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Q15014

- MO4L2_HUMAN

UniProt

Q15014 - MO4L2_HUMAN

Protein

Mortality factor 4-like protein 2

Gene

MORF4L2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. chromatin organization Source: Reactome
    3. DNA repair Source: UniProtKB-KW
    4. positive regulation of striated muscle cell differentiation Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. regulation of growth Source: UniProtKB-KW
    7. 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_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mortality factor 4-like protein 2
    Alternative name(s):
    MORF-related gene X protein
    Protein MSL3-2
    Transcription factor-like protein MRGX
    Gene namesi
    Name:MORF4L2
    Synonyms:KIAA0026, MRGX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:16849. MORF4L2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1365Missing: Abrogates both transcriptional activation and repression by MORF4L2.
    Mutagenesisi263 – 2631L → A: Abrogates both transcriptional activation and repression by MORF4L2. 1 Publication

    Organism-specific databases

    PharmGKBiPA134925837.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 288288Mortality factor 4-like protein 2PRO_0000088768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei71 – 711Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15014.
    PaxDbiQ15014.
    PRIDEiQ15014.

    PTM databases

    PhosphoSiteiQ15014.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15014.
    BgeeiQ15014.
    CleanExiHS_MORF4L2.
    GenevestigatoriQ15014.

    Organism-specific databases

    HPAiHPA054102.

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDR2Q018506EBI-399257,EBI-1181367

    Protein-protein interaction databases

    BioGridi115001. 53 interactions.
    IntActiQ15014. 15 interactions.
    MINTiMINT-7944329.
    STRINGi9606.ENSP00000341966.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15014.
    SMRiQ15014. Positions 120-288.
    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.
    HOGENOMiHOG000190863.
    HOVERGENiHBG052487.
    InParanoidiQ15014.
    KOiK11342.
    OMAiRGNMQRS.
    OrthoDBiEOG7ZPNK7.
    PhylomeDBiQ15014.
    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.

    Q15014-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSRKQGSQP RGQQSAEEEN FKKPTRSNMQ RSKMRGASSG KKTAGPQQKN    50
    LEPALPGRWG GRSAENPPSG SVRKTRKNKQ KTPGNGDGGS TSEAPQPPRK 100
    KRARADPTVE SEEAFKNRME VKVKIPEELK PWLVEDWDLV TRQKQLFQLP 150
    AKKNVDAILE EYANCKKSQG NVDNKEYAVN EVVAGIKEYF NVMLGTQLLY 200
    KFERPQYAEI LLAHPDAPMS QVYGAPHLLR LFVRIGAMLA YTPLDEKSLA 250
    LLLGYLHDFL KYLAKNSASL FTASDYKVAS AEYHRKAL 288
    Length:288
    Mass (Da):32,308
    Last modified:November 1, 1996 - v1
    Checksum:iC9EFF517C76A565D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF100620 mRNA. Translation: AAD29873.1.
    AF167174 mRNA. Translation: AAF80855.1.
    D14812 mRNA. Translation: BAA03553.1.
    AK056012 mRNA. Translation: BAG51604.1.
    AL049610 Genomic DNA. Translation: CAB55701.1.
    CH471190 Genomic DNA. Translation: EAW54698.1.
    CH471190 Genomic DNA. Translation: EAW54699.1.
    CH471190 Genomic DNA. Translation: EAW54700.1.
    CH471190 Genomic DNA. Translation: EAW54701.1.
    BC056899 mRNA. Translation: AAH56899.1.
    BC093013 mRNA. Translation: AAH93013.1.
    AB050778 mRNA. Translation: BAC22659.1.
    CCDSiCCDS14512.1.
    RefSeqiNP_001135890.1. NM_001142418.1.
    NP_001135891.1. NM_001142419.1.
    NP_001135892.1. NM_001142420.1.
    NP_001135893.1. NM_001142421.1.
    NP_001135894.1. NM_001142422.1.
    NP_001135895.1. NM_001142423.1.
    NP_001135896.1. NM_001142424.1.
    NP_001135897.1. NM_001142425.1.
    NP_001135898.1. NM_001142426.1.
    NP_001135899.1. NM_001142427.1.
    NP_001135900.1. NM_001142428.1.
    NP_001135901.1. NM_001142429.1.
    NP_001135902.1. NM_001142430.1.
    NP_001135903.1. NM_001142431.1.
    NP_001135904.1. NM_001142432.1.
    NP_036418.1. NM_012286.2.
    UniGeneiHs.326387.

    Genome annotation databases

    EnsembliENST00000360458; ENSP00000353643; ENSG00000123562.
    ENST00000422154; ENSP00000394417; ENSG00000123562.
    ENST00000423833; ENSP00000416120; ENSG00000123562.
    ENST00000433176; ENSP00000415476; ENSG00000123562.
    ENST00000441076; ENSP00000391969; ENSG00000123562.
    ENST00000451301; ENSP00000410532; ENSG00000123562.
    GeneIDi9643.
    KEGGihsa:9643.
    UCSCiuc004ekw.3. human.

    Polymorphism databases

    DMDMi3123049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF100620 mRNA. Translation: AAD29873.1 .
    AF167174 mRNA. Translation: AAF80855.1 .
    D14812 mRNA. Translation: BAA03553.1 .
    AK056012 mRNA. Translation: BAG51604.1 .
    AL049610 Genomic DNA. Translation: CAB55701.1 .
    CH471190 Genomic DNA. Translation: EAW54698.1 .
    CH471190 Genomic DNA. Translation: EAW54699.1 .
    CH471190 Genomic DNA. Translation: EAW54700.1 .
    CH471190 Genomic DNA. Translation: EAW54701.1 .
    BC056899 mRNA. Translation: AAH56899.1 .
    BC093013 mRNA. Translation: AAH93013.1 .
    AB050778 mRNA. Translation: BAC22659.1 .
    CCDSi CCDS14512.1.
    RefSeqi NP_001135890.1. NM_001142418.1.
    NP_001135891.1. NM_001142419.1.
    NP_001135892.1. NM_001142420.1.
    NP_001135893.1. NM_001142421.1.
    NP_001135894.1. NM_001142422.1.
    NP_001135895.1. NM_001142423.1.
    NP_001135896.1. NM_001142424.1.
    NP_001135897.1. NM_001142425.1.
    NP_001135898.1. NM_001142426.1.
    NP_001135899.1. NM_001142427.1.
    NP_001135900.1. NM_001142428.1.
    NP_001135901.1. NM_001142429.1.
    NP_001135902.1. NM_001142430.1.
    NP_001135903.1. NM_001142431.1.
    NP_001135904.1. NM_001142432.1.
    NP_036418.1. NM_012286.2.
    UniGenei Hs.326387.

    3D structure databases

    ProteinModelPortali Q15014.
    SMRi Q15014. Positions 120-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115001. 53 interactions.
    IntActi Q15014. 15 interactions.
    MINTi MINT-7944329.
    STRINGi 9606.ENSP00000341966.

    PTM databases

    PhosphoSitei Q15014.

    Polymorphism databases

    DMDMi 3123049.

    Proteomic databases

    MaxQBi Q15014.
    PaxDbi Q15014.
    PRIDEi Q15014.

    Protocols and materials databases

    DNASUi 9643.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360458 ; ENSP00000353643 ; ENSG00000123562 .
    ENST00000422154 ; ENSP00000394417 ; ENSG00000123562 .
    ENST00000423833 ; ENSP00000416120 ; ENSG00000123562 .
    ENST00000433176 ; ENSP00000415476 ; ENSG00000123562 .
    ENST00000441076 ; ENSP00000391969 ; ENSG00000123562 .
    ENST00000451301 ; ENSP00000410532 ; ENSG00000123562 .
    GeneIDi 9643.
    KEGGi hsa:9643.
    UCSCi uc004ekw.3. human.

    Organism-specific databases

    CTDi 9643.
    GeneCardsi GC0XM102930.
    HGNCi HGNC:16849. MORF4L2.
    HPAi HPA054102.
    MIMi 300409. gene.
    neXtProti NX_Q15014.
    PharmGKBi PA134925837.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317973.
    HOGENOMi HOG000190863.
    HOVERGENi HBG052487.
    InParanoidi Q15014.
    KOi K11342.
    OMAi RGNMQRS.
    OrthoDBi EOG7ZPNK7.
    PhylomeDBi Q15014.
    TreeFami TF323400.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii MORF4L2.
    GenomeRNAii 9643.
    NextBioi 36195.
    PROi Q15014.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15014.
    Bgeei Q15014.
    CleanExi HS_MORF4L2.
    Genevestigatori Q15014.

    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. "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].
    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].
    3. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    4. "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].
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Pancreas and Placenta.
    8. "Mortality factor related gene X 102 5'."
      Myokai F., Oyama M.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-16.
    9. "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 12-22; 82-99; 105-116; 154-166; 176-187; 188-201; 235-247 AND 266-277, IDENTIFICATION IN NUA4 COMPLEX.
    10. "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 SIN3A AND TLE FAMILY MEMBERS.
    11. "MRGX is a novel transcriptional regulator that exhibits activation or repression of the B-myb promoter in a cell type-dependent manner."
      Tominaga K., Leung J.K., Rookard P., Echigo J., Smith J.R., Pereira-Smith O.M.
      J. Biol. Chem. 278:49618-49624(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MRFAP1 AND RB1, MUTAGENESIS OF 132-TRP--ASP-136 AND LEU-263.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMO4L2_HUMAN
    AccessioniPrimary (citable) accession number: Q15014
    Secondary accession number(s): B3KP92
    , D3DXA5, Q567V0, Q8J026
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3