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Q9UBU8

- MO4L1_HUMAN

UniProt

Q9UBU8 - MO4L1_HUMAN

Protein

Mortality factor 4-like protein 1

Gene

MORF4L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones 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. Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci.2 Publications

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. protein binding Source: UniProtKB
    3. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. chromatin organization Source: Reactome
    3. double-strand break repair via homologous recombination Source: UniProtKB
    4. histone deacetylation Source: UniProtKB
    5. histone H2A acetylation Source: UniProtKB
    6. histone H4 acetylation Source: UniProtKB
    7. regulation of growth Source: UniProtKB-KW
    8. regulation of transcription, DNA-templated Source: UniProtKB-KW
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

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

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mortality factor 4-like protein 1
    Alternative name(s):
    MORF-related gene 15 protein
    Protein MSL3-1
    Transcription factor-like protein MRG15
    Gene namesi
    Name:MORF4L1
    Synonyms:MRG15
    ORF Names:FWP006, HSPC008, HSPC061, PP368
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:16989. MORF4L1.

    Subcellular locationi

    GO - Cellular componenti

    1. NuA4 histone acetyltransferase complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. Sin3 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi208 – 2081V → E: Abolishes binding to MRFAP1. 1 Publication
    Mutagenesisi234 – 2341E → R: No effect on MRFAP1 binding. 1 Publication
    Mutagenesisi251 – 2511Y → A: No effect on MRFAP1 binding. 1 Publication
    Mutagenesisi254 – 2541N → C: Reduces binding to MRFAP1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134895182.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Mortality factor 4-like protein 1PRO_0000088764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei143 – 1431N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UBU8.
    PaxDbiQ9UBU8.
    PRIDEiQ9UBU8.

    PTM databases

    PhosphoSiteiQ9UBU8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UBU8.
    BgeeiQ9UBU8.
    CleanExiHS_MORF4L1.
    GenevestigatoriQ9UBU8.

    Organism-specific databases

    HPAiHPA042360.

    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, VPS72/YL1 and MEAF6. 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 RB1 and KAT8. May also interact with PHF12 and one or more as yet undefined members of the TLE (transducin-like enhancer of split) family of transcriptional repressors. Interacts with the N-terminus of MRFAP1. Found in a complex composed of MORF4L1, MRFAP1 and RB1. Interacts with the entire BRCA complex, which contains BRCA1, PALB2, BRCA2 and RAD51. Interacts with PALB2. Forms a complex with MSL1 and NUPR1.8 Publications

    Protein-protein interaction databases

    BioGridi116134. 58 interactions.
    DIPiDIP-29017N.
    IntActiQ9UBU8. 18 interactions.
    MINTiMINT-1472718.
    STRINGi9606.ENSP00000331310.

    Structurei

    Secondary structure

    1
    362
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 3621
    Beta strandi39 – 468
    Beta strandi47 – 493
    Beta strandi94 – 974
    Helixi98 – 1003
    Beta strandi101 – 1055
    Helixi106 – 12520
    Helixi201 – 2033
    Helixi204 – 21512
    Beta strandi219 – 2213
    Beta strandi226 – 2283
    Helixi229 – 24113
    Beta strandi244 – 2463
    Helixi252 – 27120
    Helixi275 – 2773
    Helixi278 – 28710
    Helixi293 – 2964
    Helixi299 – 31315
    Helixi320 – 33920
    Helixi341 – 3444
    Helixi347 – 3493
    Beta strandi350 – 3523
    Helixi355 – 3584
    Turni359 – 3613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AQLX-ray2.30A/B190-362[»]
    2EFINMR-A1-132[»]
    2F5JX-ray2.20A/B190-360[»]
    2F5KX-ray2.20A/B/C/D/E/F1-129[»]
    2LKMNMR-B194-362[»]
    ProteinModelPortaliQ9UBU8.
    SMRiQ9UBU8. Positions 1-132, 194-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBU8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini191 – 362172MRGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 6237Interaction with KAT8Add
    BLAST
    Regioni133 – 266134Sufficient for interaction with SIN3AAdd
    BLAST
    Regioni164 – 23067Interaction with RB1-1Add
    BLAST
    Regioni188 – 342155Sufficient for interaction with PHF12Add
    BLAST
    Regioni323 – 34422Interaction with RB1-2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi135 – 14612Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MRG domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG238705.
    HOVERGENiHBG052487.
    InParanoidiQ9UBU8.
    KOiK11339.
    OMAiIVEFILY.
    PhylomeDBiQ9UBU8.
    TreeFamiTF323400.

    Family and domain databases

    InterProiIPR016197. Chromodomain-like.
    IPR017398. EAF3/MRG15.
    IPR008676. MRG.
    IPR026541. MRG_dom.
    IPR025995. Tudor-knot.
    [Graphical view]
    PANTHERiPTHR10880. PTHR10880. 1 hit.
    PfamiPF05712. MRG. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038133. HAT_Nua4_EAF3/MRG15. 1 hit.
    SUPFAMiSSF54160. SSF54160. 2 hits.
    PROSITEiPS51640. MRG. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBU8-1) [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

    MAPKQDPKPK FQEGERVLCF HGPLLYEAKC VKVAIKDKQV KYFIHYSGWN    50
    KKSAVRPRRS EKSLKTHEDI VALFPVPEGA PSVHHPLLTS SWDEWVPESR 100
    VLKYVDTNLQ KQRELQKANQ EQYAEGKMRG AAPGKKTSGL QQKNVEVKTK 150
    KNKQKTPGNG DGGSTSETPQ PPRKKRARVD PTVENEETFM NRVEVKVKIP 200
    EELKPWLVDD WDLITRQKQL FYLPAKKNVD SILEDYANYK KSRGNTDNKE 250
    YAVNEVVAGI KEYFNVMLGT QLLYKFERPQ YAEILADHPD APMSQVYGAP 300
    HLLRLFVRIG AMLAYTPLDE KSLALLLNYL HDFLKYLAKN SATLFSASDY 350
    EVAPPEYHRK AV 362
    Length:362
    Mass (Da):41,474
    Last modified:February 15, 2005 - v2
    Checksum:i96B76BCA801F1187
    GO
    Isoform 2 (identifier: Q9UBU8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-91: KSAVRPRRSEKSLKTHEDIVALFPVPEGAPSVHHPLLTSS → N

    Show »
    Length:323
    Mass (Da):37,231
    Checksum:i33CDBEC7D9CF513F
    GO
    Isoform 3 (identifier: Q9UBU8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-127: Missing.

    Show »
    Length:235
    Mass (Da):26,750
    Checksum:i04AA4B2175DF583E
    GO

    Sequence cautioni

    The sequence AAG17253.1 differs from that shown. Reason: Frameshift at positions 348 and 360.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti224 – 2241P → R in AAH67826. (PubMed:15489334)Curated
    Sequence conflicti261 – 2611K → KK in CAB70879. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 127127Missing in isoform 3. 2 PublicationsVSP_046016Add
    BLAST
    Alternative sequencei52 – 9140KSAVR…LLTSS → N in isoform 2. 6 PublicationsVSP_012889Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF100615 mRNA. Translation: AAD29872.1.
    AF167173 mRNA. Translation: AAF80854.1.
    AF218011 mRNA. Translation: AAG17253.1. Frameshift.
    AY148481 mRNA. Translation: AAN65338.1.
    AF070664 mRNA. Translation: AAD20970.1.
    AF161546 mRNA. Translation: AAF29033.1.
    AF109188 mRNA. Translation: AAQ13497.1.
    AK296650 mRNA. Translation: BAG59248.1.
    AK300789 mRNA. Translation: BAH13347.1.
    AL137697 mRNA. Translation: CAB70879.2.
    AC011944 Genomic DNA. No translation available.
    AC022748 Genomic DNA. No translation available.
    AC103975 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99145.1.
    CH471136 Genomic DNA. Translation: EAW99144.1.
    CH471136 Genomic DNA. Translation: EAW99146.1.
    CH471136 Genomic DNA. Translation: EAW99147.1.
    BC022845 mRNA. Translation: AAH22845.1.
    BC002936 mRNA. Translation: AAH02936.1.
    BC067826 mRNA. Translation: AAH67826.1.
    CX165647 mRNA. No translation available.
    AF131847 mRNA. Translation: AAD20058.1.
    CCDSiCCDS10307.1. [Q9UBU8-1]
    CCDS32304.1. [Q9UBU8-2]
    CCDS58393.1. [Q9UBU8-3]
    PIRiT46285.
    RefSeqiNP_001252532.1. NM_001265603.1. [Q9UBU8-3]
    NP_001252533.1. NM_001265604.1. [Q9UBU8-3]
    NP_001252534.1. NM_001265605.1. [Q9UBU8-3]
    NP_006782.1. NM_006791.3. [Q9UBU8-2]
    NP_996670.1. NM_206839.2. [Q9UBU8-1]
    UniGeneiHs.374503.

    Genome annotation databases

    EnsembliENST00000331268; ENSP00000331310; ENSG00000185787. [Q9UBU8-1]
    ENST00000426013; ENSP00000408880; ENSG00000185787. [Q9UBU8-2]
    ENST00000558502; ENSP00000452808; ENSG00000185787. [Q9UBU8-3]
    ENST00000559345; ENSP00000452717; ENSG00000185787. [Q9UBU8-3]
    GeneIDi10933.
    KEGGihsa:10933.
    UCSCiuc002bel.4. human. [Q9UBU8-1]
    uc002bem.4. human. [Q9UBU8-2]

    Polymorphism databases

    DMDMi59803121.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF100615 mRNA. Translation: AAD29872.1 .
    AF167173 mRNA. Translation: AAF80854.1 .
    AF218011 mRNA. Translation: AAG17253.1 . Frameshift.
    AY148481 mRNA. Translation: AAN65338.1 .
    AF070664 mRNA. Translation: AAD20970.1 .
    AF161546 mRNA. Translation: AAF29033.1 .
    AF109188 mRNA. Translation: AAQ13497.1 .
    AK296650 mRNA. Translation: BAG59248.1 .
    AK300789 mRNA. Translation: BAH13347.1 .
    AL137697 mRNA. Translation: CAB70879.2 .
    AC011944 Genomic DNA. No translation available.
    AC022748 Genomic DNA. No translation available.
    AC103975 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99145.1 .
    CH471136 Genomic DNA. Translation: EAW99144.1 .
    CH471136 Genomic DNA. Translation: EAW99146.1 .
    CH471136 Genomic DNA. Translation: EAW99147.1 .
    BC022845 mRNA. Translation: AAH22845.1 .
    BC002936 mRNA. Translation: AAH02936.1 .
    BC067826 mRNA. Translation: AAH67826.1 .
    CX165647 mRNA. No translation available.
    AF131847 mRNA. Translation: AAD20058.1 .
    CCDSi CCDS10307.1. [Q9UBU8-1 ]
    CCDS32304.1. [Q9UBU8-2 ]
    CCDS58393.1. [Q9UBU8-3 ]
    PIRi T46285.
    RefSeqi NP_001252532.1. NM_001265603.1. [Q9UBU8-3 ]
    NP_001252533.1. NM_001265604.1. [Q9UBU8-3 ]
    NP_001252534.1. NM_001265605.1. [Q9UBU8-3 ]
    NP_006782.1. NM_006791.3. [Q9UBU8-2 ]
    NP_996670.1. NM_206839.2. [Q9UBU8-1 ]
    UniGenei Hs.374503.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AQL X-ray 2.30 A/B 190-362 [» ]
    2EFI NMR - A 1-132 [» ]
    2F5J X-ray 2.20 A/B 190-360 [» ]
    2F5K X-ray 2.20 A/B/C/D/E/F 1-129 [» ]
    2LKM NMR - B 194-362 [» ]
    ProteinModelPortali Q9UBU8.
    SMRi Q9UBU8. Positions 1-132, 194-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116134. 58 interactions.
    DIPi DIP-29017N.
    IntActi Q9UBU8. 18 interactions.
    MINTi MINT-1472718.
    STRINGi 9606.ENSP00000331310.

    PTM databases

    PhosphoSitei Q9UBU8.

    Polymorphism databases

    DMDMi 59803121.

    Proteomic databases

    MaxQBi Q9UBU8.
    PaxDbi Q9UBU8.
    PRIDEi Q9UBU8.

    Protocols and materials databases

    DNASUi 10933.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331268 ; ENSP00000331310 ; ENSG00000185787 . [Q9UBU8-1 ]
    ENST00000426013 ; ENSP00000408880 ; ENSG00000185787 . [Q9UBU8-2 ]
    ENST00000558502 ; ENSP00000452808 ; ENSG00000185787 . [Q9UBU8-3 ]
    ENST00000559345 ; ENSP00000452717 ; ENSG00000185787 . [Q9UBU8-3 ]
    GeneIDi 10933.
    KEGGi hsa:10933.
    UCSCi uc002bel.4. human. [Q9UBU8-1 ]
    uc002bem.4. human. [Q9UBU8-2 ]

    Organism-specific databases

    CTDi 10933.
    GeneCardsi GC15P079102.
    HGNCi HGNC:16989. MORF4L1.
    HPAi HPA042360.
    MIMi 607303. gene.
    neXtProti NX_Q9UBU8.
    PharmGKBi PA134895182.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238705.
    HOVERGENi HBG052487.
    InParanoidi Q9UBU8.
    KOi K11339.
    OMAi IVEFILY.
    PhylomeDBi Q9UBU8.
    TreeFami TF323400.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Miscellaneous databases

    EvolutionaryTracei Q9UBU8.
    GeneWikii MORF4L1.
    GenomeRNAii 10933.
    NextBioi 41527.
    PROi Q9UBU8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBU8.
    Bgeei Q9UBU8.
    CleanExi HS_MORF4L1.
    Genevestigatori Q9UBU8.

    Family and domain databases

    InterProi IPR016197. Chromodomain-like.
    IPR017398. EAF3/MRG15.
    IPR008676. MRG.
    IPR026541. MRG_dom.
    IPR025995. Tudor-knot.
    [Graphical view ]
    PANTHERi PTHR10880. PTHR10880. 1 hit.
    Pfami PF05712. MRG. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038133. HAT_Nua4_EAF3/MRG15. 1 hit.
    SUPFAMi SSF54160. SSF54160. 2 hits.
    PROSITEi PS51640. MRG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes."
      Bertram M.J., Berube N.G., Hang-Swanson X., Ran Q., Leung J.K., Bryce S., Spurgers K., Bick R.J., Baldini A., Ning Y., Clark L.J., Parkinson E.K., Barrett J.C., Smith J.R., Pereira-Smith O.M.
      Mol. Cell. Biol. 19:1479-1485(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Two human homologs of the Drosophila dosage compensation gene msl-3 are located on the X chromosome."
      D'Esposito M., Cocchia M., Matarazzo M.R., Macmillan S., Mazzarella R.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Cloning and identification of cellular senescence associated genes from fibroblasts 2BS."
      Guo S., Tong T., Zhang Z.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    5. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Umbilical cord blood.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Aorta.
    7. "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 1 AND 3).
      Tissue: Colon and Embryonic stem cell.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Kidney.
    9. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORMS 2 AND 3).
      Tissue: Embryonic stem cell, Skin and Testis.
    12. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
      Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-29; 42-51; 118-127; 156-173; 179-192; 228-240; 244-261 AND 340-359, IDENTIFICATION IN NUA4 COMPLEX.
    13. Mei G., Yu W., Gibbs R.A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-362 (ISOFORMS 1/2).
      Tissue: Brain.
    14. "MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14."
      Leung J.K., Berube N., Venable S., Ahmed S., Timchenko N., Pereira-Smith O.M.
      J. Biol. Chem. 276:39171-39178(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MRFAP1 AND RB1.
    15. "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation."
      Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.
      J. Biol. Chem. 277:50860-50866(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH RB1 AND MRFAP1, INTERACTION WITH RB1 AND KAT8.
    16. "Role for the mortality factors MORF4, MRGX, and MRG15 in transcriptional repression via associations with Pf1, mSin3A, and transducin-like enhancer of Split."
      Yochum G.S., Ayer D.E.
      Mol. Cell. Biol. 22:7868-7876(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHF12; SIN3A AND TLE FAMILY MEMBERS.
    17. "The highly conserved and multifunctional NuA4 HAT complex."
      Doyon Y., Cote J.
      Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON NUA4 COMPLEX.
    18. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN SIN3A COMPLEX.
    19. "p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage."
      Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M., Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C., Iovanna J.L.
      J. Cell. Physiol. 221:594-602(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MSL1 AND NUPR1.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "MRG15 binds directly to PALB2 and stimulates homology-directed repair of chromosomal breaks."
      Hayakawa T., Zhang F., Hayakawa N., Ohtani Y., Shinmyozu K., Nakayama J., Andreassen P.R.
      J. Cell Sci. 123:1124-1130(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRCA COMPLEX AND PALB2.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14."
      Zhang P., Zhao J., Wang B., Du J., Lu Y., Chen J., Ding J.
      Protein Sci. 15:2423-2434(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 190-362, INTERACTION WITH MRFAP1.
    24. "Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain."
      Bowman B.R., Moure C.M., Kirtane B.M., Welschhans R.L., Tominaga K., Pereira-Smith O.M., Quiocho F.A.
      Structure 14:151-158(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 190-362, MUTAGENESIS OF VAL-208; GLU-234; TYR-251 AND ASN-254.

    Entry informationi

    Entry nameiMO4L1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBU8
    Secondary accession number(s): B4DKN6
    , B7Z6R1, D3DW88, O95899, Q5QTS1, Q6NVX8, Q86YT7, Q9HBP6, Q9NSW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 153 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3