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Protein

Pumilio homolog 1

Gene

Pum1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). 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. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. 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 (By similarity). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (By similarity). 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 (By similarity). 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). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53 (PubMed:22342750). 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 (PubMed:24412312).By similarity3 Publications

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • RNA binding Source: MGI

GO - Biological processi

  • adult locomotory behavior Source: UniProtKB
  • mRNA destabilization Source: UniProtKB
  • positive regulation of gene silencing by miRNA Source: UniProtKB
  • positive regulation of RIG-I signaling pathway Source: MGI
  • posttranscriptional gene silencing Source: UniProtKB
  • posttranscriptional regulation of gene expression Source: MGI
  • regulation of cell cycle Source: UniProtKB
  • regulation of chromosome segregation Source: UniProtKB
  • regulation of mRNA stability Source: MGI
  • spermatogenesis Source: UniProtKB
  • stem cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation, Spermatogenesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-432722. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Pumilio homolog 1Curated
Gene namesi
Name:Pum1Imported
Synonyms:Kiaa00991 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1931749. Pum1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • CytoplasmP-body By similarity
  • Cytoplasmic granule By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic stress granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are viable and grow to adulthood without apparent defects except that they are smaller than wild-type mice at 8 weeks of age (PubMed:22342750, PubMed:25768905). Males mice however show significantly reduced sperm counts and fertility: testicular hypoplasia is observed (PubMed:22342750). Mice show neurological dysfunction due to progressive loss of motor coordination that appears to be cerebellar in origin (PubMed:25768905).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000759182 – 1189Pumilio homolog 1Add BLAST1188

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei75PhosphoserineCombined sources1
Modified residuei98PhosphoserineBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei112PhosphothreonineBy similarity1
Modified residuei124PhosphoserineCombined sources1
Modified residuei159PhosphoserineBy similarity1
Modified residuei197PhosphoserineBy similarity1
Modified residuei209PhosphoserineBy similarity1
Modified residuei229PhosphoserineCombined sources1
Modified residuei710PhosphoserineCombined sources1
Modified residuei715PhosphoserineBy similarity1
Modified residuei797Omega-N-methylarginineBy similarity1
Modified residuei807PhosphoserineBy similarity1
Modified residuei823PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation at Ser-715 promotes RNA-binding activity. Following growth factor stimulation phosphorylated at Ser-715, promoting binding to the 3'-UTR of CDKN1B/p27 mRNA.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ80U78.
PeptideAtlasiQ80U78.
PRIDEiQ80U78.

PTM databases

iPTMnetiQ80U78.
PhosphoSitePlusiQ80U78.

Expressioni

Tissue specificityi

Widely expressed. Expressed in brain, heart, kidney, liver, lung, skin, intestine, spleen, testis and thymus. Weakly or not expressed in muscles and stomach. Expressed at various stages of myeloid and lymphoid cell development (PubMed:12667987). Highly expressed in testis (PubMed:22342750). Expressed in all major brain regions (at protein level) (PubMed:25768905).3 Publications

Developmental stagei

During the development of the testis, expressed 2 days postpartum (dpp) and then starts to increase at 14 dpp when pachytene spermatocytes first appear.1 Publication

Gene expression databases

BgeeiENSMUSG00000028580.
CleanExiMM_PUM1.
ExpressionAtlasiQ80U78. baseline and differential.
GenevisibleiQ80U78. MM.

Interactioni

Subunit structurei

Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation.By similarity

Protein-protein interaction databases

BioGridi219849. 1 interactor.
IntActiQ80U78. 3 interactors.
MINTiMINT-4109198.
STRINGi10090.ENSMUSP00000030315.

Structurei

3D structure databases

ProteinModelPortaliQ80U78.
SMRiQ80U78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini829 – 1171PUM-HDPROSITE-ProRule annotationAdd BLAST343
Repeati849 – 884Pumilio 1Add BLAST36
Repeati885 – 920Pumilio 2Add BLAST36
Repeati921 – 958Pumilio 3Add BLAST38
Repeati959 – 994Pumilio 4Add BLAST36
Repeati995 – 1030Pumilio 5Add BLAST36
Repeati1031 – 1066Pumilio 6Add BLAST36
Repeati1067 – 1102Pumilio 7Add BLAST36
Repeati1106 – 1145Pumilio 8Add BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni864 – 868Adenine-nucleotide binding in RNA targetBy similarity5
Regioni900 – 904Uracil-nucleotide binding in RNA targetBy similarity5
Regioni936 – 940Adenine-nucleotide binding in RNA targetBy similarity5
Regioni974 – 978Non-specific-nucleotide binding in RNA targetBy similarity5
Regioni1010 – 1014Adenine-nucleotide binding in RNA targetBy similarity5
Regioni1046 – 1050Uracil-nucleotide binding in RNA targetBy similarity5
Regioni1082 – 1086Guanine-nucleotide binding in RNA targetBy similarity5
Regioni1083 – 1086Guanine-nucleotide binding in RNA targetBy similarity4
Regioni1125 – 1129Uracil-nucleotide binding in RNA targetBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi393 – 614Ala-richAdd BLAST222
Compositional biasi476 – 524Gln-richAdd BLAST49
Compositional biasi643 – 816Ser-richAdd BLAST174

Domaini

The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. RNA-binding occurs on the concave side of the surface. PUM1 is composed of 8 pumilio repeats of 36 residues; each repeat binds a single nucleotide in its RNA target. Residues at positions 12 and 16 of the pumilio repeat bind each RNA base via hydrogen bonding or van der Waals contacts with the Watson-Crick edge, while the amino acid at position 13 makes a stacking interaction. The recognition of RNA by pumilio repeats is base specific: cysteine and glutamine at position 12 and 16, respectively, bind adenine; asparagine and glutamine bind uracil; and serine and glutamate bind guanine.By similarity

Sequence similaritiesi

Contains 1 PUM-HD domain.PROSITE-ProRule annotation
Contains 8 pumilio repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1488. Eukaryota.
COG5099. LUCA.
GeneTreeiENSGT00390000017241.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
InParanoidiQ80U78.
KOiK17943.
OMAiHHPSANG.
OrthoDBiEOG091G04QO.
PhylomeDBiQ80U78.
TreeFamiTF318160.

Family and domain databases

CDDicd07920. Pumilio. 1 hit.
Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033133. PUM-HD.
IPR033712. Pumilio_RNA-bd.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF00806. PUF. 8 hits.
[Graphical view]
SMARTiSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80U78-1) [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
MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP
60 70 80 90 100
AANQALAAGT HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG
110 120 130 140 150
GGYNTSKHRW PTGDNIHAEH QVRSMDELNH DFQALALEGR AMGEQLLPGK
160 170 180 190 200
KFWETDESSK DGPKGIFLGD QWRDSAWGTS DHSVSQPIMV QRRPGQSFHV
210 220 230 240 250
NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF GPRDADSDEN
260 270 280 290 300
DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG
310 320 330 340 350
NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM
360 370 380 390 400
EHVGMEPLQF DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT
410 420 430 440 450
AAQQQQYALA AAHQPHIAGL APAAFVPNPY IISAAPPGTD PYTAGLAAAA
460 470 480 490 500
TLGPAVVPHQ YYGVTPWGVY PASLFQQQAA AAAAATNSAT QQSAPQAQQG
510 520 530 540 550
QQQVLRGGAS QRPLTPNQNQ QGQQTDPLVA AAAVNSALAF GQGLAAGMPG
560 570 580 590 600
YPVLAPAAYY DQTGALVVNA GARNGLGAPV RLVAPAPVII SSSAAQAAVA
610 620 630 640 650
AAAASANGAA GGLAGTTNGP FRPLGTQQPQ PQPQQQPSNN LASSSFYGNN
660 670 680 690 700
SLSSNSQSSS LFSQGSAQPA NTSLGFGSSS SLGATLGSAL GGFGTAVANS
710 720 730 740 750
NTGSGSRRDS LTGSSDLYKR TSSSLAPIGH SFYSSLSYSS SPGPVGMPLP
760 770 780 790 800
SQGPGHSQTP PPSLSSHGSS SSLNLGGLTN GSGRYISAAP GAEAKYRSAS
810 820 830 840 850
SASSLFSPSS TLFSSSRLRY GMSDVMPSGR SRLLEDFRNN RYPNLQLREI
860 870 880 890 900
AGHIMEFSQD QHGSRFIQLK LERATAAERQ LVFNEILQAA YQLMVDVFGN
910 920 930 940 950
YVIQKFFEFG SHEQKLALAE RIRGHVLSLA LQMYGCRVIQ KALEFIPSDQ
960 970 980 990 1000
QVINEMVREL DGHVLKCVKD QNGNHVVQKC IECVQPQSLQ FIIDAFKGQV
1010 1020 1030 1040 1050
FALSTHPYGC RVIQRILEHC LPDQTLPILE ELHQHTEQLV QDQYGNYVIQ
1060 1070 1080 1090 1100
HVLEHGRPED KSKIVAEIRG NVLVLSQHKF ASNVVEKCVT HASRTERAVL
1110 1120 1130 1140 1150
IDEVCTMNDG PHSALYTMMK DQYANYVVQK MIDVAEPGQR KIVMHKIRPH
1160 1170 1180
IATLRKYTYG KHILAKLEKY YMKNGVDLGP ICGPPNGII
Length:1,189
Mass (Da):126,619
Last modified:February 2, 2004 - v2
Checksum:iCCB18634FBE3468A
GO
Isoform 2 (identifier: Q80U78-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     418-418: Missing.
     952-953: Missing.

Show »
Length:1,186
Mass (Da):126,336
Checksum:iE3988AF20E34091A
GO
Isoform 3 (identifier: Q80U78-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     418-418: Missing.

Show »
Length:1,188
Mass (Da):126,548
Checksum:i3959D5DC5825A160
GO
Isoform 4 (identifier: Q80U78-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-189: DHSVSQPIM → GNLALASLL
     190-1189: Missing.

Note: No experimental confirmation available.
Show »
Length:189
Mass (Da):20,206
Checksum:i41749718B6FF8B1B
GO

Sequence cautioni

The sequence BAC65487 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti186Q → H in AAG42319 (PubMed:12667987).Curated1
Sequence conflicti545A → D in AAG42319 (PubMed:12667987).Curated1
Sequence conflicti552P → T in AAG42319 (PubMed:12667987).Curated1
Sequence conflicti555A → G in AAG42319 (PubMed:12667987).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009315181 – 189DHSVSQPIM → GNLALASLL in isoform 4. 1 Publication9
Alternative sequenceiVSP_009316190 – 1189Missing in isoform 4. 1 PublicationAdd BLAST1000
Alternative sequenceiVSP_009317418Missing in isoform 2 and isoform 3. 1 Publication1
Alternative sequenceiVSP_009318952 – 953Missing in isoform 2. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321909 mRNA. Translation: AAG42319.1.
AK122205 mRNA. Translation: BAC65487.1. Different initiation.
AK052145 mRNA. Translation: BAC34857.1.
BC048174 mRNA. Translation: AAH48174.1.
BC050747 mRNA. Translation: AAH50747.1.
CCDSiCCDS18710.1. [Q80U78-1]
CCDS51311.1. [Q80U78-2]
CCDS51312.1. [Q80U78-3]
RefSeqiNP_001153075.1. NM_001159603.1. [Q80U78-2]
NP_001153076.1. NM_001159604.1. [Q80U78-3]
NP_001153077.1. NM_001159605.1.
NP_001153078.1. NM_001159606.1.
NP_109647.2. NM_030722.2. [Q80U78-1]
UniGeneiMm.440206.

Genome annotation databases

EnsembliENSMUST00000030315; ENSMUSP00000030315; ENSMUSG00000028580. [Q80U78-1]
ENSMUST00000097862; ENSMUSP00000095474; ENSMUSG00000028580. [Q80U78-3]
ENSMUST00000097864; ENSMUSP00000095476; ENSMUSG00000028580. [Q80U78-2]
ENSMUST00000200938; ENSMUSP00000144158; ENSMUSG00000106966. [Q80U78-3]
ENSMUST00000202398; ENSMUSP00000144210; ENSMUSG00000106966. [Q80U78-2]
ENSMUST00000202551; ENSMUSP00000143996; ENSMUSG00000106966. [Q80U78-1]
GeneIDi80912.
KEGGimmu:80912.
UCSCiuc008uzl.2. mouse. [Q80U78-4]
uc008uzm.3. mouse. [Q80U78-1]
uc008uzn.3. mouse. [Q80U78-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321909 mRNA. Translation: AAG42319.1.
AK122205 mRNA. Translation: BAC65487.1. Different initiation.
AK052145 mRNA. Translation: BAC34857.1.
BC048174 mRNA. Translation: AAH48174.1.
BC050747 mRNA. Translation: AAH50747.1.
CCDSiCCDS18710.1. [Q80U78-1]
CCDS51311.1. [Q80U78-2]
CCDS51312.1. [Q80U78-3]
RefSeqiNP_001153075.1. NM_001159603.1. [Q80U78-2]
NP_001153076.1. NM_001159604.1. [Q80U78-3]
NP_001153077.1. NM_001159605.1.
NP_001153078.1. NM_001159606.1.
NP_109647.2. NM_030722.2. [Q80U78-1]
UniGeneiMm.440206.

3D structure databases

ProteinModelPortaliQ80U78.
SMRiQ80U78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219849. 1 interactor.
IntActiQ80U78. 3 interactors.
MINTiMINT-4109198.
STRINGi10090.ENSMUSP00000030315.

PTM databases

iPTMnetiQ80U78.
PhosphoSitePlusiQ80U78.

Proteomic databases

PaxDbiQ80U78.
PeptideAtlasiQ80U78.
PRIDEiQ80U78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030315; ENSMUSP00000030315; ENSMUSG00000028580. [Q80U78-1]
ENSMUST00000097862; ENSMUSP00000095474; ENSMUSG00000028580. [Q80U78-3]
ENSMUST00000097864; ENSMUSP00000095476; ENSMUSG00000028580. [Q80U78-2]
ENSMUST00000200938; ENSMUSP00000144158; ENSMUSG00000106966. [Q80U78-3]
ENSMUST00000202398; ENSMUSP00000144210; ENSMUSG00000106966. [Q80U78-2]
ENSMUST00000202551; ENSMUSP00000143996; ENSMUSG00000106966. [Q80U78-1]
GeneIDi80912.
KEGGimmu:80912.
UCSCiuc008uzl.2. mouse. [Q80U78-4]
uc008uzm.3. mouse. [Q80U78-1]
uc008uzn.3. mouse. [Q80U78-2]

Organism-specific databases

CTDi9698.
MGIiMGI:1931749. Pum1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1488. Eukaryota.
COG5099. LUCA.
GeneTreeiENSGT00390000017241.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
InParanoidiQ80U78.
KOiK17943.
OMAiHHPSANG.
OrthoDBiEOG091G04QO.
PhylomeDBiQ80U78.
TreeFamiTF318160.

Enzyme and pathway databases

ReactomeiR-MMU-432722. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiPum1. mouse.
PROiQ80U78.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028580.
CleanExiMM_PUM1.
ExpressionAtlasiQ80U78. baseline and differential.
GenevisibleiQ80U78. MM.

Family and domain databases

CDDicd07920. Pumilio. 1 hit.
Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR033133. PUM-HD.
IPR033712. Pumilio_RNA-bd.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF00806. PUF. 8 hits.
[Graphical view]
SMARTiSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUM1_MOUSE
AccessioniPrimary (citable) accession number: Q80U78
Secondary accession number(s): Q80X96
, Q80YU8, Q8BPV7, Q9EPU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: November 2, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.