Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9VR99

- CATIN_DROME

UniProt

Q9VR99 - CATIN_DROME

Protein

Cactin

Gene

cactin

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role during early embryonic development. Involved in the dorsal-ventral embryonic patterning. Probably acts as a negative regulator of the NF-kappa-B (Rel) signaling pathway.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. dorsal/ventral axis specification Source: UniProtKB
    2. mRNA splicing, via spliceosome Source: FlyBase
    3. neurogenesis Source: FlyBase
    4. neuron projection morphogenesis Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cactin
    Alternative name(s):
    Cactus-interacting protein
    Gene namesi
    Name:cactin
    ORF Names:CG1676
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0031114. cactin.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 720720CactinPRO_0000419266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991Phosphoserine1 Publication
    Modified residuei104 – 1041Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9VR99.

    Expressioni

    Tissue specificityi

    Expressed in ovary (at protein level).1 Publication

    Developmental stagei

    Expressed during embryogenesis (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9VR99.

    Interactioni

    Subunit structurei

    Interacts with cact.1 Publication

    Protein-protein interaction databases

    IntActiQ9VR99. 11 interactions.
    MINTiMINT-307793.
    STRINGi7227.FBpp0076997.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili109 – 15951Sequence AnalysisAdd
    BLAST
    Coiled coili206 – 23631Sequence AnalysisAdd
    BLAST
    Coiled coili346 – 37530Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 7769Arg-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CACTIN family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    InParanoidiQ9VR99.
    OrthoDBiEOG7XM2Z3.

    Family and domain databases

    InterProiIPR019134. Cactin_C.
    IPR018816. Cactin_dom.
    [Graphical view]
    PfamiPF10312. Cactin_mid. 1 hit.
    PF09732. CactinC_cactus. 1 hit.
    [Graphical view]
    SMARTiSM01050. CactinC_cactus. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VR99-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKEKSKHRH RSRSRERRDH RSPDPRSSRN RDRDRERERE KDRDHRDHRD    50
    KERDQRRERE KDKSRDKKRE HKSRRRRSSS SSSSPSSSTS SSVPGAPRSP 100
    LVKSPMKLLQ TLEARRLVEQ KDRQRKKEEL KAHETPEEKR ARRLREKQAK 150
    EQRRRERMGW DNEYQTYSNE DNPFGDSNLT STFHWGKKLE VEGLSNLSTK 200
    TVEVLSLQKQ LENRRELEKV KKRRQERELE RQVREDDLMM QQRAKEAVQF 250
    REWQRQEDQF HLEQARLRSE IRIRDGRAKP IDLLAQYVAA GNEPLEECLE 300
    MQMHEPYVLL NGLPVEELED LLVDIKVYEE LEQGKHIDFW NDMITIVQDE 350
    LQRQQKLEAE NSSLNQRRDG IHQAVVKDVA DIFRGKNAQQ LEEMRHRIEA 400
    KISGRADGVD ISYWESLLSQ LKAHMARARL RDRHQALLRE KLSLLKREND 450
    NETLQEKVAP QVKEEEMETQ DAEDPEVEEG SPEDEEDPLN ELRKTVRLYQ 500
    AGNYSPRYIR EEDFTGRRAQ NEDVDEPEAE GLLYEEEDDE RRTQRQRLLI 550
    LHPERVDNNQ LTPQELRMRN EAKQGMQGDE AEFSVETTLD AVPQLATDKY 600
    RPRKPRYFNR VHTGFEWNKY NQTHYDMDNP PPKIVQGYKF NIFYPDLMDK 650
    SQTPQYFLTP CADNGDFAVL RFHTGPPYED IAFKIVNREW EFSYKRGFRC 700
    QFHNNIFQLW FHFKRYRYRR 720
    Length:720
    Mass (Da):86,556
    Last modified:October 3, 2012 - v3
    Checksum:iD7C5175A3925FFDB
    GO

    Sequence cautioni

    The sequence AAF66981.1 differs from that shown. Reason: Frameshift at position 697.
    The sequence AAF50904.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 712EH → DD in AAF66981. (PubMed:10842059)Curated
    Sequence conflicti93 – 931V → M in AAF66981. (PubMed:10842059)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF245116 mRNA. Translation: AAF66981.1. Frameshift.
    AE014298 Genomic DNA. Translation: AAF50904.2. Different initiation.
    UniGeneiDm.2875.

    Genome annotation databases

    KEGGidme:Dmel_CG1676.
    UCSCiCG1676-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF245116 mRNA. Translation: AAF66981.1 . Frameshift.
    AE014298 Genomic DNA. Translation: AAF50904.2 . Different initiation.
    UniGenei Dm.2875.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9VR99. 11 interactions.
    MINTi MINT-307793.
    STRINGi 7227.FBpp0076997.

    Proteomic databases

    PRIDEi Q9VR99.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    KEGGi dme:Dmel_CG1676.
    UCSCi CG1676-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0031114. cactin.

    Phylogenomic databases

    InParanoidi Q9VR99.
    OrthoDBi EOG7XM2Z3.

    Miscellaneous databases

    GenomeRNAii 33043.
    NextBioi 781659.

    Gene expression databases

    Bgeei Q9VR99.

    Family and domain databases

    InterProi IPR019134. Cactin_C.
    IPR018816. Cactin_dom.
    [Graphical view ]
    Pfami PF10312. Cactin_mid. 1 hit.
    PF09732. CactinC_cactus. 1 hit.
    [Graphical view ]
    SMARTi SM01050. CactinC_cactus. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cactin, a conserved protein that interacts with the Drosophila IkappaB protein cactus and modulates its function."
      Lin P., Huang L.H., Steward R.
      Mech. Dev. 94:57-65(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CACT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Ovary.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "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-99 AND SER-104, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiCATIN_DROME
    AccessioniPrimary (citable) accession number: Q9VR99
    Secondary accession number(s): Q9NBV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 83 of the entry and version 3 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