Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15154

- PCM1_HUMAN

UniProt

Q15154 - PCM1_HUMAN

Protein

Pericentriolar material 1 protein

Gene

PCM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1314 – 13152Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei1369 – 13702Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei1470 – 14712Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei1609 – 16102Breakpoint for translocation to form PCM1-RET fusion protein
    Sitei1947 – 19482Breakpoint for translocation to form PCM1-JAK2 fusion protein

    GO - Molecular functioni

    1. identical protein binding Source: BHF-UCL
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. centrosome organization Source: BHF-UCL
    2. cilium assembly Source: UniProtKB
    3. cytoplasmic microtubule organization Source: UniProtKB
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. interkinetic nuclear migration Source: BHF-UCL
    6. intraciliary transport involved in cilium morphogenesis Source: UniProtKB
    7. microtubule anchoring Source: BHF-UCL
    8. microtubule anchoring at centrosome Source: Ensembl
    9. mitotic cell cycle Source: Reactome
    10. negative regulation of neurogenesis Source: BHF-UCL
    11. neuronal stem cell maintenance Source: Ensembl
    12. positive regulation of intracellular protein transport Source: UniProtKB
    13. protein localization to centrosome Source: BHF-UCL

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Enzyme and pathway databases

    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pericentriolar material 1 protein
    Short name:
    PCM-1
    Short name:
    hPCM-1
    Gene namesi
    Name:PCM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:8727. PCM1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cell projection Source: UniProtKB-KW
    2. centriolar satellite Source: UniProtKB
    3. centrosome Source: UniProtKB
    4. cytoplasm Source: BHF-UCL
    5. cytosol Source: Reactome
    6. membrane Source: UniProtKB
    7. nuclear membrane Source: HPA
    8. pericentriolar material Source: BHF-UCL
    9. protein complex Source: MGI

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    MIMi188550. phenotype.
    Orphaneti146. Papillary or follicular thyroid carcinoma.
    PharmGKBiPA33073.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 20242023Pericentriolar material 1 proteinPRO_0000274037Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei65 – 651Phosphoserine7 Publications
    Modified residuei68 – 681Phosphoserine5 Publications
    Modified residuei69 – 691Phosphoserine4 Publications
    Modified residuei93 – 931Phosphoserine3 Publications
    Modified residuei110 – 1101Phosphoserine1 Publication
    Modified residuei399 – 3991N6-acetyllysine1 Publication
    Modified residuei431 – 4311Phosphoserine1 Publication
    Modified residuei643 – 6431PhosphoserineBy similarity
    Modified residuei644 – 6441PhosphoserineBy similarity
    Modified residuei861 – 8611Phosphoserine1 Publication
    Modified residuei960 – 9601Phosphoserine2 Publications
    Modified residuei1185 – 11851Phosphoserine1 Publication
    Modified residuei1231 – 12311Phosphoserine1 Publication
    Modified residuei1257 – 12571Phosphoserine1 Publication
    Modified residuei1260 – 12601Phosphoserine1 Publication
    Modified residuei1263 – 12631Phosphoserine1 Publication
    Modified residuei1697 – 16971Phosphoserine1 Publication
    Modified residuei1730 – 17301Phosphoserine4 Publications
    Modified residuei1765 – 17651Phosphoserine3 Publications
    Modified residuei1768 – 17681Phosphoserine3 Publications
    Modified residuei1776 – 17761Phosphoserine2 Publications
    Modified residuei1958 – 19581Phosphoserine1 Publication
    Modified residuei1977 – 19771Phosphoserine1 Publication

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15154.
    PaxDbiQ15154.
    PRIDEiQ15154.

    PTM databases

    PhosphoSiteiQ15154.

    Expressioni

    Tissue specificityi

    Expressed in blood, bone marrow, breast, lymph node, ovary and thyroid.4 Publications

    Inductioni

    Expression is reduced in breast and ovarian cancer.2 Publications

    Gene expression databases

    ArrayExpressiQ15154.
    BgeeiQ15154.
    CleanExiHS_PCM1.
    GenevestigatoriQ15154.

    Organism-specific databases

    HPAiCAB058695.
    HPA023370.
    HPA023374.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with C2CD3 By similarity. Interacts with BBS4, BBS8, CETN3, HAP1, NDE1, NDEL1, MAP1LC3B, GABARAPAL2, and GABARAP. Interacts with CEP131; the interaction increases in response to ultraviolet light (UV) radiation. Associates with microtubule; association to microtubule is reduced in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BBS1Q8NFJ92EBI-741421,EBI-1805484
    BBS4Q96RK416EBI-741421,EBI-1805814
    Hap1P542563EBI-741421,EBI-994539From a different organism.

    Protein-protein interaction databases

    BioGridi111139. 33 interactions.
    DIPiDIP-42189N.
    IntActiQ15154. 39 interactions.
    MINTiMINT-3295236.
    STRINGi9606.ENSP00000327077.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15154.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1279 – 1799521Interaction with HAP1Add
    BLAST
    Regioni1913 – 2024112Interaction with BBS4Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili218 – 30184Sequence AnalysisAdd
    BLAST
    Coiled coili400 – 42425Sequence AnalysisAdd
    BLAST
    Coiled coili487 – 54357Sequence AnalysisAdd
    BLAST
    Coiled coili651 – 68232Sequence AnalysisAdd
    BLAST
    Coiled coili726 – 76944Sequence AnalysisAdd
    BLAST
    Coiled coili824 – 85835Sequence AnalysisAdd
    BLAST
    Coiled coili1063 – 108927Sequence AnalysisAdd
    BLAST
    Coiled coili1515 – 153925Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PCM1 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG43239.
    HOGENOMiHOG000115473.
    HOVERGENiHBG053890.
    KOiK16537.
    OrthoDBiEOG7VTDM3.
    PhylomeDBiQ15154.
    TreeFamiTF328740.

    Family and domain databases

    InterProiIPR024138. Pericentriolar_Pcm1.
    [Graphical view]
    PANTHERiPTHR14164. PTHR14164. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15154-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK     50
    KFGVESDKRV TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL 100
    EKLKQRINFS DLDQRSIGSD SQGRATAANN KRQLSENRKP FNFLPMQINT 150
    NKSKDASTSP PNRETIGSAQ CKELFASALS NDLLQNCQVS EEDGRGEPAM 200
    ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT HLIDHLKEQE 250
    KSYMKFLKKI LARDPQQEPM EEIENLKKQH DLLKRMLQQQ EQLRALQGRQ 300
    AALLALQHKA EQAIAVMDDS VVAETAGSLS GVSITSELNE ELNDLIQRFH 350
    NQLRDSQPPA VPDNRRQAES LSLTREVSQS RKPSASERLP DEKVELFSKM 400
    RVLQEKKQKM DKLLGELHTL RDQHLNNSSS SPQRSVDQRS TSAPSASVGL 450
    APVVNGESNS LTSSVPYPTA SLVSQNESEN EGHLNPSEKL QKLNEVRKRL 500
    NELRELVHYY EQTSDMMTDA VNENRKDEET EESEYDSEHE NSEPVTNIRN 550
    PQVASTWNEV NSHSNAQCVS NNRDGRTVNS NCEINNRSAA NIRALNMPPS 600
    LDCRYNREGE QEIHVAQGED DEEEEEEAEE EGVSGASLSS HRSSLVDEHP 650
    EDAEFEQKIN RLMAAKQKLR QLQDLVAMVQ DDDAAQGVIS ASASNLDDFY 700
    PAEEDTKQNS NNTRGNANKT QKDTGVNEKA REKFYEAKLQ QQQRELKQLQ 750
    EERKKLIDIQ EKIQALQTAC PDLQLSAASV GNCPTKKYMP AVTSTPTVNQ 800
    HETSTSKSVF EPEDSSIVDN ELWSEMRRHE MLREELRQRR KQLEALMAEH 850
    QRRQGLAETA SPVAVSLRSD GSENLCTPQQ SRTEKTMATW GGSTQCALDE 900
    EGDEDGYLSE GIVRTDEEEE EEQDASSNDN FSVCPSNSVN HNSYNGKETK 950
    NRWKNNCPFS ADENYRPLAK TRQQNISMQR QENLRWVSEL SYVEEKEQWQ 1000
    EQINQLKKQL DFSVSICQTL MQDQQTLSCL LQTLLTGPYS VMPSNVASPQ 1050
    VHFIMHQLNQ CYTQLTWQQN NVQRLKQMLN ELMRQQNQHP EKPGGKERGS 1100
    SASHPPSPSL FCPFSFPTQP VNLFNIPGFT NFSSFAPGMN FSPLFPSNFG 1150
    DFSQNISTPS EQQQPLAQNS SGKTEYMAFP KPFESSSSIG AEKPRNKKLP 1200
    EEEVESSRTP WLYEQEGEVE KPFIKTGFSV SVEKSTSSNR KNQLDTNGRR 1250
    RQFDEESLES FSSMPDPVDP TTVTKTFKTR KASAQASLAS KDKTPKSKSK 1300
    KRNSTQLKSR VKNIRYESAS MSSTCEPCKS RNRHSAQTEE PVQAKVFSRK 1350
    NHEQLEKIIK CNRSTEISSE TGSDFSMFEA LRDTIYSEVA TLISQNESRP 1400
    HFLIELFHEL QLLNTDYLRQ RALYALQDIV SRHISESHEK GENVKSVNSG 1450
    TWIASNSELT PSESLATTDD ETFEKNFERE THKISEQNDA DNASVLSVSS 1500
    NFEPFATDDL GNTVIHLDQA LARMREYERM KTEAESNSNM RCTCRIIEDG 1550
    DGAGAGTTVN NLEETPVIEN RSSQQPVSEV STIPCPRIDT QQLDRQIKAI 1600
    MKEVIPFLKE HMDEVCSSQL LTSVRRMVLT LTQQNDESKE FVKFFHKQLG 1650
    SILQDSLAKF AGRKLKDCGE DLLVEISEVL FNELAFFKLM QDLDNNSITV 1700
    KQRCKRKIEA TGVIQSCAKE AKRILEDHGS PAGEIDDEDK DKDETETVKQ 1750
    TQTSEVYDGP KNVRSDISDQ EEDEESEGCP VSINLSKAET QALTNYGSGE 1800
    DENEDEEMEE FEEGPVDVQT SLQANTEATE ENEHDEQVLQ RDFKKTAESK 1850
    NVPLEREATS KNDQNNCPVK PCYLNILEDE QPLNSAAHKE SPPTVDSTQQ 1900
    PNPLPLRLPE MEPLVPRVKE VKSAQETPES SLAGSPDTES PVLVNDYEAE 1950
    SGNISQKSDE EDFVKVEDLP LKLTIYSEAD LRKKMVEEEQ KNHLSGEICE 2000
    MQTEELAGNS ETLKEPETVG AQSI 2024
    Length:2,024
    Mass (Da):228,533
    Last modified:May 18, 2010 - v4
    Checksum:i04ACFD7438F773EB
    GO
    Isoform 2 (identifier: Q15154-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,969
    Mass (Da):222,222
    Checksum:i7E696A776BDC82E6
    GO
    Isoform 3 (identifier: Q15154-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:530
    Mass (Da):59,199
    Checksum:i52B76CDE001E0690
    GO

    Sequence cautioni

    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 CAC14882.1 differs from that shown. Reason: Contaminating sequence.
    The sequence BAC03656.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941R → RG in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti311 – 3122EQ → DE in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti405 – 4051E → K in AAH27477. (PubMed:15489334)Curated
    Sequence conflicti408 – 4081Q → K in AAH27477. (PubMed:15489334)Curated
    Sequence conflicti408 – 4081Q → K in AAH65022. (PubMed:15489334)Curated
    Sequence conflicti447 – 4482SV → CL in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti760 – 7601Q → H in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti946 – 9461G → R in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti952 – 9521R → T in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1004 – 10041Missing in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1086 – 10861Q → R in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1168 – 11681Q → R in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1169 – 11691N → I in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1170 – 11701S → L in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1342 – 13421V → L in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1382 – 13821R → Q in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1532 – 15321T → A in BAC03656. (PubMed:14702039)Curated
    Sequence conflicti1849 – 18491S → G in BAC03656. (PubMed:14702039)Curated
    Sequence conflicti1853 – 186412PLERE…SKNDQ → HWNEKPLVKMTK in AAA60120. (PubMed:8120099)CuratedAdd
    BLAST
    Sequence conflicti1872 – 18721C → S in AAA60120. (PubMed:8120099)Curated
    Sequence conflicti1988 – 19881E → V in BAC03656. (PubMed:14702039)Curated
    Sequence conflicti1998 – 19981I → M in AAA60120. (PubMed:8120099)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti159 – 1591S → N.
    Corresponds to variant rs412750 [ dbSNP | Ensembl ].
    VAR_030164
    Natural varianti159 – 1591S → R.
    Corresponds to variant rs412750 [ dbSNP | Ensembl ].
    VAR_062172
    Natural varianti176 – 1761A → D.
    Corresponds to variant rs2285302 [ dbSNP | Ensembl ].
    VAR_030165
    Natural varianti597 – 5971M → V.2 Publications
    Corresponds to variant rs208753 [ dbSNP | Ensembl ].
    VAR_030166
    Natural varianti600 – 6001S → P.
    Corresponds to variant rs34325017 [ dbSNP | Ensembl ].
    VAR_047381
    Natural varianti691 – 6911A → S.
    Corresponds to variant rs17635381 [ dbSNP | Ensembl ].
    VAR_030167
    Natural varianti871 – 8711G → V.
    Corresponds to variant rs7009117 [ dbSNP | Ensembl ].
    VAR_030168
    Natural varianti1251 – 12511R → H.
    Corresponds to variant rs17514547 [ dbSNP | Ensembl ].
    VAR_030169
    Natural varianti1326 – 13261E → D.
    Corresponds to variant rs34932823 [ dbSNP | Ensembl ].
    VAR_047382
    Natural varianti1543 – 15431T → I.
    Corresponds to variant rs370429 [ dbSNP | Ensembl ].
    VAR_030170
    Natural varianti1701 – 17011K → N.
    Corresponds to variant rs36113670 [ dbSNP | Ensembl ].
    VAR_047383
    Natural varianti1865 – 18651N → D.
    Corresponds to variant rs35789133 [ dbSNP | Ensembl ].
    VAR_047384

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei263 – 2631R → RENEEEDVRTIDSAVGSGSV AESTSLNIDVQSEASDTTAR in isoform 3. 1 PublicationVSP_022609
    Alternative sequencei492 – 20241533Missing in isoform 3. 1 PublicationVSP_022610Add
    BLAST
    Alternative sequencei1315 – 137056RYESA…EISSE → K in isoform 2. 1 PublicationVSP_022611Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS47812.1. [Q15154-1]
    PIRiA54103.
    RefSeqiNP_006188.3. NM_006197.3. [Q15154-1]
    UniGeneiHs.491148.

    Genome annotation databases

    EnsembliENST00000325083; ENSP00000327077; ENSG00000078674.
    GeneIDi5108.
    KEGGihsa:5108.
    UCSCiuc003wyi.4. human. [Q15154-1]

    Polymorphism databases

    DMDMi296439495.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS47812.1. [Q15154-1 ]
    PIRi A54103.
    RefSeqi NP_006188.3. NM_006197.3. [Q15154-1 ]
    UniGenei Hs.491148.

    3D structure databases

    ProteinModelPortali Q15154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111139. 33 interactions.
    DIPi DIP-42189N.
    IntActi Q15154. 39 interactions.
    MINTi MINT-3295236.
    STRINGi 9606.ENSP00000327077.

    PTM databases

    PhosphoSitei Q15154.

    Polymorphism databases

    DMDMi 296439495.

    Proteomic databases

    MaxQBi Q15154.
    PaxDbi Q15154.
    PRIDEi Q15154.

    Protocols and materials databases

    DNASUi 5108.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325083 ; ENSP00000327077 ; ENSG00000078674 .
    GeneIDi 5108.
    KEGGi hsa:5108.
    UCSCi uc003wyi.4. human. [Q15154-1 ]

    Organism-specific databases

    CTDi 5108.
    GeneCardsi GC08P017824.
    H-InvDB HIX0007341.
    HGNCi HGNC:8727. PCM1.
    HPAi CAB058695.
    HPA023370.
    HPA023374.
    MIMi 188550. phenotype.
    600299. gene.
    neXtProti NX_Q15154.
    Orphaneti 146. Papillary or follicular thyroid carcinoma.
    PharmGKBi PA33073.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43239.
    HOGENOMi HOG000115473.
    HOVERGENi HBG053890.
    KOi K16537.
    OrthoDBi EOG7VTDM3.
    PhylomeDBi Q15154.
    TreeFami TF328740.

    Enzyme and pathway databases

    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi PCM1. human.
    GeneWikii PCM1.
    GenomeRNAii 5108.
    NextBioi 19712.
    PROi Q15154.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15154.
    Bgeei Q15154.
    CleanExi HS_PCM1.
    Genevestigatori Q15154.

    Family and domain databases

    InterProi IPR024138. Pericentriolar_Pcm1.
    [Graphical view ]
    PANTHERi PTHR14164. PTHR14164. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: CHROMOSOMAL TRANSLOCATION WITH JAK2.
    14. 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. 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. 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. 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.

    Entry informationi

    Entry nameiPCM1_HUMAN
    AccessioniPrimary (citable) accession number: Q15154
    Secondary accession number(s): Q58F13
    , Q6P1K7, Q8NB85, Q9BWC1, Q9H4A2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 113 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3