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Protein

Pumilio homolog 2

Gene

Pum2

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. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. 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. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells.By similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pumilio homolog 2
Gene namesi
Name:Pum2
Synonyms:Kiaa0235
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1931751. Pum2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmic granule 1 Publication
  • Cytoplasmperinuclear region By similarity

  • Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells (By similarity). Colocalizes with NANOS3 in the stress granules (PubMed:19861488).By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10661066Pumilio homolog 2PRO_0000075920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei82 – 821PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei181 – 1811PhosphoserineBy similarity
Modified residuei183 – 1831PhosphothreonineBy similarity
Modified residuei395 – 3951PhosphothreonineBy similarity
Modified residuei587 – 5871PhosphoserineCombined sources
Modified residuei700 – 7001PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ80U58.
PaxDbiQ80U58.
PeptideAtlasiQ80U58.
PRIDEiQ80U58.

PTM databases

iPTMnetiQ80U58.
PhosphoSiteiQ80U58.

Expressioni

Tissue specificityi

Widely expressed. Expressed in embryonic stem cells, heart, kidney, lung, skin, intestine, spleen and thymus. Expressed at intermediate level in brain and liver. Weakly or not expressed in muscles and stomach. Expressed at various stages of myeloid and lymphoid cell development. In the testis expressed in the spermatogoni, spermatocytes, spermatids and Sertoli cells.3 Publications

Gene expression databases

BgeeiENSMUSG00000020594.
CleanExiMM_PUM2.
ExpressionAtlasiQ80U58. baseline and differential.
GenevisibleiQ80U58. MM.

Interactioni

Subunit structurei

Homodimer; homodimerizes in vitro. Interacts with DAZ, DAZL and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By similarity). Interacts with SNAPIN. Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Interacts with DDX20. In case of viral infection, interacts with DHX58 (By similarity).By similarity

Protein-protein interaction databases

BioGridi219850. 3 interactions.
IntActiQ80U58. 3 interactions.
STRINGi10090.ENSMUSP00000128292.

Structurei

Secondary structure

1
1066
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi709 – 7157Combined sources
Helixi724 – 7274Combined sources
Turni728 – 7303Combined sources
Helixi731 – 7355Combined sources
Helixi738 – 74811Combined sources
Helixi753 – 76311Combined sources
Helixi764 – 7663Combined sources
Helixi767 – 7715Combined sources
Helixi776 – 78611Combined sources
Helixi789 – 79911Combined sources
Helixi803 – 8075Combined sources
Helixi812 – 82211Combined sources
Helixi825 – 8284Combined sources
Helixi831 – 8344Combined sources
Helixi835 – 8373Combined sources
Helixi841 – 8466Combined sources
Helixi850 – 86011Combined sources
Helixi863 – 8653Combined sources
Helixi867 – 8726Combined sources
Turni873 – 8764Combined sources
Helixi877 – 8815Combined sources
Helixi886 – 89611Combined sources
Helixi899 – 91012Combined sources
Helixi913 – 9175Combined sources
Helixi922 – 93211Combined sources
Helixi935 – 9439Combined sources
Turni944 – 9474Combined sources
Helixi949 – 9535Combined sources
Helixi958 – 96811Combined sources
Helixi971 – 98212Combined sources
Helixi991 – 9977Combined sources
Helixi1001 – 101111Combined sources
Helixi1014 – 102411Combined sources
Helixi1025 – 10273Combined sources
Helixi1028 – 10314Combined sources
Turni1035 – 10373Combined sources
Helixi1038 – 104710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVOX-ray1.60A706-1056[»]
3GVTX-ray2.80A/B706-1056[»]
ProteinModelPortaliQ80U58.
SMRiQ80U58. Positions 706-1049.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80U58.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini706 – 1048343PUM-HDPROSITE-ProRule annotationAdd
BLAST
Repeati726 – 76136Pumilio 1Add
BLAST
Repeati762 – 79736Pumilio 2Add
BLAST
Repeati798 – 83538Pumilio 3Add
BLAST
Repeati836 – 87136Pumilio 4Add
BLAST
Repeati872 – 90736Pumilio 5Add
BLAST
Repeati908 – 94336Pumilio 6Add
BLAST
Repeati944 – 97936Pumilio 7Add
BLAST
Repeati980 – 102243Pumilio 8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 260260Interaction with SNAPINBy similarityAdd
BLAST
Regioni741 – 7455Adenine-nucleotide binding in RNA targetBy similarity
Regioni777 – 7815Uracil-nucleotide binding in RNA targetBy similarity
Regioni813 – 8175Adenine-nucleotide binding in RNA targetBy similarity
Regioni851 – 8555Non-specific-nucleotide binding in RNA targetBy similarity
Regioni887 – 8915Adenine-nucleotide binding in RNA targetBy similarity
Regioni923 – 9275Uracil-nucleotide binding in RNA targetBy similarity
Regioni959 – 9635Guanine-nucleotide binding in RNA targetBy similarity
Regioni1002 – 10065Uracil-nucleotide binding in RNA targetBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi277 – 486210Ala-richAdd
BLAST
Compositional biasi358 – 40447Gln-richAdd
BLAST
Compositional biasi520 – 687168Ser-richAdd
BLAST

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 (PubMed:19540345). PUM2 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).By similarity1 Publication

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.
InParanoidiQ80U58.
KOiK17943.
OMAiLFDYSSQ.
OrthoDBiEOG091G04QO.
PhylomeDBiQ80U58.
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 (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q80U58-1) [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
MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW
60 70 80 90 100
GTSHHSMSQP IMVQRRSGQS FHGNSEVNAI LSPRSESGGL GVSMVEYVLS
110 120 130 140 150
SSPADKLDSR FRKGTFGTRD AETDGPEKGD QKGKASPFEE DQNRDLKQDD
160 170 180 190 200
EDSKINGRGL PNGMDADCKD FNRTPGSRQA SPTEVVERLG PSTNPPEGLG
210 220 230 240 250
PLPNPTANKP LVEEFSNPET QNLDAMDQVG LDSLQFDYPG NQVPMDSSGA
260 270 280 290 300
TVGLFDYNSQ QQLFQRTSAL TVQQLTAAQQ QQYALAAAQQ PHIAGVFSAG
310 320 330 340 350
LAPAAFVPNP YIISAAPPGT DPYTAAGLAA AATLAGPAVV PPQYYGVPWG
360 370 380 390 400
VYPANLFQQQ AAAAASNTAN QQAASQAQPG QQQVLRPGAG QRPITPSQGQ
410 420 430 440 450
QGQQAESLAA AANPTLAFGQ SLAAGMPGYQ VLAPTAYYDQ TGALVVGPGA
460 470 480 490 500
RTGLGAPVRL MAPTPVLISS TAAQAAAAAA AAGGTANSLT GSTNGLFRPI
510 520 530 540 550
GTQPPQQQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS HGPGQPGSAS
560 570 580 590 600
LGFGSGSSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS
610 620 630 640 650
SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL
660 670 680 690 700
HLGGLTNGSG RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS
710 720 730 740 750
DIMPSGRSRL LEDFRNNRFP NLQLRDLIGH IVEFSQDQHG SRFIQQKLER
760 770 780 790 800
ATPAERQIVF NEILQAAYQL MTDVFGNYVI QKFFEFGSLD QKLALATRIR
810 820 830 840 850
GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH VLKCVKDQNG
860 870 880 890 900
NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE
910 920 930 940 950
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL
960 970 980 990 1000
ALSQHKFASN VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY
1010 1020 1030 1040 1050
ANYVVQKMID MAEPAQRKII MHKIRPHITT LRKYTYGKHI LAKLEKYYLK
1060
NSPDLGPIGG PPNGML
Length:1,066
Mass (Da):114,314
Last modified:February 2, 2004 - v2
Checksum:i027AC00FA91B055E
GO
Isoform 2 (identifier: Q80U58-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     574-652: Missing.
     829-830: Missing.

Show »
Length:985
Mass (Da):106,101
Checksum:i4F4CBF32596ACC13
GO
Isoform 3 (identifier: Q80U58-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     574-652: Missing.
     829-830: Missing.

Note: No experimental confirmation available.
Show »
Length:929
Mass (Da):99,714
Checksum:iE179D3A4364053B4
GO

Sequence cautioni

The sequence BAC65507 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti461 – 4611M → I in BAC65507 (PubMed:12693553).Curated
Sequence conflicti547 – 5471G → A in AAG31805 (PubMed:12667987).Curated
Sequence conflicti553 – 5531F → C in AAG31805 (PubMed:12667987).Curated
Sequence conflicti559 – 5602LG → VR in AAG31805 (PubMed:12667987).Curated
Sequence conflicti570 – 5701F → C in AAG31805 (PubMed:12667987).Curated
Sequence conflicti592 – 5921S → A in AAG31805 (PubMed:12667987).Curated
Sequence conflicti628 – 6281S → G in AAG31805 (PubMed:12667987).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 3. 1 PublicationVSP_009321Add
BLAST
Alternative sequencei574 – 65279Missing in isoform 2 and isoform 3. 2 PublicationsVSP_009322Add
BLAST
Alternative sequencei829 – 8302Missing in isoform 2 and isoform 3. 2 PublicationsVSP_009323

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027917 mRNA. Translation: AAK21966.1.
AF315590 mRNA. Translation: AAG31805.1.
AK122225 mRNA. Translation: BAC65507.1. Different initiation.
BC013765 mRNA. Translation: AAH13765.1.
BC041773 mRNA. Translation: AAH41773.1.
CCDSiCCDS25802.1. [Q80U58-1]
CCDS49026.1. [Q80U58-2]
RefSeqiNP_001153691.1. NM_001160219.1. [Q80U58-1]
NP_001153694.1. NM_001160222.1. [Q80U58-2]
NP_109648.2. NM_030723.2. [Q80U58-1]
XP_006515340.1. XM_006515277.1. [Q80U58-1]
XP_006515341.1. XM_006515278.2. [Q80U58-1]
XP_006515342.1. XM_006515279.1. [Q80U58-1]
XP_006515348.1. XM_006515285.2. [Q80U58-2]
XP_011242227.1. XM_011243925.1. [Q80U58-1]
UniGeneiMm.341243.

Genome annotation databases

EnsembliENSMUST00000163569; ENSMUSP00000131074; ENSMUSG00000020594. [Q80U58-1]
ENSMUST00000168361; ENSMUSP00000128292; ENSMUSG00000020594. [Q80U58-1]
ENSMUST00000169089; ENSMUSP00000132122; ENSMUSG00000020594. [Q80U58-2]
ENSMUST00000178015; ENSMUSP00000137020; ENSMUSG00000020594. [Q80U58-2]
GeneIDi80913.
KEGGimmu:80913.
UCSCiuc007mzw.2. mouse. [Q80U58-3]
uc007mzy.2. mouse. [Q80U58-1]
uc007naa.2. mouse. [Q80U58-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027917 mRNA. Translation: AAK21966.1.
AF315590 mRNA. Translation: AAG31805.1.
AK122225 mRNA. Translation: BAC65507.1. Different initiation.
BC013765 mRNA. Translation: AAH13765.1.
BC041773 mRNA. Translation: AAH41773.1.
CCDSiCCDS25802.1. [Q80U58-1]
CCDS49026.1. [Q80U58-2]
RefSeqiNP_001153691.1. NM_001160219.1. [Q80U58-1]
NP_001153694.1. NM_001160222.1. [Q80U58-2]
NP_109648.2. NM_030723.2. [Q80U58-1]
XP_006515340.1. XM_006515277.1. [Q80U58-1]
XP_006515341.1. XM_006515278.2. [Q80U58-1]
XP_006515342.1. XM_006515279.1. [Q80U58-1]
XP_006515348.1. XM_006515285.2. [Q80U58-2]
XP_011242227.1. XM_011243925.1. [Q80U58-1]
UniGeneiMm.341243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVOX-ray1.60A706-1056[»]
3GVTX-ray2.80A/B706-1056[»]
ProteinModelPortaliQ80U58.
SMRiQ80U58. Positions 706-1049.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219850. 3 interactions.
IntActiQ80U58. 3 interactions.
STRINGi10090.ENSMUSP00000128292.

PTM databases

iPTMnetiQ80U58.
PhosphoSiteiQ80U58.

Proteomic databases

MaxQBiQ80U58.
PaxDbiQ80U58.
PeptideAtlasiQ80U58.
PRIDEiQ80U58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163569; ENSMUSP00000131074; ENSMUSG00000020594. [Q80U58-1]
ENSMUST00000168361; ENSMUSP00000128292; ENSMUSG00000020594. [Q80U58-1]
ENSMUST00000169089; ENSMUSP00000132122; ENSMUSG00000020594. [Q80U58-2]
ENSMUST00000178015; ENSMUSP00000137020; ENSMUSG00000020594. [Q80U58-2]
GeneIDi80913.
KEGGimmu:80913.
UCSCiuc007mzw.2. mouse. [Q80U58-3]
uc007mzy.2. mouse. [Q80U58-1]
uc007naa.2. mouse. [Q80U58-2]

Organism-specific databases

CTDi23369.
MGIiMGI:1931751. Pum2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1488. Eukaryota.
COG5099. LUCA.
GeneTreeiENSGT00390000017241.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
InParanoidiQ80U58.
KOiK17943.
OMAiLFDYSSQ.
OrthoDBiEOG091G04QO.
PhylomeDBiQ80U58.
TreeFamiTF318160.

Miscellaneous databases

ChiTaRSiPum2. mouse.
EvolutionaryTraceiQ80U58.
PROiQ80U58.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020594.
CleanExiMM_PUM2.
ExpressionAtlasiQ80U58. baseline and differential.
GenevisibleiQ80U58. 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 nameiPUM2_MOUSE
AccessioniPrimary (citable) accession number: Q80U58
Secondary accession number(s): Q80UZ9
, Q91YW4, Q925A0, Q9ERC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: September 7, 2016
This is version 122 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.