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Protein

Pumilio homolog 1

Gene

PUM1

Organism
Homo sapiens (Human)
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) (PubMed:21572425, PubMed:18328718, PubMed:21653694, PubMed:21397187). 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). 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). 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).By similarity11 Publications

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Differentiation, Spermatogenesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Pumilio homolog 1Curated
Short name:
HsPUM
Short name:
Pumilio-1
Gene namesi
Name:PUM1Imported
Synonyms:KIAA00991 Publication, PUMH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14957. PUM1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091S → A: Does not affect RNA-binding activity. 1 Publication
Mutagenesisi714 – 7141S → A: Decreased RNA-binding activity. 1 Publication
Mutagenesisi714 – 7141S → E: Phospho-mimic mutant; persistent RNA-binding activity in quiescent cells. 1 Publication
Mutagenesisi863 – 8675SRFIQ → GRFIR: B and inds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi899 – 9035NYVIQ → GYVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi935 – 9395CRVIQ → GRVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi971 – 9755NHVVQ → GHVVR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi1007 – 10115CRVIQ → GRVIR, ARVIR, SRVIR, TRVIR or CRVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi1007 – 10115CRVIQ → SRVIE: Specifically binds guanine-nucleotide in RNA target. 1 Publication
Mutagenesisi1007 – 10071C → N: Specifically binds uracil-nucleotide in RNA target. 1 Publication
Mutagenesisi1043 – 10475NYVIQ → GYVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi1043 – 10442NY → SN: Changes the specificity for RNA; when associated with E-1047. 1 Publication
Mutagenesisi1047 – 10471Q → E: Changes the specificity for RNA; when associated with 1043-SN-1044. 1 Publication
Mutagenesisi1079 – 10835SNVVE → GNVVR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication
Mutagenesisi1122 – 11265NYVVQ → GYVVR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication

Organism-specific databases

PharmGKBiPA34042.

Polymorphism and mutation databases

BioMutaiPUM1.
DMDMi41688619.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11861185Pumilio homolog 1PRO_0000075917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei75 – 751Phosphoserine3 Publications
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei124 – 1241Phosphoserine1 Publication
Modified residuei209 – 2091Phosphoserine5 Publications
Modified residuei229 – 2291Phosphoserine1 Publication
Modified residuei709 – 7091Phosphoserine4 Publications
Modified residuei714 – 7141Phosphoserine1 Publication
Modified residuei806 – 8061Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14671.
PaxDbiQ14671.
PRIDEiQ14671.

2D gel databases

UCD-2DPAGEQ14671.

PTM databases

PhosphoSiteiQ14671.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, muscle, intestine and stomach. Not expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested.1 Publication

Inductioni

Strongly down-regulated in keratinocytes upon UVB irradiation.1 Publication

Gene expression databases

BgeeiQ14671.
CleanExiHS_PUM1.
ExpressionAtlasiQ14671. baseline and differential.
GenevisibleiQ14671. HS.

Organism-specific databases

HPAiHPA027424.
HPA027430.

Interactioni

Subunit structurei

Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). In case of viral infection, interacts with DHX58 (PubMed:25340845).2 Publications

Protein-protein interaction databases

BioGridi115050. 27 interactions.
DIPiDIP-29082N.
IntActiQ14671. 12 interactions.
MINTiMINT-1199500.
STRINGi9606.ENSP00000391723.

Structurei

Secondary structure

1
1186
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi831 – 8377Combined sources
Helixi846 – 8494Combined sources
Turni850 – 8523Combined sources
Helixi853 – 8575Combined sources
Helixi860 – 87213Combined sources
Helixi875 – 88511Combined sources
Helixi886 – 8883Combined sources
Helixi889 – 8935Combined sources
Helixi898 – 90811Combined sources
Helixi911 – 92111Combined sources
Helixi925 – 9295Combined sources
Helixi934 – 94411Combined sources
Helixi947 – 9548Combined sources
Helixi955 – 9573Combined sources
Helixi961 – 9666Combined sources
Helixi970 – 98011Combined sources
Helixi983 – 9864Combined sources
Helixi987 – 9926Combined sources
Turni993 – 9964Combined sources
Helixi997 – 10015Combined sources
Helixi1006 – 101611Combined sources
Helixi1019 – 103113Combined sources
Helixi1033 – 10364Combined sources
Helixi1042 – 105211Combined sources
Helixi1055 – 106511Combined sources
Turni1066 – 10683Combined sources
Helixi1069 – 10735Combined sources
Helixi1078 – 108811Combined sources
Helixi1091 – 110313Combined sources
Beta strandi1104 – 11063Combined sources
Beta strandi1107 – 11093Combined sources
Helixi1111 – 11166Combined sources
Helixi1121 – 113111Combined sources
Helixi1134 – 11429Combined sources
Helixi1145 – 11473Combined sources
Helixi1148 – 11514Combined sources
Beta strandi1153 – 11553Combined sources
Helixi1157 – 11648Combined sources
Helixi1165 – 11673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IB2X-ray1.90A828-1176[»]
1M8WX-ray2.20A/B828-1176[»]
1M8XX-ray2.20A/B828-1176[»]
1M8YX-ray2.60A/B828-1176[»]
1M8ZX-ray1.90A828-1176[»]
2YJYX-ray2.60A/B828-1176[»]
3BSBX-ray2.80A/B828-1170[»]
3BSXX-ray2.32A/B828-1170[»]
3Q0LX-ray2.50A/B828-1176[»]
3Q0MX-ray2.70A/B828-1176[»]
3Q0NX-ray2.40A/B828-1176[»]
3Q0OX-ray2.80A/B828-1176[»]
3Q0PX-ray2.60A/B828-1176[»]
ProteinModelPortaliQ14671.
SMRiQ14671. Positions 828-1165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14671.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini828 – 1168341PUM-HDPROSITE-ProRule annotationAdd
BLAST
Repeati848 – 88336Pumilio 1PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati884 – 91936Pumilio 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati920 – 95536Pumilio 3PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati956 – 99136Pumilio 4PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati992 – 102736Pumilio 5PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati1028 – 106336Pumilio 6PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati1064 – 109936Pumilio 7PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati1103 – 114240Pumilio 8PROSITE-ProRule annotation1 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni863 – 8675Adenine-nucleotide binding in RNA target1 Publication
Regioni899 – 9035Uracil-nucleotide binding in RNA target1 Publication
Regioni935 – 9395Adenine-nucleotide binding in RNA target1 Publication
Regioni971 – 9755Non-specific-nucleotide binding in RNA target1 Publication
Regioni1007 – 10115Adenine-nucleotide binding in RNA target1 Publication
Regioni1043 – 10475Uracil-nucleotide binding in RNA targetCombined sources2 Publications
Regioni1079 – 10835Guanine-nucleotide binding in RNA targetCombined sources2 Publications
Regioni1122 – 11265Uracil-nucleotide binding in RNA targetCombined sources2 Publications

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi393 – 613221Ala-richAdd
BLAST
Compositional biasi475 – 52349Gln-richAdd
BLAST
Compositional biasi642 – 815174Ser-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:21397187). 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 (PubMed:21572425. PubMed:18328718, PubMed:21653694).4 Publications

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5099.
GeneTreeiENSGT00390000017241.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
InParanoidiQ14671.
KOiK17943.
PhylomeDBiQ14671.
TreeFamiTF318160.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
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: Q14671-1) [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
GGYNNSKHRW 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 AAHQPHIGLA PAAFVPNPYI ISAAPPGTDP YTAGLAAAAT
460 470 480 490 500
LGPAVVPHQY YGVTPWGVYP ASLFQQQAAA AAAATNSANQ QTTPQAQQGQ
510 520 530 540 550
QQVLRGGASQ RPLTPNQNQQ GQQTDPLVAA AAVNSALAFG QGLAAGMPGY
560 570 580 590 600
PVLAPAAYYD QTGALVVNAG ARNGLGAPVR LVAPAPVIIS SSAAQAAVAA
610 620 630 640 650
AAASANGAAG GLAGTTNGPF RPLGTQQPQP QPQQQPNNNL ASSSFYGNNS
660 670 680 690 700
LNSNSQSSSL FSQGSAQPAN TSLGFGSSSS LGATLGSALG GFGTAVANSN
710 720 730 740 750
TGSGSRRDSL TGSSDLYKRT SSSLTPIGHS FYNGLSFSSS PGPVGMPLPS
760 770 780 790 800
QGPGHSQTPP PSLSSHGSSS SLNLGGLTNG SGRYISAAPG AEAKYRSASS
810 820 830 840 850
ASSLFSPSST LFSSSRLRYG MSDVMPSGRS RLLEDFRNNR YPNLQLREIA
860 870 880 890 900
GHIMEFSQDQ HGSRFIQLKL ERATPAERQL VFNEILQAAY QLMVDVFGNY
910 920 930 940 950
VIQKFFEFGS LEQKLALAER IRGHVLSLAL QMYGCRVIQK ALEFIPSDQQ
960 970 980 990 1000
NEMVRELDGH VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFAL
1010 1020 1030 1040 1050
STHPYGCRVI QRILEHCLPD QTLPILEELH QHTEQLVQDQ YGNYVIQHVL
1060 1070 1080 1090 1100
EHGRPEDKSK IVAEIRGNVL VLSQHKFASN VVEKCVTHAS RTERAVLIDE
1110 1120 1130 1140 1150
VCTMNDGPHS ALYTMMKDQY ANYVVQKMID VAEPGQRKIV MHKIRPHIAT
1160 1170 1180
LRKYTYGKHI LAKLEKYYMK NGVDLGPICG PPNGII
Length:1,186
Mass (Da):126,473
Last modified:February 2, 2004 - v3
Checksum:iE1E0D8B3B0181308
GO
Isoform 2 (identifier: Q14671-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-417: I → IA
     597-623: Missing.
     950-950: Q → QVI

Note: No experimental confirmation available.
Show »
Length:1,162
Mass (Da):124,420
Checksum:i84FF134AA644F074
GO
Isoform 3 (identifier: Q14671-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     950-950: Q → QVI

Note: No experimental confirmation available.
Show »
Length:1,188
Mass (Da):126,685
Checksum:i2CA1B7A40A641F4C
GO
Isoform 4 (identifier: Q14671-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPLPPPGPGPEPIPGCTAPTQSPVGRHVVGVKGVGGM
     145-240: Missing.
     417-417: I → IA

Note: No experimental confirmation available.
Show »
Length:1,127
Mass (Da):119,558
Checksum:i296596BFAD017D3F
GO

Sequence cautioni

The sequence BAA07895.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161G → E in BAD96325 (Ref. 4) Curated
Sequence conflicti469 – 4691Y → N in BAD96325 (Ref. 4) Curated
Sequence conflicti893 – 8931M → N in BAA07895 (PubMed:7788527).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPLPPPGPGPEPIPGCTAPT QSPVGRHVVGVKGVGGM in isoform 4. 1 PublicationVSP_053703
Alternative sequencei145 – 24096Missing in isoform 4. 1 PublicationVSP_053704Add
BLAST
Alternative sequencei417 – 4171I → IA in isoform 2 and isoform 4. 2 PublicationsVSP_017059
Alternative sequencei597 – 62327Missing in isoform 2. 1 PublicationVSP_017060Add
BLAST
Alternative sequencei950 – 9501Q → QVI in isoform 2 and isoform 3. 2 PublicationsVSP_017061

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315592 mRNA. Translation: AAG31807.1.
D43951 mRNA. Translation: BAA07895.3. Different initiation.
AL356320, AL445235 Genomic DNA. Translation: CAH71203.1.
AK291779 mRNA. Translation: BAF84468.1.
AK294477 mRNA. Translation: BAG57703.1.
AK222605 mRNA. Translation: BAD96325.1.
AL445235, AL356320 Genomic DNA. Translation: CAI22246.1.
CH471059 Genomic DNA. Translation: EAX07633.1.
CH471059 Genomic DNA. Translation: EAX07634.1.
BC013398 mRNA. Translation: AAH13398.1.
CCDSiCCDS338.1. [Q14671-1]
CCDS44099.1. [Q14671-3]
RefSeqiNP_001018494.1. NM_001020658.1. [Q14671-3]
NP_055491.1. NM_014676.2. [Q14671-1]
UniGeneiHs.281707.

Genome annotation databases

EnsembliENST00000257075; ENSP00000257075; ENSG00000134644.
ENST00000373742; ENSP00000362847; ENSG00000134644. [Q14671-4]
ENST00000426105; ENSP00000391723; ENSG00000134644. [Q14671-3]
ENST00000440538; ENSP00000401777; ENSG00000134644. [Q14671-2]
GeneIDi9698.
KEGGihsa:9698.
UCSCiuc001bsi.1. human. [Q14671-1]
uc001bsj.1. human. [Q14671-2]
uc010ogb.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315592 mRNA. Translation: AAG31807.1.
D43951 mRNA. Translation: BAA07895.3. Different initiation.
AL356320, AL445235 Genomic DNA. Translation: CAH71203.1.
AK291779 mRNA. Translation: BAF84468.1.
AK294477 mRNA. Translation: BAG57703.1.
AK222605 mRNA. Translation: BAD96325.1.
AL445235, AL356320 Genomic DNA. Translation: CAI22246.1.
CH471059 Genomic DNA. Translation: EAX07633.1.
CH471059 Genomic DNA. Translation: EAX07634.1.
BC013398 mRNA. Translation: AAH13398.1.
CCDSiCCDS338.1. [Q14671-1]
CCDS44099.1. [Q14671-3]
RefSeqiNP_001018494.1. NM_001020658.1. [Q14671-3]
NP_055491.1. NM_014676.2. [Q14671-1]
UniGeneiHs.281707.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IB2X-ray1.90A828-1176[»]
1M8WX-ray2.20A/B828-1176[»]
1M8XX-ray2.20A/B828-1176[»]
1M8YX-ray2.60A/B828-1176[»]
1M8ZX-ray1.90A828-1176[»]
2YJYX-ray2.60A/B828-1176[»]
3BSBX-ray2.80A/B828-1170[»]
3BSXX-ray2.32A/B828-1170[»]
3Q0LX-ray2.50A/B828-1176[»]
3Q0MX-ray2.70A/B828-1176[»]
3Q0NX-ray2.40A/B828-1176[»]
3Q0OX-ray2.80A/B828-1176[»]
3Q0PX-ray2.60A/B828-1176[»]
ProteinModelPortaliQ14671.
SMRiQ14671. Positions 828-1165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115050. 27 interactions.
DIPiDIP-29082N.
IntActiQ14671. 12 interactions.
MINTiMINT-1199500.
STRINGi9606.ENSP00000391723.

PTM databases

PhosphoSiteiQ14671.

Polymorphism and mutation databases

BioMutaiPUM1.
DMDMi41688619.

2D gel databases

UCD-2DPAGEQ14671.

Proteomic databases

MaxQBiQ14671.
PaxDbiQ14671.
PRIDEiQ14671.

Protocols and materials databases

DNASUi9698.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257075; ENSP00000257075; ENSG00000134644.
ENST00000373742; ENSP00000362847; ENSG00000134644. [Q14671-4]
ENST00000426105; ENSP00000391723; ENSG00000134644. [Q14671-3]
ENST00000440538; ENSP00000401777; ENSG00000134644. [Q14671-2]
GeneIDi9698.
KEGGihsa:9698.
UCSCiuc001bsi.1. human. [Q14671-1]
uc001bsj.1. human. [Q14671-2]
uc010ogb.1. human.

Organism-specific databases

CTDi9698.
GeneCardsiGC01M031405.
HGNCiHGNC:14957. PUM1.
HPAiHPA027424.
HPA027430.
MIMi607204. gene.
neXtProtiNX_Q14671.
PharmGKBiPA34042.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5099.
GeneTreeiENSGT00390000017241.
HOGENOMiHOG000238461.
HOVERGENiHBG049462.
InParanoidiQ14671.
KOiK17943.
PhylomeDBiQ14671.
TreeFamiTF318160.

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiPUM1. human.
EvolutionaryTraceiQ14671.
GeneWikiiPUM1.
GenomeRNAii9698.
NextBioi35471694.
PROiQ14671.
SOURCEiSearch...

Gene expression databases

BgeeiQ14671.
CleanExiHS_PUM1.
ExpressionAtlasiQ14671. baseline and differential.
GenevisibleiQ14671. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and comparative sequence analysis of PUM1 and PUM2 genes, human members of the Pumilio family of RNA-binding proteins."
    Spassov D.S., Jurecic R.
    Gene 299:195-204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Bone marrow.
  3. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Coronary artery.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Amygdala and Placenta.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  9. "Genome-wide comparison of human keratinocyte and squamous cell carcinoma responses to UVB irradiation: implications for skin and epithelial cancer."
    Dazard J.-E., Gal H., Amariglio N., Rechavi G., Domany E., Givol D.
    Oncogene 22:2993-3006(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Comparative analysis of mRNA targets for human PUF-family proteins suggests extensive interaction with the miRNA regulatory system."
    Galgano A., Forrer M., Jaskiewicz L., Kanitz A., Zavolan M., Gerber A.P.
    PLoS ONE 3:E3164-E3164(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-75; SER-209 AND SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-209; SER-709 AND SER-806, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "A Pumilio-induced RNA structure switch in p27-3' UTR controls miR-221 and miR-222 accessibility."
    Kedde M., van Kouwenhove M., Zwart W., Oude Vrielink J.A., Elkon R., Agami R.
    Nat. Cell Biol. 12:1014-1020(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, PHOSPHORYLATION AT SER-209 AND SER-714, MUTAGENESIS OF SER-209 AND SER-714.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-209 AND SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "A structural-based statistical approach suggests a cooperative activity of PUM1 and miR-410 in human 3'-untranslated regions."
    Leibovich L., Mandel-Gutfreund Y., Yakhini Z.
    Silence 1:17-17(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A universal code for RNA recognition by PUF proteins."
    Filipovska A., Razif M.F., Nygaard K.K., Rackham O.
    Nat. Chem. Biol. 7:425-427(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, FUNCTION, MUTAGENESIS OF 863-SER--GLN-867; 899-ASN--GLN-903; 935-CYS--GLN-939; 971-ASN--GLN-975; CYS-1007; 1007-CYS--GLN-1011; 1043-ASN--GLN-1047; 1079-SER--GLU-1083 AND 1122-ASN--GLN-1126.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Pumilio facilitates miRNA regulation of the E2F3 oncogene."
    Miles W.O., Tschop K., Herr A., Ji J.Y., Dyson N.J.
    Genes Dev. 26:356-368(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Human Pumilio proteins recruit multiple deadenylases to efficiently repress messenger RNAs."
    Van Etten J., Schagat T.L., Hrit J., Weidmann C.A., Brumbaugh J., Coon J.J., Goldstrohm A.C.
    J. Biol. Chem. 287:36370-36383(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH A DEADENYLASE COMPLEX.
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  24. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection."
    Narita R., Takahasi K., Murakami E., Hirano E., Yamamoto S.P., Yoneyama M., Kato H., Fujita T.
    PLoS Pathog. 10:E1004417-E1004417(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DHX58.
  26. "Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by increasing wild-type Ataxin1 levels."
    Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y., Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A., Orr H.T., Sillitoe R.V., Zoghbi H.Y.
    Cell 160:1087-1098(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "Crystal structure of a Pumilio homology domain."
    Wang X., Zamore P.D., Hall T.M.T.
    Mol. Cell 7:855-865(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 828-1166.
  28. "Modular recognition of RNA by a human pumilio-homology domain."
    Wang X., McLachlan J., Zamore P.D., Hall T.M.T.
    Cell 110:501-512(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 828-1176 IN COMPLEX WITH RNA, MUTAGENESIS OF 1043-ASN-TYR-1044 AND GLN-1047.
  29. "Structures of human Pumilio with noncognate RNAs reveal molecular mechanisms for binding promiscuity."
    Gupta Y.K., Nair D.T., Wharton R.P., Aggarwal A.K.
    Structure 16:549-557(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 828-1170 IN COMPLEX WITH CONSENSUS MRNA, FUNCTION, RNA-BINDING, DOMAIN.
  30. "Specific and modular binding code for cytosine recognition in Pumilio/FBF (PUF) RNA-binding domains."
    Dong S., Wang Y., Cassidy-Amstutz C., Lu G., Bigler R., Jezyk M.R., Li C., Hall T.M., Wang Z.
    J. Biol. Chem. 286:26732-26742(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 828-1176, FUNCTION, RNA-BINDING, DOMAIN.
  31. "Alternate modes of cognate RNA recognition by human PUMILIO proteins."
    Lu G., Hall T.M.
    Structure 19:361-367(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 828-1176 IN COMPLEX WITH CONSENSUS MRNA, FUNCTION, RNA-BINDING, DOMAIN.

Entry informationi

Entry nameiPUM1_HUMAN
AccessioniPrimary (citable) accession number: Q14671
Secondary accession number(s): A8K6W4
, B4DG92, D3DPN3, E9PCJ0, Q53HH5, Q5VXY7, Q9HAN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: July 22, 2015
This is version 141 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.