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O95613

- PCNT_HUMAN

UniProt

O95613 - PCNT_HUMAN

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Protein

Pericentrin

Gene

PCNT

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 - 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
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 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. ciliary basal body Source: Ensembl
  5. cytoplasm Source: HPA
  6. cytosol Source: Reactome
  7. intercellular bridge Source: Ensembl
  8. membrane Source: UniProtKB
  9. microtubule Source: UniProtKB-KW
  10. motile cilium Source: Ensembl
  11. pericentriolar material Source: Ensembl
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.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. 1 Publication
Mutagenesisi3203 – 32031V → A: Decrease in calmodulin binding. 1 Publication
Mutagenesisi3208 – 32092RL → AA: Decrease in calmodulin binding. 1 Publication

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. 23 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.
GeneTreeiENSGT00730000110871.
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

        10         20         30         40         50
MEVEQEQRRR KVEAGRTKLA HFRQRKTKGD SSHSEKKTAK RKGSAVDASV
60 70 80 90 100
QEESPVTKED SALCGGGDIC KSTSCDDTPD GAGGAFAAQP EDCDGEKRED
110 120 130 140 150
LEQLQQKQVN DHPPEQCGMF TVSDHPPEQH GMFTVGDHPP EQRGMFTVSD
160 170 180 190 200
HPPEQHGMFT VSDHPPEQRG MFTISDHQPE QRGMFTVSDH TPEQRGIFTI
210 220 230 240 250
SDHPAEQRGM FTKECEQECE LAITDLESGR EDEAGLHQSQ AVHGLELEAL
260 270 280 290 300
RLSLSNMHTA QLELTQANLQ KEKETALTEL REMLNSRRAQ ELALLQSRQQ
310 320 330 340 350
HELELLREQH AREKEEVVLR CGQEAAELKE KLQSEMEKNA QIVKTLKEDW
360 370 380 390 400
ESEKDLCLEN LRKELSAKHQ SEMEDLQNQF QKELAEQRAE LEKIFQDKNQ
410 420 430 440 450
AERALRNLES HHQAAIEKLR EDLQSEHGRC LEDLEFKFKE SEKEKQLELE
460 470 480 490 500
NLQASYEDLK AQSQEEIRRL WSQLDSARTS RQELSELHEQ LLARTSRVED
510 520 530 540 550
LEQLKQREKT QHESELEQLR IYFEKKLRDA EKTYQEDLTL LQQRLQGARE
560 570 580 590 600
DALLDSVEVG LSCVGLEEKP EKGRKDHVDE LEPERHKESL PRFQAELEES
610 620 630 640 650
HRHQLEALES PLCIQHEGHV SDRCCVETSA LGHEWRLEPS EGHSQELPWV
660 670 680 690 700
HLQGVQDGDL EADTERAARV LGLETEHKVQ LSLLQTELKE EIELLKIENR
710 720 730 740 750
NLYGKLQHET RLKDDLEKVK HNLIEDHQKE LNNAKQKTEL MKQEFQRKET
760 770 780 790 800
DWKVMKEELQ REAEEKLTLM LLELREKAES EKQTIINKFE LREAEMRQLQ
810 820 830 840 850
DQQAAQILDL ERSLTEQQGR LQQLEQDLTS DDALHCSQCG REPPTAQDGE
860 870 880 890 900
LAALHVKEDC ALQLMLARSR FLEERKEITE KFSAEQDAFL QEAQEQHARE
910 920 930 940 950
LQLLQERHQQ QLLSVTAELE ARHQAALGEL TASLESKQGA LLAARVAELQ
960 970 980 990 1000
TKHAADLGAL ETRHLSSLDS LESCYLSEFQ TIREEHRQAL ELLRADFEEQ
1010 1020 1030 1040 1050
LWKKDSLHQT ILTQELEKLK RKHEGELQSV RDHLRTEVST ELAGTVAHEL
1060 1070 1080 1090 1100
QGVHQGEFGS EKKTALHEKE ETLRLQSAQA QPFHQEEKES LSLQLQKKNH
1110 1120 1130 1140 1150
QVQQLKDQVL SLSHEIEECR SELEVLQQRR ERENREGANL LSMLKADVNL
1160 1170 1180 1190 1200
SHSERGALQD ALRRLLGLFG ETLRAAVTLR SRIGERVGLC LDDAGAGLAL
1210 1220 1230 1240 1250
STAPALEETW SDVALPELDR TLSECAEMSS VAEISSHMRE SFLMSPESVR
1260 1270 1280 1290 1300
ECEQPIRRVF QSLSLAVDGL MEMALDSSRQ LEEARQIHSR FEKEFSFKNE
1310 1320 1330 1340 1350
ETAQVVRKHQ ELLECLKEES AAKAELALEL HKTQGTLEGF KVETADLKEV
1360 1370 1380 1390 1400
LAGKEDSEHR LVLELESLRR QLQQAAQEQA ALREECTRLW SRGEATATDA
1410 1420 1430 1440 1450
EAREAALRKE VEDLTKEQSE TRKQAEKDRS ALLSQMKILE SELEEQLSQH
1460 1470 1480 1490 1500
RGCAKQAEAV TALEQQVASL DKHLRNQRQF MDEQAAEREH EREEFQQEIQ
1510 1520 1530 1540 1550
RLEGQLRQAA KPQPWGPRDS QQAPLDGEVE LLQQKLREKL DEFNELAIQK
1560 1570 1580 1590 1600
ESADRQVLMQ EEEIKRLEEM NINIRKKVAQ LQEEVEKQKN IVKGLEQDKE
1610 1620 1630 1640 1650
VLKKQQMSSL LLASTLQSTL DAGRCPEPPS GSPPEGPEIQ LEVTQRALLR
1660 1670 1680 1690 1700
RESEVLDLKE QLEKMKGDLE SKNEEILHLN LKLDMQNSQT AVSLRELEEE
1710 1720 1730 1740 1750
NTSLKVIYTR SSEIEELKAT IENLQENQKR LQKEKAEEIE QLHEVIEKLQ
1760 1770 1780 1790 1800
HELSLMGPVV HEVSDSQAGS LQSELLCSQA GGPRGQALQG ELEAALEAKE
1810 1820 1830 1840 1850
ALSRLLADQE RRHSQALEAL QQRLQGAEEA AELQLAELER NVALREAEVE
1860 1870 1880 1890 1900
DMASRIQEFE AALKAKEATI AERNLEIDAL NQRKAAHSAE LEAVLLALAR
1910 1920 1930 1940 1950
IRRALEQQPL AAGAAPPELQ WLRAQCARLS RQLQVLHQRF LRCQVELDRR
1960 1970 1980 1990 2000
QARRATAHTR VPGAHPQPRM DGGAKAQVTG DVEASHDAAL EPVVPDPQGD
2010 2020 2030 2040 2050
LQPVLVTLKD APLCKQEGVM SVLTVCQRQL QSELLLVKNE MRLSLEDGGK
2060 2070 2080 2090 2100
GKEKVLEDCQ LPKVDLVAQV KQLQEKLNRL LYSMTFQNVD AADTKSLWPM
2110 2120 2130 2140 2150
ASAHLLESSW SDDSCDGEEP DISPHIDTCD ANTATGGVTD VIKNQAIDAC
2160 2170 2180 2190 2200
DANTTPGGVT DVIKNWDSLI PDEMPDSPIQ EKSECQDMSL SSPTSVLGGS
2210 2220 2230 2240 2250
RHQSHTAEAG PRKSPVGMLD LSSWSSPEVL RKDWTLEPWP SLPVTPHSGA
2260 2270 2280 2290 2300
LSLCSADTSL GDRADTSLPQ TQGPGLLCSP GVSAAALALQ WAESPPADDH
2310 2320 2330 2340 2350
HVQRTAVEKD VEDFITTSFD SQETLSSPPP GLEGKADRSE KSDGSGFGAR
2360 2370 2380 2390 2400
LSPGSGGPEA QTAGPVTPAS ISGRFQPLPE AMKEKEVRPK HVKALLQMVR
2410 2420 2430 2440 2450
DESHQILALS EGLAPPSGEP HPPRKEDEIQ DISLHGGKTQ EVPTACPDWR
2460 2470 2480 2490 2500
GDLLQVVQEA FEKEQEMQGV ELQPRLSGSD LGGHSSLLER LEKIIREQGD
2510 2520 2530 2540 2550
LQEKSLEHLR LPDRSSLLSE IQALRAQLRM THLQNQEKLQ HLRTALTSAE
2560 2570 2580 2590 2600
ARGSQQEHQL RRQVELLAYK VEQEKCIAGD LQKTLSEEQE KANSVQKLLA
2610 2620 2630 2640 2650
AEQTVVRDLK SDLCESRQKS EQLSRSLCEV QQEVLQLRSM LSSKENELKA
2660 2670 2680 2690 2700
ALQELESEQG KGRALQSQLE EEQLRHLQRE SQSAKALEEL RASLETQRAQ
2710 2720 2730 2740 2750
SSRLCVALKH EQTAKDNLQK ELRIEHSRCE ALLAQERSQL SELQKDLAAE
2760 2770 2780 2790 2800
KSRTLELSEA LRHERLLTEQ LSQRTQEACV HQDTQAHHAL LQKLKEEKSR
2810 2820 2830 2840 2850
VVDLQAMLEK VQQQALHSQQ QLEAEAQKHC EALRREKEVS ATLKSTVEAL
2860 2870 2880 2890 2900
HTQKRELRCS LEREREKPAW LQAELEQSHP RLKEQEGRKA ARRSAEARQS
2910 2920 2930 2940 2950
PAAAEQWRKW QRDKEKLREL ELQRQRDLHK IKQLQQTVRD LESKDEVPGS
2960 2970 2980 2990 3000
RLHLGSARRA AGSDADHLRE QQRELEAMRQ RLLSAARLLT SFTSQAVDRT
3010 3020 3030 3040 3050
VNDWTSSNEK AVMSLLHTLE ELKSDLSRPT SSQKKMAAEL QFQFVDVLLK
3060 3070 3080 3090 3100
DNVSLTKALS TVTQEKLELS RAVSKLEKLL KHHLQKGCSP SRSERSAWKP
3110 3120 3130 3140 3150
DETAPQSSLR RPDPGRLPPA ASEEAHTSNV KMEKLYLHYL RAESFRKALI
3160 3170 3180 3190 3200
YQKKYLLLLI GGFQDSEQET LSMIAHLGVF PSKAERKITS RPFTRFRTAV
3210 3220 3230 3240 3250
RVVIAILRLR FLVKKWQEVD RKGALAQGKA PRPGPRARQP QSPPRTRESP
3260 3270 3280 3290 3300
PTRDVPSGHT RDPARGRRLA AAASPHSGGR ATPSPNSRLE RSLTASQDPE
3310 3320 3330
HSLTEYIHHL EVIQQRLGGV LPDSTSKKSC HPMIKQ
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. Curated
The sequence BAA23698.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC04252.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 23 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.
GeneTreei ENSGT00730000110871.
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: October 29, 2014
This is version 141 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