, EBI-742102;
CC Q15154-3; Q8TBF8: FAM81A; NbExp=5; IntAct=EBI-11742977, EBI-11993062;
CC Q15154-3; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-11742977, EBI-348259;
CC Q15154-3; Q7Z6G3-2: NECAB2; NbExp=5; IntAct=EBI-11742977, EBI-10172876;
CC Q15154-3; Q15311: RALBP1; NbExp=3; IntAct=EBI-11742977, EBI-749285;
CC Q15154-3; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-11742977, EBI-712969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8AV28}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:30804208}. Cytoplasmic
CC granule {ECO:0000269|PubMed:15107855}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:20719959,
CC ECO:0000269|PubMed:31789463, ECO:0000269|PubMed:34782749}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:24121310}.
CC Note=Recruitment to the centrosome requires microtubules and dynein.
CC The majority of the protein dissociates from the centrosome during
CC metaphase and subsequently localizes to the cleavage site in telophase.
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q15154-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15154-2; Sequence=VSP_022611;
CC Name=3;
CC IsoId=Q15154-3; Sequence=VSP_022609, VSP_022610;
CC Name=4;
CC IsoId=Q15154-4; Sequence=VSP_059399, VSP_022611, VSP_059401;
CC Name=5;
CC IsoId=Q15154-5; Sequence=VSP_059400;
CC -!- TISSUE SPECIFICITY: Expressed in blood, bone marrow, breast, lymph
CC node, ovary and thyroid. {ECO:0000269|PubMed:10980597,
CC ECO:0000269|PubMed:15184884, ECO:0000269|PubMed:16270321,
CC ECO:0000269|PubMed:16424865}.
CC -!- INDUCTION: Expression is reduced in breast and ovarian cancer.
CC {ECO:0000269|PubMed:15184884, ECO:0000269|PubMed:16270321}.
CC -!- PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3
CC ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia
CC formation (PubMed:24121310). Monoubiquitination by MIB1 is inhibited in
CC response to cellular stress, such as ultraviolet light (UV) radiation
CC or heat shock, resulting in cilia formation initiation
CC (PubMed:24121310). {ECO:0000269|PubMed:24121310}.
CC -!- PTM: Variant Ser-159 is phosphorylated. {ECO:0007744|PubMed:23186163}.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues by DYRK3
CC during the G2-to-M transition, after the nuclear-envelope breakdown
CC (PubMed:29973724). Phosphorylation by DYRK3 promotes disassembly of
CC pericentriolar material (PubMed:29973724). Phosphorylation at Ser-372
CC mediated by PLK4 is required to maintain the integrity of centriolar
CC satellites (PubMed:30804208). {ECO:0000269|PubMed:29973724,
CC ECO:0000269|PubMed:30804208}.
CC -!- DISEASE: Note=A chromosomal aberration involving PCM1 is found in
CC papillary thyroid carcinomas (PTCs) (PubMed:10980597). Translocation
CC t(8;10)(p21.3;q11.2) with RET links the protein kinase domain of RET to
CC the major portion of PCM1 (PubMed:10980597).
CC {ECO:0000269|PubMed:10980597}.
CC -!- DISEASE: Note=A chromosomal aberration involving PCM1 is found in a
CC variety of hematological malignancies including atypical chronic
CC myeloid leukemia (atypical CML) and T-cell lymphoma (PubMed:15805263,
CC PubMed:16034466, PubMed:16091753, PubMed:16769584, PubMed:16424865).
CC Translocation t(8;9)(p22;p24) with JAK2 links the protein kinase domain
CC of JAK2 to the major portion of PCM1 (PubMed:15805263, PubMed:16034466,
CC PubMed:16091753, PubMed:16769584, PubMed:16424865).
CC {ECO:0000269|PubMed:15805263, ECO:0000269|PubMed:16034466,
CC ECO:0000269|PubMed:16091753, ECO:0000269|PubMed:16424865,
CC ECO:0000269|PubMed:16769584}.
CC -!- SIMILARITY: Belongs to the PCM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27477.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH65022.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC03656.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC14882.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; L27841; AAA60120.1; -; mRNA.
DR EMBL; AC087273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000453; AAH00453.1; -; mRNA.
DR EMBL; BC027477; AAH27477.1; ALT_SEQ; mRNA.
DR EMBL; BC065022; AAH65022.1; ALT_SEQ; mRNA.
DR EMBL; AK091406; BAC03656.1; ALT_INIT; mRNA.
DR EMBL; AJ297349; CAC14882.1; ALT_SEQ; mRNA.
DR CCDS; CCDS47812.1; -. [Q15154-1]
DR CCDS; CCDS83255.1; -. [Q15154-4]
DR CCDS; CCDS83256.1; -. [Q15154-5]
DR CCDS; CCDS87582.1; -. [Q15154-3]
DR PIR; A54103; A54103.
DR RefSeq; NP_001302437.1; NM_001315508.1.
DR RefSeq; NP_006188.3; NM_006197.3.
DR PDB; 6HYL; X-ray; 1.56 A; A/B=1959-1972.
DR PDB; 6HYM; X-ray; 1.86 A; A/B=1959-1972.
DR PDBsum; 6HYL; -.
DR PDBsum; 6HYM; -.
DR AlphaFoldDB; Q15154; -.
DR SMR; Q15154; -.
DR BioGRID; 111139; 438.
DR CORUM; Q15154; -.
DR DIP; DIP-42189N; -.
DR IntAct; Q15154; 315.
DR MINT; Q15154; -.
DR STRING; 9606.ENSP00000327077; -.
DR MoonDB; Q15154; Predicted.
DR CarbonylDB; Q15154; -.
DR GlyGen; Q15154; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15154; -.
DR MetOSite; Q15154; -.
DR PhosphoSitePlus; Q15154; -.
DR BioMuta; PCM1; -.
DR DMDM; 296439495; -.
DR EPD; Q15154; -.
DR jPOST; Q15154; -.
DR MassIVE; Q15154; -.
DR PaxDb; Q15154; -.
DR PeptideAtlas; Q15154; -.
DR PRIDE; Q15154; -.
DR ProteomicsDB; 1623; -.
DR ProteomicsDB; 18163; -.
DR ProteomicsDB; 18571; -.
DR ProteomicsDB; 60471; -. [Q15154-1]
DR ProteomicsDB; 60472; -. [Q15154-2]
DR ProteomicsDB; 60473; -. [Q15154-3]
DR Antibodypedia; 5155; 228 antibodies from 31 providers.
DR DNASU; 5108; -.
DR Ensembl; ENST00000325083.13; ENSP00000327077.8; ENSG00000078674.19.
DR GeneID; 5108; -.
DR KEGG; hsa:5108; -.
DR UCSC; uc003wyi.5; human. [Q15154-1]
DR UCSC; uc003wyj.5; human.
DR UCSC; uc011kyh.3; human.
DR CTD; 5108; -.
DR DisGeNET; 5108; -.
DR GeneCards; PCM1; -.
DR HGNC; HGNC:8727; PCM1.
DR HPA; ENSG00000078674; Low tissue specificity.
DR MalaCards; PCM1; -.
DR MIM; 600299; gene.
DR neXtProt; NX_Q15154; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA33073; -.
DR VEuPathDB; HostDB:ENSG00000078674; -.
DR eggNOG; ENOG502QRMF; Eukaryota.
DR InParanoid; Q15154; -.
DR OrthoDB; 500021at2759; -.
DR PhylomeDB; Q15154; -.
DR TreeFam; TF328740; -.
DR PathwayCommons; Q15154; -.
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; Q15154; -.
DR SIGNOR; Q15154; -.
DR BioGRID-ORCS; 5108; 110 hits in 1083 CRISPR screens.
DR ChiTaRS; PCM1; human.
DR GeneWiki; PCM1; -.
DR GenomeRNAi; 5108; -.
DR Pharos; Q15154; Tbio.
DR PRO; PR:Q15154; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15154; protein.
DR Bgee; ENSG00000078674; Expressed in calcaneal tendon and 203 other tissues.
DR ExpressionAtlas; Q15154; baseline and differential.
DR Genevisible; Q15154; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000242; C:pericentriolar material; ISS:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0007098; P:centrosome cycle; IMP:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0022027; P:interkinetic nuclear migration; ISS:BHF-UCL.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; ISS:BHF-UCL.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IBA:GO_Central.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISS:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:GO_Central.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:SYSCILIA_CCNET.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Chromosomal rearrangement; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..2024
FT /note="Pericentriolar material 1 protein"
FT /id="PRO_0000274037"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..1460
FT /note="Mediates interaction with DZIP1"
FT /evidence="ECO:0000269|PubMed:27979967"
FT REGION 111..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1799
FT /note="Interaction with HAP1"
FT /evidence="ECO:0000269|PubMed:9361024"
FT REGION 1725..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1880..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..2024
FT /note="Interaction with BBS4"
FT /evidence="ECO:0000269|PubMed:15107855"
FT REGION 2005..2024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..301
FT /evidence="ECO:0000255"
FT COILED 400..424
FT /evidence="ECO:0000255"
FT COILED 487..543
FT /evidence="ECO:0000255"
FT COILED 651..682
FT /evidence="ECO:0000255"
FT COILED 726..769
FT /evidence="ECO:0000255"
FT COILED 824..858
FT /evidence="ECO:0000255"
FT COILED 1063..1089
FT /evidence="ECO:0000255"
FT COILED 1515..1539
FT /evidence="ECO:0000255"
FT COMPBIAS 40..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1814
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1314..1315
FT /note="Breakpoint for translocation to form PCM1-JAK2
FT fusion protein"
FT SITE 1369..1370
FT /note="Breakpoint for translocation to form PCM1-JAK2
FT fusion protein"
FT SITE 1470..1471
FT /note="Breakpoint for translocation to form PCM1-JAK2
FT fusion protein"
FT SITE 1609..1610
FT /note="Breakpoint for translocation to form PCM1-RET fusion
FT protein"
FT SITE 1947..1948
FT /note="Breakpoint for translocation to form PCM1-JAK2
FT fusion protein"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine; in variant Ser-159"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine; by PLK4"
FT /evidence="ECO:0000269|PubMed:30804208,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 859
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 877
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 1468
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 1697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0L6"
FT MOD_RES 1958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 263
FT /note="R -> RENEEEDVRTIDSAVGSGSVAESTSLNIDVQSEASDTTAR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022609"
FT VAR_SEQ 492..2024
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022610"
FT VAR_SEQ 601
FT /note="L -> LA (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_059399"
FT VAR_SEQ 1315..1370
FT /note="RYESASMSSTCEPCKSRNRHSAQTEEPVQAKVFSRKNHEQLEKIIKCNRSTE
FT ISSE -> K (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022611"
FT VAR_SEQ 1556..1563
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_059400"
FT VAR_SEQ 1838..1947
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_059401"
FT VARIANT 159
FT /note="N -> S (phosphorylated; dbSNP:rs412750)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8120099, ECO:0007744|PubMed:23186163"
FT /id="VAR_030164"
FT VARIANT 176
FT /note="A -> D (in dbSNP:rs2285302)"
FT /id="VAR_030165"
FT VARIANT 597
FT /note="M -> V (in dbSNP:rs208753)"
FT /evidence="ECO:0000269|PubMed:8120099"
FT /id="VAR_030166"
FT VARIANT 600
FT /note="S -> P (in dbSNP:rs34325017)"
FT /id="VAR_047381"
FT VARIANT 691
FT /note="A -> S (in dbSNP:rs17635381)"
FT /id="VAR_030167"
FT VARIANT 871
FT /note="G -> V (in dbSNP:rs7009117)"
FT /id="VAR_030168"
FT VARIANT 1251
FT /note="R -> H (in dbSNP:rs17514547)"
FT /id="VAR_030169"
FT VARIANT 1326
FT /note="E -> D (in dbSNP:rs34932823)"
FT /id="VAR_047382"
FT VARIANT 1543
FT /note="T -> I (in dbSNP:rs370429)"
FT /id="VAR_030170"
FT VARIANT 1701
FT /note="K -> N (in dbSNP:rs36113670)"
FT /id="VAR_047383"
FT VARIANT 1865
FT /note="N -> D (in dbSNP:rs35789133)"
FT /id="VAR_047384"
FT MUTAGEN 372
FT /note="S->D: Phosphomimetic mutant."
FT /evidence="ECO:0000269|PubMed:30804208"
FT CONFLICT 294
FT /note="R -> RG (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="EQ -> DE (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="E -> K (in Ref. 3; AAH27477)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="Q -> K (in Ref. 3; AAH27477/AAH65022)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="A -> S (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 447..448
FT /note="SV -> CL (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="Q -> H (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="G -> R (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="R -> T (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="Missing (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1086
FT /note="Q -> R (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1168
FT /note="Q -> R (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169
FT /note="N -> I (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1170
FT /note="S -> L (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="V -> L (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="R -> Q (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1532
FT /note="T -> A (in Ref. 4; BAC03656)"
FT /evidence="ECO:0000305"
FT CONFLICT 1849
FT /note="S -> G (in Ref. 4; BAC03656)"
FT /evidence="ECO:0000305"
FT CONFLICT 1853..1864
FT /note="PLEREATSKNDQ -> HWNEKPLVKMTK (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1872
FT /note="C -> S (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1988
FT /note="E -> V (in Ref. 4; BAC03656)"
FT /evidence="ECO:0000305"
FT CONFLICT 1998
FT /note="I -> M (in Ref. 1; AAA60120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2024 AA; 228544 MW; 4625B991A443B6F3 CRC64;
MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK KFGVESDKRV
TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL EKLKQRINFS DLDQRSIGSD
SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDASTNP PNRETIGSAQ CKELFASALS
NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT
HLIDHLKEQE KSYMKFLKKI LARDPQQEPM EEIENLKKQH DLLKRMLQQQ EQLRALQGRQ
AALLALQHKA EQAIAVMDDS VVAETAGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA
VPDNRRQAES LSLTREVSQS RKPSASERLP DEKVELFSKM RVLQEKKQKM DKLLGELHTL
RDQHLNNSSA SPQRSVDQRS TSAPSASVGL APVVNGESNS LTSSVPYPTA SLVSQNESEN
EGHLNPSEKL QKLNEVRKRL NELRELVHYY EQTSDMMTDA VNENRKDEET EESEYDSEHE
NSEPVTNIRN PQVASTWNEV NSHSNAQCVS NNRDGRTVNS NCEINNRSAA NIRALNMPPS
LDCRYNREGE QEIHVAQGED DEEEEEEAEE EGVSGASLSS HRSSLVDEHP EDAEFEQKIN
RLMAAKQKLR QLQDLVAMVQ DDDAAQGVIS ASASNLDDFY PAEEDTKQNS NNTRGNANKT
QKDTGVNEKA REKFYEAKLQ QQQRELKQLQ EERKKLIDIQ EKIQALQTAC PDLQLSAASV
GNCPTKKYMP AVTSTPTVNQ HETSTSKSVF EPEDSSIVDN ELWSEMRRHE MLREELRQRR
KQLEALMAEH QRRQGLAETA SPVAVSLRSD GSENLCTPQQ SRTEKTMATW GGSTQCALDE
EGDEDGYLSE GIVRTDEEEE EEQDASSNDN FSVCPSNSVN HNSYNGKETK NRWKNNCPFS
ADENYRPLAK TRQQNISMQR QENLRWVSEL SYVEEKEQWQ EQINQLKKQL DFSVSICQTL
MQDQQTLSCL LQTLLTGPYS VMPSNVASPQ VHFIMHQLNQ CYTQLTWQQN NVQRLKQMLN
ELMRQQNQHP EKPGGKERGS SASHPPSPSL FCPFSFPTQP VNLFNIPGFT NFSSFAPGMN
FSPLFPSNFG DFSQNISTPS EQQQPLAQNS SGKTEYMAFP KPFESSSSIG AEKPRNKKLP
EEEVESSRTP WLYEQEGEVE KPFIKTGFSV SVEKSTSSNR KNQLDTNGRR RQFDEESLES
FSSMPDPVDP TTVTKTFKTR KASAQASLAS KDKTPKSKSK KRNSTQLKSR VKNIRYESAS
MSSTCEPCKS RNRHSAQTEE PVQAKVFSRK NHEQLEKIIK CNRSTEISSE TGSDFSMFEA
LRDTIYSEVA TLISQNESRP HFLIELFHEL QLLNTDYLRQ RALYALQDIV SRHISESHEK
GENVKSVNSG TWIASNSELT PSESLATTDD ETFEKNFERE THKISEQNDA DNASVLSVSS
NFEPFATDDL GNTVIHLDQA LARMREYERM KTEAESNSNM RCTCRIIEDG DGAGAGTTVN
NLEETPVIEN RSSQQPVSEV STIPCPRIDT QQLDRQIKAI MKEVIPFLKE HMDEVCSSQL
LTSVRRMVLT LTQQNDESKE FVKFFHKQLG SILQDSLAKF AGRKLKDCGE DLLVEISEVL
FNELAFFKLM QDLDNNSITV KQRCKRKIEA TGVIQSCAKE AKRILEDHGS PAGEIDDEDK
DKDETETVKQ TQTSEVYDGP KNVRSDISDQ EEDEESEGCP VSINLSKAET QALTNYGSGE
DENEDEEMEE FEEGPVDVQT SLQANTEATE ENEHDEQVLQ RDFKKTAESK NVPLEREATS
KNDQNNCPVK PCYLNILEDE QPLNSAAHKE SPPTVDSTQQ PNPLPLRLPE MEPLVPRVKE
VKSAQETPES SLAGSPDTES PVLVNDYEAE SGNISQKSDE EDFVKVEDLP LKLTIYSEAD
LRKKMVEEEQ KNHLSGEICE MQTEELAGNS ETLKEPETVG AQSI
