Q15154 (PCM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

PCM1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2024 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 including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Involved in the biogenesis of cilia. Ref.7 Ref.15 Ref.19 Ref.26
Subunit structure	Self-associates By similarity. Interacts with BBS4, BBS8, CETN3, HAP1, NDE1 and NDEL1. Ref.6 Ref.7 Ref.8 Ref.10 Ref.21
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. The majority of the protein dissociates from the centrosome during metaphase and subsequently localizes to the cleavage site in telophase. Ref.1 Ref.5 Ref.7 Ref.8 Ref.10 Ref.15 Ref.19 Ref.21
Tissue specificity	Expressed in blood, bone marrow, breast, lymph node, ovary and thyroid. Ref.5 Ref.11 Ref.12 Ref.20
Induction	Expression is reduced in breast and ovarian cancer. Ref.11 Ref.12
Involvement in disease	Thyroid papillary carcinoma (TPC) [MIM:188550]: A common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells. Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving PCM1 is found in thyroid papillary carcinomas. Translocation t(8;10)(p21.3;q11.2) with RET links the protein kinase domain of RET to the major portion of PCM1. 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.
Sequence similarities	Belongs to the PCM1 family.
Sequence caution	The sequence AAH27477.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH65022.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAC03656.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAC14882.1 differs from that shown. Reason: Contaminating sequence.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome centrosome organization Inferred from mutant phenotype PubMed 17574030. Source: BHF-UCL cilium assembly Inferred from mutant phenotype PubMed 15616553. Source: UniProtKB interkinetic nuclear migration Inferred from sequence or structural similarity. Source: BHF-UCL microtubule anchoring Inferred from sequence or structural similarity. Source: BHF-UCL microtubule anchoring at centrosome Inferred from electronic annotation. Source: Compara negative regulation of neurogenesis Inferred from sequence or structural similarity. Source: BHF-UCL neuronal stem cell maintenance Inferred from electronic annotation. Source: Compara protein localization to centrosome Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	centriolar satellite Inferred from direct assay PubMed 15616553. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nuclear membrane Inferred from direct assay. Source: HPA pericentriolar material Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	identical protein binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS1	Q8NFJ9	2	EBI-741421,EBI-1805484
BBS4	Q96RK4	16	EBI-741421,EBI-1805814

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15154-1)

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: Q15154-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1315-1370: RYESASMSSTCEPCKSRNRHSAQTEEPVQAKVFSRKNHEQLEKIIKCNRSTEISSE → K

Isoform 3 (identifier: Q15154-3)

The sequence of this isoform differs from the canonical sequence as follows:
     263-263: R → RENEEEDVRTIDSAVGSGSVAESTSLNIDVQSEASDTTAR
     492-2024: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2024	2024	Pericentriolar material 1 protein		PRO_0000274037
Regions
	Region	1279 – 1799	521	Interaction with HAP1
	Region	1913 – 2024	112	Interaction with BBS4
	Coiled coil	218 – 301	84	Potential
	Coiled coil	400 – 424	25	Potential
	Coiled coil	487 – 543	57	Potential
	Coiled coil	651 – 682	32	Potential
	Coiled coil	726 – 769	44	Potential
	Coiled coil	824 – 858	35	Potential
	Coiled coil	1063 – 1089	27	Potential
	Coiled coil	1515 – 1539	25	Potential
Sites
	Site	1314 – 1315	2	Breakpoint for translocation to form PCM1-JAK2 fusion protein
	Site	1369 – 1370	2	Breakpoint for translocation to form PCM1-JAK2 fusion protein
	Site	1470 – 1471	2	Breakpoint for translocation to form PCM1-JAK2 fusion protein
	Site	1609 – 1610	2	Breakpoint for translocation to form PCM1-RET fusion protein
	Site	1947 – 1948	2	Breakpoint for translocation to form PCM1-JAK2 fusion protein
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.9 Ref.17 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29
	Modified residue	68	1	Phosphoserine Ref.22 Ref.23 Ref.24 Ref.27 Ref.29
	Modified residue	69	1	Phosphoserine Ref.22 Ref.23 Ref.24 Ref.27
	Modified residue	93	1	Phosphoserine Ref.23 Ref.24 Ref.27
	Modified residue	110	1	Phosphoserine Ref.17
	Modified residue	399	1	N6-acetyllysine Ref.25
	Modified residue	431	1	Phosphoserine Ref.29
	Modified residue	861	1	Phosphoserine Ref.27
	Modified residue	866	1	Phosphoserine By similarity
	Modified residue	960	1	Phosphoserine Ref.23 Ref.27
	Modified residue	1185	1	Phosphoserine Ref.24
	Modified residue	1231	1	Phosphoserine Ref.23
	Modified residue	1257	1	Phosphoserine Ref.23
	Modified residue	1260	1	Phosphoserine Ref.23
	Modified residue	1263	1	Phosphoserine Ref.23
	Modified residue	1290	1	Phosphoserine By similarity
	Modified residue	1435	1	Phosphoserine By similarity
	Modified residue	1437	1	Phosphoserine By similarity
	Modified residue	1656	1	Phosphoserine By similarity
	Modified residue	1697	1	Phosphoserine Ref.24
	Modified residue	1730	1	Phosphoserine Ref.17 Ref.23 Ref.27 Ref.29
	Modified residue	1765	1	Phosphoserine Ref.23 Ref.24 Ref.29
	Modified residue	1768	1	Phosphoserine Ref.23 Ref.24 Ref.29
	Modified residue	1776	1	Phosphoserine Ref.23 Ref.24
	Modified residue	1958	1	Phosphoserine Ref.29
	Modified residue	1977	1	Phosphoserine Ref.24
Natural variations
	Alternative sequence	263	1	R → RENEEEDVRTIDSAVGSGSV AESTSLNIDVQSEASDTTAR in isoform 3.		VSP_022609
	Alternative sequence	492 – 2024	1533	Missing in isoform 3.		VSP_022610
	Alternative sequence	1315 – 1370	56	RYESA…EISSE → K in isoform 2.		VSP_022611
	Natural variant	159	1	S → N. Corresponds to variant rs412750 [ dbSNP | Ensembl ].		VAR_030164
	Natural variant	159	1	S → R. Corresponds to variant rs412750 [ dbSNP | Ensembl ].		VAR_062172
	Natural variant	176	1	A → D. Corresponds to variant rs2285302 [ dbSNP | Ensembl ].		VAR_030165
	Natural variant	597	1	M → V. Ref.1 Ref.2 Corresponds to variant rs208753 [ dbSNP | Ensembl ].		VAR_030166
	Natural variant	600	1	S → P. Corresponds to variant rs34325017 [ dbSNP | Ensembl ].		VAR_047381
	Natural variant	691	1	A → S. Corresponds to variant rs17635381 [ dbSNP | Ensembl ].		VAR_030167
	Natural variant	871	1	G → V. Corresponds to variant rs7009117 [ dbSNP | Ensembl ].		VAR_030168
	Natural variant	1251	1	R → H. Corresponds to variant rs17514547 [ dbSNP | Ensembl ].		VAR_030169
	Natural variant	1326	1	E → D. Corresponds to variant rs34932823 [ dbSNP | Ensembl ].		VAR_047382
	Natural variant	1543	1	T → I. Corresponds to variant rs370429 [ dbSNP | Ensembl ].		VAR_030170
	Natural variant	1701	1	K → N. Corresponds to variant rs36113670 [ dbSNP | Ensembl ].		VAR_047383
	Natural variant	1865	1	N → D. Corresponds to variant rs35789133 [ dbSNP | Ensembl ].		VAR_047384
Experimental info
	Sequence conflict	294	1	R → RG in AAA60120. Ref.1
	Sequence conflict	311 – 312	2	EQ → DE in AAA60120. Ref.1
	Sequence conflict	405	1	E → K in AAH27477. Ref.3
	Sequence conflict	408	1	Q → K in AAH27477. Ref.3
	Sequence conflict	408	1	Q → K in AAH65022. Ref.3
	Sequence conflict	447 – 448	2	SV → CL in AAA60120. Ref.1
	Sequence conflict	760	1	Q → H in AAA60120. Ref.1
	Sequence conflict	946	1	G → R in AAA60120. Ref.1
	Sequence conflict	952	1	R → T in AAA60120. Ref.1
	Sequence conflict	1004	1	Missing in AAA60120. Ref.1
	Sequence conflict	1086	1	Q → R in AAA60120. Ref.1
	Sequence conflict	1168	1	Q → R in AAA60120. Ref.1
	Sequence conflict	1169	1	N → I in AAA60120. Ref.1
	Sequence conflict	1170	1	S → L in AAA60120. Ref.1
	Sequence conflict	1342	1	V → L in AAA60120. Ref.1
	Sequence conflict	1382	1	R → Q in AAA60120. Ref.1
	Sequence conflict	1532	1	T → A in BAC03656. Ref.4
	Sequence conflict	1849	1	S → G in BAC03656. Ref.4
	Sequence conflict	1853 – 1864	12	PLERE…SKNDQ → HWNEKPLVKMTK in AAA60120. Ref.1
	Sequence conflict	1872	1	C → S in AAA60120. Ref.1
	Sequence conflict	1988	1	E → V in BAC03656. Ref.4
	Sequence conflict	1998	1	I → M in AAA60120. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 4. Checksum: 04ACFD7438F773EB	FASTA	2,024	228,533
	10 20 30 40 50 60 MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK KFGVESDKRV 70 80 90 100 110 120 TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL EKLKQRINFS DLDQRSIGSD 130 140 150 160 170 180 SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDASTSP PNRETIGSAQ CKELFASALS 190 200 210 220 230 240 NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT 250 260 270 280 290 300 HLIDHLKEQE KSYMKFLKKI LARDPQQEPM EEIENLKKQH DLLKRMLQQQ EQLRALQGRQ 310 320 330 340 350 360 AALLALQHKA EQAIAVMDDS VVAETAGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA 370 380 390 400 410 420 VPDNRRQAES LSLTREVSQS RKPSASERLP DEKVELFSKM RVLQEKKQKM DKLLGELHTL 430 440 450 460 470 480 RDQHLNNSSS SPQRSVDQRS TSAPSASVGL APVVNGESNS LTSSVPYPTA SLVSQNESEN 490 500 510 520 530 540 EGHLNPSEKL QKLNEVRKRL NELRELVHYY EQTSDMMTDA VNENRKDEET EESEYDSEHE 550 560 570 580 590 600 NSEPVTNIRN PQVASTWNEV NSHSNAQCVS NNRDGRTVNS NCEINNRSAA NIRALNMPPS 610 620 630 640 650 660 LDCRYNREGE QEIHVAQGED DEEEEEEAEE EGVSGASLSS HRSSLVDEHP EDAEFEQKIN 670 680 690 700 710 720 RLMAAKQKLR QLQDLVAMVQ DDDAAQGVIS ASASNLDDFY PAEEDTKQNS NNTRGNANKT 730 740 750 760 770 780 QKDTGVNEKA REKFYEAKLQ QQQRELKQLQ EERKKLIDIQ EKIQALQTAC PDLQLSAASV 790 800 810 820 830 840 GNCPTKKYMP AVTSTPTVNQ HETSTSKSVF EPEDSSIVDN ELWSEMRRHE MLREELRQRR 850 860 870 880 890 900 KQLEALMAEH QRRQGLAETA SPVAVSLRSD GSENLCTPQQ SRTEKTMATW GGSTQCALDE 910 920 930 940 950 960 EGDEDGYLSE GIVRTDEEEE EEQDASSNDN FSVCPSNSVN HNSYNGKETK NRWKNNCPFS 970 980 990 1000 1010 1020 ADENYRPLAK TRQQNISMQR QENLRWVSEL SYVEEKEQWQ EQINQLKKQL DFSVSICQTL 1030 1040 1050 1060 1070 1080 MQDQQTLSCL LQTLLTGPYS VMPSNVASPQ VHFIMHQLNQ CYTQLTWQQN NVQRLKQMLN 1090 1100 1110 1120 1130 1140 ELMRQQNQHP EKPGGKERGS SASHPPSPSL FCPFSFPTQP VNLFNIPGFT NFSSFAPGMN 1150 1160 1170 1180 1190 1200 FSPLFPSNFG DFSQNISTPS EQQQPLAQNS SGKTEYMAFP KPFESSSSIG AEKPRNKKLP 1210 1220 1230 1240 1250 1260 EEEVESSRTP WLYEQEGEVE KPFIKTGFSV SVEKSTSSNR KNQLDTNGRR RQFDEESLES 1270 1280 1290 1300 1310 1320 FSSMPDPVDP TTVTKTFKTR KASAQASLAS KDKTPKSKSK KRNSTQLKSR VKNIRYESAS 1330 1340 1350 1360 1370 1380 MSSTCEPCKS RNRHSAQTEE PVQAKVFSRK NHEQLEKIIK CNRSTEISSE TGSDFSMFEA 1390 1400 1410 1420 1430 1440 LRDTIYSEVA TLISQNESRP HFLIELFHEL QLLNTDYLRQ RALYALQDIV SRHISESHEK 1450 1460 1470 1480 1490 1500 GENVKSVNSG TWIASNSELT PSESLATTDD ETFEKNFERE THKISEQNDA DNASVLSVSS 1510 1520 1530 1540 1550 1560 NFEPFATDDL GNTVIHLDQA LARMREYERM KTEAESNSNM RCTCRIIEDG DGAGAGTTVN 1570 1580 1590 1600 1610 1620 NLEETPVIEN RSSQQPVSEV STIPCPRIDT QQLDRQIKAI MKEVIPFLKE HMDEVCSSQL 1630 1640 1650 1660 1670 1680 LTSVRRMVLT LTQQNDESKE FVKFFHKQLG SILQDSLAKF AGRKLKDCGE DLLVEISEVL 1690 1700 1710 1720 1730 1740 FNELAFFKLM QDLDNNSITV KQRCKRKIEA TGVIQSCAKE AKRILEDHGS PAGEIDDEDK 1750 1760 1770 1780 1790 1800 DKDETETVKQ TQTSEVYDGP KNVRSDISDQ EEDEESEGCP VSINLSKAET QALTNYGSGE 1810 1820 1830 1840 1850 1860 DENEDEEMEE FEEGPVDVQT SLQANTEATE ENEHDEQVLQ RDFKKTAESK NVPLEREATS 1870 1880 1890 1900 1910 1920 KNDQNNCPVK PCYLNILEDE QPLNSAAHKE SPPTVDSTQQ PNPLPLRLPE MEPLVPRVKE 1930 1940 1950 1960 1970 1980 VKSAQETPES SLAGSPDTES PVLVNDYEAE SGNISQKSDE EDFVKVEDLP LKLTIYSEAD 1990 2000 2010 2020 LRKKMVEEEQ KNHLSGEICE MQTEELAGNS ETLKEPETVG AQSI
	Isoform 2 [UniParc]. Checksum: 7E696A776BDC82E6	FASTA	1,969	222,222
	10 20 30 40 50 60 MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK KFGVESDKRV 70 80 90 100 110 120 TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL EKLKQRINFS DLDQRSIGSD 130 140 150 160 170 180 SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDASTSP PNRETIGSAQ CKELFASALS 190 200 210 220 230 240 NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT 250 260 270 280 290 300 HLIDHLKEQE KSYMKFLKKI LARDPQQEPM EEIENLKKQH DLLKRMLQQQ EQLRALQGRQ 310 320 330 340 350 360 AALLALQHKA EQAIAVMDDS VVAETAGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA 370 380 390 400 410 420 VPDNRRQAES LSLTREVSQS RKPSASERLP DEKVELFSKM RVLQEKKQKM DKLLGELHTL 430 440 450 460 470 480 RDQHLNNSSS SPQRSVDQRS TSAPSASVGL APVVNGESNS LTSSVPYPTA SLVSQNESEN 490 500 510 520 530 540 EGHLNPSEKL QKLNEVRKRL NELRELVHYY EQTSDMMTDA VNENRKDEET EESEYDSEHE 550 560 570 580 590 600 NSEPVTNIRN PQVASTWNEV NSHSNAQCVS NNRDGRTVNS NCEINNRSAA NIRALNMPPS 610 620 630 640 650 660 LDCRYNREGE QEIHVAQGED DEEEEEEAEE EGVSGASLSS HRSSLVDEHP EDAEFEQKIN 670 680 690 700 710 720 RLMAAKQKLR QLQDLVAMVQ DDDAAQGVIS ASASNLDDFY PAEEDTKQNS NNTRGNANKT 730 740 750 760 770 780 QKDTGVNEKA REKFYEAKLQ QQQRELKQLQ EERKKLIDIQ EKIQALQTAC PDLQLSAASV 790 800 810 820 830 840 GNCPTKKYMP AVTSTPTVNQ HETSTSKSVF EPEDSSIVDN ELWSEMRRHE MLREELRQRR 850 860 870 880 890 900 KQLEALMAEH QRRQGLAETA SPVAVSLRSD GSENLCTPQQ SRTEKTMATW GGSTQCALDE 910 920 930 940 950 960 EGDEDGYLSE GIVRTDEEEE EEQDASSNDN FSVCPSNSVN HNSYNGKETK NRWKNNCPFS 970 980 990 1000 1010 1020 ADENYRPLAK TRQQNISMQR QENLRWVSEL SYVEEKEQWQ EQINQLKKQL DFSVSICQTL 1030 1040 1050 1060 1070 1080 MQDQQTLSCL LQTLLTGPYS VMPSNVASPQ VHFIMHQLNQ CYTQLTWQQN NVQRLKQMLN 1090 1100 1110 1120 1130 1140 ELMRQQNQHP EKPGGKERGS SASHPPSPSL FCPFSFPTQP VNLFNIPGFT NFSSFAPGMN 1150 1160 1170 1180 1190 1200 FSPLFPSNFG DFSQNISTPS EQQQPLAQNS SGKTEYMAFP KPFESSSSIG AEKPRNKKLP 1210 1220 1230 1240 1250 1260 EEEVESSRTP WLYEQEGEVE KPFIKTGFSV SVEKSTSSNR KNQLDTNGRR RQFDEESLES 1270 1280 1290 1300 1310 1320 FSSMPDPVDP TTVTKTFKTR KASAQASLAS KDKTPKSKSK KRNSTQLKSR VKNIKTGSDF 1330 1340 1350 1360 1370 1380 SMFEALRDTI YSEVATLISQ NESRPHFLIE LFHELQLLNT DYLRQRALYA LQDIVSRHIS 1390 1400 1410 1420 1430 1440 ESHEKGENVK SVNSGTWIAS NSELTPSESL ATTDDETFEK NFERETHKIS EQNDADNASV 1450 1460 1470 1480 1490 1500 LSVSSNFEPF ATDDLGNTVI HLDQALARMR EYERMKTEAE SNSNMRCTCR IIEDGDGAGA 1510 1520 1530 1540 1550 1560 GTTVNNLEET PVIENRSSQQ PVSEVSTIPC PRIDTQQLDR QIKAIMKEVI PFLKEHMDEV 1570 1580 1590 1600 1610 1620 CSSQLLTSVR RMVLTLTQQN DESKEFVKFF HKQLGSILQD SLAKFAGRKL KDCGEDLLVE 1630 1640 1650 1660 1670 1680 ISEVLFNELA FFKLMQDLDN NSITVKQRCK RKIEATGVIQ SCAKEAKRIL EDHGSPAGEI 1690 1700 1710 1720 1730 1740 DDEDKDKDET ETVKQTQTSE VYDGPKNVRS DISDQEEDEE SEGCPVSINL SKAETQALTN 1750 1760 1770 1780 1790 1800 YGSGEDENED EEMEEFEEGP VDVQTSLQAN TEATEENEHD EQVLQRDFKK TAESKNVPLE 1810 1820 1830 1840 1850 1860 REATSKNDQN NCPVKPCYLN ILEDEQPLNS AAHKESPPTV DSTQQPNPLP LRLPEMEPLV 1870 1880 1890 1900 1910 1920 PRVKEVKSAQ ETPESSLAGS PDTESPVLVN DYEAESGNIS QKSDEEDFVK VEDLPLKLTI 1930 1940 1950 1960 YSEADLRKKM VEEEQKNHLS GEICEMQTEE LAGNSETLKE PETVGAQSI
	Isoform 3 [UniParc]. Checksum: 52B76CDE001E0690	FASTA	530	59,199
	10 20 30 40 50 60 MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK KFGVESDKRV 70 80 90 100 110 120 TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL EKLKQRINFS DLDQRSIGSD 130 140 150 160 170 180 SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDASTSP PNRETIGSAQ CKELFASALS 190 200 210 220 230 240 NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT 250 260 270 280 290 300 HLIDHLKEQE KSYMKFLKKI LARENEEEDV RTIDSAVGSG SVAESTSLNI DVQSEASDTT 310 320 330 340 350 360 ARDPQQEPME EIENLKKQHD LLKRMLQQQE QLRALQGRQA ALLALQHKAE QAIAVMDDSV 370 380 390 400 410 420 VAETAGSLSG VSITSELNEE LNDLIQRFHN QLRDSQPPAV PDNRRQAESL SLTREVSQSR 430 440 450 460 470 480 KPSASERLPD EKVELFSKMR VLQEKKQKMD KLLGELHTLR DQHLNNSSSS PQRSVDQRST 490 500 510 520 530 SAPSASVGLA PVVNGESNSL TSSVPYPTAS LVSQNESENE GHLNPSEKLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle distribution." Balczon R., Bao L., Zimmer W.E. J. Cell Biol. 124:783-793(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT VAL-597. Tissue: Liver.
[2]	"DNA sequence and analysis of human chromosome 8." 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. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-597.
[3]	"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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-404 (ISOFORMS 1/2). Tissue: Lung, Testis and Uterus.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1244-2024 (ISOFORM 2). Tissue: Brain.
[5]	"RET/PCM-1: a novel fusion gene in papillary thyroid carcinoma." Corvi R., Berger N., Balczon R., Romeo G. Oncogene 19:4236-4242(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1527-1610 (ISOFORMS 1/2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH RET.
[6]	"Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin." Engelender S., Sharp A.H., Colomer V., Tokito M.K., Lanahan A., Worley P., Holzbaur E.L.F., Ross C.A. Hum. Mol. Genet. 6:2205-2212(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HAP1.
[7]	"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: FUNCTION, INTERACTION WITH CETN3, SUBCELLULAR LOCATION.
[8]	"Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome." 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. Nature 425:628-633(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BBS8, SUBCELLULAR LOCATION.
[9]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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: INTERACTION WITH BBS4, SUBCELLULAR LOCATION.
[11]	"Candidate tumor-suppressor genes on chromosome arm 8p in early-onset and high-grade breast cancers." 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. Oncogene 23:5697-5702(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[12]	"Five genes from chromosomal band 8p22 are significantly down-regulated in ovarian carcinoma: N33 and EFA6R have a potential impact on overall survival." Pils D., Horak P., Gleiss A., Sax C., Fabjani G., Moebus V.J., Zielinski C., Reinthaller A., Zeillinger R., Krainer M. Cancer 104:2417-2429(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[13]	"The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2." 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. Cancer Res. 65:2662-2667(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH JAK2.
[14]	"PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid leukemia with t(8;9) translocation." 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. Leukemia 19:1692-1696(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH JAK2.
[15]	"Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation." Hames R.S., Crookes R.E., Straatman K.R., Merdes A., Hayes M.J., Faragher A.J., Fry A.M. Mol. Biol. Cell 16:1711-1724(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene." Bousquet M., Quelen C., De Mas V., Duchayne E., Roquefeuil B., Delsol G., Laurent G., Dastugue N., Brousset P. Oncogene 24:7248-7252(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH JAK2.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-110 AND SER-1730, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"A combination of cytomorphology, cytogenetic analysis, fluorescence in situ hybridization and reverse transcriptase polymerase chain reaction for establishing clonality in cases of persisting hypereosinophilia." Bacher U., Reiter A., Haferlach T., Mueller L., Schnittger S., Kern W., Schoch C. Haematologica 91:817-820(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH JAK2.
[19]	"Inhibition of centrosome protein assembly leads to p53-dependent exit from the cell cycle." Srsen V., Gnadt N., Dammermann A., Merdes A. J. Cell Biol. 174:625-630(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]	"A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell lymphoma." Adelaide J., Perot C., Gelsi-Boyer V., Pautas C., Murati A., Copie-Bergman C., Imbert M., Chaffanet M., Birnbaum D., Mozziconacci M.-J. Leukemia 20:536-537(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH JAK2.
[21]	"Nudel contributes to microtubule anchoring at the mother centriole and is involved in both dynein-dependent and -independent centrosomal protein assembly." Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X. Mol. Biol. Cell 17:680-689(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDE1 AND NDEL1, SUBCELLULAR LOCATION.
[22]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-69, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: 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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399, MASS SPECTROMETRY.
[26]	"Control of ciliogenesis by FOR20, a novel centrosome and pericentriolar satellite protein." Sedjai F., Acquaviva C., Chevrier V., Chauvin J.P., Coppin E., Aouane A., Coulier F., Tolun A., Pierres M., Birnbaum D., Rosnet O. J. Cell Sci. 123:2391-2401(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-69; SER-93; SER-861; SER-960 AND SER-1730, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-431; SER-1730; SER-1765; SER-1768 AND SER-1958, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L27841 mRNA. Translation: AAA60120.1. AC087273 Genomic DNA. No translation available. AC087625 Genomic DNA. No translation available. BC000453 mRNA. Translation: AAH00453.1. BC027477 mRNA. Translation: AAH27477.1. Sequence problems. BC065022 mRNA. Translation: AAH65022.1. Sequence problems. AK091406 mRNA. Translation: BAC03656.1. Different initiation. AJ297349 mRNA. Translation: CAC14882.1. Sequence problems.
IPI	IPI00006213. IPI00795923. IPI01012680.
PIR	A54103.
RefSeq	NP_006188.3. NM_006197.3.
UniGene	Hs.491148.
3D structure databases
ProteinModelPortal	Q15154.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15154. 30 interactions.
MINT	MINT-3295236.
STRING	9606.ENSP00000327077.
PTM databases
PhosphoSite	Q15154.
Polymorphism databases
DMDM	296439495.
Proteomic databases
PaxDb	Q15154.
PRIDE	Q15154.
Protocols and materials databases
DNASU	5108.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000325083; ENSP00000327077; ENSG00000078674.
GeneID	5108.
KEGG	hsa:5108.
UCSC	uc003wyi.4. human.
Organism-specific databases
CTD	5108.
GeneCards	GC08P017824.
H-InvDB	HIX0007341.
HGNC	HGNC:8727. PCM1.
HPA	CAB058695. HPA023370. HPA023374.
MIM	188550. phenotype. 600299. gene.
neXtProt	NX_Q15154.
Orphanet	146. Papillary or follicular thyroid carcinoma.
PharmGKB	PA33073.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG43239.
HOGENOM	HOG000115473.
HOVERGEN	HBG053890.
KO	K16537.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	Q15154.
Bgee	Q15154.
CleanEx	HS_PCM1.
Genevestigator	Q15154.
Family and domain databases
InterPro	IPR024138. Pericentriolar_Pcm1. [Graphical view]
PANTHER	PTHR14164. PTHR14164. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PCM1. human.
GenomeRNAi	5108.
NextBio	19712.
SOURCE	Search...

Entry information

Entry name

PCM1_HUMAN

Accession

Primary (citable) accession number: Q15154
Secondary accession number(s): Q58F13 , Q6P1K7, Q8NB85, Q9BWC1, Q9H4A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 100 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.