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Q68DK7

- MSL1_HUMAN

UniProt

Q68DK7 - MSL1_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ68DK7.
CleanExiHS_MSL1.
ExpressionAtlasiQ68DK7. baseline and differential.
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. 20 interactions.
IntActiQ68DK7. 5 interactions.
STRINGi9606.ENSP00000341409.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000018292.
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

        10         20         30         40         50
MTMRSAVFKA AAAPAGGNPE QRLDYERAAA LGGPEDEPGA AEAHFLPRHR
60 70 80 90 100
KLKEPGPPLA SSQGGSPAPS PAGCGGKGRG LLLPAGAAPG QQEESWGGSV
110 120 130 140 150
PLPCPPPATK QAGIGGEPAA AGAGCSPRPK YQAVLPIQTG SLVAAAKEPT
160 170 180 190 200
PWAGDKGGAA SPAATASDPA GPPPLPLPGP PPLAPTATAG TLAASEGRWK
210 220 230 240 250
SMRKSPLGGG GGSGASSQAA CLKQILLLQL DLIEQQQQQL QAKEKEIEEL
260 270 280 290 300
KSERDTLLAR IERMERRMQL VKKDNEKERH KLFQGYETEE REETELSEKI
310 320 330 340 350
KLECQPELSE TSQTLPPKPF SCGRSGKGHK RKSPFGSTER KTPVKKLAPE
360 370 380 390 400
FSKVKTKTPK HSPIKEEPCG SLSETVCKRE LRSQETPEKP RSSVDTPPRL
410 420 430 440 450
STPQKGPSTH PKEKAFSSEI EDLPYLSTTE MYLCRWHQPP PSPLPLRESS
460 470 480 490 500
PKKEETVARC LMPSSVAGET SVLAVPSWRD HSVEPLRDPN PSDLLENLDD
510 520 530 540 550
SVFSKRHAKL ELDEKRRKRW DIQRIREQRI LQRLQLRMYK KKGIQESEPE
560 570 580 590 600
VTSFFPEPDD VESLMITPFL PVVAFGRPLP KLTPQNFELP WLDERSRCRL
610
EIQKKQTPHR TCRK

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 20 interactions.
IntActi Q68DK7. 5 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.
GeneTreei ENSGT00390000018292.
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

Bgeei Q68DK7.
CleanExi HS_MSL1.
ExpressionAtlasi Q68DK7. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 77 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