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Q15154 (PCM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pericentriolar material 1 protein

Short name=PCM-1
Short name=hPCM-1
Gene names
Name:PCM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2024 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.27 Ref.32

Subunit structure

Self-associates 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. Ref.6 Ref.7 Ref.8 Ref.10 Ref.21 Ref.32 Ref.33

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmic granule. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite. Cytoplasmcytoskeletoncilium basal body. Note: Recruitement 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. Ref.1 Ref.5 Ref.7 Ref.8 Ref.10 Ref.15 Ref.19 Ref.21 Ref.32

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

Post-translational modification

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. Ref.32

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 processCilium biogenesis/degradation
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/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

cytoplasmic microtubule organization

Inferred from mutant phenotype PubMed 22797915. Source: UniProtKB

interkinetic nuclear migration

Inferred from sequence or structural similarity. Source: BHF-UCL

intraciliary transport involved in cilium morphogenesis

Inferred from mutant phenotype PubMed 24550735. Source: UniProtKB

microtubule anchoring

Inferred from sequence or structural similarity. Source: BHF-UCL

microtubule anchoring at centrosome

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of neurogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

neuronal stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular protein transport

Inferred from mutant phenotype PubMed 22797915PubMed 24550735. Source: UniProtKB

protein localization to centrosome

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcell projection

Inferred from electronic annotation. Source: UniProtKB-KW

centriolar satellite

Inferred from direct assay PubMed 15616553PubMed 24550735. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614PubMed 22797915PubMed 24550735. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

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_functionidentical protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.10Ref.33PubMed 24550735. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.31
Chain2 – 20242023Pericentriolar material 1 protein
PRO_0000274037

Regions

Region1279 – 1799521Interaction with HAP1
Region1913 – 2024112Interaction with BBS4
Coiled coil218 – 30184 Potential
Coiled coil400 – 42425 Potential
Coiled coil487 – 54357 Potential
Coiled coil651 – 68232 Potential
Coiled coil726 – 76944 Potential
Coiled coil824 – 85835 Potential
Coiled coil1063 – 108927 Potential
Coiled coil1515 – 153925 Potential

Sites

Site1314 – 13152Breakpoint for translocation to form PCM1-JAK2 fusion protein
Site1369 – 13702Breakpoint for translocation to form PCM1-JAK2 fusion protein
Site1470 – 14712Breakpoint for translocation to form PCM1-JAK2 fusion protein
Site1609 – 16102Breakpoint for translocation to form PCM1-RET fusion protein
Site1947 – 19482Breakpoint for translocation to form PCM1-JAK2 fusion protein

Amino acid modifications

Modified residue21N-acetylalanine Ref.31
Modified residue651Phosphoserine Ref.9 Ref.17 Ref.22 Ref.23 Ref.25 Ref.28 Ref.30
Modified residue681Phosphoserine Ref.22 Ref.23 Ref.25 Ref.28 Ref.30
Modified residue691Phosphoserine Ref.22 Ref.23 Ref.25 Ref.28
Modified residue931Phosphoserine Ref.23 Ref.25 Ref.28
Modified residue1101Phosphoserine Ref.17
Modified residue3991N6-acetyllysine Ref.26
Modified residue4311Phosphoserine Ref.30
Modified residue6431Phosphoserine By similarity
Modified residue6441Phosphoserine By similarity
Modified residue8611Phosphoserine Ref.28
Modified residue9601Phosphoserine Ref.23 Ref.28
Modified residue11851Phosphoserine Ref.25
Modified residue12311Phosphoserine Ref.23
Modified residue12571Phosphoserine Ref.23
Modified residue12601Phosphoserine Ref.23
Modified residue12631Phosphoserine Ref.23
Modified residue16971Phosphoserine Ref.25
Modified residue17301Phosphoserine Ref.17 Ref.23 Ref.28 Ref.30
Modified residue17651Phosphoserine Ref.23 Ref.25 Ref.30
Modified residue17681Phosphoserine Ref.23 Ref.25 Ref.30
Modified residue17761Phosphoserine Ref.23 Ref.25
Modified residue19581Phosphoserine Ref.30
Modified residue19771Phosphoserine Ref.25

Natural variations

Alternative sequence2631R → RENEEEDVRTIDSAVGSGSV AESTSLNIDVQSEASDTTAR in isoform 3.
VSP_022609
Alternative sequence492 – 20241533Missing in isoform 3.
VSP_022610
Alternative sequence1315 – 137056RYESA…EISSE → K in isoform 2.
VSP_022611
Natural variant1591S → N.
Corresponds to variant rs412750 [ dbSNP | Ensembl ].
VAR_030164
Natural variant1591S → R.
Corresponds to variant rs412750 [ dbSNP | Ensembl ].
VAR_062172
Natural variant1761A → D.
Corresponds to variant rs2285302 [ dbSNP | Ensembl ].
VAR_030165
Natural variant5971M → V. Ref.1 Ref.2
Corresponds to variant rs208753 [ dbSNP | Ensembl ].
VAR_030166
Natural variant6001S → P.
Corresponds to variant rs34325017 [ dbSNP | Ensembl ].
VAR_047381
Natural variant6911A → S.
Corresponds to variant rs17635381 [ dbSNP | Ensembl ].
VAR_030167
Natural variant8711G → V.
Corresponds to variant rs7009117 [ dbSNP | Ensembl ].
VAR_030168
Natural variant12511R → H.
Corresponds to variant rs17514547 [ dbSNP | Ensembl ].
VAR_030169
Natural variant13261E → D.
Corresponds to variant rs34932823 [ dbSNP | Ensembl ].
VAR_047382
Natural variant15431T → I.
Corresponds to variant rs370429 [ dbSNP | Ensembl ].
VAR_030170
Natural variant17011K → N.
Corresponds to variant rs36113670 [ dbSNP | Ensembl ].
VAR_047383
Natural variant18651N → D.
Corresponds to variant rs35789133 [ dbSNP | Ensembl ].
VAR_047384

Experimental info

Sequence conflict2941R → RG in AAA60120. Ref.1
Sequence conflict311 – 3122EQ → DE in AAA60120. Ref.1
Sequence conflict4051E → K in AAH27477. Ref.3
Sequence conflict4081Q → K in AAH27477. Ref.3
Sequence conflict4081Q → K in AAH65022. Ref.3
Sequence conflict447 – 4482SV → CL in AAA60120. Ref.1
Sequence conflict7601Q → H in AAA60120. Ref.1
Sequence conflict9461G → R in AAA60120. Ref.1
Sequence conflict9521R → T in AAA60120. Ref.1
Sequence conflict10041Missing in AAA60120. Ref.1
Sequence conflict10861Q → R in AAA60120. Ref.1
Sequence conflict11681Q → R in AAA60120. Ref.1
Sequence conflict11691N → I in AAA60120. Ref.1
Sequence conflict11701S → L in AAA60120. Ref.1
Sequence conflict13421V → L in AAA60120. Ref.1
Sequence conflict13821R → Q in AAA60120. Ref.1
Sequence conflict15321T → A in BAC03656. Ref.4
Sequence conflict18491S → G in BAC03656. Ref.4
Sequence conflict1853 – 186412PLERE…SKNDQ → HWNEKPLVKMTK in AAA60120. Ref.1
Sequence conflict18721C → S in AAA60120. Ref.1
Sequence conflict19881E → V in BAC03656. Ref.4
Sequence conflict19981I → M in AAA60120. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 04ACFD7438F773EB

FASTA2,024228,533
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7E696A776BDC82E6
Show »

FASTA1,969222,222
Isoform 3 [UniParc].

Checksum: 52B76CDE001E0690
Show »

FASTA53059,199

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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.
[28]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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].
[30]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[32]"A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis."
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.
EMBO J. 32:3029-3040(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CILIOGENESIS, UBIQUITINATION BY MIB1, INTERACTION WITH CEP131, ASSOCIATION WITH MICROTUBULE, SUBCELLULAR LOCATION.
[33]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3B; GABARAPAL2 AND GABARAP.
+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.
CCDSCCDS47812.1. [Q15154-1]
PIRA54103.
RefSeqNP_006188.3. NM_006197.3. [Q15154-1]
UniGeneHs.491148.

3D structure databases

ProteinModelPortalQ15154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111139. 34 interactions.
DIPDIP-42189N.
IntActQ15154. 37 interactions.
MINTMINT-3295236.
STRING9606.ENSP00000327077.

PTM databases

PhosphoSiteQ15154.

Polymorphism databases

DMDM296439495.

Proteomic databases

MaxQBQ15154.
PaxDbQ15154.
PRIDEQ15154.

Protocols and materials databases

DNASU5108.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325083; ENSP00000327077; ENSG00000078674.
GeneID5108.
KEGGhsa:5108.
UCSCuc003wyi.4. human. [Q15154-1]

Organism-specific databases

CTD5108.
GeneCardsGC08P017824.
H-InvDBHIX0007341.
HGNCHGNC:8727. PCM1.
HPACAB058695.
HPA023370.
HPA023374.
MIM188550. phenotype.
600299. gene.
neXtProtNX_Q15154.
Orphanet146. Papillary or follicular thyroid carcinoma.
PharmGKBPA33073.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43239.
HOGENOMHOG000115473.
HOVERGENHBG053890.
KOK16537.
OrthoDBEOG7VTDM3.
PhylomeDBQ15154.
TreeFamTF328740.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ15154.
BgeeQ15154.
CleanExHS_PCM1.
GenevestigatorQ15154.

Family and domain databases

InterProIPR024138. Pericentriolar_Pcm1.
[Graphical view]
PANTHERPTHR14164. PTHR14164. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPCM1. human.
GeneWikiPCM1.
GenomeRNAi5108.
NextBio19712.
PROQ15154.
SOURCESearch...

Entry information

Entry namePCM1_HUMAN
AccessionPrimary (citable) accession number: Q15154
Secondary accession number(s): Q58F13 expand/collapse secondary AC list , Q6P1K7, Q8NB85, Q9BWC1, Q9H4A2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM