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Q8TB72

- PUM2_HUMAN

UniProt

Q8TB72 - PUM2_HUMAN

Protein

Pumilio homolog 2

Gene

PUM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (02 Feb 2004)
      Previous versions | rss
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    Functioni

    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. Its interactions and tissue specificity suggest that it may be required to support proliferation and self-renewal of stem cells by regulating the translation of key transcripts.2 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. regulation of translation Source: UniProtKB-KW
    2. stress granule assembly Source: Ensembl

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pumilio homolog 2
    Short name:
    Pumilio-2
    Gene namesi
    Name:PUM2
    Synonyms:KIAA0235, PUMH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14958. PUM2.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmic granule By similarity. Cytoplasmperinuclear region 1 Publication
    Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules By similarity. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic stress granule Source: UniProtKB
    3. nuclear membrane Source: HPA
    4. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34043.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10661066Pumilio homolog 2PRO_0000075919Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei82 – 821Phosphoserine2 Publications
    Modified residuei136 – 1361Phosphoserine3 Publications
    Modified residuei178 – 1781Phosphoserine1 Publication
    Modified residuei182 – 1821Phosphoserine3 Publications
    Modified residuei184 – 1841Phosphothreonine2 Publications
    Modified residuei587 – 5871Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8TB72.
    PaxDbiQ8TB72.
    PRIDEiQ8TB72.

    PTM databases

    PhosphoSiteiQ8TB72.

    Expressioni

    Tissue specificityi

    Expressed in male germ cells of adult testis (at protein level). Highly expressed in testis and ovary. Predominantly expressed in stem cells and germ cells. Expressed at lower level in brain, heart, kidney, liver, muscle, placenta, intestine and stomach Expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed in all fetal tissues tested.3 Publications

    Inductioni

    Down-regulated in keratinocytes upon UVB irradiation.1 Publication

    Gene expression databases

    ArrayExpressiQ8TB72.
    BgeeiQ8TB72.
    CleanExiHS_PUM2.
    GenevestigatoriQ8TB72.

    Organism-specific databases

    HPAiHPA030316.
    HPA049670.

    Interactioni

    Subunit structurei

    Homodimer; homodimerizes in vitro. Interacts with DAZ, DAZL and NANOS1 via its pumilio repeats. Interacts with NANOS3 By similarity. Interacts with SNAPIN. Recruits the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Interacts with DDX20.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAZ1Q9NQZ35EBI-311190,EBI-997955
    ORFQ9Q2G43EBI-311190,EBI-6248094From a different organism.

    Protein-protein interaction databases

    BioGridi116949. 10 interactions.
    IntActiQ8TB72. 6 interactions.
    MINTiMINT-254513.
    STRINGi9606.ENSP00000338173.

    Structurei

    Secondary structure

    1
    1066
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi709 – 7157
    Helixi724 – 7274
    Turni728 – 7303
    Helixi731 – 7355
    Helixi738 – 74811
    Helixi753 – 76513
    Helixi767 – 7715
    Turni774 – 7763
    Helixi777 – 78610
    Helixi789 – 79911
    Helixi803 – 8086
    Helixi812 – 82211
    Helixi828 – 8358
    Turni836 – 8394
    Helixi841 – 8466
    Helixi850 – 86011
    Helixi863 – 8664
    Helixi867 – 8726
    Turni873 – 8764
    Helixi877 – 8815
    Helixi886 – 89611
    Helixi899 – 91113
    Helixi913 – 9164
    Helixi922 – 93211
    Helixi935 – 94511
    Helixi949 – 9535
    Helixi958 – 96811
    Helixi971 – 98212
    Beta strandi987 – 9893
    Helixi991 – 9966
    Helixi1001 – 101111
    Helixi1014 – 102411
    Helixi1025 – 10273
    Helixi1028 – 10336
    Helixi1035 – 10373
    Helixi1040 – 10456

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q0QX-ray2.00A706-1056[»]
    3Q0RX-ray2.00A706-1056[»]
    3Q0SX-ray2.00A706-1056[»]
    ProteinModelPortaliQ8TB72.
    SMRiQ8TB72. Positions 706-1048.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TB72.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini706 – 1048343PUM-HDPROSITE-ProRule annotationAdd
    BLAST
    Repeati726 – 76136Pumilio 11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati762 – 79736Pumilio 21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati798 – 83538Pumilio 31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati836 – 87136Pumilio 41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati872 – 90736Pumilio 51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati908 – 94336Pumilio 61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati944 – 97936Pumilio 71 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati983 – 102240Pumilio 81 PublicationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 260260Interaction with SNAPINAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi278 – 488211Ala-richAdd
    BLAST
    Compositional biasi359 – 40547Gln-richAdd
    BLAST
    Compositional biasi520 – 687168Ser-richAdd
    BLAST

    Domaini

    The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half doughnut. RNA-binding occurs on the concave side of the surface (PubMed:21397187).1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5099.
    HOGENOMiHOG000238461.
    HOVERGENiHBG049462.
    InParanoidiQ8TB72.
    KOiK17943.
    OMAiSDERARC.
    OrthoDBiEOG7T7GT5.
    PhylomeDBiQ8TB72.
    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.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TB72-1) [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

    MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW     50
    GASHHSMSQP IMVQRRSGQG FHGNSEVNAI LSPRSESGGL GVSMVEYVLS 100
    SSPADKLDSR FRKGNFGTRD AETDGPEKGD QKGKASPFEE DQNRDLKQGD 150
    DDDSKINGRG LPNGMDADCK DFNRTPGSRQ ASPTEVVERL GPNTNPSEGL 200
    GPLPNPTANK PLVEEFSNPE TQNLDAMEQV GLESLQFDYP GNQVPMDSSG 250
    ATVGLFDYNS QQQLFQRTNA LTVQQLTAAQ QQQYALAAAQ QPHIAGVFSA 300
    GLAPAAFVPN PYIISAAPPG TDPYTAAGLA AAATLAGPAV VPPQYYGVPW 350
    GVYPANLFQQ QAAAAANNTA SQQAASQAQP GQQQVLRAGA GQRPLTPNQG 400
    QQGQQAESLA AAAAANPTLA FGQGLATGMP GYQVLAPTAY YDQTGALVVG 450
    PGARTGLGAP VRLMAPTPVL ISSAAAQAAA AAAAGGTASS LTGSTNGLFR 500
    PIGTQPPQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS HGPGQPGSTS 550
    LGFGSGNSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS 600
    SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL 650
    HLGGLTNGSG RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS 700
    DIMPSGRSRL LEDFRNNRFP NLQLRDLIGH IVEFSQDQHG SRFIQQKLER 750
    ATPAERQMVF NEILQAAYQL MTDVFGNYVI QKFFEFGSLD QKLALATRIR 800
    GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH VLKCVKDQNG 850
    NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE 900
    QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL 950
    ALSQHKFASN VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY 1000
    ANYVVQKMID MAEPAQRKII MHKIRPHITT LRKYTYGKHI LAKLEKYYLK 1050
    NSPDLGPIGG PPNGML 1066
    Length:1,066
    Mass (Da):114,216
    Last modified:February 2, 2004 - v2
    Checksum:iCF6F9D7998CD5D9E
    GO
    Isoform 2 (identifier: Q8TB72-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:987
    Mass (Da):106,215
    Checksum:i99F119F5E3CFCCCF
    GO
    Isoform 3 (identifier: Q8TB72-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,064
    Mass (Da):114,003
    Checksum:i99BC2A2711306F18
    GO
    Isoform 4 (identifier: Q8TB72-4) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:1,008
    Mass (Da):107,646
    Checksum:i44DA760E31DD5F62
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti367 – 3671N → S.
    Corresponds to variant rs34032508 [ dbSNP | Ensembl ].
    VAR_057100

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 4. 1 PublicationVSP_053705Add
    BLAST
    Alternative sequencei574 – 65279Missing in isoform 2. 1 PublicationVSP_009319Add
    BLAST
    Alternative sequencei829 – 8302Missing in isoform 3 and isoform 4. 4 PublicationsVSP_009320

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF315591 mRNA. Translation: AAG31806.1.
    D87078 mRNA. Translation: BAA19665.3.
    AK093847 mRNA. Translation: BAG52772.1.
    AK304198 mRNA. Translation: BAG65078.1.
    AC007041 Genomic DNA. Translation: AAY15026.1.
    CH471053 Genomic DNA. Translation: EAX00821.1.
    CH471053 Genomic DNA. Translation: EAX00823.1.
    BC024218 mRNA. Translation: AAH24218.2.
    BC112046 mRNA. Translation: AAI12047.1.
    BC112048 mRNA. Translation: AAI12049.1.
    AF272350 mRNA. Translation: AAL36981.1.
    CCDSiCCDS1698.1. [Q8TB72-3]
    RefSeqiNP_001269681.1. NM_001282752.1. [Q8TB72-4]
    NP_001269719.1. NM_001282790.1.
    NP_001269720.1. NM_001282791.1.
    NP_056132.1. NM_015317.2. [Q8TB72-3]
    XP_005262664.1. XM_005262607.1. [Q8TB72-1]
    XP_005262666.1. XM_005262609.1. [Q8TB72-2]
    XP_006712035.1. XM_006711972.1. [Q8TB72-1]
    XP_006712036.1. XM_006711973.1. [Q8TB72-1]
    XP_006712037.1. XM_006711974.1. [Q8TB72-1]
    UniGeneiHs.467824.

    Genome annotation databases

    EnsembliENST00000319801; ENSP00000326746; ENSG00000055917. [Q8TB72-2]
    ENST00000338086; ENSP00000338173; ENSG00000055917. [Q8TB72-3]
    ENST00000361078; ENSP00000354370; ENSG00000055917. [Q8TB72-1]
    ENST00000403432; ENSP00000385992; ENSG00000055917. [Q8TB72-3]
    ENST00000440577; ENSP00000409905; ENSG00000055917.
    GeneIDi23369.
    KEGGihsa:23369.
    UCSCiuc002rds.1. human. [Q8TB72-3]

    Polymorphism databases

    DMDMi41688714.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF315591 mRNA. Translation: AAG31806.1 .
    D87078 mRNA. Translation: BAA19665.3 .
    AK093847 mRNA. Translation: BAG52772.1 .
    AK304198 mRNA. Translation: BAG65078.1 .
    AC007041 Genomic DNA. Translation: AAY15026.1 .
    CH471053 Genomic DNA. Translation: EAX00821.1 .
    CH471053 Genomic DNA. Translation: EAX00823.1 .
    BC024218 mRNA. Translation: AAH24218.2 .
    BC112046 mRNA. Translation: AAI12047.1 .
    BC112048 mRNA. Translation: AAI12049.1 .
    AF272350 mRNA. Translation: AAL36981.1 .
    CCDSi CCDS1698.1. [Q8TB72-3 ]
    RefSeqi NP_001269681.1. NM_001282752.1. [Q8TB72-4 ]
    NP_001269719.1. NM_001282790.1.
    NP_001269720.1. NM_001282791.1.
    NP_056132.1. NM_015317.2. [Q8TB72-3 ]
    XP_005262664.1. XM_005262607.1. [Q8TB72-1 ]
    XP_005262666.1. XM_005262609.1. [Q8TB72-2 ]
    XP_006712035.1. XM_006711972.1. [Q8TB72-1 ]
    XP_006712036.1. XM_006711973.1. [Q8TB72-1 ]
    XP_006712037.1. XM_006711974.1. [Q8TB72-1 ]
    UniGenei Hs.467824.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3Q0Q X-ray 2.00 A 706-1056 [» ]
    3Q0R X-ray 2.00 A 706-1056 [» ]
    3Q0S X-ray 2.00 A 706-1056 [» ]
    ProteinModelPortali Q8TB72.
    SMRi Q8TB72. Positions 706-1048.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116949. 10 interactions.
    IntActi Q8TB72. 6 interactions.
    MINTi MINT-254513.
    STRINGi 9606.ENSP00000338173.

    PTM databases

    PhosphoSitei Q8TB72.

    Polymorphism databases

    DMDMi 41688714.

    Proteomic databases

    MaxQBi Q8TB72.
    PaxDbi Q8TB72.
    PRIDEi Q8TB72.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319801 ; ENSP00000326746 ; ENSG00000055917 . [Q8TB72-2 ]
    ENST00000338086 ; ENSP00000338173 ; ENSG00000055917 . [Q8TB72-3 ]
    ENST00000361078 ; ENSP00000354370 ; ENSG00000055917 . [Q8TB72-1 ]
    ENST00000403432 ; ENSP00000385992 ; ENSG00000055917 . [Q8TB72-3 ]
    ENST00000440577 ; ENSP00000409905 ; ENSG00000055917 .
    GeneIDi 23369.
    KEGGi hsa:23369.
    UCSCi uc002rds.1. human. [Q8TB72-3 ]

    Organism-specific databases

    CTDi 23369.
    GeneCardsi GC02M020448.
    HGNCi HGNC:14958. PUM2.
    HPAi HPA030316.
    HPA049670.
    MIMi 607205. gene.
    neXtProti NX_Q8TB72.
    PharmGKBi PA34043.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5099.
    HOGENOMi HOG000238461.
    HOVERGENi HBG049462.
    InParanoidi Q8TB72.
    KOi K17943.
    OMAi SDERARC.
    OrthoDBi EOG7T7GT5.
    PhylomeDBi Q8TB72.
    TreeFami TF318160.

    Miscellaneous databases

    ChiTaRSi PUM2. human.
    EvolutionaryTracei Q8TB72.
    GeneWikii PUM2.
    GenomeRNAii 23369.
    NextBioi 35477241.
    PROi Q8TB72.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TB72.
    Bgeei Q8TB72.
    CleanExi HS_PUM2.
    Genevestigatori Q8TB72.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR001313. Pumilio_RNA-bd_rpt.
    [Graphical view ]
    Pfami PF00806. PUF. 8 hits.
    [Graphical view ]
    SMARTi SM00025. Pumilio. 8 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50302. PUM. 8 hits.
    PS50303. PUM_HD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 3), TISSUE SPECIFICITY.
    2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      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.
      , 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 3 AND 4).
      Tissue: Trachea.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 578-1066 (ISOFORM 1).
      Tissue: Lung and Placenta.
    8. "Human Pumilio-2 is expressed in embryonic stem cells and germ cells and interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins."
      Moore F.L., Jaruzelska J., Fox M.S., Urano J., Firpo M.T., Turek P.J., Dorfman D.M., Reijo Pera R.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:538-543(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-1066 (ISOFORM 2), TISSUE SPECIFICITY, RNA-BINDING, INTERACTION WITH DAZ AND DAZL.
    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. "Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to human germ cells."
      Jaruzelska J., Kotecki M., Kusz K., Spik A., Firpo M., Reijo Pera R.A.
      Dev. Genes Evol. 213:120-126(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, INTERACTION WITH NANOS1.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-178; SER-182; THR-184 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells."
      Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C., Kupryjanczyk J., Jaruzelska J.
      Mol. Hum. Reprod. 15:173-179(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SNAPIN AND NANOS1.
    16. "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 THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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-136; SER-182 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within chromatoid body in human germ cells."
      Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A., Kupryjanczyk J., Jaruzelska J.
      Histochem. Cell Biol. 136:279-287(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX20.
    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-136; SER-182 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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.
    22. "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 (2.0 ANGSTROMS) OF 706-1056 IN COMPLEX WITH CONSENSUS MRNA, FUNCTION, PUMILIO REPEATS.

    Entry informationi

    Entry nameiPUM2_HUMAN
    AccessioniPrimary (citable) accession number: Q8TB72
    Secondary accession number(s): B3KSL0
    , B4E2B6, D6W527, O00234, Q53TV7, Q8WY43, Q9HAN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 2, 2004
    Last sequence update: February 2, 2004
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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 2
      Human chromosome 2: 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
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3