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Q14671 (PUM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. 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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1186 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells By similarity.

Subunit structure

Binds in a sequence-specific manner to the 3'-UTR of some mRNAs.

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.8

Domain

The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs.

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
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular membrane 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 functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11861186Pumilio 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 residue191Phosphoserine Ref.12
Modified residue751Phosphoserine Ref.12 Ref.13
Modified residue1241Phosphoserine By similarity
Modified residue2091Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue7091Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue7141Phosphoserine Ref.10
Modified residue8061Phosphoserine Ref.13

Natural variations

Alternative sequence4171I → IA in isoform 2.
VSP_017059
Alternative sequence597 – 62327Missing in isoform 2.
VSP_017060
Alternative sequence9501Q → QVI in isoform 2.
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.16
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

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: 12459267] [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: 7788527] [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]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[5]"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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[8]"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: 12771951] [Abstract]
Cited for: INDUCTION.
[9]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, MASS SPECTROMETRY.
Tissue: Prostate cancer.
[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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709, MASS SPECTROMETRY.
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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-75; SER-209 AND SER-709, MASS SPECTROMETRY.
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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-209; SER-709 AND SER-806, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[14]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Crystal structure of a Pumilio homology domain."
Wang X., Zamore P.D., Hall T.M.T.
Mol. Cell 7:855-865(2001) [PubMed: 11336708] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 828-1166.
[16]"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: 12202039] [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.
+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.
AL445235, AL356320 Genomic DNA. Translation: CAI22246.1.
CH471059 Genomic DNA. Translation: EAX07633.1.
CH471059 Genomic DNA. Translation: EAX07634.1.
BC013398 mRNA. Translation: AAH13398.1.
IPIIPI00551014.
IPI00941189.
RefSeqNP_001018494.1. NM_001020658.1.
NP_055491.1. NM_014676.2.
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 828-1165.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29082N.
IntActQ14671. 3 interactions.
MINTMINT-1199500.
STRINGQ14671.

PTM databases

PhosphoSiteQ14671.

Polymorphism databases

DMDM41688619.

2D gel databases

UCD-2DPAGEQ14671.

Proteomic databases

PRIDEQ14671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257075; ENSP00000257075; ENSG00000134644.
GeneID9698.
KEGGhsa:9698.
UCSCuc001bsi.1. human.
uc001bsj.1. human.

Organism-specific databases

CTD9698.
GeneCardsGC01M031405.
H-InvDBHIX0000349.
HGNCHGNC:14957. PUM1.
HPAHPA027424.
MIM607204. gene.
neXtProtNX_Q14671.
PharmGKBPA34042.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15759.
GeneTreeENSGT00390000017241.
HOVERGENHBG049462.
OrthoDBEOG4P8FHP.
PhylomeDBQ14671.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ14671.
BgeeQ14671.
CleanExHS_PUM1.
GenevestigatorQ14671.
GermOnlineENSG00000134644. Homo sapiens.

Family and domain databases

InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 1 hit.
PfamPF00806. PUF. 8 hits.
[Graphical view]
SMARTSM00025. Pumilio. 8 hits.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
PROSITEPS50302. PUM. 8 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio36439.
SOURCESearch...

Entry information

Entry namePUM1_HUMAN
AccessionPrimary (citable) accession number: Q14671
Secondary accession number(s): A8K6W4 expand/collapse secondary AC list , D3DPN3, Q5VXY7, Q9HAN1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: January 25, 2012
This is version 106 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

Human chromosome 1

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families