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Q8N5Y2

- MS3L1_HUMAN

UniProt

Q8N5Y2 - MS3L1_HUMAN

Protein

Male-specific lethal 3 homolog

Gene

MSL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.6 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. methylated histone binding Source: UniProtKB
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H4-K16 acetylation Source: UniProtKB
    3. multicellular organismal development Source: ProtInc
    4. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Male-specific lethal 3 homolog
    Alternative name(s):
    Male-specific lethal-3 homolog 1
    Male-specific lethal-3 protein-like 1
    Short name:
    MSL3-like 1
    Gene namesi
    Name:MSL3
    Synonyms:MSL3L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:7370. MSL3.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311Y → A: Diminishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1). 1 Publication
    Mutagenesisi55 – 551H → A: Diminishes DNA-binding; when associated with A-65. 1 Publication
    Mutagenesisi56 – 561F → A: Abolishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1).
    Mutagenesisi59 – 591W → G: Diminishes DNA-binding. 1 Publication
    Mutagenesisi65 – 651R → A: Diminishes DNA-binding; when associated with A-55. 1 Publication

    Organism-specific databases

    PharmGKBiPA164723161.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 521521Male-specific lethal 3 homologPRO_0000080247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei311 – 3111Phosphoserine1 Publication
    Modified residuei367 – 3671Phosphoserine2 Publications
    Modified residuei400 – 4001Phosphoserine1 Publication
    Modified residuei405 – 4051Phosphothreonine1 Publication
    Modified residuei407 – 4071Phosphoserine2 Publications
    Modified residuei411 – 4111Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8N5Y2.
    PaxDbiQ8N5Y2.
    PRIDEiQ8N5Y2.

    PTM databases

    PhosphoSiteiQ8N5Y2.

    Expressioni

    Tissue specificityi

    Expressed in many tissues including liver, pancreas, heart, lung, kidney, skeletal muscle, brain, and placenta, with highest expression in skeletal muscle and heart.

    Gene expression databases

    ArrayExpressiQ8N5Y2.
    BgeeiQ8N5Y2.
    CleanExiHS_MSL3.
    GenevestigatoriQ8N5Y2.

    Organism-specific databases

    HPAiHPA034535.
    HPA034536.

    Interactioni

    Subunit structurei

    Component the MSL histone acetyltransferase complex at least composed of the MOF/KAT8, MSL1/hampin, MSL2 and MSL3. Interacts (via the MRG domain) with MSL1.4 Publications

    Protein-protein interaction databases

    BioGridi116143. 15 interactions.
    DIPiDIP-56857N.
    IntActiQ8N5Y2. 5 interactions.
    STRINGi9606.ENSP00000312244.

    Structurei

    Secondary structure

    1
    521
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 205
    Beta strandi30 – 4213
    Beta strandi48 – 569
    Helixi61 – 633
    Beta strandi65 – 684
    Helixi69 – 713
    Beta strandi72 – 743
    Helixi77 – 9115
    Helixi178 – 19215
    Helixi206 – 22217
    Helixi251 – 27222
    Helixi276 – 2783
    Helixi279 – 2879
    Helixi447 – 4493
    Helixi453 – 46917
    Helixi474 – 49320
    Helixi495 – 4984
    Helixi501 – 5033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y0NX-ray3.00A/B/C/D167-289[»]
    A/B/C/D442-518[»]
    3OA6X-ray2.35A/B1-101[»]
    3OB9X-ray2.50A/B/C/D/E2-93[»]
    ProteinModelPortaliQ8N5Y2.
    SMRiQ8N5Y2. Positions 9-92, 171-293, 442-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N5Y2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 9059ChromoAdd
    BLAST
    Domaini168 – 517350MRGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 440151Required for the histone acetyltransferase activity of the MSL complexAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chromo domain.Curated
    Contains 1 MRG domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG293760.
    HOGENOMiHOG000293161.
    HOVERGENiHBG052511.
    InParanoidiQ8N5Y2.
    OMAiGMKFKFH.
    OrthoDBiEOG7BCNBQ.
    PhylomeDBiQ8N5Y2.
    TreeFamiTF323400.

    Family and domain databases

    InterProiIPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    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]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 2 hits.
    PROSITEiPS51640. MRG. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N5Y2-1) [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

    MSASEGMKFK FHSGEKVLCF EPDPTKARVL YDAKIVDVIV GKDEKGRKIP    50
    EYLIHFNGWN RSWDRWAAED HVLRDTDENR RLQRKLARKA VARLRSTGRK 100
    KKRCRLPGVD SVLKGLPTEE KDENDENSLS SSSDCSENKD EEISEESDIE 150
    EKTEVKEEPE LQTRREMEER TITIEIPEVL KKQLEDDCYY INRRKRLVKL 200
    PCQTNIITIL ESYVKHFAIN AAFSANERPR HHHVMPHANM NVHYIPAEKN 250
    VDLCKEMVDG LRITFDYTLP LVLLYPYEQA QYKKVTSSKF FLPIKESATS 300
    TNRSQEELSP SPPLLNPSTP QSTESQPTTG EPATPKRRKA EPEALQSLRR 350
    STRHSANCDR LSESSASPQP KRRQQDTSAS MPKLFLHLEK KTPVHSRSSS 400
    PIPLTPSKEG SAVFAGFEGR RTNEINEVLS WKLVPDNYPP GDQPPPPSYI 450
    YGAQHLLRLF VKLPEILGKM SFSEKNLKAL LKHFDLFLRF LAEYHDDFFP 500
    ESAYVAACEA HYSTKNPRAI Y 521
    Length:521
    Mass (Da):59,824
    Last modified:October 1, 2002 - v1
    Checksum:i6DFFB9E183D0CFB9
    GO
    Isoform 2 (identifier: Q8N5Y2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.
         60-61: NR → MP

    Show »
    Length:462
    Mass (Da):53,043
    Checksum:i88D09081DA2C7F1A
    GO
    Isoform 3 (identifier: Q8N5Y2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAK → MSPSVRPGAGWAPVGRPGRPIQ

    Note: No experimental confirmation available.

    Show »
    Length:509
    Mass (Da):58,249
    Checksum:i50F8B10061D5E89E
    GO
    Isoform 4 (identifier: Q8N5Y2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-166: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:355
    Mass (Da):40,577
    Checksum:i86211AD697FA2C88
    GO
    Isoform 5 (identifier: Q8N5Y2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         391-416: KTPVHSRSSSPIPLTPSKEGSAVFAG → SRFILGCPRPGRASVYFVFSQCQAWC
         417-521: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:416
    Mass (Da):47,950
    Checksum:i97B2DC9F80BE09BE
    GO
    Isoform 6 (identifier: Q8N5Y2-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MSASEG → MKMMKT
         7-155: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:372
    Mass (Da):42,725
    Checksum:iFD52D6BBAFA528D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371D → V in AAD38499. (PubMed:10395802)Curated
    Sequence conflicti346 – 3461Q → R in AK025642. (PubMed:14702039)Curated
    Sequence conflicti391 – 3911K → E in AK025642. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21S → T.1 Publication
    Corresponds to variant rs150938844 [ dbSNP | Ensembl ].
    VAR_069061
    Natural varianti199 – 1991K → Q.
    Corresponds to variant rs1051595 [ dbSNP | Ensembl ].
    VAR_048732
    Natural varianti251 – 2511V → I.
    Corresponds to variant rs1051600 [ dbSNP | Ensembl ].
    VAR_048733

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 166166Missing in isoform 4. 1 PublicationVSP_045652Add
    BLAST
    Alternative sequencei1 – 5959Missing in isoform 2. 1 PublicationVSP_007636Add
    BLAST
    Alternative sequencei1 – 3434MSASE…LYDAK → MSPSVRPGAGWAPVGRPGRP IQ in isoform 3. 1 PublicationVSP_043342Add
    BLAST
    Alternative sequencei1 – 66MSASEG → MKMMKT in isoform 6. 1 PublicationVSP_055376
    Alternative sequencei7 – 155149Missing in isoform 6. 1 PublicationVSP_055377Add
    BLAST
    Alternative sequencei60 – 612NR → MP in isoform 2. 1 PublicationVSP_007637
    Alternative sequencei391 – 41626KTPVH…AVFAG → SRFILGCPRPGRASVYFVFS QCQAWC in isoform 5. 1 PublicationVSP_045653Add
    BLAST
    Alternative sequencei417 – 521105Missing in isoform 5. 1 PublicationVSP_045654Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117065 mRNA. Translation: AAD38499.1.
    AK025642 mRNA. No translation available.
    AK289780 mRNA. Translation: BAF82469.1.
    AK294255 mRNA. Translation: BAH11713.1.
    AK300814 mRNA. Translation: BAG62470.1.
    AC004554 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98799.1.
    CH471074 Genomic DNA. Translation: EAW98801.1.
    BC031210 mRNA. Translation: AAH31210.1.
    AL050178 mRNA. Translation: CAB43308.1.
    AL713667 mRNA. Translation: CAD28473.1.
    CCDSiCCDS14147.1. [Q8N5Y2-1]
    CCDS14148.1. [Q8N5Y2-5]
    CCDS14149.1. [Q8N5Y2-4]
    CCDS55369.1. [Q8N5Y2-3]
    CCDS65213.1. [Q8N5Y2-6]
    PIRiT08795.
    RefSeqiNP_001180199.1. NM_001193270.2. [Q8N5Y2-3]
    NP_001269103.1. NM_001282174.1.
    NP_006791.2. NM_006800.3. [Q8N5Y2-4]
    NP_523352.1. NM_078628.1. [Q8N5Y2-5]
    NP_523353.2. NM_078629.3. [Q8N5Y2-1]
    XP_005274497.1. XM_005274440.2. [Q8N5Y2-4]
    XP_006724524.1. XM_006724461.1.
    UniGeneiHs.655288.

    Genome annotation databases

    EnsembliENST00000312196; ENSP00000312244; ENSG00000005302. [Q8N5Y2-1]
    ENST00000337339; ENSP00000338078; ENSG00000005302. [Q8N5Y2-5]
    ENST00000361672; ENSP00000354562; ENSG00000005302. [Q8N5Y2-6]
    ENST00000380693; ENSP00000370069; ENSG00000005302. [Q8N5Y2-4]
    ENST00000398527; ENSP00000381538; ENSG00000005302. [Q8N5Y2-3]
    GeneIDi10943.
    KEGGihsa:10943.
    UCSCiuc004cuv.1. human.
    uc004cuw.3. human. [Q8N5Y2-1]
    uc011mih.2. human. [Q8N5Y2-3]

    Polymorphism databases

    DMDMi32171482.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117065 mRNA. Translation: AAD38499.1 .
    AK025642 mRNA. No translation available.
    AK289780 mRNA. Translation: BAF82469.1 .
    AK294255 mRNA. Translation: BAH11713.1 .
    AK300814 mRNA. Translation: BAG62470.1 .
    AC004554 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98799.1 .
    CH471074 Genomic DNA. Translation: EAW98801.1 .
    BC031210 mRNA. Translation: AAH31210.1 .
    AL050178 mRNA. Translation: CAB43308.1 .
    AL713667 mRNA. Translation: CAD28473.1 .
    CCDSi CCDS14147.1. [Q8N5Y2-1 ]
    CCDS14148.1. [Q8N5Y2-5 ]
    CCDS14149.1. [Q8N5Y2-4 ]
    CCDS55369.1. [Q8N5Y2-3 ]
    CCDS65213.1. [Q8N5Y2-6 ]
    PIRi T08795.
    RefSeqi NP_001180199.1. NM_001193270.2. [Q8N5Y2-3 ]
    NP_001269103.1. NM_001282174.1.
    NP_006791.2. NM_006800.3. [Q8N5Y2-4 ]
    NP_523352.1. NM_078628.1. [Q8N5Y2-5 ]
    NP_523353.2. NM_078629.3. [Q8N5Y2-1 ]
    XP_005274497.1. XM_005274440.2. [Q8N5Y2-4 ]
    XP_006724524.1. XM_006724461.1.
    UniGenei Hs.655288.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y0N X-ray 3.00 A/B/C/D 167-289 [» ]
    A/B/C/D 442-518 [» ]
    3OA6 X-ray 2.35 A/B 1-101 [» ]
    3OB9 X-ray 2.50 A/B/C/D/E 2-93 [» ]
    ProteinModelPortali Q8N5Y2.
    SMRi Q8N5Y2. Positions 9-92, 171-293, 442-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116143. 15 interactions.
    DIPi DIP-56857N.
    IntActi Q8N5Y2. 5 interactions.
    STRINGi 9606.ENSP00000312244.

    PTM databases

    PhosphoSitei Q8N5Y2.

    Polymorphism databases

    DMDMi 32171482.

    Proteomic databases

    MaxQBi Q8N5Y2.
    PaxDbi Q8N5Y2.
    PRIDEi Q8N5Y2.

    Protocols and materials databases

    DNASUi 10943.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312196 ; ENSP00000312244 ; ENSG00000005302 . [Q8N5Y2-1 ]
    ENST00000337339 ; ENSP00000338078 ; ENSG00000005302 . [Q8N5Y2-5 ]
    ENST00000361672 ; ENSP00000354562 ; ENSG00000005302 . [Q8N5Y2-6 ]
    ENST00000380693 ; ENSP00000370069 ; ENSG00000005302 . [Q8N5Y2-4 ]
    ENST00000398527 ; ENSP00000381538 ; ENSG00000005302 . [Q8N5Y2-3 ]
    GeneIDi 10943.
    KEGGi hsa:10943.
    UCSCi uc004cuv.1. human.
    uc004cuw.3. human. [Q8N5Y2-1 ]
    uc011mih.2. human. [Q8N5Y2-3 ]

    Organism-specific databases

    CTDi 10943.
    GeneCardsi GC0XP011776.
    HGNCi HGNC:7370. MSL3.
    HPAi HPA034535.
    HPA034536.
    MIMi 300609. gene.
    neXtProti NX_Q8N5Y2.
    PharmGKBi PA164723161.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293760.
    HOGENOMi HOG000293161.
    HOVERGENi HBG052511.
    InParanoidi Q8N5Y2.
    OMAi GMKFKFH.
    OrthoDBi EOG7BCNBQ.
    PhylomeDBi Q8N5Y2.
    TreeFami TF323400.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi MSL3. human.
    EvolutionaryTracei Q8N5Y2.
    GenomeRNAii 10943.
    NextBioi 35463804.
    PROi Q8N5Y2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N5Y2.
    Bgeei Q8N5Y2.
    CleanExi HS_MSL3.
    Genevestigatori Q8N5Y2.

    Family and domain databases

    InterProi IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    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 ]
    SMARTi SM00298. CHROMO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 2 hits.
    PROSITEi PS51640. MRG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a novel chromo domain gene in Xp22.3 with homology to Drosophila msl-3."
      Prakash S.K., Van den Veyver I.B., Franco B., Volta M., Ballabio A., Zoghbi H.Y.
      Genomics 59:77-84(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "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 3; 4; 5 AND 6), VARIANT THR-2.
      Tissue: Amygdala, Brain and Hepatoma.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-521.
      Tissue: Uterus.
    7. "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: IDENTIFICATION OF MSL COMPLEX COMPONENTS, FUNCTION OF THE MSL COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. Erratum
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 26:387-387(2006)
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-407 AND SER-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; THR-405 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
      Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MSL COMPLEX, FUNCTION OF THE MSL COMPLEX.
    12. "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-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-400, 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: FUNCTION IN MSL COMPLEX, INTERACTION WITH MSL1.
    15. "Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain."
      Kim D., Blus B.J., Chandra V., Huang P., Rastinejad F., Khorasanizadeh S.
      Nat. Struct. Mol. Biol. 17:1027-1029(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-101 IN COMPLEX WITH DNA AND HISTONE H4, MUTAGENESIS OF HIS-55; TRP-59 AND ARG-65, FUNCTION.
    16. "Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4."
      Moore S.A., Ferhatoglu Y., Jia Y., Al-Jiab R.A., Scott M.J.
      J. Biol. Chem. 285:40879-40890(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-93, MUTAGENESIS OF TYR-31, FUNCTION.
    17. "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: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 167-517 IN COMPLEX WITH MSL1, FUNCTION IN MSL COMPLEX, INTERACTION WITH MSL1.

    Entry informationi

    Entry nameiMS3L1_HUMAN
    AccessioniPrimary (citable) accession number: Q8N5Y2
    Secondary accession number(s): A6NCU2
    , A6NHW8, A8K165, B4DUV8, B7Z227, Q9UG70, Q9Y5Z8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 123 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

    Miscellaneous

    MSL3L1 gene undergoes X inactivation.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3