PCM1
entrez
5108
canonical
uniprot
Q15154
canonical
ensembl
ENSG00000078674
resolver
ensp
ENSP00000327077
resolver
ensp
ENSP00000428123
resolver
ensp
ENSP00000430521
resolver
ensp
ENSP00000431099
resolver
ensp
ENSP00000527116
resolver
ensp
ENSP00000527117
resolver
ensp
ENSP00000527120
resolver
ensp
ENSP00000527122
resolver
ensp
ENSP00000607168
resolver
ensp
ENSP00000607169
resolver
ensp
ENSP00000607171
resolver
ensp
ENSP00000607178
resolver
ensp
ENSP00000607191
resolver
ensp
ENSP00000639463
resolver
ensp
ENSP00000639464
resolver
ensp
ENSP00000753693
resolver
ensp
ENSP00000753694
resolver
ensp
ENSP00000792820
resolver
ensp
ENSP00000792822
resolver
enst
ENST00000518537
resolver
enst
ENST00000519253
resolver
enst
ENST00000524226
resolver
genesymbol
PCM1
resolver
hgnc
HGNC:8727
resolver
uniprot
A0A4W8VX11
resolver
uniprot
A0A5H1ZRS1
resolver
uniprot
A2RUU9
resolver
uniprot
A6NNN6
resolver
uniprot
B4DYD5
resolver
uniprot
B9EIS5
resolver
uniprot
E7ETA6
resolver
uniprot
E7EV56
resolver
uniprot
E9PGW9
resolver
uniprot
Q58F13
resolver
uniprot
Q6P1K7
resolver
uniprot
Q8NB85
resolver
uniprot
Q9BWC1
resolver
uniprot
Q9H4A2
resolver
uniprot_entry
A0A4W8VX11_HUMAN
resolver
uniprot_entry
A0A5H1ZRS1_HUMAN
resolver
uniprot_entry
A2RUU9_HUMAN
resolver
uniprot_entry
B9EIS5_HUMAN
resolver
uniprot_entry
E9PGW9_HUMAN
resolver
uniprot_entry
PCM1_HUMAN
resolver
uniprot_sec
A6NNN6
resolver
uniprot_sec
B4DYD5
resolver
uniprot_sec
E7ETA6
resolver
uniprot_sec
E7EV56
resolver
uniprot_sec
Q58F13
resolver
uniprot_sec
Q6P1K7
resolver
uniprot_sec
Q8NB85
resolver
uniprot_sec
Q9BWC1
resolver
uniprot_sec
Q9H4A2
resolver
amino_acid_sequence
MATGGGPFEDGMNDQDLPNWSNENVDDRLNNMDWGAQQKKANRSSEKNKKKFGVESDKRVTNDISPESSPGVGRRRTKTPHTFPHSRYMSQMSVPEQAELEKLKQRINFSDLDQRSIGSDSQGRATAANNKRQLSENRKPFNFLPMQINTNKSKDASTNPPNRETIGSAQCKELFASALSNDLLQNCQVSEEDGRGEPAMESSQIVSRLVQIRDYITKASSMREDLVEKNERSANVERLTHLIDHLKEQEKSYMKFLKKILARDPQQEPMEEIENLKKQHDLLKRMLQQQEQLRALQGRQAALLALQHKAEQAIAVMDDSVVAETAGSLSGVSITSELNEELNDLIQRFHNQLRDSQPPAVPDNRRQAESLSLTREVSQSRKPSASERLPDEKVELFSKMRVLQEKKQKMDKLLGELHTLRDQHLNNSSSSPQRSVDQRSTSAPSASVGLAPVVNGESNSLTSSVPYPTASLVSQNESENEGHLNPSEKLQKLNEVRKRLNELRELVHYYEQTSDMMTDAVNENRKDEETEESEYDSEHENSEPVTNIRNPQVASTWNEVNSHSNAQCVSNNRDGRTVNSNCEINNRSAANIRALNMPPSLDCRYNREGEQEIHVAQGEDDEEEEEEAEEEGVSGASLSSHRSSLVDEHPEDAEFEQKINRLMAAKQKLRQLQDLVAMVQDDDAAQGVISASASNLDDFYPAEEDTKQNSNNTRGNANKTQKDTGVNEKAREKFYEAKLQQQQRELKQLQEERKKLIDIQEKIQALQTACPDLQLSAASVGNCPTKKYMPAVTSTPTVNQHETSTSKSVFEPEDSSIVDNELWSEMRRHEMLREELRQRRKQLEALMAEHQRRQGLAETASPVAVSLRSDGSENLCTPQQSRTEKTMATWGGSTQCALDEEGDEDGYLSEGIVRTDEEEEEEQDASSNDNFSVCPSNSVNHNSYNGKETKNRWKNNCPFSADENYRPLAKTRQQNISMQRQENLRWVSELSYVEEKEQWQEQINQLKKQLDFSVSICQTLMQDQQTLSCLLQTLLTGPYSVMPSNVASPQVHFIMHQLNQCYTQLTWQQNNVQRLKQMLNELMRQQNQHPEKPGGKERGSSASHPPSPSLFCPFSFPTQPVNLFNIPGFTNFSSFAPGMNFSPLFPSNFGDFSQNISTPSEQQQPLAQNSSGKTEYMAFPKPFESSSSIGAEKPRNKKLPEEEVESSRTPWLYEQEGEVEKPFIKTGFSVSVEKSTSSNRKNQLDTNGRRRQFDEESLESFSSMPDPVDPTTVTKTFKTRKASAQASLASKDKTPKSKSKKRNSTQLKSRVKNIRYESASMSSTCEPCKSRNRHSAQTEEPVQAKVFSRKNHEQLEKIIKCNRSTEISSETGSDFSMFEALRDTIYSEVATLISQNESRPHFLIELFHELQLLNTDYLRQRALYALQDIVSRHISESHEKGENVKSVNSGTWIASNSELTPSESLATTDDETFEKNFERETHKISEQNDADNASVLSVSSNFEPFATDDLGNTVIHLDQALARMREYERMKTEAESNSNMRCTCRIIEDGDGAGAGTTVNNLEETPVIENRSSQQPVSEVSTIPCPRIDTQQLDRQIKAIMKEVIPFLKEHMDEVCSSQLLTSVRRMVLTLTQQNDESKEFVKFFHKQLGSILQDSLAKFAGRKLKDCGEDLLVEISEVLFNELAFFKLMQDLDNNSITVKQRCKRKIEATGVIQSCAKEAKRILEDHGSPAGEIDDEDKDKDETETVKQTQTSEVYDGPKNVRSDISDQEEDEESEGCPVSINLSKAETQALTNYGSGEDENEDEEMEEFEEGPVDVQTSLQANTEATEENEHDEQVLQRDFKKTAESKNVPLEREATSKNDQNNCPVKPCYLNILEDEQPLNSAAHKESPPTVDSTQQPNPLPLRLPEMEPLVPRVKEVKSAQETPESSLAGSPDTESPVLVNDYEAESGNISQKSDEEDFVKVEDLPLKLTIYSEADLRKKMVEEEQKNHLSGEICEMQTEELAGNSETLKEPETVGAQSI
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving PCM1 is found in papillary thyroid carcinomas (PTCs) (PubMed:10980597). Translocation t(8;10)(p21.3;q11.2) with RET links the protein kinase domain of RET to the major portion of PCM1 (PubMed:10980597). {ECO:0000269|PubMed:10980597}.; DISEASE: Note=A chromosomal aberration involving PCM1 is found in a variety of hematological malignancies including atypical chronic myeloid leukemia (atypical CML) and T-cell lymphoma (PubMed:15805263, PubMed:16034466, PubMed:16091753, PubMed:16424865, PubMed:16769584). Translocation t(8;9)(p22;p24) with JAK2 links the protein kinase domain of JAK2 to the major portion of PCM1 (PubMed:15805263, PubMed:16034466, PubMed:16091753, PubMed:16424865, PubMed:16769584). {ECO:0000269|PubMed:15805263, ECO:0000269|PubMed:16034466, ECO:0000269|PubMed:16091753, ECO:0000269|PubMed:16424865, ECO:0000269|PubMed:16769584}.
uniprot
proteins
function
FUNCTION: Required for centrosome assembly and function (PubMed:12403812, PubMed:15659651, PubMed:16943179). Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2 (PubMed:12403812, PubMed:15659651). Required to anchor microtubules to the centrosome (PubMed:12403812, PubMed:15659651). Also involved in cilium biogenesis by recruiting the BBSome, a ciliary protein complex involved in cilium biogenesis, to the centriolar satellites (PubMed:20551181, PubMed:24121310, PubMed:27979967). Recruits the tubulin polyglutamylase complex (TPGC) to centriolar satellites (PubMed:34782749). {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:15659651, ECO:0000269|PubMed:16943179, ECO:0000269|PubMed:20551181, ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:34782749}.
uniprot
proteins
mass_dalton
228560
uniprot
proteins
mutagenesis
MUTAGEN 372; /note="S->D: Phosphomimetic mutant."; /evidence="ECO:0000269|PubMed:30804208
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Undergoes monoubiquitination catalyzed by the E3 ubiquitin-protein ligase MIB1 in proliferating cells, preventing cilia formation (PubMed:24121310). Monoubiquitination by MIB1 is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, resulting in cilia formation initiation (PubMed:24121310). {ECO:0000269|PubMed:24121310}.; PTM: Variant Ser-159 is phosphorylated. {ECO:0007744|PubMed:23186163}.; PTM: Phosphorylated on multiple serine and threonine residues by DYRK3 during the G2-to-M transition, after the nuclear-envelope breakdown (PubMed:29973724). Phosphorylation by DYRK3 promotes disassembly of pericentriolar material (PubMed:29973724). Phosphorylation at Ser-372 mediated by PLK4 is required to maintain the integrity of centriolar satellites (PubMed:30804208). {ECO:0000269|PubMed:29973724, ECO:0000269|PubMed:30804208}.
uniprot
proteins
protein_family
PCM1 family
uniprot
proteins
pubmed
10980597
uniprot
proteins
pubmed
12403812
uniprot
proteins
pubmed
14520415
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15107855
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15184884
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15659651
uniprot
proteins
pubmed
15805263
uniprot
proteins
pubmed
16034466
uniprot
proteins
pubmed
16091753
uniprot
proteins
pubmed
16270321
uniprot
proteins
pubmed
16291865
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
16424865
uniprot
proteins
pubmed
16769584
uniprot
proteins
pubmed
16943179
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20551181
uniprot
proteins
pubmed
20719959
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24089205
uniprot
proteins
pubmed
24121310
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24816561
uniprot
proteins
pubmed
25074808
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26538025
uniprot
proteins
pubmed
26643951
uniprot
proteins
pubmed
27979967
uniprot
proteins
pubmed
28235840
uniprot
proteins
pubmed
29973724
uniprot
proteins
pubmed
30804208
uniprot
proteins
pubmed
31789463
uniprot
proteins
pubmed
32946374
uniprot
proteins
pubmed
34782749
uniprot
proteins
pubmed
36606424
uniprot
proteins
pubmed
8120099
uniprot
proteins
pubmed
9361024
uniprot
proteins
sequence_length
2024
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8AV28}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:30804208}. Cytoplasmic granule {ECO:0000269|PubMed:15107855}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:31789463, ECO:0000269|PubMed:32946374, ECO:0000269|PubMed:34782749}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24121310}. Note=Recruitment to the centrosome requires microtubules and dynein. The majority of the protein dissociates from the centrosome during metaphase and subsequently localizes to the cleavage site in telophase. Displaced from centriolar satellites and centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling.
uniprot
proteins