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Pericentriolar material 1 protein (PCM-1) (hPCM-1)

 PCM1_HUMAN              Reviewed;        2024 AA.
Q15154; Q58F13; Q6P1K7; Q8NB85; Q9BWC1; Q9H4A2;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
30-AUG-2017, entry version 139.
RecName: Full=Pericentriolar material 1 protein;
Short=PCM-1;
Short=hPCM-1;
Name=PCM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
VARIANT VAL-597.
TISSUE=Liver;
PubMed=8120099; DOI=10.1083/jcb.124.5.783;
Balczon R., Bao L., Zimmer W.E.;
"PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle
distribution.";
J. Cell Biol. 124:783-793(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-597.
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-404 (ISOFORMS 1/2).
TISSUE=Lung, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1244-2024 (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1527-1610 (ISOFORMS 1/2), SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH RET.
PubMed=10980597; DOI=10.1038/sj.onc.1203772;
Corvi R., Berger N., Balczon R., Romeo G.;
"RET/PCM-1: a novel fusion gene in papillary thyroid carcinoma.";
Oncogene 19:4236-4242(2000).
[6]
INTERACTION WITH HAP1.
PubMed=9361024; DOI=10.1093/hmg/6.13.2205;
Engelender S., Sharp A.H., Colomer V., Tokito M.K., Lanahan A.,
Worley P., Holzbaur E.L.F., Ross C.A.;
"Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued
subunit of dynactin.";
Hum. Mol. Genet. 6:2205-2212(1997).
[7]
FUNCTION, INTERACTION WITH CETN3, AND SUBCELLULAR LOCATION.
PubMed=12403812; DOI=10.1083/jcb.200204023;
Dammermann A., Merdes A.;
"Assembly of centrosomal proteins and microtubule organization depends
on PCM-1.";
J. Cell Biol. 159:255-266(2002).
[8]
INTERACTION WITH BBS8, AND SUBCELLULAR LOCATION.
PubMed=14520415; DOI=10.1038/nature02030;
Ansley S.J., Badano J.L., Blacque O.E., Hill J., Hoskins B.E.,
Leitch C.C., Kim J.C., Ross A.J., Eichers E.R., Teslovich T.M.,
Mah A.K., Johnsen R.C., Cavender J.C., Lewis R.A., Leroux M.R.,
Beales P.L., Katsanis N.;
"Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl
syndrome.";
Nature 425:628-633(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
INTERACTION WITH BBS4, AND SUBCELLULAR LOCATION.
PubMed=15107855; DOI=10.1038/ng1352;
Kim J.C., Badano J.L., Sibold S., Esmail M.A., Hill J., Hoskins B.E.,
Leitch C.C., Venner K., Ansley S.J., Ross A.J., Leroux M.R.,
Katsanis N., Beales P.L.;
"The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar
region and is required for microtubule anchoring and cell cycle
progression.";
Nat. Genet. 36:462-470(2004).
[11]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15184884; DOI=10.1038/sj.onc.1207740;
Armes J.E., Hammet F., de Silva M., Ciciulla J., Ramus S.J.,
Soo W.-K., Mahoney A., Yarovaya N., Henderson M.A., Gish K.,
Hutchins A.-M., Price G.R., Venter D.J.;
"Candidate tumor-suppressor genes on chromosome arm 8p in early-onset
and high-grade breast cancers.";
Oncogene 23:5697-5702(2004).
[12]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16270321; DOI=10.1002/cncr.21538;
Pils D., Horak P., Gleiss A., Sax C., Fabjani G., Moebus V.J.,
Zielinski C., Reinthaller A., Zeillinger R., Krainer M.;
"Five genes from chromosomal band 8p22 are significantly down-
regulated in ovarian carcinoma: N33 and EFA6R have a potential impact
on overall survival.";
Cancer 104:2417-2429(2005).
[13]
CHROMOSOMAL TRANSLOCATION WITH JAK2.
PubMed=15805263; DOI=10.1158/0008-5472.CAN-04-4263;
Reiter A., Walz C., Watmore A., Schoch C., Blau I., Schlegelberger B.,
Berger U., Telford N., Aruliah S., Yin J.A., Vanstraelen D.,
Barker H.F., Taylor P.C., O'Driscoll A., Benedetti F., Rudolph C.,
Kolb H.-J., Hochhaus A., Hehlmann R., Chase A., Cross N.C.P.;
"The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute
leukemia that fuses PCM1 to JAK2.";
Cancer Res. 65:2662-2667(2005).
[14]
CHROMOSOMAL TRANSLOCATION WITH JAK2.
PubMed=16034466; DOI=10.1038/sj.leu.2403879;
Murati A., Gelsi-Boyer V., Adelaide J., Perot C., Talmant P.,
Giraudier S., Lode L., Letessier A., Delaval B., Brunel V., Imbert M.,
Garand R., Xerri L., Birnbaum D., Mozziconacci M.-J., Chaffanet M.;
"PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid
leukemia with t(8;9) translocation.";
Leukemia 19:1692-1696(2005).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15659651; DOI=10.1091/mbc.E04-08-0688;
Hames R.S., Crookes R.E., Straatman K.R., Merdes A., Hayes M.J.,
Faragher A.J., Fry A.M.;
"Dynamic recruitment of Nek2 kinase to the centrosome involves
microtubules, PCM-1, and localized proteasomal degradation.";
Mol. Biol. Cell 16:1711-1724(2005).
[16]
CHROMOSOMAL TRANSLOCATION WITH JAK2.
PubMed=16091753; DOI=10.1038/sj.onc.1208850;
Bousquet M., Quelen C., De Mas V., Duchayne E., Roquefeuil B.,
Delsol G., Laurent G., Dastugue N., Brousset P.;
"The t(8;9)(p22;p24) translocation in atypical chronic myeloid
leukaemia yields a new PCM1-JAK2 fusion gene.";
Oncogene 24:7248-7252(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-110 AND
SER-1730, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[18]
CHROMOSOMAL TRANSLOCATION WITH JAK2.
PubMed=16769584;
Bacher U., Reiter A., Haferlach T., Mueller L., Schnittger S.,
Kern W., Schoch C.;
"A combination of cytomorphology, cytogenetic analysis, fluorescence
in situ hybridization and reverse transcriptase polymerase chain
reaction for establishing clonality in cases of persisting
hypereosinophilia.";
Haematologica 91:817-820(2006).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16943179; DOI=10.1083/jcb.200606051;
Srsen V., Gnadt N., Dammermann A., Merdes A.;
"Inhibition of centrosome protein assembly leads to p53-dependent exit
from the cell cycle.";
J. Cell Biol. 174:625-630(2006).
[20]
TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH JAK2.
PubMed=16424865; DOI=10.1038/sj.leu.2404104;
Adelaide J., Perot C., Gelsi-Boyer V., Pautas C., Murati A.,
Copie-Bergman C., Imbert M., Chaffanet M., Birnbaum D.,
Mozziconacci M.-J.;
"A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell
lymphoma.";
Leukemia 20:536-537(2006).
[21]
INTERACTION WITH NDE1 AND NDEL1, AND SUBCELLULAR LOCATION.
PubMed=16291865; DOI=10.1091/mbc.E05-04-0360;
Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.;
"Nudel contributes to microtubule anchoring at the mother centriole
and is involved in both dynein-dependent and -independent centrosomal
protein assembly.";
Mol. Biol. Cell 17:680-689(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-69,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;
SER-93; SER-960; SER-1231; SER-1257; SER-1260; SER-1263; SER-1730;
SER-1765; SER-1768 AND SER-1776, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;
SER-93; SER-1185; SER-1697; SER-1765; SER-1768; SER-1776 AND SER-1977,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
FUNCTION.
PubMed=20551181; DOI=10.1242/jcs.065045;
Sedjai F., Acquaviva C., Chevrier V., Chauvin J.P., Coppin E.,
Aouane A., Coulier F., Tolun A., Pierres M., Birnbaum D., Rosnet O.;
"Control of ciliogenesis by FOR20, a novel centrosome and
pericentriolar satellite protein.";
J. Cell Sci. 123:2391-2401(2010).
[28]
INTERACTION WITH PARD6A, AND SUBCELLULAR LOCATION.
PubMed=20719959; DOI=10.1091/mbc.E10-05-0430;
Kodani A., Tonthat V., Wu B., Suetterlin C.;
"Par6 alpha interacts with the dynactin subunit p150 Glued and is a
critical regulator of centrosomal protein recruitment.";
Mol. Biol. Cell 21:3376-3385(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;
SER-93; SER-861; SER-960 AND SER-1730, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-431;
SER-1730; SER-1765; SER-1768 AND SER-1958, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[33]
FUNCTION IN CILIOGENESIS, UBIQUITINATION BY MIB1, INTERACTION WITH
CEP131, ASSOCIATION WITH MICROTUBULE, AND SUBCELLULAR LOCATION.
PubMed=24121310; DOI=10.1038/emboj.2013.223;
Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B.,
Merdes A., Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N.,
Bekker-Jensen S.;
"A new cellular stress response that triggers centriolar satellite
reorganization and ciliogenesis.";
EMBO J. 32:3029-3040(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69;
SER-93; SER-110; SER-116; SER-119; SER-159; SER-370; SER-372; SER-384;
SER-588; THR-859; SER-861; SER-960; SER-977; SER-988; SER-991;
SER-1229; SER-1231; SER-1257; SER-1697; SER-1730 AND SER-1977, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
INTERACTION WITH MAP1LC3B; GABARAPAL2 AND GABARAP.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from
centriolar satellites.";
Nature 502:254-257(2013).
[36]
INTERACTION WITH CCDC13.
PubMed=24816561; DOI=10.1242/jcs.147785;
Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Howard A.E.,
Barone G., Lee A.J., Swanton C., Howell M., Maslen S., Skehel J.M.,
Boulton S.J., Collis S.J.;
"Ccdc13 is a novel human centriolar satellite protein required for
ciliogenesis and genome stability.";
J. Cell Sci. 127:2910-2919(2014).
[37]
INTERACTION WITH CCDC113.
PubMed=25074808; DOI=10.1242/jcs.157008;
Firat-Karalar E.N., Sante J., Elliott S., Stearns T.;
"Proteomic analysis of mammalian sperm cells identifies new components
of the centrosome.";
J. Cell Sci. 127:4128-4133(2014).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1468, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[40]
INTERACTION WITH KIAA0753; FOPNL AND OFD1.
PubMed=26643951; DOI=10.1093/hmg/ddv488;
Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M.,
Lembo F., Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P.,
Kuentz P., Thevenon J., Burglen L., Faivre L., Riviere J.B.,
Huynen M.A., Birnbaum D., Rosnet O., Thauvin-Robinet C.;
"OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
satellites and centrosomes and is mutated in one individual with oral-
facial-digital syndrome.";
Hum. Mol. Genet. 25:497-513(2016).
-!- FUNCTION: Required for centrosome assembly and function. Essential
for the correct localization of several centrosomal proteins
including CEP250, CETN3, PCNT and NEK2. Required to anchor
microtubules to the centrosome. Involved in the biogenesis of
cilia. {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:15659651,
ECO:0000269|PubMed:16943179, ECO:0000269|PubMed:20551181,
ECO:0000269|PubMed:24121310}.
-!- SUBUNIT: Self-associates. Interacts with C2CD3 (By similarity).
Interacts with BBS4, BBS8, CETN3, HAP1, NDE1, NDEL1, MAP1LC3B,
GABARAPAL2, and GABARAP. Interacts with CEP131; the interaction
increases in response to ultraviolet light (UV) radiation.
Associates with microtubule; association to microtubule is reduced
in response to cellular stress, such as ultraviolet light (UV)
radiation or heat shock, in a process that requires p38 MAP kinase
signaling. Interacts with CCDC113. Interacts with SSX2IP (By
similarity). Interacts with CCDC13 (PubMed:24816561). Interacts
with CEP290 (By similarity). Interacts with PARD6A
(PubMed:20719959). Interacts with KIAA0753/OFIP, FOPNL/FOR20 and
OFD1; the interaction with FOPNL/FOR20 and OFD1 may be mediated by
KIAA0753/OFIP (PubMed:26643951). {ECO:0000250|UniProtKB:Q9R0L6,
ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:14520415,
ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:16291865,
ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:24089205,
ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:24816561,
ECO:0000269|PubMed:25074808, ECO:0000269|PubMed:26643951,
ECO:0000269|PubMed:9361024}.
-!- INTERACTION:
Q8NFJ9:BBS1; NbExp=2; IntAct=EBI-741421, EBI-1805484;
Q96RK4:BBS4; NbExp=16; IntAct=EBI-741421, EBI-1805814;
Q8TD31-3:CCHCR1; NbExp=4; IntAct=EBI-11742977, EBI-10175300;
Q9P209:CEP72; NbExp=4; IntAct=EBI-741421, EBI-739498;
Q9UIA0:CYTH4; NbExp=4; IntAct=EBI-11742977, EBI-11521003;
P54256:Hap1 (xeno); NbExp=3; IntAct=EBI-741421, EBI-994539;
O95613:PCNT; NbExp=7; IntAct=EBI-741421, EBI-530012;
Q9Y2D8:SSX2IP; NbExp=10; IntAct=EBI-741421, EBI-2212028;
Q9Y3C0:WASHC3; NbExp=4; IntAct=EBI-741421, EBI-712969;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:20719959}. Cytoplasmic granule
{ECO:0000269|PubMed:15107855}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriolar satellite
{ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:20719959}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000269|PubMed:24121310}. Note=Recruitment to the centrosome
requires microtubules and dynein. The majority of the protein
dissociates from the centrosome during metaphase and subsequently
localizes to the cleavage site in telophase. Displaced from
centriolar satellites and centrosome in response to cellular
stress, such as ultraviolet light (UV) radiation or heat shock, in
a process that requires p38 MAP kinase signaling.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q15154-1; Sequence=Displayed;
Name=2;
IsoId=Q15154-2; Sequence=VSP_022611;
Name=3;
IsoId=Q15154-3; Sequence=VSP_022609, VSP_022610;
-!- TISSUE SPECIFICITY: Expressed in blood, bone marrow, breast, lymph
node, ovary and thyroid. {ECO:0000269|PubMed:10980597,
ECO:0000269|PubMed:15184884, ECO:0000269|PubMed:16270321,
ECO:0000269|PubMed:16424865}.
-!- INDUCTION: Expression is reduced in breast and ovarian cancer.
{ECO:0000269|PubMed:15184884, ECO:0000269|PubMed:16270321}.
-!- PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the
E3 ubiquitin-protein ligase MIB1 in proliferating cells,
preventing cilia formation. Monoubiquitination by MIB1 is
inhibited in response to cellular stress, such as ultraviolet
light (UV) radiation or heat shock, resulting in cilia formation
initiation. {ECO:0000269|PubMed:24121310}.
-!- DISEASE: Note=A chromosomal aberration involving PCM1 is found in
papillary thyroid carcinomas (PTCs). Translocation
t(8;10)(p21.3;q11.2) with RET links the protein kinase domain of
RET to the major portion of PCM1. {ECO:0000269|PubMed:10980597}.
-!- DISEASE: Note=A chromosomal aberration involving PCM1 is found in
a variety of hematological malignancies including atypical chronic
myeloid leukemia (atypical CML) and T-cell lymphoma. Translocation
t(8;9)(p22;p24) with JAK2 links the protein kinase domain of JAK2
to the major portion of PCM1.
-!- SIMILARITY: Belongs to the PCM1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH27477.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH65022.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAC03656.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAC14882.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L27841; AAA60120.1; -; mRNA.
EMBL; AC087273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000453; AAH00453.1; -; mRNA.
EMBL; BC027477; AAH27477.1; ALT_SEQ; mRNA.
EMBL; BC065022; AAH65022.1; ALT_SEQ; mRNA.
EMBL; AK091406; BAC03656.1; ALT_INIT; mRNA.
EMBL; AJ297349; CAC14882.1; ALT_SEQ; mRNA.
CCDS; CCDS47812.1; -. [Q15154-1]
PIR; A54103; A54103.
RefSeq; NP_001302437.1; NM_001315508.1.
RefSeq; NP_006188.3; NM_006197.3. [Q15154-1]
UniGene; Hs.491148; -.
ProteinModelPortal; Q15154; -.
SMR; Q15154; -.
BioGrid; 111139; 276.
DIP; DIP-42189N; -.
IntAct; Q15154; 263.
MINT; MINT-3295236; -.
STRING; 9606.ENSP00000327077; -.
iPTMnet; Q15154; -.
PhosphoSitePlus; Q15154; -.
BioMuta; PCM1; -.
DMDM; 296439495; -.
EPD; Q15154; -.
MaxQB; Q15154; -.
PaxDb; Q15154; -.
PeptideAtlas; Q15154; -.
PRIDE; Q15154; -.
DNASU; 5108; -.
Ensembl; ENST00000325083; ENSP00000327077; ENSG00000078674.
GeneID; 5108; -.
KEGG; hsa:5108; -.
UCSC; uc003wyi.5; human. [Q15154-1]
CTD; 5108; -.
DisGeNET; 5108; -.
GeneCards; PCM1; -.
H-InvDB; HIX0007341; -.
HGNC; HGNC:8727; PCM1.
HPA; CAB058695; -.
HPA; HPA023370; -.
HPA; HPA023374; -.
MalaCards; PCM1; -.
MIM; 600299; gene.
neXtProt; NX_Q15154; -.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
PharmGKB; PA33073; -.
eggNOG; ENOG410IEGR; Eukaryota.
eggNOG; ENOG410YNFX; LUCA.
HOGENOM; HOG000115473; -.
HOVERGEN; HBG053890; -.
InParanoid; Q15154; -.
KO; K16537; -.
OrthoDB; EOG091G00C3; -.
PhylomeDB; Q15154; -.
TreeFam; TF328740; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; Q15154; -.
ChiTaRS; PCM1; human.
GeneWiki; PCM1; -.
GenomeRNAi; 5108; -.
PRO; PR:Q15154; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000078674; -.
CleanEx; HS_PCM1; -.
ExpressionAtlas; Q15154; baseline and differential.
Genevisible; Q15154; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
GO; GO:0005814; C:centriole; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0000242; C:pericentriolar material; ISS:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
GO; GO:0007098; P:centrosome cycle; IMP:BHF-UCL.
GO; GO:0097711; P:ciliary basal body docking; TAS:Reactome.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0022027; P:interkinetic nuclear migration; ISS:BHF-UCL.
GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
GO; GO:0034453; P:microtubule anchoring; ISS:BHF-UCL.
GO; GO:0034454; P:microtubule anchoring at centrosome; IBA:GO_Central.
GO; GO:0050768; P:negative regulation of neurogenesis; ISS:BHF-UCL.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:1905515; P:non-motile cilium assembly; IMP:GO_Central.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0071539; P:protein localization to centrosome; IMP:SYSCILIA_CCNET.
GO; GO:0035176; P:social behavior; IEA:Ensembl.
InterPro; IPR031446; PCM1_C.
InterPro; IPR024138; Pericentriolar_Pcm1.
PANTHER; PTHR14164; PTHR14164; 1.
Pfam; PF15717; PCM1_C; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell projection;
Chromosomal rearrangement; Cilium biogenesis/degradation; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 2024 Pericentriolar material 1 protein.
/FTId=PRO_0000274037.
REGION 1279 1799 Interaction with HAP1.
{ECO:0000269|PubMed:9361024}.
REGION 1913 2024 Interaction with BBS4.
{ECO:0000269|PubMed:15107855}.
COILED 218 301 {ECO:0000255}.
COILED 400 424 {ECO:0000255}.
COILED 487 543 {ECO:0000255}.
COILED 651 682 {ECO:0000255}.
COILED 726 769 {ECO:0000255}.
COILED 824 858 {ECO:0000255}.
COILED 1063 1089 {ECO:0000255}.
COILED 1515 1539 {ECO:0000255}.
SITE 1314 1315 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 1369 1370 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 1470 1471 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 1609 1610 Breakpoint for translocation to form
PCM1-RET fusion protein.
SITE 1947 1948 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 399 399 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 859 859 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 861 861 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 872 872 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 877 877 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 960 960 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 977 977 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 988 988 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1185 1185 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1188 1188 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 1229 1229 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1231 1231 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1257 1257 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1260 1260 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1262 1262 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 1263 1263 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1318 1318 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 1320 1320 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 1468 1468 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1573 1573 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 1697 1697 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1730 1730 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1765 1765 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1768 1768 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1776 1776 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1782 1782 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0L6}.
MOD_RES 1958 1958 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1977 1977 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 263 263 R -> RENEEEDVRTIDSAVGSGSVAESTSLNIDVQSEASD
TTAR (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022609.
VAR_SEQ 492 2024 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022610.
VAR_SEQ 1315 1370 RYESASMSSTCEPCKSRNRHSAQTEEPVQAKVFSRKNHEQL
EKIIKCNRSTEISSE -> K (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_022611.
VARIANT 159 159 S -> N (in dbSNP:rs412750).
/FTId=VAR_030164.
VARIANT 159 159 S -> R (in dbSNP:rs412750).
/FTId=VAR_062172.
VARIANT 176 176 A -> D (in dbSNP:rs2285302).
/FTId=VAR_030165.
VARIANT 597 597 M -> V (in dbSNP:rs208753).
{ECO:0000269|PubMed:16421571,
ECO:0000269|PubMed:8120099}.
/FTId=VAR_030166.
VARIANT 600 600 S -> P (in dbSNP:rs34325017).
/FTId=VAR_047381.
VARIANT 691 691 A -> S (in dbSNP:rs17635381).
/FTId=VAR_030167.
VARIANT 871 871 G -> V (in dbSNP:rs7009117).
/FTId=VAR_030168.
VARIANT 1251 1251 R -> H (in dbSNP:rs17514547).
/FTId=VAR_030169.
VARIANT 1326 1326 E -> D (in dbSNP:rs34932823).
/FTId=VAR_047382.
VARIANT 1543 1543 T -> I (in dbSNP:rs370429).
/FTId=VAR_030170.
VARIANT 1701 1701 K -> N (in dbSNP:rs36113670).
/FTId=VAR_047383.
VARIANT 1865 1865 N -> D (in dbSNP:rs35789133).
/FTId=VAR_047384.
CONFLICT 294 294 R -> RG (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 311 312 EQ -> DE (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 405 405 E -> K (in Ref. 3; AAH27477).
{ECO:0000305}.
CONFLICT 408 408 Q -> K (in Ref. 3; AAH27477/AAH65022).
{ECO:0000305}.
CONFLICT 447 448 SV -> CL (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 760 760 Q -> H (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 946 946 G -> R (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 952 952 R -> T (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1004 1004 Missing (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1086 1086 Q -> R (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1168 1168 Q -> R (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1169 1169 N -> I (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1170 1170 S -> L (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1342 1342 V -> L (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1382 1382 R -> Q (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1532 1532 T -> A (in Ref. 4; BAC03656).
{ECO:0000305}.
CONFLICT 1849 1849 S -> G (in Ref. 4; BAC03656).
{ECO:0000305}.
CONFLICT 1853 1864 PLEREATSKNDQ -> HWNEKPLVKMTK (in Ref. 1;
AAA60120). {ECO:0000305}.
CONFLICT 1872 1872 C -> S (in Ref. 1; AAA60120).
{ECO:0000305}.
CONFLICT 1988 1988 E -> V (in Ref. 4; BAC03656).
{ECO:0000305}.
CONFLICT 1998 1998 I -> M (in Ref. 1; AAA60120).
{ECO:0000305}.
SEQUENCE 2024 AA; 228533 MW; 04ACFD7438F773EB CRC64;
MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK KFGVESDKRV
TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL EKLKQRINFS DLDQRSIGSD
SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDASTSP 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


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