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)

Q497M3

- ABEC4_MOUSE

UniProt

Q497M3 - ABEC4_MOUSE

Protein

Putative C->U-editing enzyme APOBEC-4

Gene

Apobec4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Putative C to U editing enzyme whose physiological substrate is not yet known.By similarity

    Cofactori

    Zinc.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921Zinc; catalyticBy similarity
    Active sitei94 – 941Proton donorBy similarity
    Metal bindingi126 – 1261Zinc; catalyticBy similarity
    Metal bindingi133 – 1331Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines Source: InterPro
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative C->U-editing enzyme APOBEC-4 (EC:3.5.4.-)
    Alternative name(s):
    Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 4
    Gene namesi
    Name:Apobec4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1918531. Apobec4.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 374374Putative C->U-editing enzyme APOBEC-4PRO_0000239357Add
    BLAST

    Proteomic databases

    PRIDEiQ497M3.

    Expressioni

    Tissue specificityi

    Predominantly expressed in testis.1 Publication

    Gene expression databases

    BgeeiQ497M3.
    GenevestigatoriQ497M3.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000069723.

    Structurei

    3D structure databases

    ProteinModelPortaliQ497M3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG43268.
    GeneTreeiENSGT00390000014243.
    HOGENOMiHOG000033767.
    HOVERGENiHBG080811.
    InParanoidiQ497M3.
    OMAiFSQLYHT.
    OrthoDBiEOG7FV3QM.
    PhylomeDBiQ497M3.
    TreeFamiTF338173.

    Family and domain databases

    InterProiIPR013158. APOBEC_N.
    [Graphical view]
    PfamiPF08210. APOBEC_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q497M3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPLYEEILT QGGTIVKPYY WLSLSLGCTN CPYHIRTGEE ARVPYTEFHQ    50
    TFGFPWSTYP QTKHLTFYEL RSSSKNLIQK GLASNCTGSH NHPEAMLFEK 100
    NGYLDAVIFH NSNIRHIILY SNNSPCNEAK HCCISKMYNF LMNYPEVTLS 150
    VFFSQLYHTE KQFPTSAWNR KALQSLASLW PQVTLSPICG GLWHAILEKF 200
    VSNISGSTVP QPFIAGRILA DRYNTYEINS IIAAKPYFTD GLLSRQKENQ 250
    NREAWAAFEK HPLGSAAPAQ RQPTRGQDPR TPAVLMLVSN RDLPPIHVGS 300
    TPQKPRTVVR HLNMLQLSSF KVKDVKKPPS GRPVEEVEVM KESARSQKAN 350
    KKNRSQWKKQ TLVIKPRICR LLER 374
    Length:374
    Mass (Da):42,721
    Last modified:June 13, 2006 - v2
    Checksum:i43AC40F70049F9CD
    GO

    Sequence cautioni

    The sequence AAI00466.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK017014 mRNA. No translation available.
    BC100465 mRNA. Translation: AAI00466.1. Sequence problems.
    CCDSiCCDS35738.1.
    UniGeneiMm.158650.

    Genome annotation databases

    EnsembliENSMUST00000068875; ENSMUSP00000069723; ENSMUSG00000055547.
    UCSCiuc007czi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK017014 mRNA. No translation available.
    BC100465 mRNA. Translation: AAI00466.1 . Sequence problems.
    CCDSi CCDS35738.1.
    UniGenei Mm.158650.

    3D structure databases

    ProteinModelPortali Q497M3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000069723.

    Proteomic databases

    PRIDEi Q497M3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000068875 ; ENSMUSP00000069723 ; ENSMUSG00000055547 .
    UCSCi uc007czi.1. mouse.

    Organism-specific databases

    MGIi MGI:1918531. Apobec4.

    Phylogenomic databases

    eggNOGi NOG43268.
    GeneTreei ENSGT00390000014243.
    HOGENOMi HOG000033767.
    HOVERGENi HBG080811.
    InParanoidi Q497M3.
    OMAi FSQLYHT.
    OrthoDBi EOG7FV3QM.
    PhylomeDBi Q497M3.
    TreeFami TF338173.

    Miscellaneous databases

    PROi Q497M3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q497M3.
    Genevestigatori Q497M3.

    Family and domain databases

    InterProi IPR013158. APOBEC_N.
    [Graphical view ]
    Pfami PF08210. APOBEC_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    2. "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] OF 1-350.
      Tissue: Testis.
    3. "APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis."
      Rogozin I.B., Basu M.K., Jordan I.K., Pavlov Y.I., Koonin E.V.
      Cell Cycle 4:1281-1285(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiABEC4_MOUSE
    AccessioniPrimary (citable) accession number: Q497M3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 62 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3