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Q9R0Q4

- MO4L2_MOUSE

UniProt

Q9R0Q4 - MO4L2_MOUSE

Protein

Mortality factor 4-like protein 2

Gene

Morf4l2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones By similarity.By similarity

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. DNA repair Source: UniProtKB-KW
    3. positive regulation of striated muscle cell differentiation Source: Ensembl
    4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. regulation of growth Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    DNA damage, DNA repair, Growth regulation, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mortality factor 4-like protein 2
    Alternative name(s):
    MORF-related gene X protein
    Sid 393
    Transcription factor-like protein MRGX
    Gene namesi
    Name:Morf4l2
    Synonyms:Kiaa0026, Sid393
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1927167. Morf4l2.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 288288Mortality factor 4-like protein 2PRO_0000088769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei71 – 711PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9R0Q4.
    PaxDbiQ9R0Q4.
    PRIDEiQ9R0Q4.

    PTM databases

    PhosphoSiteiQ9R0Q4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9R0Q4.
    BgeeiQ9R0Q4.
    CleanExiMM_MORF4L2.
    GenevestigatoriQ9R0Q4.

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41 and VPS72/YL1. The NuA4 complex interacts with MYC and the adenovirus E1A protein. MORF4L1 may also participate in the formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit, but which include the SWI/SNF related protein SRCAP. Component of the MSIN3A histone deacetylase complex, which includes SIN3A, HDAC2, ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with MRFAP1 and RB1. May also interact with one or more as yet undefined members of the TLE (transducin-like enhancer of split) family of transcriptional repressors By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000108722.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0Q4.
    SMRiQ9R0Q4. Positions 117-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini117 – 288172MRGPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MRG domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG317973.
    GeneTreeiENSGT00530000063018.
    HOVERGENiHBG052487.
    InParanoidiA2AEB2.
    KOiK11342.
    OMAiRGNMQRS.
    OrthoDBiEOG7ZPNK7.
    PhylomeDBiQ9R0Q4.
    TreeFamiTF323400.

    Family and domain databases

    InterProiIPR008676. MRG.
    IPR026541. MRG_dom.
    [Graphical view]
    PANTHERiPTHR10880. PTHR10880. 1 hit.
    PfamiPF05712. MRG. 1 hit.
    [Graphical view]
    PROSITEiPS51640. MRG. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9R0Q4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSRKQASQT RGQQSAEEDN FKKPTRSNMQ RSKMRGAASG KKSAGSQPKN    50
    LDPALPGRWG GRSAENPPSG SVRKTRKNKQ KAPGNGDGGS TSEVPQPPRK 100
    KRARADPTVE SEEAFKSRME VKVKIPEELK PWLVEDWDLV TRQKQLFQLP 150
    AKKNVDAILE EYANCKKSQG NVDNKEYAVN EVVGGIKEYF NVMLGTQLLY 200
    KFERPQYAEI LLAHPDAPMS QIYGAPHLLR LFVRIGAMLA YTPLDEKSLA 250
    LLLGYLHDFL KYLAKNSASL FTASDYKVAS ADYHRKAL 288
    Length:288
    Mass (Da):32,184
    Last modified:May 1, 2000 - v1
    Checksum:iDE371EDD3D4DF4E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371A → S in AAH75653. (PubMed:15489334)Curated
    Sequence conflicti145 – 1451Q → P in BAC36075. (PubMed:16141072)Curated
    Sequence conflicti176 – 1761E → D in BAC97848. (PubMed:14621295)Curated
    Sequence conflicti186 – 1861I → T in BAC41017. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025049 mRNA. Translation: BAA84687.1.
    AK075946 mRNA. Translation: BAC36075.1.
    AK088849 mRNA. Translation: BAC40611.1.
    AK089963 mRNA. Translation: BAC41017.1.
    AK129038 mRNA. Translation: BAC97848.1.
    AK131944 mRNA. Translation: BAE20890.1.
    AK145686 mRNA. Translation: BAE26588.1.
    AK150401 mRNA. Translation: BAE29527.1.
    AK150670 mRNA. Translation: BAE29752.1.
    AK151570 mRNA. Translation: BAE30512.1.
    AK160012 mRNA. Translation: BAE35559.1.
    AK161610 mRNA. Translation: BAE36491.1.
    AK164433 mRNA. Translation: BAE37786.1.
    AK166637 mRNA. Translation: BAE38909.1.
    AL671887 Genomic DNA. Translation: CAM17215.1.
    BC075653 mRNA. Translation: AAH75653.1.
    BC088731 mRNA. Translation: AAH88731.1.
    CCDSiCCDS30422.1.
    RefSeqiNP_001161697.1. NM_001168225.1.
    NP_001161698.1. NM_001168226.1.
    NP_001161699.1. NM_001168227.1.
    NP_001161700.1. NM_001168228.1.
    NP_001161701.1. NM_001168229.1.
    NP_001161702.1. NM_001168230.1.
    NP_062742.4. NM_019768.4.
    XP_006528647.1. XM_006528584.1.
    UniGeneiMm.27218.

    Genome annotation databases

    EnsembliENSMUST00000033797; ENSMUSP00000033797; ENSMUSG00000031422.
    ENSMUST00000080411; ENSMUSP00000108722; ENSMUSG00000031422.
    ENSMUST00000113097; ENSMUSP00000108720; ENSMUSG00000031422.
    ENSMUST00000164609; ENSMUSP00000129774; ENSMUSG00000031422.
    ENSMUST00000166478; ENSMUSP00000131909; ENSMUSG00000031422.
    ENSMUST00000166930; ENSMUSP00000126363; ENSMUSG00000031422.
    ENSMUST00000169418; ENSMUSP00000132643; ENSMUSG00000031422.
    GeneIDi56397.
    KEGGimmu:56397.
    UCSCiuc009uiu.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025049 mRNA. Translation: BAA84687.1 .
    AK075946 mRNA. Translation: BAC36075.1 .
    AK088849 mRNA. Translation: BAC40611.1 .
    AK089963 mRNA. Translation: BAC41017.1 .
    AK129038 mRNA. Translation: BAC97848.1 .
    AK131944 mRNA. Translation: BAE20890.1 .
    AK145686 mRNA. Translation: BAE26588.1 .
    AK150401 mRNA. Translation: BAE29527.1 .
    AK150670 mRNA. Translation: BAE29752.1 .
    AK151570 mRNA. Translation: BAE30512.1 .
    AK160012 mRNA. Translation: BAE35559.1 .
    AK161610 mRNA. Translation: BAE36491.1 .
    AK164433 mRNA. Translation: BAE37786.1 .
    AK166637 mRNA. Translation: BAE38909.1 .
    AL671887 Genomic DNA. Translation: CAM17215.1 .
    BC075653 mRNA. Translation: AAH75653.1 .
    BC088731 mRNA. Translation: AAH88731.1 .
    CCDSi CCDS30422.1.
    RefSeqi NP_001161697.1. NM_001168225.1.
    NP_001161698.1. NM_001168226.1.
    NP_001161699.1. NM_001168227.1.
    NP_001161700.1. NM_001168228.1.
    NP_001161701.1. NM_001168229.1.
    NP_001161702.1. NM_001168230.1.
    NP_062742.4. NM_019768.4.
    XP_006528647.1. XM_006528584.1.
    UniGenei Mm.27218.

    3D structure databases

    ProteinModelPortali Q9R0Q4.
    SMRi Q9R0Q4. Positions 117-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000108722.

    PTM databases

    PhosphoSitei Q9R0Q4.

    Proteomic databases

    MaxQBi Q9R0Q4.
    PaxDbi Q9R0Q4.
    PRIDEi Q9R0Q4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033797 ; ENSMUSP00000033797 ; ENSMUSG00000031422 .
    ENSMUST00000080411 ; ENSMUSP00000108722 ; ENSMUSG00000031422 .
    ENSMUST00000113097 ; ENSMUSP00000108720 ; ENSMUSG00000031422 .
    ENSMUST00000164609 ; ENSMUSP00000129774 ; ENSMUSG00000031422 .
    ENSMUST00000166478 ; ENSMUSP00000131909 ; ENSMUSG00000031422 .
    ENSMUST00000166930 ; ENSMUSP00000126363 ; ENSMUSG00000031422 .
    ENSMUST00000169418 ; ENSMUSP00000132643 ; ENSMUSG00000031422 .
    GeneIDi 56397.
    KEGGi mmu:56397.
    UCSCi uc009uiu.3. mouse.

    Organism-specific databases

    CTDi 9643.
    MGIi MGI:1927167. Morf4l2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG317973.
    GeneTreei ENSGT00530000063018.
    HOVERGENi HBG052487.
    InParanoidi A2AEB2.
    KOi K11342.
    OMAi RGNMQRS.
    OrthoDBi EOG7ZPNK7.
    PhylomeDBi Q9R0Q4.
    TreeFami TF323400.

    Enzyme and pathway databases

    Reactomei REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi MORF4L2. mouse.
    NextBioi 312500.
    PROi Q9R0Q4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R0Q4.
    Bgeei Q9R0Q4.
    CleanExi MM_MORF4L2.
    Genevestigatori Q9R0Q4.

    Family and domain databases

    InterProi IPR008676. MRG.
    IPR026541. MRG_dom.
    [Graphical view ]
    PANTHERi PTHR10880. PTHR10880. 1 hit.
    Pfami PF05712. MRG. 1 hit.
    [Graphical view ]
    PROSITEi PS51640. MRG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse homolog of KIAA0026."
      Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: C3H/HeJ, C57BL/6J and NOD.
      Tissue: Bone marrow, Embryonic stem cell, Eye and Thymus.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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].
      Strain: 129 and C57BL/6.
      Tissue: Eye and Mammary tumor.

    Entry informationi

    Entry nameiMO4L2_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0Q4
    Secondary accession number(s): A2AEB2
    , Q3UL62, Q6DIB1, Q6ZQK7, Q8C201, Q8C6C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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