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O95613

- PCNT_HUMAN

UniProt

O95613 - PCNT_HUMAN

Protein

Pericentrin

Gene

PCNT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome.4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. brain morphogenesis Source: Ensembl
    2. cerebellar cortex morphogenesis Source: Ensembl
    3. cilium assembly Source: MGI
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. in utero embryonic development Source: Ensembl
    6. limb morphogenesis Source: Ensembl
    7. microtubule cytoskeleton organization Source: UniProtKB
    8. mitotic cell cycle Source: Reactome
    9. multicellular organism growth Source: Ensembl
    10. negative regulation of apoptotic process Source: Ensembl
    11. neural precursor cell proliferation Source: Ensembl
    12. neuron migration Source: Ensembl
    13. olfactory bulb development Source: Ensembl
    14. positive regulation of intracellular protein transport Source: UniProtKB
    15. spindle organization Source: Ensembl

    Keywords - Ligandi

    Calmodulin-binding

    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:
    Pericentrin
    Alternative name(s):
    Kendrin
    Pericentrin-B
    Gene namesi
    Name:PCNT
    Synonyms:KIAA0402, PCNT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:16068. PCNT.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 4 Publications
    Note: Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome.

    GO - Cellular componenti

    1. centriolar satellite Source: UniProtKB
    2. centriole Source: MGI
    3. centrosome Source: UniProtKB
    4. cytoplasm Source: HPA
    5. cytosol Source: Reactome
    6. intercellular bridge Source: Ensembl
    7. membrane Source: UniProtKB
    8. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Microcephalic osteodysplastic primordial dwarfism 2 (MOPD2) [MIM:210720]: Adults with this rare inherited condition have an average height of 100 centimeters and a brain size comparable to that of a 3-month-old baby, but are of near-normal intelligence.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi3196 – 31972FR → AA: Decrease in calmodulin binding.
    Mutagenesisi3203 – 32031V → A: Decrease in calmodulin binding. 1 Publication
    Mutagenesisi3208 – 32092RL → AA: Decrease in calmodulin binding.

    Keywords - Diseasei

    Dwarfism

    Organism-specific databases

    MIMi210720. phenotype.
    Orphaneti2637. Microcephalic osteodysplastic primordial dwarfism type II.
    808. Seckel syndrome.
    PharmGKBiPA33079.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 33363336PericentrinPRO_0000058257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei191 – 1911Phosphothreonine1 Publication
    Modified residuei682 – 6821Phosphoserine1 Publication
    Modified residuei1712 – 17121PhosphoserineBy similarity
    Modified residuei2044 – 20441Phosphoserine1 Publication
    Modified residuei2177 – 21771Phosphoserine1 Publication
    Modified residuei2327 – 23271Phosphoserine1 Publication
    Modified residuei2477 – 24771Phosphoserine1 Publication
    Modified residuei2486 – 24861Phosphoserine1 Publication
    Modified residuei3302 – 33021Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95613.
    PaxDbiO95613.
    PRIDEiO95613.

    PTM databases

    PhosphoSiteiO95613.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, including placenta, liver, kidney and thymus.1 Publication

    Gene expression databases

    BgeeiO95613.
    CleanExiHS_PCNT.
    GenevestigatoriO95613.

    Organism-specific databases

    HPAiHPA016820.
    HPA019887.
    HPA032101.

    Interactioni

    Subunit structurei

    Interacts with CHD3. Interacts with CHD4; the interaction regulates centrosome integrity By similarity. Interacts with DISC1 and PCM1. Binds calmodulin. Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of PCNT and CDK5RAP2. Interacts with isoform 1 of NEK2. Interacts with CEP131.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI55EBI-530012,EBI-529989

    Protein-protein interaction databases

    BioGridi111146. 17 interactions.
    IntActiO95613. 7 interactions.
    MINTiMINT-4527763.
    STRINGi9606.ENSP00000352572.

    Structurei

    3D structure databases

    ProteinModelPortaliO95613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2983 – 3246264Interaction with NEK2Add
    BLAST
    Regioni3195 – 320814Calmodulin-bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili258 – 553296Sequence AnalysisAdd
    BLAST
    Coiled coili675 – 835161Sequence AnalysisAdd
    BLAST
    Coiled coili1010 – 1146137Sequence AnalysisAdd
    BLAST
    Coiled coili1299 – 1949651Sequence AnalysisAdd
    BLAST
    Coiled coili2064 – 208219Sequence AnalysisAdd
    BLAST
    Coiled coili2536 – 3086551Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi214 – 795582Glu-richAdd
    BLAST

    Domaini

    Composed of a coiled-coil central region flanked by non-helical N- and C-terminals.

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000168229.
    HOVERGENiHBG079443.
    InParanoidiO95613.
    KOiK16481.
    OMAiEQRGMFT.
    OrthoDBiEOG7DRJ25.
    PhylomeDBiO95613.
    TreeFamiTF336114.

    Family and domain databases

    InterProiIPR019528. PACT_domain.
    IPR024151. Pericentrin.
    [Graphical view]
    PANTHERiPTHR18932:SF11. PTHR18932:SF11. 1 hit.
    PfamiPF10495. PACT_coil_coil. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95613-1) [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

    MEVEQEQRRR KVEAGRTKLA HFRQRKTKGD SSHSEKKTAK RKGSAVDASV     50
    QEESPVTKED SALCGGGDIC KSTSCDDTPD GAGGAFAAQP EDCDGEKRED 100
    LEQLQQKQVN DHPPEQCGMF TVSDHPPEQH GMFTVGDHPP EQRGMFTVSD 150
    HPPEQHGMFT VSDHPPEQRG MFTISDHQPE QRGMFTVSDH TPEQRGIFTI 200
    SDHPAEQRGM FTKECEQECE LAITDLESGR EDEAGLHQSQ AVHGLELEAL 250
    RLSLSNMHTA QLELTQANLQ KEKETALTEL REMLNSRRAQ ELALLQSRQQ 300
    HELELLREQH AREKEEVVLR CGQEAAELKE KLQSEMEKNA QIVKTLKEDW 350
    ESEKDLCLEN LRKELSAKHQ SEMEDLQNQF QKELAEQRAE LEKIFQDKNQ 400
    AERALRNLES HHQAAIEKLR EDLQSEHGRC LEDLEFKFKE SEKEKQLELE 450
    NLQASYEDLK AQSQEEIRRL WSQLDSARTS RQELSELHEQ LLARTSRVED 500
    LEQLKQREKT QHESELEQLR IYFEKKLRDA EKTYQEDLTL LQQRLQGARE 550
    DALLDSVEVG LSCVGLEEKP EKGRKDHVDE LEPERHKESL PRFQAELEES 600
    HRHQLEALES PLCIQHEGHV SDRCCVETSA LGHEWRLEPS EGHSQELPWV 650
    HLQGVQDGDL EADTERAARV LGLETEHKVQ LSLLQTELKE EIELLKIENR 700
    NLYGKLQHET RLKDDLEKVK HNLIEDHQKE LNNAKQKTEL MKQEFQRKET 750
    DWKVMKEELQ REAEEKLTLM LLELREKAES EKQTIINKFE LREAEMRQLQ 800
    DQQAAQILDL ERSLTEQQGR LQQLEQDLTS DDALHCSQCG REPPTAQDGE 850
    LAALHVKEDC ALQLMLARSR FLEERKEITE KFSAEQDAFL QEAQEQHARE 900
    LQLLQERHQQ QLLSVTAELE ARHQAALGEL TASLESKQGA LLAARVAELQ 950
    TKHAADLGAL ETRHLSSLDS LESCYLSEFQ TIREEHRQAL ELLRADFEEQ 1000
    LWKKDSLHQT ILTQELEKLK RKHEGELQSV RDHLRTEVST ELAGTVAHEL 1050
    QGVHQGEFGS EKKTALHEKE ETLRLQSAQA QPFHQEEKES LSLQLQKKNH 1100
    QVQQLKDQVL SLSHEIEECR SELEVLQQRR ERENREGANL LSMLKADVNL 1150
    SHSERGALQD ALRRLLGLFG ETLRAAVTLR SRIGERVGLC LDDAGAGLAL 1200
    STAPALEETW SDVALPELDR TLSECAEMSS VAEISSHMRE SFLMSPESVR 1250
    ECEQPIRRVF QSLSLAVDGL MEMALDSSRQ LEEARQIHSR FEKEFSFKNE 1300
    ETAQVVRKHQ ELLECLKEES AAKAELALEL HKTQGTLEGF KVETADLKEV 1350
    LAGKEDSEHR LVLELESLRR QLQQAAQEQA ALREECTRLW SRGEATATDA 1400
    EAREAALRKE VEDLTKEQSE TRKQAEKDRS ALLSQMKILE SELEEQLSQH 1450
    RGCAKQAEAV TALEQQVASL DKHLRNQRQF MDEQAAEREH EREEFQQEIQ 1500
    RLEGQLRQAA KPQPWGPRDS QQAPLDGEVE LLQQKLREKL DEFNELAIQK 1550
    ESADRQVLMQ EEEIKRLEEM NINIRKKVAQ LQEEVEKQKN IVKGLEQDKE 1600
    VLKKQQMSSL LLASTLQSTL DAGRCPEPPS GSPPEGPEIQ LEVTQRALLR 1650
    RESEVLDLKE QLEKMKGDLE SKNEEILHLN LKLDMQNSQT AVSLRELEEE 1700
    NTSLKVIYTR SSEIEELKAT IENLQENQKR LQKEKAEEIE QLHEVIEKLQ 1750
    HELSLMGPVV HEVSDSQAGS LQSELLCSQA GGPRGQALQG ELEAALEAKE 1800
    ALSRLLADQE RRHSQALEAL QQRLQGAEEA AELQLAELER NVALREAEVE 1850
    DMASRIQEFE AALKAKEATI AERNLEIDAL NQRKAAHSAE LEAVLLALAR 1900
    IRRALEQQPL AAGAAPPELQ WLRAQCARLS RQLQVLHQRF LRCQVELDRR 1950
    QARRATAHTR VPGAHPQPRM DGGAKAQVTG DVEASHDAAL EPVVPDPQGD 2000
    LQPVLVTLKD APLCKQEGVM SVLTVCQRQL QSELLLVKNE MRLSLEDGGK 2050
    GKEKVLEDCQ LPKVDLVAQV KQLQEKLNRL LYSMTFQNVD AADTKSLWPM 2100
    ASAHLLESSW SDDSCDGEEP DISPHIDTCD ANTATGGVTD VIKNQAIDAC 2150
    DANTTPGGVT DVIKNWDSLI PDEMPDSPIQ EKSECQDMSL SSPTSVLGGS 2200
    RHQSHTAEAG PRKSPVGMLD LSSWSSPEVL RKDWTLEPWP SLPVTPHSGA 2250
    LSLCSADTSL GDRADTSLPQ TQGPGLLCSP GVSAAALALQ WAESPPADDH 2300
    HVQRTAVEKD VEDFITTSFD SQETLSSPPP GLEGKADRSE KSDGSGFGAR 2350
    LSPGSGGPEA QTAGPVTPAS ISGRFQPLPE AMKEKEVRPK HVKALLQMVR 2400
    DESHQILALS EGLAPPSGEP HPPRKEDEIQ DISLHGGKTQ EVPTACPDWR 2450
    GDLLQVVQEA FEKEQEMQGV ELQPRLSGSD LGGHSSLLER LEKIIREQGD 2500
    LQEKSLEHLR LPDRSSLLSE IQALRAQLRM THLQNQEKLQ HLRTALTSAE 2550
    ARGSQQEHQL RRQVELLAYK VEQEKCIAGD LQKTLSEEQE KANSVQKLLA 2600
    AEQTVVRDLK SDLCESRQKS EQLSRSLCEV QQEVLQLRSM LSSKENELKA 2650
    ALQELESEQG KGRALQSQLE EEQLRHLQRE SQSAKALEEL RASLETQRAQ 2700
    SSRLCVALKH EQTAKDNLQK ELRIEHSRCE ALLAQERSQL SELQKDLAAE 2750
    KSRTLELSEA LRHERLLTEQ LSQRTQEACV HQDTQAHHAL LQKLKEEKSR 2800
    VVDLQAMLEK VQQQALHSQQ QLEAEAQKHC EALRREKEVS ATLKSTVEAL 2850
    HTQKRELRCS LEREREKPAW LQAELEQSHP RLKEQEGRKA ARRSAEARQS 2900
    PAAAEQWRKW QRDKEKLREL ELQRQRDLHK IKQLQQTVRD LESKDEVPGS 2950
    RLHLGSARRA AGSDADHLRE QQRELEAMRQ RLLSAARLLT SFTSQAVDRT 3000
    VNDWTSSNEK AVMSLLHTLE ELKSDLSRPT SSQKKMAAEL QFQFVDVLLK 3050
    DNVSLTKALS TVTQEKLELS RAVSKLEKLL KHHLQKGCSP SRSERSAWKP 3100
    DETAPQSSLR RPDPGRLPPA ASEEAHTSNV KMEKLYLHYL RAESFRKALI 3150
    YQKKYLLLLI GGFQDSEQET LSMIAHLGVF PSKAERKITS RPFTRFRTAV 3200
    RVVIAILRLR FLVKKWQEVD RKGALAQGKA PRPGPRARQP QSPPRTRESP 3250
    PTRDVPSGHT RDPARGRRLA AAASPHSGGR ATPSPNSRLE RSLTASQDPE 3300
    HSLTEYIHHL EVIQQRLGGV LPDSTSKKSC HPMIKQ 3336
    Length:3,336
    Mass (Da):378,037
    Last modified:November 30, 2010 - v4
    Checksum:i4F182D2C201662A8
    GO
    Isoform 2 (identifier: O95613-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.
         2839-2917: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:3,139
    Mass (Da):355,882
    Checksum:iA0FD227ABCF410FD
    GO

    Sequence cautioni

    The sequence AAD10838.1 differs from that shown. Reason: Frameshift at position 3320.
    The sequence BAA23698.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC04252.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti703 – 7031Y → F in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti789 – 7891F → L in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti819 – 8191G → A in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti890 – 90011Missing in AAD10838. (PubMed:11171385)CuratedAdd
    BLAST
    Sequence conflicti967 – 9671S → T in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti1024 – 10241E → K in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti1036 – 10361T → A in BAC04252. (PubMed:14702039)Curated
    Sequence conflicti1287 – 12871I → L in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti1317 – 13171K → T in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti1534 – 15341Q → H in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti3136 – 31361Y → S in AAD10838. (PubMed:11171385)Curated
    Sequence conflicti3300 – 33001E → G in AAD10838. (PubMed:11171385)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti539 – 5391T → I.
    Corresponds to variant rs2249060 [ dbSNP | Ensembl ].
    VAR_043878
    Natural varianti704 – 7041G → E.3 Publications
    Corresponds to variant rs2839223 [ dbSNP | Ensembl ].
    VAR_043879
    Natural varianti879 – 8791T → A.1 Publication
    Corresponds to variant rs2839227 [ dbSNP | Ensembl ].
    VAR_043880
    Natural varianti1038 – 10381V → A.3 Publications
    Corresponds to variant rs6518289 [ dbSNP | Ensembl ].
    VAR_043881
    Natural varianti1163 – 11631R → C.
    Corresponds to variant rs7279204 [ dbSNP | Ensembl ].
    VAR_043882
    Natural varianti1194 – 11941A → T.
    Corresponds to variant rs35044802 [ dbSNP | Ensembl ].
    VAR_043883
    Natural varianti1452 – 14521G → R Found in a patient with mental retardation, no speech, facial and limbs dysmorphisms. 1 Publication
    VAR_069420
    Natural varianti1639 – 16391I → V.
    Corresponds to variant rs6518291 [ dbSNP | Ensembl ].
    VAR_043884
    Natural varianti1841 – 18411N → S.
    Corresponds to variant rs35940413 [ dbSNP | Ensembl ].
    VAR_043885
    Natural varianti1953 – 19531R → H.
    Corresponds to variant rs34268261 [ dbSNP | Ensembl ].
    VAR_043886
    Natural varianti1960 – 19601R → Q.
    Corresponds to variant rs34813667 [ dbSNP | Ensembl ].
    VAR_043887
    Natural varianti2097 – 20971L → P.
    Corresponds to variant rs2839245 [ dbSNP | Ensembl ].
    VAR_043888
    Natural varianti2125 – 21251H → P.
    Corresponds to variant rs35978208 [ dbSNP | Ensembl ].
    VAR_043889
    Natural varianti2188 – 21881M → R.1 Publication
    Corresponds to variant rs1044998 [ dbSNP | Ensembl ].
    VAR_043890
    Natural varianti2191 – 21911S → P.
    Corresponds to variant rs34151633 [ dbSNP | Ensembl ].
    VAR_043891
    Natural varianti2239 – 22391W → R.
    Corresponds to variant rs35346764 [ dbSNP | Ensembl ].
    VAR_056961
    Natural varianti2274 – 22741P → L.
    Corresponds to variant rs2070425 [ dbSNP | Ensembl ].
    VAR_056962
    Natural varianti2329 – 23291P → R.
    Corresponds to variant rs35848602 [ dbSNP | Ensembl ].
    VAR_056963
    Natural varianti2361 – 23611Q → R.
    Corresponds to variant rs7277175 [ dbSNP | Ensembl ].
    VAR_056964
    Natural varianti2424 – 24241R → Q Found in a patient with mental retardation, no speech, facial and limbs dysmorphisms. 1 Publication
    VAR_069421
    Natural varianti2549 – 25491A → T.1 Publication
    Corresponds to variant rs2839256 [ dbSNP | Ensembl ].
    VAR_056965
    Natural varianti2625 – 26251R → Q.
    Corresponds to variant rs8131693 [ dbSNP | Ensembl ].
    VAR_056966
    Natural varianti2659 – 26591Q → H.
    Corresponds to variant rs2070426 [ dbSNP | Ensembl ].
    VAR_056967
    Natural varianti2753 – 27531R → H.
    Corresponds to variant rs743346 [ dbSNP | Ensembl ].
    VAR_056968
    Natural varianti2792 – 27921Q → R.
    Corresponds to variant rs2073376 [ dbSNP | Ensembl ].
    VAR_056969
    Natural varianti2903 – 29031A → T.
    Corresponds to variant rs35147998 [ dbSNP | Ensembl ].
    VAR_056970
    Natural varianti2975 – 29751L → P.
    Corresponds to variant rs35881595 [ dbSNP | Ensembl ].
    VAR_056971
    Natural varianti3091 – 30911S → G.
    Corresponds to variant rs4818842 [ dbSNP | Ensembl ].
    VAR_056972
    Natural varianti3245 – 32451R → S.
    Corresponds to variant rs2073380 [ dbSNP | Ensembl ].
    VAR_056973

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 2. 1 PublicationVSP_040104Add
    BLAST
    Alternative sequencei2839 – 291779Missing in isoform 2. 1 PublicationVSP_040105Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52962 mRNA. Translation: AAD10838.1. Frameshift.
    AF515282 mRNA. Translation: AAP46636.1.
    AB007862 mRNA. Translation: BAA23698.3. Different initiation.
    AP000471 Genomic DNA. No translation available.
    AP001477 Genomic DNA. No translation available.
    AP000335 Genomic DNA. No translation available.
    AP000336 Genomic DNA. No translation available.
    AP000337 Genomic DNA. No translation available.
    AK093923 mRNA. Translation: BAC04252.1. Different initiation.
    CCDSiCCDS33592.1. [O95613-1]
    RefSeqiNP_006022.3. NM_006031.5. [O95613-1]
    XP_005261186.1. XM_005261129.1. [O95613-2]
    UniGeneiHs.474069.

    Genome annotation databases

    EnsembliENST00000359568; ENSP00000352572; ENSG00000160299. [O95613-1]
    GeneIDi5116.
    KEGGihsa:5116.
    UCSCiuc002zji.4. human. [O95613-1]
    uc002zjj.3. human. [O95613-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52962 mRNA. Translation: AAD10838.1 . Frameshift.
    AF515282 mRNA. Translation: AAP46636.1 .
    AB007862 mRNA. Translation: BAA23698.3 . Different initiation.
    AP000471 Genomic DNA. No translation available.
    AP001477 Genomic DNA. No translation available.
    AP000335 Genomic DNA. No translation available.
    AP000336 Genomic DNA. No translation available.
    AP000337 Genomic DNA. No translation available.
    AK093923 mRNA. Translation: BAC04252.1 . Different initiation.
    CCDSi CCDS33592.1. [O95613-1 ]
    RefSeqi NP_006022.3. NM_006031.5. [O95613-1 ]
    XP_005261186.1. XM_005261129.1. [O95613-2 ]
    UniGenei Hs.474069.

    3D structure databases

    ProteinModelPortali O95613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111146. 17 interactions.
    IntActi O95613. 7 interactions.
    MINTi MINT-4527763.
    STRINGi 9606.ENSP00000352572.

    PTM databases

    PhosphoSitei O95613.

    Proteomic databases

    MaxQBi O95613.
    PaxDbi O95613.
    PRIDEi O95613.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359568 ; ENSP00000352572 ; ENSG00000160299 . [O95613-1 ]
    GeneIDi 5116.
    KEGGi hsa:5116.
    UCSCi uc002zji.4. human. [O95613-1 ]
    uc002zjj.3. human. [O95613-2 ]

    Organism-specific databases

    CTDi 5116.
    GeneCardsi GC21P047744.
    H-InvDB HIX0203117.
    HGNCi HGNC:16068. PCNT.
    HPAi HPA016820.
    HPA019887.
    HPA032101.
    MIMi 210720. phenotype.
    605925. gene.
    neXtProti NX_O95613.
    Orphaneti 2637. Microcephalic osteodysplastic primordial dwarfism type II.
    808. Seckel syndrome.
    PharmGKBi PA33079.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000168229.
    HOVERGENi HBG079443.
    InParanoidi O95613.
    KOi K16481.
    OMAi EQRGMFT.
    OrthoDBi EOG7DRJ25.
    PhylomeDBi O95613.
    TreeFami TF336114.

    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 PCNT. human.
    GeneWikii PCNT.
    GenomeRNAii 5116.
    NextBioi 19730.
    PROi O95613.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95613.
    CleanExi HS_PCNT.
    Genevestigatori O95613.

    Family and domain databases

    InterProi IPR019528. PACT_domain.
    IPR024151. Pericentrin.
    [Graphical view ]
    PANTHERi PTHR18932:SF11. PTHR18932:SF11. 1 hit.
    Pfami PF10495. PACT_coil_coil. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin that complexes with PCM-1."
      Li Q., Hansen D., Killilea A., Joshi H.C., Palazzo R.E., Balczon R.
      J. Cell Sci. 114:797-809(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, VARIANTS GLU-704; ALA-879; ALA-1038; ARG-2188 AND THR-2549.
    2. "Vertebrate centrosome proteins that share homology with yeast mitotic exit proteins are required for cytokinesis and cell cycle progression."
      Gromley A.S., Jurczyk A., Sillibourne J.E., Halilovic E., Doxsey S.J.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-704.
    3. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
      Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS GLU-704 AND ALA-1038.
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 3023.
    5. Ohara O.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 787-1533 (ISOFORM 1), VARIANT ALA-1038.
      Tissue: Trachea.
    8. "Identification of a human centrosomal calmodulin-binding protein that shares homology with pericentrin."
      Flory M.R., Moser M.J., Monnat R.J. Jr., Davis T.N.
      Proc. Natl. Acad. Sci. U.S.A. 97:5919-5923(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CALMODULIN-BINDING DOMAIN, MUTAGENESIS OF 3196-PHE-ARG-3197; VAL-3203 AND 3208-ARG-LEU-3209.
    9. "DISC1-kendrin interaction is involved in centrosomal microtubule network formation."
      Shimizu S., Matsuzaki S., Hattori T., Kumamoto N., Miyoshi K., Katayama T., Tohyama M.
      Biochem. Biophys. Res. Commun. 377:1051-1056(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DISC1, SUBCELLULAR LOCATION.
    10. "Mutations in pericentrin cause Seckel syndrome with defective ATR-dependent DNA damage signaling."
      Griffith E., Walker S., Martin C.-A., Vagnarelli P., Stiff T., Vernay B., Al Sanna N., Saggar A., Hamel B., Earnshaw W.C., Jeggo P.A., Jackson A.P., O'Driscoll M.
      Nat. Genet. 40:232-236(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MOPD2.
    11. Cited for: INVOLVEMENT IN MOPD2.
    12. "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-2177 AND SER-2327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Involvement of a centrosomal protein kendrin in the maintenance of centrosome cohesion by modulating Nek2A kinase activity."
      Matsuo K., Nishimura T., Hayakawa A., Ono Y., Takahashi M.
      Biochem. Biophys. Res. Commun. 398:217-223(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEK2.
    14. "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex."
      Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.
      J. Biol. Chem. 285:22658-22665(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK5RAP2.
    15. "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 THR-191; SER-682; SER-2044; SER-2477; SER-2486 AND SER-3302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: INTERACTION WITH CEP131, SUBCELLULAR LOCATION.
    18. Cited for: VARIANTS ARG-1452 AND GLN-2424.

    Entry informationi

    Entry nameiPCNT_HUMAN
    AccessioniPrimary (citable) accession number: O95613
    Secondary accession number(s): O43152, Q7Z7C9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 140 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 21
      Human chromosome 21: 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

    External Data

    Dasty 3