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Protein

Pericentriolar material 1 protein

Gene

PCM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for centrosome assembly and function. Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Involved in the biogenesis of cilia.5 Publications

GO - Molecular functioni

GO - Biological processi

  • centrosome organization Source: BHF-UCL
  • cilium assembly Source: UniProtKB
  • cytoplasmic microtubule organization Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: Reactome
  • interkinetic nuclear migration Source: BHF-UCL
  • intraciliary transport involved in cilium morphogenesis Source: UniProtKB
  • microtubule anchoring Source: BHF-UCL
  • microtubule anchoring at centrosome Source: GO_Central
  • negative regulation of neurogenesis Source: BHF-UCL
  • neuronal stem cell population maintenance Source: Ensembl
  • neuron migration Source: Ensembl
  • non-motile cilium assembly Source: GO_Central
  • positive regulation of intracellular protein transport Source: UniProtKB
  • protein localization to centrosome Source: SYSCILIA_CCNET
  • social behavior Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.
SIGNORiQ15154.

Names & Taxonomyi

Protein namesi
Recommended name:
Pericentriolar material 1 protein
Short name:
PCM-1
Short name:
hPCM-1
Gene namesi
Name:PCM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:8727. PCM1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • centriolar satellite Source: UniProtKB
  • centriole Source: Ensembl
  • centrosome Source: UniProtKB
  • ciliary basal body Source: Ensembl
  • ciliary transition zone Source: GO_Central
  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nuclear membrane Source: HPA
  • pericentriolar material Source: BHF-UCL
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving PCM1 is found in papillary thyroid carcinomas (PTCs). Translocation t(8;10)(p21.3;q11.2) with RET links the protein kinase domain of RET to the major portion of PCM1.

A chromosomal aberration involving PCM1 is found in a variety of hematological malignancies including atypical chronic myeloid leukemia (atypical CML) and T-cell lymphoma. Translocation t(8;9)(p22;p24) with JAK2 links the protein kinase domain of JAK2 to the major portion of PCM1.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1314 – 1315Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei1369 – 1370Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei1470 – 1471Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei1609 – 1610Breakpoint for translocation to form PCM1-RET fusion protein2
Sitei1947 – 1948Breakpoint for translocation to form PCM1-JAK2 fusion protein2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi5108.
MalaCardsiPCM1.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA33073.

Polymorphism and mutation databases

BioMutaiPCM1.
DMDMi296439495.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002740372 – 2024Pericentriolar material 1 proteinAdd BLAST2023

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei65PhosphoserineCombined sources1
Modified residuei68PhosphoserineCombined sources1
Modified residuei69PhosphoserineCombined sources1
Modified residuei93PhosphoserineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei116PhosphoserineCombined sources1
Modified residuei119PhosphoserineCombined sources1
Modified residuei159PhosphoserineCombined sources1
Modified residuei370PhosphoserineCombined sources1
Modified residuei372PhosphoserineCombined sources1
Modified residuei384PhosphoserineCombined sources1
Modified residuei399N6-acetyllysineCombined sources1
Modified residuei431PhosphoserineCombined sources1
Modified residuei588PhosphoserineCombined sources1
Modified residuei643PhosphoserineBy similarity1
Modified residuei859PhosphothreonineCombined sources1
Modified residuei861PhosphoserineCombined sources1
Modified residuei866PhosphoserineBy similarity1
Modified residuei869PhosphoserineBy similarity1
Modified residuei872PhosphoserineBy similarity1
Modified residuei877PhosphothreonineBy similarity1
Modified residuei960PhosphoserineCombined sources1
Modified residuei977PhosphoserineCombined sources1
Modified residuei988PhosphoserineCombined sources1
Modified residuei991PhosphoserineCombined sources1
Modified residuei1185PhosphoserineCombined sources1
Modified residuei1188PhosphoserineBy similarity1
Modified residuei1229PhosphoserineCombined sources1
Modified residuei1231PhosphoserineCombined sources1
Modified residuei1257PhosphoserineCombined sources1
Modified residuei1260PhosphoserineCombined sources1
Modified residuei1262PhosphoserineBy similarity1
Modified residuei1263PhosphoserineCombined sources1
Modified residuei1318PhosphoserineBy similarity1
Modified residuei1320PhosphoserineBy similarity1
Modified residuei1468PhosphothreonineCombined sources1
Modified residuei1573PhosphoserineBy similarity1
Modified residuei1697PhosphoserineCombined sources1
Modified residuei1730PhosphoserineCombined sources1
Modified residuei1765PhosphoserineCombined sources1
Modified residuei1768PhosphoserineCombined sources1
Modified residuei1776PhosphoserineCombined sources1
Modified residuei1782PhosphoserineBy similarity1
Modified residuei1958PhosphoserineCombined sources1
Modified residuei1977PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3 ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia formation. Monoubiquitination by MIB1 is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, resulting in cilia formation initiation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15154.
MaxQBiQ15154.
PaxDbiQ15154.
PeptideAtlasiQ15154.
PRIDEiQ15154.

PTM databases

iPTMnetiQ15154.
PhosphoSitePlusiQ15154.

Expressioni

Tissue specificityi

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

Inductioni

Expression is reduced in breast and ovarian cancer.2 Publications

Gene expression databases

BgeeiENSG00000078674.
CleanExiHS_PCM1.
ExpressionAtlasiQ15154. baseline and differential.
GenevisibleiQ15154. HS.

Organism-specific databases

HPAiCAB058695.
HPA023370.
HPA023374.

Interactioni

Subunit structurei

Self-associates. Interacts with C2CD3 (By similarity). Interacts with BBS4, BBS8, CETN3, HAP1, NDE1, NDEL1, MAP1LC3B, GABARAPAL2, and GABARAP. Interacts with CEP131; the interaction increases in response to ultraviolet light (UV) radiation. Associates with microtubule; association to microtubule is reduced in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling. Interacts with CCDC113. Interacts with SSX2IP (By similarity). Interacts with CCDC13 (PubMed:24816561). Interacts with CEP290 (By similarity). Interacts with PARD6A (PubMed:20719959).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BBS1Q8NFJ92EBI-741421,EBI-1805484
BBS4Q96RK416EBI-741421,EBI-1805814
CCDC53Q9Y3C04EBI-741421,EBI-712969
CEP72Q9P2094EBI-741421,EBI-739498
Hap1P542563EBI-741421,EBI-994539From a different organism.
PCNTO956137EBI-741421,EBI-530012
SSX2IPQ9Y2D810EBI-741421,EBI-2212028

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111139. 267 interactors.
DIPiDIP-42189N.
IntActiQ15154. 262 interactors.
MINTiMINT-3295236.
STRINGi9606.ENSP00000327077.

Structurei

3D structure databases

ProteinModelPortaliQ15154.
SMRiQ15154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1279 – 1799Interaction with HAP11 PublicationAdd BLAST521
Regioni1913 – 2024Interaction with BBS41 PublicationAdd BLAST112

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili218 – 301Sequence analysisAdd BLAST84
Coiled coili400 – 424Sequence analysisAdd BLAST25
Coiled coili487 – 543Sequence analysisAdd BLAST57
Coiled coili651 – 682Sequence analysisAdd BLAST32
Coiled coili726 – 769Sequence analysisAdd BLAST44
Coiled coili824 – 858Sequence analysisAdd BLAST35
Coiled coili1063 – 1089Sequence analysisAdd BLAST27
Coiled coili1515 – 1539Sequence analysisAdd BLAST25

Sequence similaritiesi

Belongs to the PCM1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEGR. Eukaryota.
ENOG410YNFX. LUCA.
HOGENOMiHOG000115473.
HOVERGENiHBG053890.
InParanoidiQ15154.
KOiK16537.
OrthoDBiEOG091G00C3.
PhylomeDBiQ15154.
TreeFamiTF328740.

Family and domain databases

InterProiIPR031446. PCM1_C.
IPR024138. Pericentriolar_Pcm1.
[Graphical view]
PANTHERiPTHR14164. PTHR14164. 1 hit.
PfamiPF15717. PCM1_C. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK
60 70 80 90 100
KFGVESDKRV TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL
110 120 130 140 150
EKLKQRINFS DLDQRSIGSD SQGRATAANN KRQLSENRKP FNFLPMQINT
160 170 180 190 200
NKSKDASTSP PNRETIGSAQ CKELFASALS NDLLQNCQVS EEDGRGEPAM
210 220 230 240 250
ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT HLIDHLKEQE
260 270 280 290 300
KSYMKFLKKI LARDPQQEPM EEIENLKKQH DLLKRMLQQQ EQLRALQGRQ
310 320 330 340 350
AALLALQHKA EQAIAVMDDS VVAETAGSLS GVSITSELNE ELNDLIQRFH
360 370 380 390 400
NQLRDSQPPA VPDNRRQAES LSLTREVSQS RKPSASERLP DEKVELFSKM
410 420 430 440 450
RVLQEKKQKM DKLLGELHTL RDQHLNNSSS SPQRSVDQRS TSAPSASVGL
460 470 480 490 500
APVVNGESNS LTSSVPYPTA SLVSQNESEN EGHLNPSEKL QKLNEVRKRL
510 520 530 540 550
NELRELVHYY EQTSDMMTDA VNENRKDEET EESEYDSEHE NSEPVTNIRN
560 570 580 590 600
PQVASTWNEV NSHSNAQCVS NNRDGRTVNS NCEINNRSAA NIRALNMPPS
610 620 630 640 650
LDCRYNREGE QEIHVAQGED DEEEEEEAEE EGVSGASLSS HRSSLVDEHP
660 670 680 690 700
EDAEFEQKIN RLMAAKQKLR QLQDLVAMVQ DDDAAQGVIS ASASNLDDFY
710 720 730 740 750
PAEEDTKQNS NNTRGNANKT QKDTGVNEKA REKFYEAKLQ QQQRELKQLQ
760 770 780 790 800
EERKKLIDIQ EKIQALQTAC PDLQLSAASV GNCPTKKYMP AVTSTPTVNQ
810 820 830 840 850
HETSTSKSVF EPEDSSIVDN ELWSEMRRHE MLREELRQRR KQLEALMAEH
860 870 880 890 900
QRRQGLAETA SPVAVSLRSD GSENLCTPQQ SRTEKTMATW GGSTQCALDE
910 920 930 940 950
EGDEDGYLSE GIVRTDEEEE EEQDASSNDN FSVCPSNSVN HNSYNGKETK
960 970 980 990 1000
NRWKNNCPFS ADENYRPLAK TRQQNISMQR QENLRWVSEL SYVEEKEQWQ
1010 1020 1030 1040 1050
EQINQLKKQL DFSVSICQTL MQDQQTLSCL LQTLLTGPYS VMPSNVASPQ
1060 1070 1080 1090 1100
VHFIMHQLNQ CYTQLTWQQN NVQRLKQMLN ELMRQQNQHP EKPGGKERGS
1110 1120 1130 1140 1150
SASHPPSPSL FCPFSFPTQP VNLFNIPGFT NFSSFAPGMN FSPLFPSNFG
1160 1170 1180 1190 1200
DFSQNISTPS EQQQPLAQNS SGKTEYMAFP KPFESSSSIG AEKPRNKKLP
1210 1220 1230 1240 1250
EEEVESSRTP WLYEQEGEVE KPFIKTGFSV SVEKSTSSNR KNQLDTNGRR
1260 1270 1280 1290 1300
RQFDEESLES FSSMPDPVDP TTVTKTFKTR KASAQASLAS KDKTPKSKSK
1310 1320 1330 1340 1350
KRNSTQLKSR VKNIRYESAS MSSTCEPCKS RNRHSAQTEE PVQAKVFSRK
1360 1370 1380 1390 1400
NHEQLEKIIK CNRSTEISSE TGSDFSMFEA LRDTIYSEVA TLISQNESRP
1410 1420 1430 1440 1450
HFLIELFHEL QLLNTDYLRQ RALYALQDIV SRHISESHEK GENVKSVNSG
1460 1470 1480 1490 1500
TWIASNSELT PSESLATTDD ETFEKNFERE THKISEQNDA DNASVLSVSS
1510 1520 1530 1540 1550
NFEPFATDDL GNTVIHLDQA LARMREYERM KTEAESNSNM RCTCRIIEDG
1560 1570 1580 1590 1600
DGAGAGTTVN NLEETPVIEN RSSQQPVSEV STIPCPRIDT QQLDRQIKAI
1610 1620 1630 1640 1650
MKEVIPFLKE HMDEVCSSQL LTSVRRMVLT LTQQNDESKE FVKFFHKQLG
1660 1670 1680 1690 1700
SILQDSLAKF AGRKLKDCGE DLLVEISEVL FNELAFFKLM QDLDNNSITV
1710 1720 1730 1740 1750
KQRCKRKIEA TGVIQSCAKE AKRILEDHGS PAGEIDDEDK DKDETETVKQ
1760 1770 1780 1790 1800
TQTSEVYDGP KNVRSDISDQ EEDEESEGCP VSINLSKAET QALTNYGSGE
1810 1820 1830 1840 1850
DENEDEEMEE FEEGPVDVQT SLQANTEATE ENEHDEQVLQ RDFKKTAESK
1860 1870 1880 1890 1900
NVPLEREATS KNDQNNCPVK PCYLNILEDE QPLNSAAHKE SPPTVDSTQQ
1910 1920 1930 1940 1950
PNPLPLRLPE MEPLVPRVKE VKSAQETPES SLAGSPDTES PVLVNDYEAE
1960 1970 1980 1990 2000
SGNISQKSDE EDFVKVEDLP LKLTIYSEAD LRKKMVEEEQ KNHLSGEICE
2010 2020
MQTEELAGNS ETLKEPETVG AQSI
Length:2,024
Mass (Da):228,533
Last modified:May 18, 2010 - v4
Checksum:i04ACFD7438F773EB
GO
Isoform 2 (identifier: Q15154-2) [UniParc]FASTAAdd to basket

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

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

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

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

Sequence cautioni

The sequence AAH27477 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH65022 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAC03656 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAC14882 differs from that shown. Contaminating sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti294R → RG in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti311 – 312EQ → DE in AAA60120 (PubMed:8120099).Curated2
Sequence conflicti405E → K in AAH27477 (PubMed:15489334).Curated1
Sequence conflicti408Q → K in AAH27477 (PubMed:15489334).Curated1
Sequence conflicti408Q → K in AAH65022 (PubMed:15489334).Curated1
Sequence conflicti447 – 448SV → CL in AAA60120 (PubMed:8120099).Curated2
Sequence conflicti760Q → H in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti946G → R in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti952R → T in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1004Missing in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1086Q → R in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1168Q → R in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1169N → I in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1170S → L in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1342V → L in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1382R → Q in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1532T → A in BAC03656 (PubMed:14702039).Curated1
Sequence conflicti1849S → G in BAC03656 (PubMed:14702039).Curated1
Sequence conflicti1853 – 1864PLERE…SKNDQ → HWNEKPLVKMTK in AAA60120 (PubMed:8120099).CuratedAdd BLAST12
Sequence conflicti1872C → S in AAA60120 (PubMed:8120099).Curated1
Sequence conflicti1988E → V in BAC03656 (PubMed:14702039).Curated1
Sequence conflicti1998I → M in AAA60120 (PubMed:8120099).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030164159S → N.Corresponds to variant rs412750dbSNPEnsembl.1
Natural variantiVAR_062172159S → R.Corresponds to variant rs412750dbSNPEnsembl.1
Natural variantiVAR_030165176A → D.Corresponds to variant rs2285302dbSNPEnsembl.1
Natural variantiVAR_030166597M → V.2 PublicationsCorresponds to variant rs208753dbSNPEnsembl.1
Natural variantiVAR_047381600S → P.Corresponds to variant rs34325017dbSNPEnsembl.1
Natural variantiVAR_030167691A → S.Corresponds to variant rs17635381dbSNPEnsembl.1
Natural variantiVAR_030168871G → V.Corresponds to variant rs7009117dbSNPEnsembl.1
Natural variantiVAR_0301691251R → H.Corresponds to variant rs17514547dbSNPEnsembl.1
Natural variantiVAR_0473821326E → D.Corresponds to variant rs34932823dbSNPEnsembl.1
Natural variantiVAR_0301701543T → I.Corresponds to variant rs370429dbSNPEnsembl.1
Natural variantiVAR_0473831701K → N.Corresponds to variant rs36113670dbSNPEnsembl.1
Natural variantiVAR_0473841865N → D.Corresponds to variant rs35789133dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_022609263R → RENEEEDVRTIDSAVGSGSV AESTSLNIDVQSEASDTTAR in isoform 3. 1 Publication1
Alternative sequenceiVSP_022610492 – 2024Missing in isoform 3. 1 PublicationAdd BLAST1533
Alternative sequenceiVSP_0226111315 – 1370RYESA…EISSE → K in isoform 2. 1 PublicationAdd BLAST56

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27841 mRNA. Translation: AAA60120.1.
AC087273 Genomic DNA. No translation available.
AC087625 Genomic DNA. No translation available.
BC000453 mRNA. Translation: AAH00453.1.
BC027477 mRNA. Translation: AAH27477.1. Sequence problems.
BC065022 mRNA. Translation: AAH65022.1. Sequence problems.
AK091406 mRNA. Translation: BAC03656.1. Different initiation.
AJ297349 mRNA. Translation: CAC14882.1. Sequence problems.
CCDSiCCDS47812.1. [Q15154-1]
PIRiA54103.
RefSeqiNP_001302437.1. NM_001315508.1.
NP_006188.3. NM_006197.3. [Q15154-1]
UniGeneiHs.491148.

Genome annotation databases

EnsembliENST00000325083; ENSP00000327077; ENSG00000078674.
GeneIDi5108.
KEGGihsa:5108.
UCSCiuc003wyi.5. human. [Q15154-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27841 mRNA. Translation: AAA60120.1.
AC087273 Genomic DNA. No translation available.
AC087625 Genomic DNA. No translation available.
BC000453 mRNA. Translation: AAH00453.1.
BC027477 mRNA. Translation: AAH27477.1. Sequence problems.
BC065022 mRNA. Translation: AAH65022.1. Sequence problems.
AK091406 mRNA. Translation: BAC03656.1. Different initiation.
AJ297349 mRNA. Translation: CAC14882.1. Sequence problems.
CCDSiCCDS47812.1. [Q15154-1]
PIRiA54103.
RefSeqiNP_001302437.1. NM_001315508.1.
NP_006188.3. NM_006197.3. [Q15154-1]
UniGeneiHs.491148.

3D structure databases

ProteinModelPortaliQ15154.
SMRiQ15154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111139. 267 interactors.
DIPiDIP-42189N.
IntActiQ15154. 262 interactors.
MINTiMINT-3295236.
STRINGi9606.ENSP00000327077.

PTM databases

iPTMnetiQ15154.
PhosphoSitePlusiQ15154.

Polymorphism and mutation databases

BioMutaiPCM1.
DMDMi296439495.

Proteomic databases

EPDiQ15154.
MaxQBiQ15154.
PaxDbiQ15154.
PeptideAtlasiQ15154.
PRIDEiQ15154.

Protocols and materials databases

DNASUi5108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325083; ENSP00000327077; ENSG00000078674.
GeneIDi5108.
KEGGihsa:5108.
UCSCiuc003wyi.5. human. [Q15154-1]

Organism-specific databases

CTDi5108.
DisGeNETi5108.
GeneCardsiPCM1.
H-InvDBHIX0007341.
HGNCiHGNC:8727. PCM1.
HPAiCAB058695.
HPA023370.
HPA023374.
MalaCardsiPCM1.
MIMi600299. gene.
neXtProtiNX_Q15154.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA33073.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEGR. Eukaryota.
ENOG410YNFX. LUCA.
HOGENOMiHOG000115473.
HOVERGENiHBG053890.
InParanoidiQ15154.
KOiK16537.
OrthoDBiEOG091G00C3.
PhylomeDBiQ15154.
TreeFamiTF328740.

Enzyme and pathway databases

ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.
SIGNORiQ15154.

Miscellaneous databases

ChiTaRSiPCM1. human.
GeneWikiiPCM1.
GenomeRNAii5108.
PROiQ15154.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078674.
CleanExiHS_PCM1.
ExpressionAtlasiQ15154. baseline and differential.
GenevisibleiQ15154. HS.

Family and domain databases

InterProiIPR031446. PCM1_C.
IPR024138. Pericentriolar_Pcm1.
[Graphical view]
PANTHERiPTHR14164. PTHR14164. 1 hit.
PfamiPF15717. PCM1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCM1_HUMAN
AccessioniPrimary (citable) accession number: Q15154
Secondary accession number(s): Q58F13
, Q6P1K7, Q8NB85, Q9BWC1, Q9H4A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.