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O95613

- PCNT_HUMAN

UniProt

O95613 - PCNT_HUMAN

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Protein
Pericentrin
Gene
PCNT, KIAA0402, PCNT2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. G2/M transition of mitotic cell cycle Source: Reactome
  2. brain morphogenesis Source: Ensembl
  3. cerebellar cortex morphogenesis Source: Ensembl
  4. cilium assembly Source: MGI
  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
Complete GO annotation...

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

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. microtubule Source: UniProtKB-KW
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications

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 – 33363336Pericentrin
PRO_0000058257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911Phosphothreonine1 Publication
Modified residuei682 – 6821Phosphoserine1 Publication
Modified residuei1712 – 17121Phosphoserine By 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 CEP131.5 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2983 – 3246264Interaction with NEK2
Add
BLAST
Regioni3195 – 320814Calmodulin-binding
Add
BLAST

Coiled coil

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

Compositional bias

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

Domaini

Composed of a coiled-coil central region flanked by non-helical N- and C-terminals.1 Publication

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.

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.
VSP_040104Add
BLAST
Alternative sequencei2839 – 291779Missing in isoform 2.
VSP_040105Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti703 – 7031Y → F in AAD10838. 1 Publication
Sequence conflicti789 – 7891F → L in AAD10838. 1 Publication
Sequence conflicti819 – 8191G → A in AAD10838. 1 Publication
Sequence conflicti890 – 90011Missing in AAD10838. 1 Publication
Add
BLAST
Sequence conflicti967 – 9671S → T in AAD10838. 1 Publication
Sequence conflicti1024 – 10241E → K in AAD10838. 1 Publication
Sequence conflicti1036 – 10361T → A in BAC04252. 1 Publication
Sequence conflicti1287 – 12871I → L in AAD10838. 1 Publication
Sequence conflicti1317 – 13171K → T in AAD10838. 1 Publication
Sequence conflicti1534 – 15341Q → H in AAD10838. 1 Publication
Sequence conflicti3136 – 31361Y → S in AAD10838. 1 Publication
Sequence conflicti3300 – 33001E → G in AAD10838. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

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