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Q14671 (PUM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pumilio homolog 1

Short name=HsPUM
Short name=Pumilio-1
Gene names
Name:PUM1
Synonyms:KIAA0099, PUMH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1186 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sequence-specific RNA-binding protein that negatively regulates translation and mRNA stability 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). Capable of deadenylation-dependent and -independent modes of repression. May be required to support proliferation and self-renewal of stem cells. Ref.17 Ref.21

Subunit structure

Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Ref.17

Subcellular location

Cytoplasm Probable.

Tissue specificity

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. Ref.1

Induction

Strongly down-regulated in keratinocytes upon UVB irradiation. Ref.9

Domain

The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half doughnut. RNA-binding occurs on the concave side of the surface (Ref.21).

Sequence similarities

Contains 1 PUM-HD domain.

Contains 8 pumilio repeats.

Sequence caution

The sequence BAA07895.3 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranslation regulation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmembrane organization

Traceable author statement. Source: Reactome

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14671-1)

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.
Isoform 2 (identifier: Q14671-2)

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.
Isoform 3 (identifier: Q14671-3)

The sequence of this isoform differs from the canonical sequence as follows:
     950-950: Q → QVI
Note: No experimental confirmation available.
Isoform 4 (identifier: Q14671-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 11861185Pumilio homolog 1
PRO_0000075917

Regions

Domain828 – 1168341PUM-HD
Repeat848 – 88336Pumilio 1
Repeat884 – 91936Pumilio 2
Repeat920 – 95536Pumilio 3
Repeat956 – 99136Pumilio 4
Repeat992 – 102736Pumilio 5
Repeat1028 – 106336Pumilio 6
Repeat1064 – 109936Pumilio 7
Repeat1103 – 114240Pumilio 8
Compositional bias393 – 613221Ala-rich
Compositional bias475 – 52349Gln-rich
Compositional bias642 – 815174Ser-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.18
Modified residue191Phosphoserine Ref.12
Modified residue751Phosphoserine Ref.12 Ref.13 Ref.16
Modified residue981Phosphoserine Ref.14
Modified residue1061Phosphoserine Ref.14
Modified residue1241Phosphoserine By similarity
Modified residue2091Phosphoserine Ref.10 Ref.12 Ref.13 Ref.14
Modified residue7091Phosphoserine Ref.12 Ref.13 Ref.14 Ref.16
Modified residue8061Phosphoserine Ref.13

Natural variations

Alternative sequence11M → MPLPPPGPGPEPIPGCTAPT QSPVGRHVVGVKGVGGM in isoform 4.
VSP_053703
Alternative sequence145 – 24096Missing in isoform 4.
VSP_053704
Alternative sequence4171I → IA in isoform 2 and isoform 4.
VSP_017059
Alternative sequence597 – 62327Missing in isoform 2.
VSP_017060
Alternative sequence9501Q → QVI in isoform 2 and isoform 3.
VSP_017061

Experimental info

Mutagenesis1043 – 10442NY → SN: Changes the specificity for RNA; when associated with E-1047.
Mutagenesis10471Q → E: Changes the specificity for RNA; when associated with 1043-SN-1044. Ref.20
Sequence conflict2161G → E in BAD96325. Ref.4
Sequence conflict4691Y → N in BAD96325. Ref.4
Sequence conflict8931M → N in BAA07895. Ref.2

Secondary structure

................................................................. 1186
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 2, 2004. Version 3.
Checksum: E1E0D8B3B0181308

FASTA1,186126,473
        10         20         30         40         50         60 
MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP AANQALAAGT 

        70         80         90        100        110        120 
HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG GGYNNSKHRW PTGDNIHAEH 

       130        140        150        160        170        180 
QVRSMDELNH DFQALALEGR AMGEQLLPGK KFWETDESSK DGPKGIFLGD QWRDSAWGTS 

       190        200        210        220        230        240 
DHSVSQPIMV QRRPGQSFHV NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF 

       250        260        270        280        290        300 
GPRDADSDEN DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG 

       310        320        330        340        350        360 
NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM EHVGMEPLQF 

       370        380        390        400        410        420 
DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT AAQQQQYALA AAHQPHIGLA 

       430        440        450        460        470        480 
PAAFVPNPYI ISAAPPGTDP YTAGLAAAAT LGPAVVPHQY YGVTPWGVYP ASLFQQQAAA 

       490        500        510        520        530        540 
AAAATNSANQ QTTPQAQQGQ QQVLRGGASQ RPLTPNQNQQ GQQTDPLVAA AAVNSALAFG 

       550        560        570        580        590        600 
QGLAAGMPGY PVLAPAAYYD QTGALVVNAG ARNGLGAPVR LVAPAPVIIS SSAAQAAVAA 

       610        620        630        640        650        660 
AAASANGAAG GLAGTTNGPF RPLGTQQPQP QPQQQPNNNL ASSSFYGNNS LNSNSQSSSL 

       670        680        690        700        710        720 
FSQGSAQPAN TSLGFGSSSS LGATLGSALG GFGTAVANSN TGSGSRRDSL TGSSDLYKRT 

       730        740        750        760        770        780 
SSSLTPIGHS FYNGLSFSSS PGPVGMPLPS QGPGHSQTPP PSLSSHGSSS SLNLGGLTNG 

       790        800        810        820        830        840 
SGRYISAAPG AEAKYRSASS ASSLFSPSST LFSSSRLRYG MSDVMPSGRS RLLEDFRNNR 

       850        860        870        880        890        900 
YPNLQLREIA GHIMEFSQDQ HGSRFIQLKL ERATPAERQL VFNEILQAAY QLMVDVFGNY 

       910        920        930        940        950        960 
VIQKFFEFGS LEQKLALAER IRGHVLSLAL QMYGCRVIQK ALEFIPSDQQ NEMVRELDGH 

       970        980        990       1000       1010       1020 
VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFAL STHPYGCRVI QRILEHCLPD 

      1030       1040       1050       1060       1070       1080 
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVAEIRGNVL VLSQHKFASN 

      1090       1100       1110       1120       1130       1140 
VVEKCVTHAS RTERAVLIDE VCTMNDGPHS ALYTMMKDQY ANYVVQKMID VAEPGQRKIV 

      1150       1160       1170       1180 
MHKIRPHIAT LRKYTYGKHI LAKLEKYYMK NGVDLGPICG PPNGII 

« Hide

Isoform 2 [UniParc].

Checksum: 84FF134AA644F074
Show »

FASTA1,162124,420
Isoform 3 [UniParc].

Checksum: 2CA1B7A40A641F4C
Show »

FASTA1,188126,685
Isoform 4 [UniParc].

Checksum: 296596BFAD017D3F
Show »

FASTA1,127119,558

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
[13]"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.
[14]"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.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"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.
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[19]"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.
[20]"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.
[21]"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, PUMILIO REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS338.1. [Q14671-1]
CCDS44099.1. [Q14671-3]
RefSeqNP_001018494.1. NM_001020658.1. [Q14671-3]
NP_055491.1. NM_014676.2. [Q14671-1]
UniGeneHs.281707.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ14671.
SMRQ14671. Positions 792-1165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115050. 21 interactions.
DIPDIP-29082N.
IntActQ14671. 12 interactions.
MINTMINT-1199500.
STRING9606.ENSP00000391723.

PTM databases

PhosphoSiteQ14671.

Polymorphism databases

DMDM41688619.

2D gel databases

UCD-2DPAGEQ14671.

Proteomic databases

MaxQBQ14671.
PaxDbQ14671.
PRIDEQ14671.

Protocols and materials databases

DNASU9698.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257075; ENSP00000257075; ENSG00000134644. [Q14671-1]
ENST00000373742; ENSP00000362847; ENSG00000134644. [Q14671-4]
ENST00000426105; ENSP00000391723; ENSG00000134644. [Q14671-3]
ENST00000440538; ENSP00000401777; ENSG00000134644. [Q14671-2]
GeneID9698.
KEGGhsa:9698.
UCSCuc001bsi.1. human. [Q14671-1]
uc001bsj.1. human. [Q14671-2]

Organism-specific databases

CTD9698.
GeneCardsGC01M031405.
HGNCHGNC:14957. PUM1.
HPAHPA027424.
MIM607204. gene.
neXtProtNX_Q14671.
PharmGKBPA34042.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5099.
HOGENOMHOG000238461.
HOVERGENHBG049462.
KOK17943.
PhylomeDBQ14671.
TreeFamTF318160.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ14671.
BgeeQ14671.
CleanExHS_PUM1.
GenevestigatorQ14671.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamPF00806. PUF. 8 hits.
[Graphical view]
SMARTSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPUM1. human.
EvolutionaryTraceQ14671.
GeneWikiPUM1.
GenomeRNAi9698.
NextBio35471694.
PROQ14671.
SOURCESearch...

Entry information

Entry namePUM1_HUMAN
AccessionPrimary (citable) accession number: Q14671
Secondary accession number(s): A8K6W4 expand/collapse secondary AC list , B4DG92, D3DPN3, E9PCJ0, Q53HH5, Q5VXY7, Q9HAN1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: July 9, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM