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P31369

- PDM2A_DROME

UniProt

P31369 - PDM2A_DROME

Protein

POU domain protein 2, isoform A

Gene

pdm2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    DNA-binding regulatory protein implicated in early development. Involved in neuronal cell fate decision. May act as an octamer-dependent activator of transcription. Could also play an early role in specific ectodermal cells, and a subsequent role in the embryonic nervous system.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi391 – 45060HomeoboxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: FlyBase
    3. sequence-specific DNA binding Source: InterPro

    GO - Biological processi

    1. central nervous system development Source: UniProtKB
    2. ectoderm development Source: UniProtKB
    3. generation of neurons Source: FlyBase
    4. neuroblast development Source: FlyBase
    5. positive regulation of transcription from RNA polymerase II promoter Source: GOC
    6. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_208061. RNA Polymerase III Abortive And Retractive Initiation.
    REACT_217491. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    POU domain protein 2, isoform A
    Alternative name(s):
    Miti-mere
    Pdm-2
    Protein didymous
    dOct2
    dPOU-28
    Gene namesi
    Name:pdm2
    Synonyms:dim, OCT2, pdm-2, POU-28
    ORF Names:CG12287
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0004394. pdm2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498POU domain protein 2, isoform APRO_0000100778Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei72 – 721Phosphoserine1 Publication
    Modified residuei211 – 2111Phosphoserine1 Publication
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei217 – 2171Phosphoserine1 Publication
    Modified residuei219 – 2191Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP31369.
    PRIDEiP31369.

    Expressioni

    Tissue specificityi

    Initial expression in cellular blastoderm stage, then in ectodermal stripes during germband extension. Broad expression in the neuroectoderm followed by limitation to discrete subsets of CNS cells, and expression in specific PNS neurons and support cells.4 Publications

    Developmental stagei

    Expressed primarily during the first half of embryogenesis.2 Publications

    Gene expression databases

    BgeeiP31369.

    Interactioni

    Protein-protein interaction databases

    BioGridi60717. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP31369.
    SMRiP31369. Positions 289-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini286 – 36075POU-specificPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 106Poly-Gln
    Compositional biasi74 – 796Poly-Glu

    Sequence similaritiesi

    Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 POU-specific domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Homeobox

    Phylogenomic databases

    eggNOGiNOG267922.
    GeneTreeiENSGT00750000117373.
    InParanoidiP31369.
    KOiK09364.
    OrthoDBiEOG7DJSMG.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    1.10.260.40. 1 hit.
    InterProiIPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    IPR010982. Lambda_DNA-bd_dom.
    IPR013847. POU.
    IPR000327. POU_specific.
    [Graphical view]
    PfamiPF00046. Homeobox. 1 hit.
    PF00157. Pou. 1 hit.
    [Graphical view]
    PRINTSiPR00028. POUDOMAIN.
    SMARTiSM00389. HOX. 1 hit.
    SM00352. POU. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    SSF47413. SSF47413. 1 hit.
    PROSITEiPS00027. HOMEOBOX_1. 1 hit.
    PS50071. HOMEOBOX_2. 1 hit.
    PS00035. POU_1. 1 hit.
    PS00465. POU_2. 1 hit.
    PS51179. POU_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P31369-1) [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

    MMVLQQQQQQ RLWDATTTSN TNTQTQQSAN VESTPTKVCH QENAATHTFM    50
    RHMSNSPTPP SPLRSLSDCG KSFEEEELEL GENCEMPQNL SSKRQARELD 100
    SELENEVLDL APPPKRLAEE QEEEKVASVN PPQPVAFAPE EMHQALQLQL 150
    HSYIEMVRQL APEAFPNPNL ATQFLLQNSL QALAQFQALQ QMKQQQREDP 200
    LPSYSTPLAK SPLRSPSLSP VPRHSKSQQR TPPNSMTANS LGMSSAVMTP 250
    NTPSMQQQPQ LQQSTPKPTS GLTVASAMAK LEQSPEETTD LEELEQFAKT 300
    FKQRRIKLGF TQGDVGLAMG KLYGNDFSQT TISRFEALNL SFKNMCKLKP 350
    LLQKWLEDAD STVAKSGGGV FNINTMTSTL SSTPESILGR RRKKRTSIET 400
    TVRTTLEKAF LMNCKPTSEE ISQLSERLNM DKEVIRVWFC NRRQKEKRIN 450
    PSLDLDSPTG TPLSSHAFGY PPQALNMSHM QMEGGSGSFC GSSISSGE 498
    Length:498
    Mass (Da):55,463
    Last modified:July 1, 1993 - v1
    Checksum:i60F17AF776603974
    GO
    Isoform B (identifier: Q9VK71-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q9VK71.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: No experimental confirmation available.

    Length:893
    Mass (Da):98,465
    GO

    Sequence cautioni

    The sequence AAQ23557.1 differs from that shown. Reason: Frameshift at position 95.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2244VPRH → GAPAR in AAA28481. (PubMed:1881906)Curated
    Sequence conflicti248 – 2481M → S in AAA28732. (PubMed:10731132)Curated
    Sequence conflicti447 – 4471K → N in AAA28732. (PubMed:10731132)Curated
    Sequence conflicti472 – 4743PQA → RRL in AAA28481. (PubMed:1881906)Curated
    Sequence conflicti475 – 49824Missing in AAA28481. (PubMed:1881906)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S80559 mRNA. Translation: AAB21408.1.
    M65016 mRNA. Translation: AAA28481.1.
    M93149 mRNA. Translation: AAA28732.1.
    AE014134 Genomic DNA. Translation: AAF53209.1.
    BT010239 mRNA. Translation: AAQ23557.1. Frameshift.
    M81958 Transcribed RNA. Translation: AAA28830.2.
    PIRiA56564.
    RefSeqiNP_523558.2. NM_078834.2. [P31369-1]
    UniGeneiDm.4704.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080393; FBpp0079974; FBgn0004394. [P31369-1]
    GeneIDi34673.
    KEGGidme:Dmel_CG12287.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S80559 mRNA. Translation: AAB21408.1 .
    M65016 mRNA. Translation: AAA28481.1 .
    M93149 mRNA. Translation: AAA28732.1 .
    AE014134 Genomic DNA. Translation: AAF53209.1 .
    BT010239 mRNA. Translation: AAQ23557.1 . Frameshift.
    M81958 Transcribed RNA. Translation: AAA28830.2 .
    PIRi A56564.
    RefSeqi NP_523558.2. NM_078834.2. [P31369-1 ]
    UniGenei Dm.4704.

    3D structure databases

    ProteinModelPortali P31369.
    SMRi P31369. Positions 289-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60717. 1 interaction.

    Proteomic databases

    PaxDbi P31369.
    PRIDEi P31369.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080393 ; FBpp0079974 ; FBgn0004394 . [P31369-1 ]
    GeneIDi 34673.
    KEGGi dme:Dmel_CG12287.

    Organism-specific databases

    CTDi 34673.
    FlyBasei FBgn0004394. pdm2.

    Phylogenomic databases

    eggNOGi NOG267922.
    GeneTreei ENSGT00750000117373.
    InParanoidi P31369.
    KOi K09364.
    OrthoDBi EOG7DJSMG.

    Enzyme and pathway databases

    Reactomei REACT_208061. RNA Polymerase III Abortive And Retractive Initiation.
    REACT_217491. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

    Miscellaneous databases

    GenomeRNAii 34673.
    NextBioi 789620.

    Gene expression databases

    Bgeei P31369.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    1.10.260.40. 1 hit.
    InterProi IPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    IPR010982. Lambda_DNA-bd_dom.
    IPR013847. POU.
    IPR000327. POU_specific.
    [Graphical view ]
    Pfami PF00046. Homeobox. 1 hit.
    PF00157. Pou. 1 hit.
    [Graphical view ]
    PRINTSi PR00028. POUDOMAIN.
    SMARTi SM00389. HOX. 1 hit.
    SM00352. POU. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    SSF47413. SSF47413. 1 hit.
    PROSITEi PS00027. HOMEOBOX_1. 1 hit.
    PS50071. HOMEOBOX_2. 1 hit.
    PS00035. POU_1. 1 hit.
    PS00465. POU_2. 1 hit.
    PS51179. POU_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of two Drosophila POU domain genes, related to oct-1 and oct-2, and the regulation of their expression patterns."
      Lloyd A., Sakonju S.
      Mech. Dev. 36:87-102(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "Two closely linked Drosophila POU domain genes are expressed in neuroblasts and sensory elements."
      Dick T., Yang X., Yeo S., Chia W.
      Proc. Natl. Acad. Sci. U.S.A. 88:7645-7649(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    3. "dOct2, a Drosophila Oct transcription factor that functions in yeast."
      Prakash K., Fang X.D., Engelberg D., Behal A., Parker C.S.
      Proc. Natl. Acad. Sci. U.S.A. 89:7080-7084(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    4. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    7. "Isolation of a family of Drosophila POU domain genes expressed in early development."
      Billin A.N., Cockerill K.A., Poole S.J.
      Mech. Dev. 34:75-84(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-498, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Oregon-R.
      Tissue: Embryo.
    8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-211; SER-215; SER-217 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPDM2A_DROME
    AccessioniPrimary (citable) accession number: P31369
    Secondary accession number(s): Q24430, Q6NR41, Q9VK70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3