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Q68DK7 (MSL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MSL1
Synonyms:MSL1L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.11 Ref.14

Subunit structure

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. Ref.5 Ref.8 Ref.12 Ref.14 Ref.15

Subcellular location

Nucleus Ref.4.

Induction

Up-regulated by gamma-irradiation. Ref.8

Domain

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

Post-translational modification

Sumoylated with SUMO1. Ref.4

Sequence similarities

Belongs to the msl-1 family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H4-K16 acetylation

Inferred from direct assay PubMed 20018852. Source: UniProtKB

   Cellular_componentMSL complex

Inferred from direct assay PubMed 20018852. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q68DK7-1)

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.
Note: Gene prediction based on EST data. No experimental confirmation available.
Isoform 2 (identifier: Q68DK7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-201: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q68DK7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 614614Male-specific lethal 1 homolog
PRO_0000349236

Regions

Region223 – 23715Interaction with MSL2
Region498 – 51821Interaction with KAT8
Region550 – 59142Sufficient for interaction with MSL3 MRG domain
Coiled coil213 – 28270 Ref.15
Compositional bias10 – 156Poly-Ala
Compositional bias55 – 185131Pro-rich
Compositional bias208 – 2147Poly-Gly

Amino acid modifications

Modified residue1261Phosphoserine Ref.13
Modified residue2051Phosphoserine Ref.7 Ref.10 Ref.13
Modified residue3531N6-acetyllysine Ref.9

Natural variations

Alternative sequence1 – 263263Missing in isoform 3.
VSP_035236
Alternative sequence1 – 201201Missing in isoform 2.
VSP_035237

Experimental info

Sequence conflict4271S → P in CAH18213. Ref.1

Secondary structure

....... 614
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 8, 2011. Version 3.
Checksum: D48D845C1C2ABF45

FASTA61467,128
        10         20         30         40         50         60 
MTMRSAVFKA AAAPAGGNPE QRLDYERAAA LGGPEDEPGA AEAHFLPRHR KLKEPGPPLA 

        70         80         90        100        110        120 
SSQGGSPAPS PAGCGGKGRG LLLPAGAAPG QQEESWGGSV PLPCPPPATK QAGIGGEPAA 

       130        140        150        160        170        180 
AGAGCSPRPK YQAVLPIQTG SLVAAAKEPT PWAGDKGGAA SPAATASDPA GPPPLPLPGP 

       190        200        210        220        230        240 
PPLAPTATAG TLAASEGRWK SMRKSPLGGG GGSGASSQAA CLKQILLLQL DLIEQQQQQL 

       250        260        270        280        290        300 
QAKEKEIEEL KSERDTLLAR IERMERRMQL VKKDNEKERH KLFQGYETEE REETELSEKI 

       310        320        330        340        350        360 
KLECQPELSE TSQTLPPKPF SCGRSGKGHK RKSPFGSTER KTPVKKLAPE FSKVKTKTPK 

       370        380        390        400        410        420 
HSPIKEEPCG SLSETVCKRE LRSQETPEKP RSSVDTPPRL STPQKGPSTH PKEKAFSSEI 

       430        440        450        460        470        480 
EDLPYLSTTE MYLCRWHQPP PSPLPLRESS PKKEETVARC LMPSSVAGET SVLAVPSWRD 

       490        500        510        520        530        540 
HSVEPLRDPN PSDLLENLDD SVFSKRHAKL ELDEKRRKRW DIQRIREQRI LQRLQLRMYK 

       550        560        570        580        590        600 
KKGIQESEPE VTSFFPEPDD VESLMITPFL PVVAFGRPLP KLTPQNFELP WLDERSRCRL 

       610 
EIQKKQTPHR TCRK 

« Hide

Isoform 2 [UniParc].

Checksum: 846A85F75A0B626F
Show »

FASTA41347,593
Isoform 3 [UniParc].

Checksum: 4D18D5EC95550885
Show »

FASTA35140,778

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45670.1. [Q68DK7-3]
RefSeqNP_001012241.1. NM_001012241.1. [Q68DK7-3]
XP_005257355.1. XM_005257298.2. [Q68DK7-1]
UniGeneHs.532786.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B7YX-ray3.25A/B212-252[»]
4B86X-ray3.50A/B/E/F/I/J212-267[»]
4DNCX-ray2.05D/E473-520[»]
ProteinModelPortalQ68DK7.
SMRQ68DK7. Positions 214-264, 493-534, 549-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130859. 9 interactions.
IntActQ68DK7. 4 interactions.
STRING9606.ENSP00000341409.

PTM databases

PhosphoSiteQ68DK7.

Polymorphism databases

DMDM322510113.

Proteomic databases

MaxQBQ68DK7.
PaxDbQ68DK7.
PRIDEQ68DK7.

Protocols and materials databases

DNASU339287.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398532; ENSP00000381543; ENSG00000188895. [Q68DK7-1]
ENST00000579565; ENSP00000462945; ENSG00000188895. [Q68DK7-3]
GeneID339287.
KEGGhsa:339287.
UCSCuc002hua.4. human. [Q68DK7-1]
uc002huc.2. human. [Q68DK7-3]

Organism-specific databases

CTD339287.
GeneCardsGC17P038278.
HGNCHGNC:27905. MSL1.
HPAHPA022800.
HPA023567.
MIM614801. gene.
neXtProtNX_Q68DK7.
PharmGKBPA164723127.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG48092.
HOGENOMHOG000113663.
HOVERGENHBG060802.
InParanoidQ68DK7.
KOK13163.
OMAHKRKTPF.
OrthoDBEOG72VH59.
PhylomeDBQ68DK7.
TreeFamTF330735.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ68DK7.
BgeeQ68DK7.
CleanExHS_MSL1.
GenevestigatorQ68DK7.

Family and domain databases

InterProIPR026711. Msl-1.
IPR029332. PEHE_dom.
[Graphical view]
PANTHERPTHR21656. PTHR21656. 1 hit.
PfamPF15275. PEHE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSL1. human.
GenomeRNAi339287.
NextBio97320.
PROQ68DK7.
SOURCESearch...

Entry information

Entry nameMSL1_HUMAN
AccessionPrimary (citable) accession number: Q68DK7
Secondary accession number(s): Q0VF46, Q69Z03
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM