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Protein

E3 ubiquitin-protein ligase msl-2

Gene

msl-2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The Msl proteins are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). Msl-2 is required for translation and/or stability of msl-1 in males. In complex with msl-1, acts as an E3 ubiquitin ligase that promotes ubiquitination of histone H2B.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri41 – 8545RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • DNA binding Source: FlyBase
  • ligase activity Source: UniProtKB-KW
  • transcription factor binding Source: FlyBase
  • ubiquitin protein ligase activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • dosage compensation Source: FlyBase
  • dosage compensation by hyperactivation of X chromosome Source: FlyBase
  • dosage compensation complex assembly involved in dosage compensation by hyperactivation of X chromosome Source: FlyBase
  • protein autoubiquitination Source: FlyBase
  • protein ubiquitination Source: FlyBase
  • sensory perception of pain Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase msl-2 (EC:6.3.2.-)
Alternative name(s):
Protein male-specific lethal-2
Gene namesi
Name:msl-2
ORF Names:CG3241
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0005616. msl-2.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Msl-1 and msl-2 colocalize to many sites on the male X chromosome.

GO - Cellular componenti

  • chromosome Source: FlyBase
  • dosage compensation complex Source: FlyBase
  • MSL complex Source: FlyBase
  • nuclear chromosome Source: FlyBase
  • nucleus Source: FlyBase
  • X chromosome Source: FlyBase
  • X chromosome located dosage compensation complex, transcription activating Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 773773E3 ubiquitin-protein ligase msl-2PRO_0000055962Add
BLAST

Proteomic databases

PaxDbiP50534.
PRIDEiP50534.

Expressioni

Developmental stagei

Only produced in males.

Gene expression databases

BgeeiP50534.
ExpressionAtlasiP50534. differential.
GenevisibleiP50534. DM.

Interactioni

Subunit structurei

Interacts with msl-1 in a tight complex to form a dosage compensation protein complex.3 Publications

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi59776. 10 interactions.
IntActiP50534. 1 interaction.
STRINGi7227.FBpp0077259.

Structurei

Secondary structure

1
773
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi530 – 5334Combined sources
Helixi535 – 5373Combined sources
Turni538 – 5403Combined sources
Helixi545 – 5484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LUANMR-A520-570[»]
4RKGX-ray2.50A/B520-570[»]
4RKHX-ray2.00C/D/E/F520-570[»]
ProteinModelPortaliP50534.
SMRiP50534. Positions 2-115, 520-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili424 – 46845Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi525 – 56137Cys-richAdd
BLAST
Compositional biasi685 – 71329Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the MSL2 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri41 – 8545RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGUA. Eukaryota.
ENOG410ZJAZ. LUCA.
GeneTreeiENSGT00390000016814.
InParanoidiP50534.
KOiK13164.
OMAiGKRCQHN.
OrthoDBiEOG7BKCSX.
PhylomeDBiP50534.

Family and domain databases

InterProiIPR032049. Msl2-CXC.
IPR032043. Msl2_Znf-RING.
IPR033467. Tesmin/TSO1-like_CXC.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF16682. MSL2-CXC. 1 hit.
PF16685. zf-RING_10. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQTAYLKVT RIAMRSASNL SKRRVEELNS GLGELRQLLS CVVCCQLLVD
60 70 80 90 100
PYSPKGKRCQ HNVCRLCLRG KKHLFPSCTQ CEGCSDFKTY EENRMMAAQL
110 120 130 140 150
LCYKTLCVHL LHSALFGELA GMRPQVAREL VPRIKLPPKT TQEFIREGSN
160 170 180 190 200
ISDTFDIFLP QPDLPFLKDM PTSLPAETPP TSAVTTPELP YDHHLNISDI
210 220 230 240 250
EAEAAATAEQ GHFSPLPLLP TGSRMGMLSH AGQIVIATES SESGFMDQAW
260 270 280 290 300
TDQVDLSGTV SVSKYTNSGN NFAVSYVMPT SATTKFDPQE LQIGQVVQMA
310 320 330 340 350
DSTQLAVLAA VEETVETSTQ LTVLSTTVEE TVETSTQLEV LTSAEEPNEI
360 370 380 390 400
SDQLANLQVE ESDEALVEET VEEAEGTSIP SEVVAEHMEE DQHLDVHTSQ
410 420 430 440 450
SPTQTEMEEA VEEHVATKTQ LGHVQTELQD AESLQKDFED AKAAAEEAKE
460 470 480 490 500
KEKDLHAISA ELQKEDSDEP TLKRKRTRTL KASQAAKIEP VPSEVKTKVQ
510 520 530 540 550
SGKGALRRIR GKDKEEKVKP PKPKCRCGIS GSSNTLTTCR NSRCPCYKSY
560 570 580 590 600
NSCAGCHCVC CKNPHKEDYV ESDEDDDLED FEMPKDVPEP MTQSEEPVVA
610 620 630 640 650
EPRQEENSMA PPDSSAPISL VPLNNLQQSQ HPLVLVQNEK GEYQGFNIFQ
660 670 680 690 700
GSKPLDPVTV GFTIRVQLQH TDGFGSLPQY AYIMPTIDPP NPPAPSLSPP
710 720 730 740 750
PPPAPDREVI EPPAKKFRTS RTRRGRANFS ALDTVDELVS GGSRSNSAAG
760 770
DRSSATDNAH SLFEEIMSGS DDL
Length:773
Mass (Da):84,856
Last modified:September 27, 2005 - v2
Checksum:i31830142AD64F4D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801T → N in CAA88358 (PubMed:7796814).Curated
Sequence conflicti367 – 3704Missing (PubMed:7796814).Curated
Sequence conflicti371 – 3733VEE → LKT in AAA75573 (PubMed:7781064).Curated
Sequence conflicti380 – 3801P → Q in CAA88358 (PubMed:7796814).Curated
Sequence conflicti403 – 4053TQT → IQA in CAA88358 (PubMed:7796814).Curated
Sequence conflicti423 – 4231H → Q in CAA61529 (PubMed:7588059).Curated
Sequence conflicti429 – 4291Q → H (PubMed:7796814).Curated
Sequence conflicti431 – 4333AES → EEP (PubMed:7796814).Curated
Sequence conflicti431 – 4333AES → EEP (PubMed:7588059).Curated
Sequence conflicti439 – 4391E → V in CAA88358 (PubMed:7796814).Curated
Sequence conflicti443 – 4431A → P in CAA88358 (PubMed:7796814).Curated
Sequence conflicti471 – 4711T → A in CAA61529 (PubMed:7588059).Curated
Sequence conflicti591 – 5911M → L in CAA61529 (PubMed:7588059).Curated
Sequence conflicti642 – 6421E → D in CAA88358 (PubMed:7796814).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42553 Genomic DNA. Translation: AAA75573.1.
Z48443 Genomic DNA. Translation: CAA88358.1.
X89241 Genomic DNA. Translation: CAA61529.1.
AE014134 Genomic DNA. Translation: AAF51104.1.
AY128426 mRNA. Translation: AAM75019.1.
PIRiS55554.
RefSeqiNP_523467.1. NM_078743.5.
NP_722907.1. NM_164536.2.
UniGeneiDm.14311.

Genome annotation databases

EnsemblMetazoaiFBtr0077570; FBpp0077259; FBgn0005616.
FBtr0077571; FBpp0077260; FBgn0005616.
GeneIDi33565.
KEGGidme:Dmel_CG3241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42553 Genomic DNA. Translation: AAA75573.1.
Z48443 Genomic DNA. Translation: CAA88358.1.
X89241 Genomic DNA. Translation: CAA61529.1.
AE014134 Genomic DNA. Translation: AAF51104.1.
AY128426 mRNA. Translation: AAM75019.1.
PIRiS55554.
RefSeqiNP_523467.1. NM_078743.5.
NP_722907.1. NM_164536.2.
UniGeneiDm.14311.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LUANMR-A520-570[»]
4RKGX-ray2.50A/B520-570[»]
4RKHX-ray2.00C/D/E/F520-570[»]
ProteinModelPortaliP50534.
SMRiP50534. Positions 2-115, 520-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59776. 10 interactions.
IntActiP50534. 1 interaction.
STRINGi7227.FBpp0077259.

Proteomic databases

PaxDbiP50534.
PRIDEiP50534.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077570; FBpp0077259; FBgn0005616.
FBtr0077571; FBpp0077260; FBgn0005616.
GeneIDi33565.
KEGGidme:Dmel_CG3241.

Organism-specific databases

CTDi33565.
FlyBaseiFBgn0005616. msl-2.

Phylogenomic databases

eggNOGiENOG410IGUA. Eukaryota.
ENOG410ZJAZ. LUCA.
GeneTreeiENSGT00390000016814.
InParanoidiP50534.
KOiK13164.
OMAiGKRCQHN.
OrthoDBiEOG7BKCSX.
PhylomeDBiP50534.

Enzyme and pathway databases

ReactomeiR-DME-3214847. HATs acetylate histones.

Miscellaneous databases

GenomeRNAii33565.
PROiP50534.

Gene expression databases

BgeeiP50534.
ExpressionAtlasiP50534. differential.
GenevisibleiP50534. DM.

Family and domain databases

InterProiIPR032049. Msl2-CXC.
IPR032043. Msl2_Znf-RING.
IPR033467. Tesmin/TSO1-like_CXC.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF16682. MSL2-CXC. 1 hit.
PF16685. zf-RING_10. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila."
    Kelley R.L., Solovyeva I., Lyman L.M., Richman R., Solovyev V., Kuroda M.I.
    Cell 81:867-877(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSL-1, SUBCELLULAR LOCATION.
  2. "Male-specific lethal 2, a dosage compensation gene of Drosophila, undergoes sex-specific regulation and encodes a protein with a RING finger and a metallothionein-like cysteine cluster."
    Zhou S., Yang Y., Scott M.J., Pannuti A., Fehr K.C., Eisen A., Koonin E.V., Fouts D.L., Wrightsman R., Manning J.E., Lucchesi J.C.
    EMBO J. 14:2884-2895(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSL-1, SUBCELLULAR LOCATION.
  3. "The msl-2 dosage compensation gene of Drosophila encodes a putative DNA-binding protein whose expression is sex specifically regulated by Sex-lethal."
    Bashaw G.J., Baker B.S.
    Development 121:3245-3258(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSL-1, SUBCELLULAR LOCATION.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  7. "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.

Entry informationi

Entry nameiMSL2_DROME
AccessioniPrimary (citable) accession number: P50534
Secondary accession number(s): Q9VQR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 27, 2005
Last modified: June 8, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.