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Q9HCI7 (MSL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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:
E3 ubiquitin-protein ligase MSL2

EC=6.3.2.-
Alternative name(s):
Male-specific lethal 2-like 1
Short name=MSL2-like 1
Male-specific lethal-2 homolog
Short name=MSL-2
Male-specific lethal-2 homolog 1
RING finger protein 184
Gene names
Name:MSL2
Synonyms:KIAA1585, MSL2L1, RNF184
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 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 lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. Ref.9

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 MSL1. Ref.10

Sequence similarities

Belongs to the MSL2 family.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAH32719.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA91673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB13411.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   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

   Molecular_functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCI7-1)

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.
Isoform 2 (identifier: Q9HCI7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577E3 ubiquitin-protein ligase MSL2
PRO_0000299536

Regions

Zinc finger44 – 8542RING-type
Region1 – 116116Sufficient for interaction with MSL1
Compositional bias396 – 46368Lys-rich

Natural variations

Alternative sequence1 – 7474Missing in isoform 2.
VSP_046200

Experimental info

Mutagenesis641H → Y: Great redution in H2B ubiquitination. No effect on MSL1-binding. Ref.9
Sequence conflict3481D → E in BAG63776. Ref.2
Sequence conflict4111S → G in BAA91673. Ref.2

Secondary structure

................ 577
Helix Strand Turn

Details...

Sequences

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

Last modified September 11, 2007. Version 2.
Checksum: 756C7625E0AF1CA6

FASTA57762,541
        10         20         30         40         50         60 
MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL LQDPIAPTNS 

        70         80         90        100        110        120 
TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV NCYKKLCEYI TQTTLARDII 

       130        140        150        160        170        180 
EAVDCSSDIL ALLNDGSLFC EETEKPSDSS FTLCLTHSPL PSTSEPTTDP QASLSPMSES 

       190        200        210        220        230        240 
TLSIAIGSSV INGLPTYNGL SIDRFGINIP SPEHSNTIDV CNTVDIKTED LSDSLPPVCD 

       250        260        270        280        290        300 
TVATDLCSTG IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN 

       310        320        330        340        350        360 
GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKIAKLNR KRSRSESDSE KVQPLPISTI 

       370        380        390        400        410        420 
IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT VLLSTKSMKK SHEHGSKKSH 

       430        440        450        460        470        480 
SKTKPGILKK DKAVKEKIPS HHFMPGSPTK TVYKKPQEKK GCKCGRATQN PSVLTCRGQR 

       490        500        510        520        530        540 
CPCYSNRKAC LDCICRGCQN SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS 

       550        560        570 
TSTSVINVTG SPVTTFLAAS THDDKSLDEA IDMRFDC 

« Hide

Isoform 2 [UniParc].

Checksum: F591F7182AA9937D
Show »

FASTA50354,339

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 339-577 (ISOFORM 1).
[3]"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 1).
Tissue: Lymph node.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 and 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, 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]"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 AS E3 UBIQUITIN LIGASE, MUTAGENESIS OF HIS-64.
[10]"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 1-116 IN COMPLEX WITH MSL1 AND ZINC IONS, SUBUNIT, INTERACTION WITH MSL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046805 mRNA. Translation: BAB13411.1. Different initiation.
AK001408 mRNA. Translation: BAA91673.1. Different initiation.
AK302491 mRNA. Translation: BAG63776.1.
AL834289 mRNA. Translation: CAD38963.2.
AC092991 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79119.1.
CH471052 Genomic DNA. Translation: EAW79120.1.
BC032719 mRNA. Translation: AAH32719.1. Different initiation.
BC093764 mRNA. Translation: AAH93764.1.
BC093790 mRNA. Translation: AAH93790.1.
RefSeqNP_001138889.1. NM_001145417.1.
NP_060603.2. NM_018133.3.
XP_005247628.1. XM_005247571.1.
XP_005247629.1. XM_005247572.1.
UniGeneHs.18631.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B7YX-ray3.25C/D1-116[»]
4B86X-ray3.50C/D/G/H/K/L1-116[»]
ProteinModelPortalQ9HCI7.
SMRQ9HCI7. Positions 1-115, 457-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120467. 17 interactions.
IntActQ9HCI7. 7 interactions.
STRING9606.ENSP00000311827.

PTM databases

PhosphoSiteQ9HCI7.

Polymorphism databases

DMDM158564022.

Proteomic databases

PaxDbQ9HCI7.
PRIDEQ9HCI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309993; ENSP00000311827; ENSG00000174579. [Q9HCI7-1]
ENST00000434835; ENSP00000387948; ENSG00000174579. [Q9HCI7-2]
GeneID55167.
KEGGhsa:55167.
UCSCuc003eqx.1. human. [Q9HCI7-1]

Organism-specific databases

CTD55167.
GeneCardsGC03M135867.
HGNCHGNC:25544. MSL2.
HPAHPA003413.
MIM614802. gene.
neXtProtNX_Q9HCI7.
PharmGKBPA164723152.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86640.
HOGENOMHOG000043091.
HOVERGENHBG108149.
InParanoidQ9HCI7.
KOK13164.
OMAQHYVCKS.
OrthoDBEOG7JX33Z.
PhylomeDBQ9HCI7.
TreeFamTF328848.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ9HCI7.
BgeeQ9HCI7.
CleanExHS_MSL2.
GenevestigatorQ9HCI7.

Family and domain databases

InterProIPR001841. Znf_RING.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSL2. human.
GenomeRNAi55167.
NextBio35476248.
PROQ9HCI7.
SOURCESearch...

Entry information

Entry nameMSL2_HUMAN
AccessionPrimary (citable) accession number: Q9HCI7
Secondary accession number(s): B4DYL4 expand/collapse secondary AC list , G5E9I1, Q0D2P1, Q8NDB4, Q9NVS4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 84 of the entry and version 2 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 3

Human chromosome 3: entries, gene names and cross-references to MIM