Q68DK7 (MSL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MSL1
Synonyms:	MSL1L1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.5 Ref.11
Subunit structure	Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and MSL3. Directly interacts with MSL2 via its coiled coil domain. 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
Subcellular location	Nucleus Ref.4.
Induction	Up-regulated by gamma-irradiation. Ref.8
Post-translational modification	Sumoylated with SUMO1. Ref.4
Sequence similarities	Belongs to the msl-1 family.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H4-K16 acetylation Inferred from direct assay PubMed 20018852. Source: UniProtKB
Cellular_component	MSL complex Inferred from direct assay PubMed 20018852. Source: UniProtKB
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 614

614

Male-specific lethal 1 homolog

PRO_0000349236

Regions

Coiled coil

223 – 282

60

Potential

Compositional bias

10 – 15

6

Poly-Ala

Compositional bias

55 – 185

131

Pro-rich

Compositional bias

208 – 214

7

Poly-Gly

Amino acid modifications

Modified residue

126

1

Phosphoserine Ref.12

Modified residue

205

1

Phosphoserine Ref.7 Ref.10 Ref.12

Modified residue

353

1

N6-acetyllysine Ref.9

Natural variations

Alternative sequence

1 – 263

263

Missing in isoform 3.

VSP_035236

Alternative sequence

1 – 201

201

Missing in isoform 2.

VSP_035237

Experimental info

Sequence conflict

427

1

S → P in CAH18213. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

614

Helix Strand Turn

Details...

Helix

215 – 250

36

Beta strand

478 – 480

3

Helix

500 – 518

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 8, 2011. Version 3. Checksum: D48D845C1C2ABF45	FASTA	614	67,128
	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
	Isoform 2 [UniParc]. Checksum: 846A85F75A0B626F	FASTA	413	47,593
	10 20 30 40 50 60 MRKSPLGGGG GSGASSQAAC LKQILLLQLD LIEQQQQQLQ AKEKEIEELK SERDTLLARI 70 80 90 100 110 120 ERMERRMQLV KKDNEKERHK LFQGYETEER EETELSEKIK LECQPELSET SQTLPPKPFS 130 140 150 160 170 180 CGRSGKGHKR KSPFGSTERK TPVKKLAPEF SKVKTKTPKH SPIKEEPCGS LSETVCKREL 190 200 210 220 230 240 RSQETPEKPR SSVDTPPRLS TPQKGPSTHP KEKAFSSEIE DLPYLSTTEM YLCRWHQPPP 250 260 270 280 290 300 SPLPLRESSP KKEETVARCL MPSSVAGETS VLAVPSWRDH SVEPLRDPNP SDLLENLDDS 310 320 330 340 350 360 VFSKRHAKLE LDEKRRKRWD IQRIREQRIL QRLQLRMYKK KGIQESEPEV TSFFPEPDDV 370 380 390 400 410 ESLMITPFLP VVAFGRPLPK LTPQNFELPW LDERSRCRLE IQKKQTPHRT CRK
	Isoform 3 [UniParc]. Checksum: 4D18D5EC95550885	FASTA	351	40,778
	10 20 30 40 50 60 MERRMQLVKK DNEKERHKLF QGYETEEREE TELSEKIKLE CQPELSETSQ TLPPKPFSCG 70 80 90 100 110 120 RSGKGHKRKS PFGSTERKTP VKKLAPEFSK VKTKTPKHSP IKEEPCGSLS ETVCKRELRS 130 140 150 160 170 180 QETPEKPRSS VDTPPRLSTP QKGPSTHPKE KAFSSEIEDL PYLSTTEMYL CRWHQPPPSP 190 200 210 220 230 240 LPLRESSPKK EETVARCLMP SSVAGETSVL AVPSWRDHSV EPLRDPNPSD LLENLDDSVF 250 260 270 280 290 300 SKRHAKLELD EKRRKRWDIQ RIREQRILQR LQLRMYKKKG IQESEPEVTS FFPEPDDVES 310 320 330 340 350 LMITPFLPVV AFGRPLPKLT PQNFELPWLD ERSRCRLEIQ KKQTPHRTCR K

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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.

IPI

IPI00784883.
IPI00787950.
IPI00953625.

RefSeq

NP_001012241.1. NM_001012241.1.

UniGene

Hs.532786.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q68DK7.

SMR

Q68DK7. Positions 493-534, 549-592.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q68DK7. 4 interactions.

STRING

9606.ENSP00000341409.

PTM databases

PhosphoSite

Q68DK7.

Polymorphism databases

DMDM

205829212.

Proteomic databases

PaxDb

Q68DK7.

PRIDE

Q68DK7.

Protocols and materials databases

DNASU

339287.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398532; ENSP00000381543; ENSG00000188895.
ENST00000579565; ENSP00000462945; ENSG00000188895.

GeneID

339287.

KEGG

hsa:339287.

UCSC

uc002hua.4. human.
uc002huc.2. human.

Organism-specific databases

CTD

339287.

GeneCards

GC17P038278.

HGNC

HGNC:27905. MSL1.

HPA

HPA022800.
HPA023567.

MIM

614801. gene.

neXtProt

NX_Q68DK7.

PharmGKB

PA164723127.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG48092.

HOGENOM

HOG000113663.

HOVERGEN

HBG060802.

InParanoid

Q68DK7.

KO

K13163.

OMA

GHKRKTP.

OrthoDB

EOG4Z62NT.

Gene expression databases

ArrayExpress

Q68DK7.

Bgee

Q68DK7.

CleanEx

HS_MSL1.

Genevestigator

Q68DK7.

Family and domain databases

InterPro

IPR026711. Msl-1.
[Graphical view]

PANTHER

PTHR21656. PTHR21656. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

MSL1. human.

GenomeRNAi

339287.

NextBio

97320.

SOURCE

Search...

Entry information

Entry name

MSL1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 62 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.