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Q68DK7

- MSL1_HUMAN

UniProt

Q68DK7 - MSL1_HUMAN

Protein

Male-specific lethal 1 homolog

Gene

MSL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
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    Functioni

    Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.3 Publications

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H4-K16 acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Male-specific lethal 1 homolog
    Short name:
    MSL-1
    Alternative name(s):
    Male-specific lethal 1-like 1
    Short name:
    MSL1-like 1
    Male-specific lethal-1 homolog 1
    Gene namesi
    Name:MSL1
    Synonyms:MSL1L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:27905. MSL1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. MSL complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164723127.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 614614Male-specific lethal 1 homologPRO_0000349236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261Phosphoserine1 Publication
    Modified residuei205 – 2051Phosphoserine3 Publications
    Modified residuei353 – 3531N6-acetyllysine1 Publication

    Post-translational modificationi

    Sumoylated with SUMO1.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ68DK7.
    PaxDbiQ68DK7.
    PRIDEiQ68DK7.

    PTM databases

    PhosphoSiteiQ68DK7.

    Expressioni

    Inductioni

    Up-regulated by gamma-irradiation.1 Publication

    Gene expression databases

    ArrayExpressiQ68DK7.
    BgeeiQ68DK7.
    CleanExiHS_MSL1.
    GenevestigatoriQ68DK7.

    Organism-specific databases

    HPAiHPA022800.
    HPA023567.

    Interactioni

    Subunit structurei

    Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and MSL3. Forms a MSL heterotetrameric core with MSL2. Interacts with KAT8 and MSL3; both interactions are direct. Directly interacts with NUPR1. Interacts with TP53BP1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity.5 Publications

    Protein-protein interaction databases

    BioGridi130859. 16 interactions.
    IntActiQ68DK7. 4 interactions.
    STRINGi9606.ENSP00000341409.

    Structurei

    Secondary structure

    1
    614
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi215 – 25036
    Beta strandi478 – 4803
    Helixi500 – 51819

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B7YX-ray3.25A/B212-252[»]
    4B86X-ray3.50A/B/E/F/I/J212-267[»]
    4DNCX-ray2.05D/E473-520[»]
    ProteinModelPortaliQ68DK7.
    SMRiQ68DK7. Positions 214-264, 493-534, 549-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni223 – 23715Interaction with MSL2Add
    BLAST
    Regioni498 – 51821Interaction with KAT8Add
    BLAST
    Regioni550 – 59142Sufficient for interaction with MSL3 MRG domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili213 – 282701 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 156Poly-Ala
    Compositional biasi55 – 185131Pro-richAdd
    BLAST
    Compositional biasi208 – 2147Poly-Gly

    Domaini

    The coiled coil is formed by helices from two subunits in the MSL1 homodimer.

    Sequence similaritiesi

    Belongs to the msl-1 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG48092.
    HOGENOMiHOG000113663.
    HOVERGENiHBG060802.
    InParanoidiQ68DK7.
    KOiK13163.
    OMAiHKRKTPF.
    OrthoDBiEOG72VH59.
    PhylomeDBiQ68DK7.
    TreeFamiTF330735.

    Family and domain databases

    InterProiIPR026711. Msl-1.
    IPR029332. PEHE_dom.
    [Graphical view]
    PANTHERiPTHR21656. PTHR21656. 1 hit.
    PfamiPF15275. PEHE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q68DK7-1) [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

    MTMRSAVFKA AAAPAGGNPE QRLDYERAAA LGGPEDEPGA AEAHFLPRHR    50
    KLKEPGPPLA SSQGGSPAPS PAGCGGKGRG LLLPAGAAPG QQEESWGGSV 100
    PLPCPPPATK QAGIGGEPAA AGAGCSPRPK YQAVLPIQTG SLVAAAKEPT 150
    PWAGDKGGAA SPAATASDPA GPPPLPLPGP PPLAPTATAG TLAASEGRWK 200
    SMRKSPLGGG GGSGASSQAA CLKQILLLQL DLIEQQQQQL QAKEKEIEEL 250
    KSERDTLLAR IERMERRMQL VKKDNEKERH KLFQGYETEE REETELSEKI 300
    KLECQPELSE TSQTLPPKPF SCGRSGKGHK RKSPFGSTER KTPVKKLAPE 350
    FSKVKTKTPK HSPIKEEPCG SLSETVCKRE LRSQETPEKP RSSVDTPPRL 400
    STPQKGPSTH PKEKAFSSEI EDLPYLSTTE MYLCRWHQPP PSPLPLRESS 450
    PKKEETVARC LMPSSVAGET SVLAVPSWRD HSVEPLRDPN PSDLLENLDD 500
    SVFSKRHAKL ELDEKRRKRW DIQRIREQRI LQRLQLRMYK KKGIQESEPE 550
    VTSFFPEPDD VESLMITPFL PVVAFGRPLP KLTPQNFELP WLDERSRCRL 600
    EIQKKQTPHR TCRK 614

    Note: Gene prediction based on EST data. No experimental confirmation available.

    Length:614
    Mass (Da):67,128
    Last modified:February 8, 2011 - v3
    Checksum:iD48D845C1C2ABF45
    GO
    Isoform 2 (identifier: Q68DK7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-201: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:413
    Mass (Da):47,593
    Checksum:i846A85F75A0B626F
    GO
    Isoform 3 (identifier: Q68DK7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-263: Missing.

    Show »
    Length:351
    Mass (Da):40,778
    Checksum:i4D18D5EC95550885
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti427 – 4271S → P in CAH18213. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 263263Missing in isoform 3. 1 PublicationVSP_035236Add
    BLAST
    Alternative sequencei1 – 201201Missing in isoform 2. 1 PublicationVSP_035237Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL049450 mRNA. Translation: CAH10734.1.
    CR749360 mRNA. Translation: CAH18213.1.
    AC068669 Genomic DNA. No translation available.
    BC118997 mRNA. Translation: AAI18998.1.
    BC122543 mRNA. Translation: AAI22544.1.
    CCDSiCCDS45670.1. [Q68DK7-3]
    RefSeqiNP_001012241.1. NM_001012241.1. [Q68DK7-3]
    XP_005257355.1. XM_005257298.2. [Q68DK7-1]
    UniGeneiHs.532786.

    Genome annotation databases

    EnsembliENST00000398532; ENSP00000381543; ENSG00000188895. [Q68DK7-1]
    ENST00000579565; ENSP00000462945; ENSG00000188895. [Q68DK7-3]
    GeneIDi339287.
    KEGGihsa:339287.
    UCSCiuc002hua.4. human. [Q68DK7-1]
    uc002huc.2. human. [Q68DK7-3]

    Polymorphism databases

    DMDMi322510113.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL049450 mRNA. Translation: CAH10734.1 .
    CR749360 mRNA. Translation: CAH18213.1 .
    AC068669 Genomic DNA. No translation available.
    BC118997 mRNA. Translation: AAI18998.1 .
    BC122543 mRNA. Translation: AAI22544.1 .
    CCDSi CCDS45670.1. [Q68DK7-3 ]
    RefSeqi NP_001012241.1. NM_001012241.1. [Q68DK7-3 ]
    XP_005257355.1. XM_005257298.2. [Q68DK7-1 ]
    UniGenei Hs.532786.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B7Y X-ray 3.25 A/B 212-252 [» ]
    4B86 X-ray 3.50 A/B/E/F/I/J 212-267 [» ]
    4DNC X-ray 2.05 D/E 473-520 [» ]
    ProteinModelPortali Q68DK7.
    SMRi Q68DK7. Positions 214-264, 493-534, 549-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130859. 16 interactions.
    IntActi Q68DK7. 4 interactions.
    STRINGi 9606.ENSP00000341409.

    PTM databases

    PhosphoSitei Q68DK7.

    Polymorphism databases

    DMDMi 322510113.

    Proteomic databases

    MaxQBi Q68DK7.
    PaxDbi Q68DK7.
    PRIDEi Q68DK7.

    Protocols and materials databases

    DNASUi 339287.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398532 ; ENSP00000381543 ; ENSG00000188895 . [Q68DK7-1 ]
    ENST00000579565 ; ENSP00000462945 ; ENSG00000188895 . [Q68DK7-3 ]
    GeneIDi 339287.
    KEGGi hsa:339287.
    UCSCi uc002hua.4. human. [Q68DK7-1 ]
    uc002huc.2. human. [Q68DK7-3 ]

    Organism-specific databases

    CTDi 339287.
    GeneCardsi GC17P038278.
    HGNCi HGNC:27905. MSL1.
    HPAi HPA022800.
    HPA023567.
    MIMi 614801. gene.
    neXtProti NX_Q68DK7.
    PharmGKBi PA164723127.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG48092.
    HOGENOMi HOG000113663.
    HOVERGENi HBG060802.
    InParanoidi Q68DK7.
    KOi K13163.
    OMAi HKRKTPF.
    OrthoDBi EOG72VH59.
    PhylomeDBi Q68DK7.
    TreeFami TF330735.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi MSL1. human.
    GenomeRNAii 339287.
    NextBioi 97320.
    PROi Q68DK7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q68DK7.
    Bgeei Q68DK7.
    CleanExi HS_MSL1.
    Genevestigatori Q68DK7.

    Family and domain databases

    InterProi IPR026711. Msl-1.
    IPR029332. PEHE_dom.
    [Graphical view ]
    PANTHERi PTHR21656. PTHR21656. 1 hit.
    Pfami PF15275. PEHE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Rectum tumor and Uterus.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Rectum tumor.
    3. "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] (ISOFORM 3).
    4. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
      Gocke C.B., Yu H., Kang J.
      J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION WITH SUMO1, SUBCELLULAR LOCATION.
    5. "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16."
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 25:9175-9188(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH MSL2, FUNCTION.
    6. Erratum
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 26:387-387(2006)
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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 NUPR1 AND TP53BP1, INDUCTION BY GAMMA-IRRADIATION.
    9. "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-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation."
      Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.
      Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN H2B UBIQUITINATION.
    12. "Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
      Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
      Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAT8 AND MSL3.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex."
      Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
      Cell Res. 22:1078-1081(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 473-520 IN COMPLEX WITH KAT8, FUNCTION IN MSL COMPLEX, INTERACTION WITH KAT8 AND MSL3.
    15. "Msl1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila."
      Hallacli E., Lipp M., Georgiev P., Spielman C., Cusack S., Akhtar A., Kadlec J.
      Mol. Cell 48:587-600(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 212-267 IN COMPLEX WITH MSL2, COILED COIL, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH MSL2.

    Entry informationi

    Entry nameiMSL1_HUMAN
    AccessioniPrimary (citable) accession number: Q68DK7
    Secondary accession number(s): Q0VF46, Q69Z03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 75 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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