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Protein

Pumilio homolog 1

Gene

PUM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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, 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).By similarity14 Publications

GO - Molecular functioni

  • miRNA binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processDifferentiation, Spermatogenesis, Translation regulation

Enzyme and pathway databases

ReactomeiR-HSA-432722 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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000134644.15
HGNCiHGNC:14957 PUM1
MIMi607204 gene
neXtProtiNX_Q14671

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 47 (SCA47)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA47 is an autosomal dominant disease with a highly variable phenotype and incomplete penetrance. Clinical features include developmental disability, ataxia, and seizures.
See also OMIM:617931
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0807841033T → S in SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1. 1 Publication1
Natural variantiVAR_0807851137R → W in SCA47; decreased post-transcriptional repression of E2F3 and ATXN1. 1 Publication1
Natural variantiVAR_0807861145R → W in SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi209S → A: Does not affect RNA-binding activity. 1 Publication1
Mutagenesisi714S → A: Decreased RNA-binding activity. 1 Publication1
Mutagenesisi714S → E: Phospho-mimic mutant; persistent RNA-binding activity in quiescent cells. 1 Publication1
Mutagenesisi863 – 867SRFIQ → GRFIR: B and inds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi899 – 903NYVIQ → GYVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi935 – 939CRVIQ → GRVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi971 – 975NHVVQ → GHVVR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi1007 – 1011CRVIQ → GRVIR, ARVIR, SRVIR, TRVIR or CRVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi1007 – 1011CRVIQ → SRVIE: Specifically binds guanine-nucleotide in RNA target. 1 Publication5
Mutagenesisi1007C → N: Specifically binds uracil-nucleotide in RNA target. 1 Publication1
Mutagenesisi1043 – 1047NYVIQ → GYVIR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi1043 – 1044NY → SN: Changes the specificity for RNA; when associated with E-1047. 1 Publication2
Mutagenesisi1047Q → E: Changes the specificity for RNA; when associated with 1043-SN-1044. 1 Publication1
Mutagenesisi1079 – 1083SNVVE → GNVVR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5
Mutagenesisi1122 – 1126NYVVQ → GYVVR: Specifically binds cytosine-nucleotide in RNA target. 1 Publication5

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNETi9698
MalaCardsiPUM1
MIMi617931 phenotype
OpenTargetsiENSG00000134644
PharmGKBiPA34042

Polymorphism and mutation databases

BioMutaiPUM1
DMDMi41688619

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000759172 – 1186Pumilio homolog 1Add BLAST1185

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei19PhosphoserineCombined sources1
Modified residuei75PhosphoserineCombined sources1
Modified residuei98PhosphoserineCombined sources1
Modified residuei106PhosphoserineCombined sources1
Modified residuei112PhosphothreonineCombined sources1
Modified residuei124PhosphoserineCombined sources1
Modified residuei159PhosphoserineCombined sources1
Modified residuei197PhosphoserineCombined sources1
Modified residuei209PhosphoserineCombined sources1 Publication1
Modified residuei229PhosphoserineCombined sources1
Modified residuei305PhosphoserineBy similarity1
Modified residuei514PhosphothreonineBy similarity1
Modified residuei709PhosphoserineCombined sources1
Modified residuei714Phosphoserine1 Publication1
Modified residuei796Omega-N-methylarginineCombined sources1
Modified residuei806PhosphoserineCombined sources1
Modified residuei822PhosphoserineCombined sources1

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, Methylation, Phosphoprotein

Proteomic databases

EPDiQ14671
MaxQBiQ14671
PaxDbiQ14671
PeptideAtlasiQ14671
PRIDEiQ14671
ProteomicsDBi60101
60102 [Q14671-2]

2D gel databases

UCD-2DPAGEiQ14671

PTM databases

iPTMnetiQ14671
PhosphoSitePlusiQ14671

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

BgeeiENSG00000134644 Expressed in 243 organ(s), highest expression level in cerebral cortex
CleanExiHS_PUM1
ExpressionAtlasiQ14671 baseline and differential
GenevisibleiQ14671 HS

Organism-specific databases

HPAiHPA027424
HPA027449

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). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (PubMed:23125361).3 Publications

Protein-protein interaction databases

BioGridi115050, 90 interactors
DIPiDIP-29082N
IntActiQ14671, 23 interactors
MINTiQ14671
STRINGi9606.ENSP00000391723

Structurei

Secondary structure

11186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ14671
SMRiQ14671
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14671

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini828 – 1168PUM-HDPROSITE-ProRule annotationAdd BLAST341
Repeati848 – 883Pumilio 1PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati884 – 919Pumilio 2PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati920 – 955Pumilio 3PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati956 – 991Pumilio 4PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati992 – 1027Pumilio 5PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati1028 – 1063Pumilio 6PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati1064 – 1099Pumilio 7PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati1103 – 1142Pumilio 8PROSITE-ProRule annotation1 PublicationAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni863 – 867Adenine-nucleotide binding in RNA target1 Publication5
Regioni899 – 903Uracil-nucleotide binding in RNA target1 Publication5
Regioni935 – 939Adenine-nucleotide binding in RNA target1 Publication5
Regioni971 – 975Non-specific-nucleotide binding in RNA target1 Publication5
Regioni1007 – 1011Adenine-nucleotide binding in RNA target1 Publication5
Regioni1043 – 1047Uracil-nucleotide binding in RNA targetCombined sources2 Publications5
Regioni1079 – 1083Guanine-nucleotide binding in RNA targetCombined sources2 Publications5
Regioni1122 – 1126Uracil-nucleotide binding in RNA targetCombined sources2 Publications5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi393 – 613Ala-richAdd BLAST221
Compositional biasi475 – 523Gln-richAdd BLAST49
Compositional biasi642 – 815Ser-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 (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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1488 Eukaryota
COG5099 LUCA
GeneTreeiENSGT00390000017241
HOGENOMiHOG000238461
HOVERGENiHBG049462
InParanoidiQ14671
KOiK17943
PhylomeDBiQ14671
TreeFamiTF318160

Family and domain databases

CDDicd07920 Pumilio, 1 hit
Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR033133 PUM-HD
IPR033712 Pumilio_RNA-bd
IPR001313 Pumilio_RNA-bd_rpt
PfamiView protein in Pfam
PF00806 PUF, 8 hits
SMARTiView protein in SMART
SM00025 Pumilio, 8 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50302 PUM, 8 hits
PS50303 PUM_HD, 1 hit

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

This entry has 4 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T1Z8Q5T1Z8_HUMAN
Pumilio homolog 1 (Drosophila), iso...
PUM1 hCG_19946
1,224Annotation score:
Q5T1Z4Q5T1Z4_HUMAN
Pumilio homolog 1 (Drosophila), iso...
PUM1 hCG_19946
1,189Annotation score:
H0YEH2H0YEH2_HUMAN
Pumilio homolog 1
PUM1
1,125Annotation score:
E9PR38E9PR38_HUMAN
Pumilio homolog 1
PUM1
944Annotation score:
E9PL65E9PL65_HUMAN
Pumilio homolog 1
PUM1
96Annotation score:
H0YDK8H0YDK8_HUMAN
Pumilio homolog 1
PUM1
900Annotation score:
H0YC97H0YC97_HUMAN
Pumilio homolog 1
PUM1
227Annotation score:
H0YDC5H0YDC5_HUMAN
Pumilio homolog 1
PUM1
217Annotation score:
H0YDQ6H0YDQ6_HUMAN
Pumilio homolog 1
PUM1
76Annotation score:
H0YED4H0YED4_HUMAN
Pumilio homolog 1
PUM1
265Annotation score:
There are more potential isoformsShow all

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti216G → E in BAD96325 (Ref. 4) Curated1
Sequence conflicti469Y → N in BAD96325 (Ref. 4) Curated1
Sequence conflicti893M → N in BAA07895 (PubMed:7788527).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0807841033T → S in SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1. 1 Publication1
Natural variantiVAR_0807851137R → W in SCA47; decreased post-transcriptional repression of E2F3 and ATXN1. 1 Publication1
Natural variantiVAR_0807861145R → W in SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0537031M → MPLPPPGPGPEPIPGCTAPT QSPVGRHVVGVKGVGGM in isoform 4. 1 Publication1
Alternative sequenceiVSP_053704145 – 240Missing in isoform 4. 1 PublicationAdd BLAST96
Alternative sequenceiVSP_017059417I → IA in isoform 2 and isoform 4. 2 Publications1
Alternative sequenceiVSP_017060597 – 623Missing in isoform 2. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_017061950Q → QVI in isoform 2 and isoform 3. 2 Publications1

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 [Q14671-1]
ENST00000373742; ENSP00000362847; ENSG00000134644 [Q14671-4]
ENST00000426105; ENSP00000391723; ENSG00000134644 [Q14671-3]
ENST00000440538; ENSP00000401777; ENSG00000134644 [Q14671-2]
GeneIDi9698
KEGGihsa:9698
UCSCiuc001bsh.2 human [Q14671-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

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
PDB 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[»]
5YKHX-ray2.46A898-1176[»]
5YKIX-ray2.25A898-1176[»]
ProteinModelPortaliQ14671
SMRiQ14671
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115050, 90 interactors
DIPiDIP-29082N
IntActiQ14671, 23 interactors
MINTiQ14671
STRINGi9606.ENSP00000391723

PTM databases

iPTMnetiQ14671
PhosphoSitePlusiQ14671

Polymorphism and mutation databases

BioMutaiPUM1
DMDMi41688619

2D gel databases

UCD-2DPAGEiQ14671

Proteomic databases

EPDiQ14671
MaxQBiQ14671
PaxDbiQ14671
PeptideAtlasiQ14671
PRIDEiQ14671
ProteomicsDBi60101
60102 [Q14671-2]

Protocols and materials databases

DNASUi9698
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257075; ENSP00000257075; ENSG00000134644 [Q14671-1]
ENST00000373742; ENSP00000362847; ENSG00000134644 [Q14671-4]
ENST00000426105; ENSP00000391723; ENSG00000134644 [Q14671-3]
ENST00000440538; ENSP00000401777; ENSG00000134644 [Q14671-2]
GeneIDi9698
KEGGihsa:9698
UCSCiuc001bsh.2 human [Q14671-1]

Organism-specific databases

CTDi9698
DisGeNETi9698
EuPathDBiHostDB:ENSG00000134644.15
GeneCardsiPUM1
HGNCiHGNC:14957 PUM1
HPAiHPA027424
HPA027449
MalaCardsiPUM1
MIMi607204 gene
617931 phenotype
neXtProtiNX_Q14671
OpenTargetsiENSG00000134644
PharmGKBiPA34042
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1488 Eukaryota
COG5099 LUCA
GeneTreeiENSGT00390000017241
HOGENOMiHOG000238461
HOVERGENiHBG049462
InParanoidiQ14671
KOiK17943
PhylomeDBiQ14671
TreeFamiTF318160

Enzyme and pathway databases

ReactomeiR-HSA-432722 Golgi Associated Vesicle Biogenesis

Miscellaneous databases

ChiTaRSiPUM1 human
EvolutionaryTraceiQ14671
GeneWikiiPUM1
GenomeRNAii9698
PROiPR:Q14671
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134644 Expressed in 243 organ(s), highest expression level in cerebral cortex
CleanExiHS_PUM1
ExpressionAtlasiQ14671 baseline and differential
GenevisibleiQ14671 HS

Family and domain databases

CDDicd07920 Pumilio, 1 hit
Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR033133 PUM-HD
IPR033712 Pumilio_RNA-bd
IPR001313 Pumilio_RNA-bd_rpt
PfamiView protein in Pfam
PF00806 PUF, 8 hits
SMARTiView protein in SMART
SM00025 Pumilio, 8 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50302 PUM, 8 hits
PS50303 PUM_HD, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPUM1_HUMAN
AccessioniPrimary (citable) accession number: Q14671
Secondary accession number(s): A8K6W4
, B4DG92, D3DPN3, E9PCJ0, Q53HH5, Q5VXY7, Q9HAN1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: November 7, 2018
This is version 169 of the entry and version 3 of the sequence. See 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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