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O95613 (PCNT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Pericentrin
Alternative name(s):
Kendrin
Pericentrin-B
Gene names
Name:PCNT
Synonyms:KIAA0402, PCNT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3336 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9 Ref.13

Subunit structure

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. Ref.1 Ref.9 Ref.13 Ref.14

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome. Ref.1 Ref.8 Ref.9

Tissue specificity

Expressed in all tissues tested, including placenta, liver, kidney and thymus. Ref.8

Domain

Composed of a coiled-coil central region flanked by non-helical N- and C-terminals. Ref.8

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11

Sequence caution

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDwarfism
   DomainCoiled coil
   LigandCalmodulin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

brain morphogenesis

Inferred from electronic annotation. Source: Ensembl

cerebellar cortex morphogenesis

Inferred from electronic annotation. Source: Ensembl

cilium assembly

Inferred from direct assay PubMed 15337773. Source: MGI

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

neural precursor cell proliferation

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

olfactory bulb development

Inferred from electronic annotation. Source: Ensembl

spindle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentriole

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay Ref.9PubMed 19543530PubMed 21399614. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

intercellular bridge

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DISC1Q9NRI55EBI-530012,EBI-529989

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95613-1)

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: O95613-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
     2839-2917: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 33363336Pericentrin
PRO_0000058257

Regions

Region2983 – 3246264Interaction with NEK2
Region3195 – 320814Calmodulin-binding
Coiled coil258 – 553296 Potential
Coiled coil675 – 835161 Potential
Coiled coil1010 – 1146137 Potential
Coiled coil1299 – 1949651 Potential
Coiled coil2064 – 208219 Potential
Coiled coil2536 – 3086551 Potential
Compositional bias214 – 795582Glu-rich

Amino acid modifications

Modified residue1911Phosphothreonine Ref.15
Modified residue6821Phosphoserine Ref.15
Modified residue17121Phosphoserine By similarity
Modified residue20441Phosphoserine Ref.15
Modified residue21771Phosphoserine Ref.12
Modified residue23271Phosphoserine Ref.12
Modified residue24771Phosphoserine Ref.15
Modified residue24861Phosphoserine Ref.15
Modified residue33021Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 118118Missing in isoform 2.
VSP_040104
Alternative sequence2839 – 291779Missing in isoform 2.
VSP_040105
Natural variant5391T → I.
Corresponds to variant rs2249060 [ dbSNP | Ensembl ].
VAR_043878
Natural variant7041G → E. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2839223 [ dbSNP | Ensembl ].
VAR_043879
Natural variant8791T → A. Ref.1
Corresponds to variant rs2839227 [ dbSNP | Ensembl ].
VAR_043880
Natural variant10381V → A. Ref.1 Ref.3 Ref.7
Corresponds to variant rs6518289 [ dbSNP | Ensembl ].
VAR_043881
Natural variant11631R → C.
Corresponds to variant rs7279204 [ dbSNP | Ensembl ].
VAR_043882
Natural variant11941A → T.
Corresponds to variant rs35044802 [ dbSNP | Ensembl ].
VAR_043883
Natural variant14521G → R Found in a patient with mental retardation, no speech, facial and limbs dysmorphisms. Ref.17
VAR_069420
Natural variant16391I → V.
Corresponds to variant rs6518291 [ dbSNP | Ensembl ].
VAR_043884
Natural variant18411N → S.
Corresponds to variant rs35940413 [ dbSNP | Ensembl ].
VAR_043885
Natural variant19531R → H.
Corresponds to variant rs34268261 [ dbSNP | Ensembl ].
VAR_043886
Natural variant19601R → Q.
Corresponds to variant rs34813667 [ dbSNP | Ensembl ].
VAR_043887
Natural variant20971L → P.
Corresponds to variant rs2839245 [ dbSNP | Ensembl ].
VAR_043888
Natural variant21251H → P.
Corresponds to variant rs35978208 [ dbSNP | Ensembl ].
VAR_043889
Natural variant21881M → R. Ref.1
Corresponds to variant rs1044998 [ dbSNP | Ensembl ].
VAR_043890
Natural variant21911S → P.
Corresponds to variant rs34151633 [ dbSNP | Ensembl ].
VAR_043891
Natural variant22391W → R.
Corresponds to variant rs35346764 [ dbSNP | Ensembl ].
VAR_056961
Natural variant22741P → L.
Corresponds to variant rs2070425 [ dbSNP | Ensembl ].
VAR_056962
Natural variant23291P → R.
Corresponds to variant rs35848602 [ dbSNP | Ensembl ].
VAR_056963
Natural variant23611Q → R.
Corresponds to variant rs7277175 [ dbSNP | Ensembl ].
VAR_056964
Natural variant24241R → Q Found in a patient with mental retardation, no speech, facial and limbs dysmorphisms. Ref.17
VAR_069421
Natural variant25491A → T. Ref.1
Corresponds to variant rs2839256 [ dbSNP | Ensembl ].
VAR_056965
Natural variant26251R → Q.
Corresponds to variant rs8131693 [ dbSNP | Ensembl ].
VAR_056966
Natural variant26591Q → H.
Corresponds to variant rs2070426 [ dbSNP | Ensembl ].
VAR_056967
Natural variant27531R → H.
Corresponds to variant rs743346 [ dbSNP | Ensembl ].
VAR_056968
Natural variant27921Q → R.
Corresponds to variant rs2073376 [ dbSNP | Ensembl ].
VAR_056969
Natural variant29031A → T.
Corresponds to variant rs35147998 [ dbSNP | Ensembl ].
VAR_056970
Natural variant29751L → P.
Corresponds to variant rs35881595 [ dbSNP | Ensembl ].
VAR_056971
Natural variant30911S → G.
Corresponds to variant rs4818842 [ dbSNP | Ensembl ].
VAR_056972
Natural variant32451R → S.
Corresponds to variant rs2073380 [ dbSNP | Ensembl ].
VAR_056973

Experimental info

Mutagenesis3196 – 31972FR → AA: Decrease in calmodulin binding.
Mutagenesis32031V → A: Decrease in calmodulin binding. Ref.8
Mutagenesis3208 – 32092RL → AA: Decrease in calmodulin binding.
Sequence conflict7031Y → F in AAD10838. Ref.1
Sequence conflict7891F → L in AAD10838. Ref.1
Sequence conflict8191G → A in AAD10838. Ref.1
Sequence conflict890 – 90011Missing in AAD10838. Ref.1
Sequence conflict9671S → T in AAD10838. Ref.1
Sequence conflict10241E → K in AAD10838. Ref.1
Sequence conflict10361T → A in BAC04252. Ref.7
Sequence conflict12871I → L in AAD10838. Ref.1
Sequence conflict13171K → T in AAD10838. Ref.1
Sequence conflict15341Q → H in AAD10838. Ref.1
Sequence conflict31361Y → S in AAD10838. Ref.1
Sequence conflict33001E → G in AAD10838. Ref.1

Sequences

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

Last modified November 30, 2010. Version 4.
Checksum: 4F182D2C201662A8

FASTA3,336378,037
        10         20         30         40         50         60 
MEVEQEQRRR KVEAGRTKLA HFRQRKTKGD SSHSEKKTAK RKGSAVDASV QEESPVTKED 

        70         80         90        100        110        120 
SALCGGGDIC KSTSCDDTPD GAGGAFAAQP EDCDGEKRED LEQLQQKQVN DHPPEQCGMF 

       130        140        150        160        170        180 
TVSDHPPEQH GMFTVGDHPP EQRGMFTVSD HPPEQHGMFT VSDHPPEQRG MFTISDHQPE 

       190        200        210        220        230        240 
QRGMFTVSDH TPEQRGIFTI SDHPAEQRGM FTKECEQECE LAITDLESGR EDEAGLHQSQ 

       250        260        270        280        290        300 
AVHGLELEAL RLSLSNMHTA QLELTQANLQ KEKETALTEL REMLNSRRAQ ELALLQSRQQ 

       310        320        330        340        350        360 
HELELLREQH AREKEEVVLR CGQEAAELKE KLQSEMEKNA QIVKTLKEDW ESEKDLCLEN 

       370        380        390        400        410        420 
LRKELSAKHQ SEMEDLQNQF QKELAEQRAE LEKIFQDKNQ AERALRNLES HHQAAIEKLR 

       430        440        450        460        470        480 
EDLQSEHGRC LEDLEFKFKE SEKEKQLELE NLQASYEDLK AQSQEEIRRL WSQLDSARTS 

       490        500        510        520        530        540 
RQELSELHEQ LLARTSRVED LEQLKQREKT QHESELEQLR IYFEKKLRDA EKTYQEDLTL 

       550        560        570        580        590        600 
LQQRLQGARE DALLDSVEVG LSCVGLEEKP EKGRKDHVDE LEPERHKESL PRFQAELEES 

       610        620        630        640        650        660 
HRHQLEALES PLCIQHEGHV SDRCCVETSA LGHEWRLEPS EGHSQELPWV HLQGVQDGDL 

       670        680        690        700        710        720 
EADTERAARV LGLETEHKVQ LSLLQTELKE EIELLKIENR NLYGKLQHET RLKDDLEKVK 

       730        740        750        760        770        780 
HNLIEDHQKE LNNAKQKTEL MKQEFQRKET DWKVMKEELQ REAEEKLTLM LLELREKAES 

       790        800        810        820        830        840 
EKQTIINKFE LREAEMRQLQ DQQAAQILDL ERSLTEQQGR LQQLEQDLTS DDALHCSQCG 

       850        860        870        880        890        900 
REPPTAQDGE LAALHVKEDC ALQLMLARSR FLEERKEITE KFSAEQDAFL QEAQEQHARE 

       910        920        930        940        950        960 
LQLLQERHQQ QLLSVTAELE ARHQAALGEL TASLESKQGA LLAARVAELQ TKHAADLGAL 

       970        980        990       1000       1010       1020 
ETRHLSSLDS LESCYLSEFQ TIREEHRQAL ELLRADFEEQ LWKKDSLHQT ILTQELEKLK 

      1030       1040       1050       1060       1070       1080 
RKHEGELQSV RDHLRTEVST ELAGTVAHEL QGVHQGEFGS EKKTALHEKE ETLRLQSAQA 

      1090       1100       1110       1120       1130       1140 
QPFHQEEKES LSLQLQKKNH QVQQLKDQVL SLSHEIEECR SELEVLQQRR ERENREGANL 

      1150       1160       1170       1180       1190       1200 
LSMLKADVNL SHSERGALQD ALRRLLGLFG ETLRAAVTLR SRIGERVGLC LDDAGAGLAL 

      1210       1220       1230       1240       1250       1260 
STAPALEETW SDVALPELDR TLSECAEMSS VAEISSHMRE SFLMSPESVR ECEQPIRRVF 

      1270       1280       1290       1300       1310       1320 
QSLSLAVDGL MEMALDSSRQ LEEARQIHSR FEKEFSFKNE ETAQVVRKHQ ELLECLKEES 

      1330       1340       1350       1360       1370       1380 
AAKAELALEL HKTQGTLEGF KVETADLKEV LAGKEDSEHR LVLELESLRR QLQQAAQEQA 

      1390       1400       1410       1420       1430       1440 
ALREECTRLW SRGEATATDA EAREAALRKE VEDLTKEQSE TRKQAEKDRS ALLSQMKILE 

      1450       1460       1470       1480       1490       1500 
SELEEQLSQH RGCAKQAEAV TALEQQVASL DKHLRNQRQF MDEQAAEREH EREEFQQEIQ 

      1510       1520       1530       1540       1550       1560 
RLEGQLRQAA KPQPWGPRDS QQAPLDGEVE LLQQKLREKL DEFNELAIQK ESADRQVLMQ 

      1570       1580       1590       1600       1610       1620 
EEEIKRLEEM NINIRKKVAQ LQEEVEKQKN IVKGLEQDKE VLKKQQMSSL LLASTLQSTL 

      1630       1640       1650       1660       1670       1680 
DAGRCPEPPS GSPPEGPEIQ LEVTQRALLR RESEVLDLKE QLEKMKGDLE SKNEEILHLN 

      1690       1700       1710       1720       1730       1740 
LKLDMQNSQT AVSLRELEEE NTSLKVIYTR SSEIEELKAT IENLQENQKR LQKEKAEEIE 

      1750       1760       1770       1780       1790       1800 
QLHEVIEKLQ HELSLMGPVV HEVSDSQAGS LQSELLCSQA GGPRGQALQG ELEAALEAKE 

      1810       1820       1830       1840       1850       1860 
ALSRLLADQE RRHSQALEAL QQRLQGAEEA AELQLAELER NVALREAEVE DMASRIQEFE 

      1870       1880       1890       1900       1910       1920 
AALKAKEATI AERNLEIDAL NQRKAAHSAE LEAVLLALAR IRRALEQQPL AAGAAPPELQ 

      1930       1940       1950       1960       1970       1980 
WLRAQCARLS RQLQVLHQRF LRCQVELDRR QARRATAHTR VPGAHPQPRM DGGAKAQVTG 

      1990       2000       2010       2020       2030       2040 
DVEASHDAAL EPVVPDPQGD LQPVLVTLKD APLCKQEGVM SVLTVCQRQL QSELLLVKNE 

      2050       2060       2070       2080       2090       2100 
MRLSLEDGGK GKEKVLEDCQ LPKVDLVAQV KQLQEKLNRL LYSMTFQNVD AADTKSLWPM 

      2110       2120       2130       2140       2150       2160 
ASAHLLESSW SDDSCDGEEP DISPHIDTCD ANTATGGVTD VIKNQAIDAC DANTTPGGVT 

      2170       2180       2190       2200       2210       2220 
DVIKNWDSLI PDEMPDSPIQ EKSECQDMSL SSPTSVLGGS RHQSHTAEAG PRKSPVGMLD 

      2230       2240       2250       2260       2270       2280 
LSSWSSPEVL RKDWTLEPWP SLPVTPHSGA LSLCSADTSL GDRADTSLPQ TQGPGLLCSP 

      2290       2300       2310       2320       2330       2340 
GVSAAALALQ WAESPPADDH HVQRTAVEKD VEDFITTSFD SQETLSSPPP GLEGKADRSE 

      2350       2360       2370       2380       2390       2400 
KSDGSGFGAR LSPGSGGPEA QTAGPVTPAS ISGRFQPLPE AMKEKEVRPK HVKALLQMVR 

      2410       2420       2430       2440       2450       2460 
DESHQILALS EGLAPPSGEP HPPRKEDEIQ DISLHGGKTQ EVPTACPDWR GDLLQVVQEA 

      2470       2480       2490       2500       2510       2520 
FEKEQEMQGV ELQPRLSGSD LGGHSSLLER LEKIIREQGD LQEKSLEHLR LPDRSSLLSE 

      2530       2540       2550       2560       2570       2580 
IQALRAQLRM THLQNQEKLQ HLRTALTSAE ARGSQQEHQL RRQVELLAYK VEQEKCIAGD 

      2590       2600       2610       2620       2630       2640 
LQKTLSEEQE KANSVQKLLA AEQTVVRDLK SDLCESRQKS EQLSRSLCEV QQEVLQLRSM 

      2650       2660       2670       2680       2690       2700 
LSSKENELKA ALQELESEQG KGRALQSQLE EEQLRHLQRE SQSAKALEEL RASLETQRAQ 

      2710       2720       2730       2740       2750       2760 
SSRLCVALKH EQTAKDNLQK ELRIEHSRCE ALLAQERSQL SELQKDLAAE KSRTLELSEA 

      2770       2780       2790       2800       2810       2820 
LRHERLLTEQ LSQRTQEACV HQDTQAHHAL LQKLKEEKSR VVDLQAMLEK VQQQALHSQQ 

      2830       2840       2850       2860       2870       2880 
QLEAEAQKHC EALRREKEVS ATLKSTVEAL HTQKRELRCS LEREREKPAW LQAELEQSHP 

      2890       2900       2910       2920       2930       2940 
RLKEQEGRKA ARRSAEARQS PAAAEQWRKW QRDKEKLREL ELQRQRDLHK IKQLQQTVRD 

      2950       2960       2970       2980       2990       3000 
LESKDEVPGS RLHLGSARRA AGSDADHLRE QQRELEAMRQ RLLSAARLLT SFTSQAVDRT 

      3010       3020       3030       3040       3050       3060 
VNDWTSSNEK AVMSLLHTLE ELKSDLSRPT SSQKKMAAEL QFQFVDVLLK DNVSLTKALS 

      3070       3080       3090       3100       3110       3120 
TVTQEKLELS RAVSKLEKLL KHHLQKGCSP SRSERSAWKP DETAPQSSLR RPDPGRLPPA 

      3130       3140       3150       3160       3170       3180 
ASEEAHTSNV KMEKLYLHYL RAESFRKALI YQKKYLLLLI GGFQDSEQET LSMIAHLGVF 

      3190       3200       3210       3220       3230       3240 
PSKAERKITS RPFTRFRTAV RVVIAILRLR FLVKKWQEVD RKGALAQGKA PRPGPRARQP 

      3250       3260       3270       3280       3290       3300 
QSPPRTRESP PTRDVPSGHT RDPARGRRLA AAASPHSGGR ATPSPNSRLE RSLTASQDPE 

      3310       3320       3330 
HSLTEYIHHL EVIQQRLGGV LPDSTSKKSC HPMIKQ 

« Hide

Isoform 2 [UniParc].

Checksum: A0FD227ABCF410FD
Show »

FASTA3,139355,882

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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 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]"Mutations in the pericentrin (PCNT) gene cause primordial dwarfism."
Rauch A., Thiel C.T., Schindler D., Wick U., Crow Y.J., Ekici A.B., van Essen A.J., Goecke T.O., Al-Gazali L., Chrzanowska K.H., Zweier C., Brunner H.G., Becker K., Curry C.J., Dallapiccola B., Devriendt K., Doerfler A., Kinning E. expand/collapse author list , Megarbane A., Meinecke P., Semple R.K., Spranger S., Toutain A., Trembath R.C., Voss E., Wilson L., Hennekam R., de Zegher F., Doerr H.-G., Reis A.
Science 319:816-819(2008) [PubMed] [Europe PMC] [Abstract]
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]"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].
[17]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-1452 AND GLN-2424.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006022.3. NM_006031.5.
XP_005261186.1. XM_005261129.1.
UniGeneHs.474069.

3D structure databases

ProteinModelPortalO95613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111146. 16 interactions.
IntActO95613. 7 interactions.
MINTMINT-4527763.
STRING9606.ENSP00000352572.

PTM databases

PhosphoSiteO95613.

Proteomic databases

PaxDbO95613.
PRIDEO95613.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359568; ENSP00000352572; ENSG00000160299. [O95613-1]
GeneID5116.
KEGGhsa:5116.
UCSCuc002zji.4. human. [O95613-1]
uc002zjj.3. human. [O95613-2]

Organism-specific databases

CTD5116.
GeneCardsGC21P047744.
H-InvDBHIX0203117.
HGNCHGNC:16068. PCNT.
HPAHPA016820.
HPA019887.
HPA032101.
MIM210720. phenotype.
605925. gene.
neXtProtNX_O95613.
Orphanet2637. Microcephalic osteodysplastic primordial dwarfism type 2.
808. Seckel syndrome.
PharmGKBPA33079.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000168229.
HOVERGENHBG079443.
InParanoidO95613.
KOK16481.
OMAEQRGMFT.
OrthoDBEOG7DRJ25.
PhylomeDBO95613.
TreeFamTF336114.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

BgeeO95613.
CleanExHS_PCNT.
GenevestigatorO95613.

Family and domain databases

InterProIPR019528. PACT_domain.
IPR024151. Pericentrin.
[Graphical view]
PANTHERPTHR18932:SF3. PTHR18932:SF3. 1 hit.
PfamPF10495. PACT_coil_coil. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPCNT. human.
GeneWikiPCNT.
GenomeRNAi5116.
NextBio19730.
PROO95613.
SOURCESearch...

Entry information

Entry namePCNT_HUMAN
AccessionPrimary (citable) accession number: O95613
Secondary accession number(s): O43152, Q7Z7C9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 135 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

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 21

Human chromosome 21: entries, gene names and cross-references to MIM