PUM1
entrez
9698
canonical
uniprot
Q14671
canonical
ensembl
ENSG00000134644
resolver
ensp
ENSP00000257075
resolver
ensp
ENSP00000391723
resolver
genesymbol
PUM1
resolver
genesymbol_syn
KIAA0099
resolver
genesymbol_syn
PUMH1
resolver
hgnc
HGNC:14957
resolver
uniprot
A8K6W4
resolver
uniprot
B4DG92
resolver
uniprot
D3DPN3
resolver
uniprot
E9PCJ0
resolver
uniprot
Q53HH5
resolver
uniprot
Q5VXY7
resolver
uniprot
Q9HAN1
resolver
uniprot_entry
PUM1_HUMAN
resolver
uniprot_sec
A8K6W4
resolver
uniprot_sec
B4DG92
resolver
uniprot_sec
D3DPN3
resolver
uniprot_sec
E9PCJ0
resolver
uniprot_sec
Q53HH5
resolver
uniprot_sec
Q5VXY7
resolver
uniprot_sec
Q9HAN1
resolver
amino_acid_sequence
MSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNNSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWETDESSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQSFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDADSDENDKGEKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDADVKDFSRTPGNCQNSANEVDLLGPNQNGSEGLAQLTSTNGAKPVEDFSNMESQSVPLDPMEHVGMEPLQFDYSGTQVPVDSAAATVGLFDYNSQQQLFQRPNALAVQQLTAAQQQQYALAAAHQPHIGLAPAAFVPNPYIISAAPPGTDPYTAGLAAAATLGPAVVPHQYYGVTPWGVYPASLFQQQAAAAAAATNSANQQTTPQAQQGQQQVLRGGASQRPLTPNQNQQGQQTDPLVAAAAVNSALAFGQGLAAGMPGYPVLAPAAYYDQTGALVVNAGARNGLGAPVRLVAPAPVIISSSAAQAAVAAAAASANGAAGGLAGTTNGPFRPLGTQQPQPQPQQQPNNNLASSSFYGNNSLNSNSQSSSLFSQGSAQPANTSLGFGSSSSLGATLGSALGGFGTAVANSNTGSGSRRDSLTGSSDLYKRTSSSLTPIGHSFYNGLSFSSSPGPVGMPLPSQGPGHSQTPPPSLSSHGSSSSLNLGGLTNGSGRYISAAPGAEAKYRSASSASSLFSPSSTLFSSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHIMEFSQDQHGSRFIQLKLERATPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLEQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQNEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPDQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVAEIRGNVLVLSQHKFASNVVEKCVTHASRTERAVLIDEVCTMNDGPHSALYTMMKDQYANYVVQKMIDVAEPGQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPICGPPNGII
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with motor abnormalities, seizures, and facial dysmorphism (NEDMSF) [MIM:620719]: An autosomal dominant disorder characterized by global developmental delay, impaired intellectual development, early-onset seizures, poor overall growth, delayed walking, hypotonia and/or ataxia, and facial dysmorphism. Some patients have hypoplasia of the corpus callosum and cerebral atrophy. {ECO:0000269|PubMed:29474920, ECO:0000269|PubMed:30903679, ECO:0000269|PubMed:31859446, ECO:0000269|PubMed:35386260}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:18328718, PubMed:21397187, PubMed:21572425, PubMed:21653694). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517, PubMed:29474920). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905, PubMed:29474920). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). Binds specifically to miRNA MIR199A precursor, with PUM2, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000250|UniProtKB:Q80U78, ECO:0000269|PubMed:18328718, ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:20818387, ECO:0000269|PubMed:20860814, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:21572425, ECO:0000269|PubMed:21653694, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25768905, ECO:0000269|PubMed:26724866, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:29474920}.
uniprot
proteins
mass_dalton
126473
uniprot
proteins
mutagenesis
MUTAGEN 209; /note="S->A: Does not affect RNA-binding activity."; /evidence="ECO:0000269|PubMed:20818387"; MUTAGEN 714; /note="S->A: Decreased RNA-binding activity."; /evidence="ECO:0000269|PubMed:20818387"; MUTAGEN 714; /note="S->E: Phospho-mimic mutant; persistent RNA-binding activity in quiescent cells."; /evidence="ECO:0000269|PubMed:20818387"; MUTAGEN 863..867; /note="SRFIQ->GRFIR: B and inds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 899..903; /note="NYVIQ->GYVIR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 935..939; /note="CRVIQ->GRVIR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 971..975; /note="NHVVQ->GHVVR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 1007..1011; /note="CRVIQ->GRVIR,ARVIR,SRVIR,TRVIR,CRVIR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 1007..1011; /note="CRVIQ->SRVIE: Specifically binds guanine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 1007; /note="C->N: Specifically binds uracil-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 1043..1047; /note="NYVIQ->GYVIR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 1043..1044; /note="NY->SN: Changes the specificity for RNA; when associated with E-1047."; /evidence="ECO:0000269|PubMed:12202039"; MUTAGEN 1047; /note="Q->E: Changes the specificity for RNA; when associated with 1043-SN-1044."; /evidence="ECO:0000269|PubMed:12202039"; MUTAGEN 1079..1083; /note="SNVVE->GNVVR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425"; MUTAGEN 1122..1126; /note="NYVVQ->GYVVR: Specifically binds cytosine-nucleotide in RNA target."; /evidence="ECO:0000269|PubMed:21572425
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-714 promotes RNA-binding activity. Following growth factor stimulation phosphorylated at Ser-714, promoting binding to the 3'-UTR of CDKN1B/p27 mRNA. {ECO:0000269|PubMed:20818387}.
uniprot
proteins
pubmed
11336708
uniprot
proteins
pubmed
12202039
uniprot
proteins
pubmed
12459267
uniprot
proteins
pubmed
12771951
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18328718
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18776931
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20818387
uniprot
proteins
pubmed
20860814
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21397187
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21572425
uniprot
proteins
pubmed
21653694
uniprot
proteins
pubmed
22345517
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22955276
uniprot
proteins
pubmed
23125361
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25340845
uniprot
proteins
pubmed
25768905
uniprot
proteins
pubmed
26724866
uniprot
proteins
pubmed
28431233
uniprot
proteins
pubmed
29474920
uniprot
proteins
pubmed
30903679
uniprot
proteins
pubmed
31859446
uniprot
proteins
pubmed
35386260
uniprot
proteins
pubmed
7788527
uniprot
proteins
sequence_length
1186
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26724866}. Cytoplasm, P-body {ECO:0000305|PubMed:20818387}. Cytoplasmic granule {ECO:0000269|PubMed:25340845}. Note=Recruited to cytoplasmic stress granules upon viral infection. {ECO:0000269|PubMed:25340845}.
uniprot
proteins