Q9R0L6 (PCM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pericentriolar material 1 protein
Short name=PCM-1
Short name=mPCM-1

Gene names

Name:

Pcm1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2025 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for centrosome assembly and function. Essential for the correct localization of several centrosomal proteins probably including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Probably involved in the biogenesis of cilia. Ref.9
Subunit structure	Self-associates. Interacts with BBS4, BBS8, CETN3, HAP1, NDE1 and NDEL1 By similarity.
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Cytoplasmic granule. Note: Localizes to cytoplasmic granules which are enriched around the centrosome. This centrosomal enrichment requires microtubules and dynein By similarity. The majority of the protein dissociates from the centrosome during metaphase and subsequently localizes to the cleavage site in telophase. Ref.1 Ref.9 Ref.10 Ref.11
Tissue specificity	Expressed in the hippocampus and dentate gyrus, the columnar epithelial cells of bronchioles, the olfactory epithelium, the pericardium and the inner segment of the retina. Ref.13
Developmental stage	Maternally derived during fertilization. Expressed in the pericardium of the developing embryo and in the epidermal layer surrounding the digits. Ref.9
Sequence similarities	Belongs to the PCM1 family.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	centrosome organization Inferred from electronic annotation. Source: Compara cilium assembly Inferred from sequence or structural similarity. Source: UniProtKB interkinetic nuclear migration Inferred from mutant phenotype PubMed 20152126. Source: BHF-UCL microtubule anchoring at centrosome Inferred from mutant phenotype PubMed 20152126. Source: MGI negative regulation of neurogenesis Inferred from mutant phenotype PubMed 20152126. Source: BHF-UCL neuronal stem cell maintenance Inferred from mutant phenotype PubMed 20152126. Source: MGI protein localization to centrosome Inferred from mutant phenotype PubMed 20152126. Source: BHF-UCL
Cellular_component	centriolar satellite Inferred from direct assay Ref.1. Source: BHF-UCL nuclear membrane Inferred from electronic annotation. Source: Compara pericentriolar material Inferred from direct assay PubMed 20152126. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9R0L6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9R0L6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     263-263: R → RENEEEDVRTVDSAVGSGSVAESTSLNADVQSEASDTTAR

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2025	2025	Pericentriolar material 1 protein		PRO_0000274038
Regions
	Coiled coil	218 – 301	84	Potential
	Coiled coil	399 – 426	28	Potential
	Coiled coil	492 – 518	27	Potential
	Coiled coil	652 – 772	121	Potential
	Coiled coil	822 – 856	35	Potential
	Coiled coil	985 – 1017	33	Potential
	Coiled coil	1061 – 1086	26	Potential
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	69	1	Phosphoserine Ref.15
	Modified residue	93	1	Phosphoserine By similarity
	Modified residue	110	1	Phosphoserine By similarity
	Modified residue	399	1	N6-acetyllysine By similarity
	Modified residue	859	1	Phosphoserine By similarity
	Modified residue	864	1	Phosphoserine Ref.16
	Modified residue	957	1	Phosphoserine By similarity
	Modified residue	1182	1	Phosphoserine By similarity
	Modified residue	1228	1	Phosphoserine By similarity
	Modified residue	1254	1	Phosphoserine By similarity
	Modified residue	1257	1	Phosphoserine By similarity
	Modified residue	1260	1	Phosphoserine By similarity
	Modified residue	1287	1	Phosphoserine Ref.16
	Modified residue	1432	1	Phosphoserine Ref.16
	Modified residue	1434	1	Phosphoserine Ref.16
	Modified residue	1654	1	Phosphoserine Ref.17
	Modified residue	1695	1	Phosphoserine By similarity
	Modified residue	1729	1	Phosphoserine Ref.16
	Modified residue	1766	1	Phosphoserine Ref.12 Ref.15 Ref.16
	Modified residue	1769	1	Phosphoserine Ref.12 Ref.15 Ref.16
	Modified residue	1777	1	Phosphoserine Ref.15
	Modified residue	1959	1	Phosphoserine By similarity
	Modified residue	1978	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	263	1	R → RENEEEDVRTVDSAVGSGSV AESTSLNADVQSEASDTTAR in isoform 2.		VSP_022612
Experimental info
	Sequence conflict	305	1	A → T in AAH53728. Ref.4
	Sequence conflict	408	1	Q → R in AAH53728. Ref.4
	Sequence conflict	1216	1	V → I in AAK39513. Ref.6
	Sequence conflict	1329	1	N → S in AAK39513. Ref.6
	Sequence conflict	1819	1	I → V in BAA87861. Ref.1
	Sequence conflict	1819	1	I → V in AAK21980. Ref.6
	Sequence conflict	2018 – 2025	8	ETVGAQSI → GKSYQF in BAC30604. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 39D790997E6C5418	FASTA	2,025	228,847
	10 20 30 40 50 60 MATGGGPFEE VMHDQDLPNW SNDSVDDRLN NMEWGGQQKK ANRSSEKNKK KFGVASDKRV 70 80 90 100 110 120 TNAISPESSP GVGRRRTKIP HTFPHSRYMT QMSVPEQAEL EKLKQRINFS DLDQRSIGSD 130 140 150 160 170 180 SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDATASL PKREMTTSAQ CKELFASALS 190 200 210 220 230 240 NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT 250 260 270 280 290 300 HLIEHLKEQE KSYMKFLQKI LARDPQQEPM EETENLKKQH DLLKRMLQQQ EQLRALQGRQ 310 320 330 340 350 360 AALLALQHKA EQAIAVMDDS VVTETTGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA 370 380 390 400 410 420 VPDNRRQAES LSLTREISQS RNPSVSEHLP DEKVQLFSKM RVLQEKKQKM DKLLGELHNL 430 440 450 460 470 480 RDQHLNNSSF VPSTSLQRSG DKRSSTVALS APVGFASAVN GEANSLISSV PCPATSLVSQ 490 500 510 520 530 540 NESENEGHLN PAEKLQKLNE VQKRLNELRE LVHYYEQTSD MMTDAVNENT KDEETEESEY 550 560 570 580 590 600 DSEHENSEPV TNIRNPQVAS TWNEVNTNSN TQCGSNNRDG RPVNSNCEIN NRSAANIRAL 610 620 630 640 650 660 NMPPLDCRYN REGEQRLHVA HGEDEEEEVE EEGVSGASLS SRRSSLVDEA PEDEEFEQKI 670 680 690 700 710 720 SRLMAAKEKL KQLQDLVAMV QDDDATQVVV PAASNLDDFY AAEEDIKQNS NNARENSNKI 730 740 750 760 770 780 DTGVNEKTRE KFYEAKLQQQ QRELKQLQEE RKKLIEIQEK IQAVQKACPD LQLSATSISS 790 800 810 820 830 840 GPTKKYLPAI TSTPTVNEND SSTSKCVIDP EDSSVVDNEL WSDMRRHEML REELRQRRKQ 850 860 870 880 890 900 LEALMAEHQR RQGLAETSSP VAISLRSDGS ENLCTPQQSR TEKTMATWGG STQCALDEEG 910 920 930 940 950 960 DEDGYLSEGI VRTDEEEEEE QDASSNDNFP IYPPSMNQNS YNVKETKTRW KSNRPVSADG 970 980 990 1000 1010 1020 NYRPLAKTRQ QNISMQRQEN LRWVSELSYI EEKEQWQEQI NQLKKQLDFS VNICQTLMQD 1030 1040 1050 1060 1070 1080 QQTLSCLLQT LLTGPYSVLP SNVASPQVHL IMHQLNQCYT QLTWQQNNVQ RLKQMLTELM 1090 1100 1110 1120 1130 1140 RQQNQHPEKP RSKERGSSAS HPSSPNLFCP FSFPTQPVNL FNLPGFTNFP SFAPGMNFSP 1150 1160 1170 1180 1190 1200 LFPSNFGDFS QNVSTPTEQQ QPLAQNPSGK TEYMAFPKPF ESSSSLGAEK QRNQKQPEEE 1210 1220 1230 1240 1250 1260 AENTKTPWLY DQEGGVEKPF FKTGFTESVE KATNSNRKNQ PDTSRRRRQF DEESLESFSS 1270 1280 1290 1300 1310 1320 MPDPIDPTTV TKTFKTRKAS AQASLASKDK TPKSKSKKRN STQLKSRVKN IGYESASVSS 1330 1340 1350 1360 1370 1380 TCEPCKNRNR HSAQTEEPVQ AKLFSRKNHE QLEKIIKYSR SAEISSETGS DFSMFEALRD 1390 1400 1410 1420 1430 1440 TIYSEVATLI SQNESRPHFL IELFHELQLL NTDYLRQRAL YALQDIVSRH ISESDEREGE 1450 1460 1470 1480 1490 1500 NVKPVNSGTW VASNSELTPS ESLVTTDDET FEKNFERETH KVSEQNDADN VSVMSVSSNF 1510 1520 1530 1540 1550 1560 EPFATDDLGN TVIHLDQALA RMREYERMKT ETESHSNMRC TCRVIEDEDG AAAAATVSNS 1570 1580 1590 1600 1610 1620 EETPIIENHN SPQPISDVSA VPCPRIDTQQ LDRQIKAIMK EVIPFLKEHM DEVCSSQLLT 1630 1640 1650 1660 1670 1680 SVRRMVLTLT QQNDESKEFV KFFHKQLGSI LQDSLAKFAG RKLKDCGEDL LVEISEVLFN 1690 1700 1710 1720 1730 1740 ELAFFKLMQD LDNNSIAVKQ RCKRKIEAAG VRQSYAKEAK RILEGDHGSP AGEIDDEDKD 1750 1760 1770 1780 1790 1800 KDETETVKQT QTSEVYDAKG PKNVRSDVSD QEEDEESERC PVSINLSKAE SQALTNYGSG 1810 1820 1830 1840 1850 1860 EDENEDEEME DFEESPVDIQ TSLQANTETT EENEHDSQIL QHDLEKTPES TNVPSDQEPT 1870 1880 1890 1900 1910 1920 SKNDQDSSPV KPCYLNILEN EQQLNSATHK DSLTTTDSSK QPEPLPLPLA ASETLVPRVK 1930 1940 1950 1960 1970 1980 EVKSAQETPE SSLAGSPDTE SPVLVNDYEA ESGNISQKSD EEDFVKVEDL PLKLTVYSEE 1990 2000 2010 2020 ELRKKMIEEE QKNHLSGEIC EMQTEELAGN SQILKEPETV GAQSI
	Isoform 2 [UniParc]. Checksum: 38384D030FEC47BE	FASTA	2,064	232,843
	10 20 30 40 50 60 MATGGGPFEE VMHDQDLPNW SNDSVDDRLN NMEWGGQQKK ANRSSEKNKK KFGVASDKRV 70 80 90 100 110 120 TNAISPESSP GVGRRRTKIP HTFPHSRYMT QMSVPEQAEL EKLKQRINFS DLDQRSIGSD 130 140 150 160 170 180 SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDATASL PKREMTTSAQ CKELFASALS 190 200 210 220 230 240 NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT 250 260 270 280 290 300 HLIEHLKEQE KSYMKFLQKI LARENEEEDV RTVDSAVGSG SVAESTSLNA DVQSEASDTT 310 320 330 340 350 360 ARDPQQEPME ETENLKKQHD LLKRMLQQQE QLRALQGRQA ALLALQHKAE QAIAVMDDSV 370 380 390 400 410 420 VTETTGSLSG VSITSELNEE LNDLIQRFHN QLRDSQPPAV PDNRRQAESL SLTREISQSR 430 440 450 460 470 480 NPSVSEHLPD EKVQLFSKMR VLQEKKQKMD KLLGELHNLR DQHLNNSSFV PSTSLQRSGD 490 500 510 520 530 540 KRSSTVALSA PVGFASAVNG EANSLISSVP CPATSLVSQN ESENEGHLNP AEKLQKLNEV 550 560 570 580 590 600 QKRLNELREL VHYYEQTSDM MTDAVNENTK DEETEESEYD SEHENSEPVT NIRNPQVAST 610 620 630 640 650 660 WNEVNTNSNT QCGSNNRDGR PVNSNCEINN RSAANIRALN MPPLDCRYNR EGEQRLHVAH 670 680 690 700 710 720 GEDEEEEVEE EGVSGASLSS RRSSLVDEAP EDEEFEQKIS RLMAAKEKLK QLQDLVAMVQ 730 740 750 760 770 780 DDDATQVVVP AASNLDDFYA AEEDIKQNSN NARENSNKID TGVNEKTREK FYEAKLQQQQ 790 800 810 820 830 840 RELKQLQEER KKLIEIQEKI QAVQKACPDL QLSATSISSG PTKKYLPAIT STPTVNENDS 850 860 870 880 890 900 STSKCVIDPE DSSVVDNELW SDMRRHEMLR EELRQRRKQL EALMAEHQRR QGLAETSSPV 910 920 930 940 950 960 AISLRSDGSE NLCTPQQSRT EKTMATWGGS TQCALDEEGD EDGYLSEGIV RTDEEEEEEQ 970 980 990 1000 1010 1020 DASSNDNFPI YPPSMNQNSY NVKETKTRWK SNRPVSADGN YRPLAKTRQQ NISMQRQENL 1030 1040 1050 1060 1070 1080 RWVSELSYIE EKEQWQEQIN QLKKQLDFSV NICQTLMQDQ QTLSCLLQTL LTGPYSVLPS 1090 1100 1110 1120 1130 1140 NVASPQVHLI MHQLNQCYTQ LTWQQNNVQR LKQMLTELMR QQNQHPEKPR SKERGSSASH 1150 1160 1170 1180 1190 1200 PSSPNLFCPF SFPTQPVNLF NLPGFTNFPS FAPGMNFSPL FPSNFGDFSQ NVSTPTEQQQ 1210 1220 1230 1240 1250 1260 PLAQNPSGKT EYMAFPKPFE SSSSLGAEKQ RNQKQPEEEA ENTKTPWLYD QEGGVEKPFF 1270 1280 1290 1300 1310 1320 KTGFTESVEK ATNSNRKNQP DTSRRRRQFD EESLESFSSM PDPIDPTTVT KTFKTRKASA 1330 1340 1350 1360 1370 1380 QASLASKDKT PKSKSKKRNS TQLKSRVKNI GYESASVSST CEPCKNRNRH SAQTEEPVQA 1390 1400 1410 1420 1430 1440 KLFSRKNHEQ LEKIIKYSRS AEISSETGSD FSMFEALRDT IYSEVATLIS QNESRPHFLI 1450 1460 1470 1480 1490 1500 ELFHELQLLN TDYLRQRALY ALQDIVSRHI SESDEREGEN VKPVNSGTWV ASNSELTPSE 1510 1520 1530 1540 1550 1560 SLVTTDDETF EKNFERETHK VSEQNDADNV SVMSVSSNFE PFATDDLGNT VIHLDQALAR 1570 1580 1590 1600 1610 1620 MREYERMKTE TESHSNMRCT CRVIEDEDGA AAAATVSNSE ETPIIENHNS PQPISDVSAV 1630 1640 1650 1660 1670 1680 PCPRIDTQQL DRQIKAIMKE VIPFLKEHMD EVCSSQLLTS VRRMVLTLTQ QNDESKEFVK 1690 1700 1710 1720 1730 1740 FFHKQLGSIL QDSLAKFAGR KLKDCGEDLL VEISEVLFNE LAFFKLMQDL DNNSIAVKQR 1750 1760 1770 1780 1790 1800 CKRKIEAAGV RQSYAKEAKR ILEGDHGSPA GEIDDEDKDK DETETVKQTQ TSEVYDAKGP 1810 1820 1830 1840 1850 1860 KNVRSDVSDQ EEDEESERCP VSINLSKAES QALTNYGSGE DENEDEEMED FEESPVDIQT 1870 1880 1890 1900 1910 1920 SLQANTETTE ENEHDSQILQ HDLEKTPEST NVPSDQEPTS KNDQDSSPVK PCYLNILENE 1930 1940 1950 1960 1970 1980 QQLNSATHKD SLTTTDSSKQ PEPLPLPLAA SETLVPRVKE VKSAQETPES SLAGSPDTES 1990 2000 2010 2020 2030 2040 PVLVNDYEAE SGNISQKSDE EDFVKVEDLP LKLTVYSEEE LRKKMIEEEQ KNHLSGEICE 2050 2060 MQTEELAGNS QILKEPETVG AQSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Centriolar satellites: molecular characterization, ATP-dependent movement toward centrioles and possible involvement in ciliogenesis." Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N. J. Cell Biol. 147:969-980(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]	Erratum Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N. J. Cell Biol. 147:1585-1585(1999)
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-448 (ISOFORM 2). Strain: C57BL/6NCr. Tissue: Hematopoietic stem cell.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-443 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1978-2025 (ISOFORMS 1/2).
[6]	"Comparative analysis of an evolutionary chromosomal breakpoint indicates a recent origin for the human 4q telomere." van Geel M., Bolland D.J., Carim Todd L., Frants R.R., Hewitt J.E., de Jong P.J. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-78 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [MRNA] OF 41-2004 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1922-2025 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1193-2025. Strain: 129S6/SvEvTac and C57BL/6J. Tissue: Placenta.
[7]	"High-resolution mapping of mouse chromosome 8 identifies an evolutionary chromosomal breakpoint." Grewal P.K., Bolland D.J., Todd L.C., Hewitt J.E. Mamm. Genome 9:603-607(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1722-1784.
[8]	"Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs." Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T. , Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., Birney E., Hayashizaki Y. Nature 420:563-573(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1779-2005 (ISOFORMS 1/2). Strain: C57BL/6J. Tissue: Embryo.
[9]	"Arrest of cell cycle progression during first interphase in murine zygotes microinjected with anti-PCM-1 antibodies." Balczon R., Simerly C., Takahashi D., Schatten G. Cell Motil. Cytoskeleton 52:183-192(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[10]	"Assembly of centrosomal proteins and microtubule organization depends on PCM-1." Dammermann A., Merdes A. J. Cell Biol. 159:255-266(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Non-membranous granular organelle consisting of PCM-1: subcellular distribution and cell-cycle-dependent assembly/disassembly." Kubo A., Tsukita S. J. Cell Sci. 116:919-928(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-1766 AND SER-1769, MASS SPECTROMETRY. Tissue: Embryonic brain.
[13]	"The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression." 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. Nat. Genet. 36:462-470(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[14]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY. Tissue: Brain cortex.
[15]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-69; SER-1766; SER-1769 AND SER-1777, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-864; SER-1287; SER-1432; SER-1434; SER-1729; SER-1766 AND SER-1769, MASS SPECTROMETRY. Tissue: Melanoma.
[17]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-1654, MASS SPECTROMETRY. Tissue: Macrophage.
[18]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB029291 mRNA. Translation: BAA87861.1. AC144926 Genomic DNA. No translation available. AC156554 Genomic DNA. No translation available. BC053728 mRNA. Translation: AAH53728.1. AK011147 mRNA. Translation: BAB27430.3. AK040482 mRNA. Translation: BAC30604.1. AK141516 mRNA. Translation: BAE24712.1. AY028080 Genomic DNA. Translation: AAK21980.1. AF352180 mRNA. Translation: AAK39513.1. AF369838 mRNA. Translation: AAK39564.1. AF369839 mRNA. Translation: AAK39565.1. AF039021 Genomic DNA. Translation: AAC96068.1. AK020493 mRNA. Translation: BAB32121.1.
IPI	IPI00127764. IPI00828325.
RefSeq	NP_076151.2. NM_023662.3.
UniGene	Mm.117896.
3D structure databases
ProteinModelPortal	Q9R0L6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9R0L6. 2 interactions.
PTM databases
PhosphoSite	Q9R0L6.
Proteomic databases
PaxDb	Q9R0L6.
PRIDE	Q9R0L6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045218; ENSMUSP00000039709; ENSMUSG00000031592.
GeneID	18536.
KEGG	mmu:18536.
UCSC	uc009lns.1. mouse.
Organism-specific databases
CTD	5108.
MGI	MGI:1277958. Pcm1.
Phylogenomic databases
eggNOG	NOG43239.
GeneTree	ENSGT00390000006641.
HOVERGEN	HBG053890.
KO	K16537.
OMA	PNSVNRN.
OrthoDB	EOG4Q84WK.
Gene expression databases
Bgee	Q9R0L6.
CleanEx	MM_PCM1.
Genevestigator	Q9R0L6.
Family and domain databases
InterPro	IPR024138. Pericentriolar_Pcm1. [Graphical view]
PANTHER	PTHR14164. PTHR14164. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PCM1. mouse.
NextBio	294304.
SOURCE	Search...

Entry information

Entry name

PCM1_MOUSE

Accession

Primary (citable) accession number: Q9R0L6
Secondary accession number(s): E9QLK2 , O70287, Q3URH6, Q7TMS7, Q8C9V2, Q91Y27, Q91Y28, Q91Y51, Q923L0, Q9CRK8, Q9CT57

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program