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 24-JAN-2024, sequence version 6. DT 27-MAR-2024, entry version 182. 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 CFAP263. 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 CFAP263 (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; P62258: YWHAE; NbExp=3; IntAct=EBI-741421, EBI-356498; CC Q15154; P63104: YWHAZ; NbExp=2; IntAct=EBI-741421, EBI-347088; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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. [Q15154-4] DR RefSeq; NP_006188.3; NM_006197.3. [Q15154-1] DR RefSeq; XP_016868972.1; XM_017013483.1. DR RefSeq; XP_016868973.1; XM_017013484.1. DR RefSeq; XP_016868983.1; XM_017013494.1. DR RefSeq; XP_016868984.1; XM_017013495.1. DR RefSeq; XP_016868985.1; XM_017013496.1. 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 PDB; 7Q46; X-ray; 2.46 A; B/D/F=1737-1751. DR PDBsum; 6HYL; -. DR PDBsum; 6HYM; -. DR PDBsum; 7Q46; -. DR AlphaFoldDB; Q15154; -. DR SMR; Q15154; -. DR BioGRID; 111139; 475. DR CORUM; Q15154; -. DR DIP; DIP-42189N; -. DR IntAct; Q15154; 328. DR MINT; Q15154; -. DR STRING; 9606.ENSP00000327077; -. DR MoonDB; Q15154; Predicted. DR TCDB; 3.A.33.1.1; the bbsome complex (bbsome) family. DR CarbonylDB; Q15154; -. DR GlyGen; Q15154; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000327077; -. DR PeptideAtlas; 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 Pumba; Q15154; -. DR Antibodypedia; 5155; 246 antibodies from 31 providers. DR DNASU; 5108; -. DR Ensembl; ENST00000325083.13; ENSP00000327077.8; ENSG00000078674.20. [Q15154-1] DR Ensembl; ENST00000518537.5; ENSP00000428123.1; ENSG00000078674.20. [Q15154-3] DR Ensembl; ENST00000519253.5; ENSP00000431099.1; ENSG00000078674.20. [Q15154-5] DR Ensembl; ENST00000524226.5; ENSP00000430521.1; ENSG00000078674.20. [Q15154-4] DR GeneID; 5108; -. DR KEGG; hsa:5108; -. DR MANE-Select; ENST00000325083.13; ENSP00000327077.8; NM_006197.4; NP_006188.4. DR UCSC; uc003wyi.5; human. [Q15154-1] DR UCSC; uc003wyj.5; human. DR UCSC; uc011kyh.3; human. DR AGR; HGNC:8727; -. 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 OpenTargets; ENSG00000078674; -. DR Orphanet; 146; Differentiated thyroid carcinoma. DR PharmGKB; PA33073; -. DR VEuPathDB; HostDB:ENSG00000078674; -. DR eggNOG; ENOG502QRMF; Eukaryota. DR GeneTree; ENSGT00390000006641; -. DR InParanoid; Q15154; -. DR OrthoDB; 3090106at2759; -. 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; 123 hits in 1163 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 205 other cell types or tissues. DR ExpressionAtlas; Q15154; baseline and differential. 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:0060090; F:molecular adaptor activity; IDA:UniProt. 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:0140706; P:protein-containing complex localization to centriolar satellite; IDA:UniProt. DR GO; GO:0061635; P:regulation of protein complex stability; IDA:UniProt. DR GO; GO:0035176; P:social behavior; IEA:Ensembl. DR InterPro; IPR031446; PCM1_C. DR InterPro; IPR024138; Pericentriolar_Pcm1. DR PANTHER; PTHR14164:SF12; PERICENTRIOLAR MATERIAL 1 PROTEIN; 1. DR PANTHER; PTHR14164; PERICENTRIOLAR MATERIAL 1-RELATED; 1. DR Pfam; PF15717; PCM1_C; 1. DR Genevisible; Q15154; HS. 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 421..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 421..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 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; 228560 MW; E798EB3903036E23 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 RDQHLNNSSS 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 //