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Protein

E3 ubiquitin-protein ligase MSL2

Gene

Msl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity). 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 histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 8542RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Msl2
Synonyms:Kiaa1585, Msl2l1, Rnf184
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1925103. Msl2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577E3 ubiquitin-protein ligase MSL2PRO_0000299537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki375 – 375Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ69ZF8.
MaxQBiQ69ZF8.
PaxDbiQ69ZF8.
PRIDEiQ69ZF8.

PTM databases

iPTMnetiQ69ZF8.
PhosphoSiteiQ69ZF8.

Expressioni

Gene expression databases

BgeeiQ69ZF8.
ExpressionAtlasiQ69ZF8. baseline and differential.
GenevisibleiQ69ZF8. MM.

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 MSL1.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000082270.

Structurei

3D structure databases

ProteinModelPortaliQ69ZF8.
SMRiQ69ZF8. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 116116Sufficient for interaction with MSL1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi396 – 46368Lys-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 fingeri44 – 8542RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGUA. Eukaryota.
ENOG410ZJAZ. LUCA.
GeneTreeiENSGT00390000016814.
HOGENOMiHOG000043091.
HOVERGENiHBG108149.
InParanoidiQ69ZF8.
KOiK13164.
OMAiNVMPGSP.
OrthoDBiEOG7JX33Z.
PhylomeDBiQ69ZF8.
TreeFamiTF328848.

Family and domain databases

InterProiIPR032049. Msl2-CXC.
IPR032043. Msl2_Znf-RING.
IPR033467. Tesmin/TSO1-like_CXC.
IPR001841. Znf_RING.
[Graphical view]
PfamiPF16682. MSL2-CXC. 1 hit.
PF16685. zf-RING_10. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q69ZF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL
60 70 80 90 100
LQDPIAPTNS TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV
110 120 130 140 150
NCYKKLCEYI TQTTLARDII EAVDCSSDIL ALLNDGSLFC EETEKPSDSS
160 170 180 190 200
FTLCLTHSPL PSTSEPTADP QASLSPMSES TLSIAIGSSV INGLPTYNGL
210 220 230 240 250
SIDRFGINIP SPEHPNTIDV CNTVDIKTED LSDNLPPVCD TVATDLCSTG
260 270 280 290 300
IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN
310 320 330 340 350
GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKVAKLNR KRSRSESDSE
360 370 380 390 400
KVQPLPISTI IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT
410 420 430 440 450
VLLSTKSMKK SHEHGSKKSH SKSKPGILKK DKAVKEKMPS HHFMPGSPTK
460 470 480 490 500
TVYKKPQEKK GCKCGRATQN PSVLTCRGQR CPCYSNRKAC LDCICRGCQN
510 520 530 540 550
SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS TSTSVINVTG
560 570
SPVTTFLAAS THDDKSLDEA IDMRFDC
Length:577
Mass (Da):62,538
Last modified:September 11, 2007 - v2
Checksum:i5B76E902299191C1
GO

Sequence cautioni

The sequence BAD32486.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173208 mRNA. Translation: BAD32486.1. Different initiation.
BC100371 mRNA. Translation: AAI00372.1.
AK035934 mRNA. Translation: BAC29248.1.
RefSeqiNP_001093921.1. NM_001100451.2.
UniGeneiMm.326206.
Mm.436586.
Mm.491280.

Genome annotation databases

EnsembliENSMUST00000085177; ENSMUSP00000082270; ENSMUSG00000066415.
GeneIDi77853.
KEGGimmu:77853.
UCSCiuc033jml.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173208 mRNA. Translation: BAD32486.1. Different initiation.
BC100371 mRNA. Translation: AAI00372.1.
AK035934 mRNA. Translation: BAC29248.1.
RefSeqiNP_001093921.1. NM_001100451.2.
UniGeneiMm.326206.
Mm.436586.
Mm.491280.

3D structure databases

ProteinModelPortaliQ69ZF8.
SMRiQ69ZF8. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000082270.

PTM databases

iPTMnetiQ69ZF8.
PhosphoSiteiQ69ZF8.

Proteomic databases

EPDiQ69ZF8.
MaxQBiQ69ZF8.
PaxDbiQ69ZF8.
PRIDEiQ69ZF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085177; ENSMUSP00000082270; ENSMUSG00000066415.
GeneIDi77853.
KEGGimmu:77853.
UCSCiuc033jml.1. mouse.

Organism-specific databases

CTDi55167.
MGIiMGI:1925103. Msl2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IGUA. Eukaryota.
ENOG410ZJAZ. LUCA.
GeneTreeiENSGT00390000016814.
HOGENOMiHOG000043091.
HOVERGENiHBG108149.
InParanoidiQ69ZF8.
KOiK13164.
OMAiNVMPGSP.
OrthoDBiEOG7JX33Z.
PhylomeDBiQ69ZF8.
TreeFamiTF328848.

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.

Miscellaneous databases

PROiQ69ZF8.
SOURCEiSearch...

Gene expression databases

BgeeiQ69ZF8.
ExpressionAtlasiQ69ZF8. baseline and differential.
GenevisibleiQ69ZF8. MM.

Family and domain databases

InterProiIPR032049. Msl2-CXC.
IPR032043. Msl2_Znf-RING.
IPR033467. Tesmin/TSO1-like_CXC.
IPR001841. Znf_RING.
[Graphical view]
PfamiPF16682. MSL2-CXC. 1 hit.
PF16685. zf-RING_10. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. "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] OF 111-577.
    Tissue: Placenta.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-577.
    Strain: C57BL/6J.
    Tissue: Cerebellum.

Entry informationi

Entry nameiMSL2_MOUSE
AccessioniPrimary (citable) accession number: Q69ZF8
Secondary accession number(s): Q497U7, Q8CBI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: June 8, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.