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Q9HCI7

- MSL2_HUMAN

UniProt

Q9HCI7 - MSL2_HUMAN

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Protein

E3 ubiquitin-protein ligase MSL2

Gene

MSL2

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 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 MEIS1.1 Publication

Regions

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

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H4-K16 acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:25544. MSL2.

Subcellular locationi

GO - Cellular componenti

  1. MSL complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641H → Y: Great redution in H2B ubiquitination. No effect on MSL1-binding. 1 Publication

Organism-specific databases

PharmGKBiPA164723152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577E3 ubiquitin-protein ligase MSL2PRO_0000299536Add
BLAST

Proteomic databases

MaxQBiQ9HCI7.
PaxDbiQ9HCI7.
PRIDEiQ9HCI7.

PTM databases

PhosphoSiteiQ9HCI7.

Expressioni

Gene expression databases

BgeeiQ9HCI7.
CleanExiHS_MSL2.
ExpressionAtlasiQ9HCI7. baseline and differential.
GenevestigatoriQ9HCI7.

Organism-specific databases

HPAiHPA003413.

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 MSL1.1 Publication

Protein-protein interaction databases

BioGridi120467. 22 interactions.
IntActiQ9HCI7. 7 interactions.
STRINGi9606.ENSP00000311827.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Helixi25 – 4016Combined sources
Turni45 – 473Combined sources
Beta strandi48 – 503Combined sources
Helixi68 – 703Combined sources
Beta strandi77 – 793Combined sources
Turni82 – 843Combined sources
Helixi94 – 11421Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B7YX-ray3.25C/D1-116[»]
4B86X-ray3.50C/D/G/H/K/L1-116[»]
ProteinModelPortaliQ9HCI7.
SMRiQ9HCI7. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 116116Sufficient for interaction with MSL1Add
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

eggNOGiNOG86640.
GeneTreeiENSGT00390000016814.
HOGENOMiHOG000043091.
HOVERGENiHBG108149.
InParanoidiQ9HCI7.
KOiK13164.
OMAiNVMPGSP.
OrthoDBiEOG7JX33Z.
PhylomeDBiQ9HCI7.
TreeFamiTF328848.

Family and domain databases

InterProiIPR001841. Znf_RING.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9HCI7-1) [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
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 PSTSEPTTDP QASLSPMSES TLSIAIGSSV INGLPTYNGL
210 220 230 240 250
SIDRFGINIP SPEHSNTIDV CNTVDIKTED LSDSLPPVCD TVATDLCSTG
260 270 280 290 300
IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN
310 320 330 340 350
GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKIAKLNR KRSRSESDSE
360 370 380 390 400
KVQPLPISTI IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT
410 420 430 440 450
VLLSTKSMKK SHEHGSKKSH SKTKPGILKK DKAVKEKIPS 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):62,541
Last modified:September 11, 2007 - v2
Checksum:i756C7625E0AF1CA6
GO
Isoform 2 (identifier: Q9HCI7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.

Note: No experimental confirmation available.

Show »
Length:503
Mass (Da):54,339
Checksum:iF591F7182AA9937D
GO

Sequence cautioni

The sequence AAH32719.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA91673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB13411.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481D → E in BAG63776. (PubMed:14702039)Curated
Sequence conflicti411 – 4111S → G in BAA91673. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7474Missing in isoform 2. 1 PublicationVSP_046200Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33861.1. [Q9HCI7-1]
CCDS46922.1. [Q9HCI7-2]
RefSeqiNP_001138889.1. NM_001145417.1. [Q9HCI7-2]
NP_060603.2. NM_018133.3. [Q9HCI7-1]
XP_005247628.1. XM_005247571.1. [Q9HCI7-2]
XP_005247629.1. XM_005247572.1. [Q9HCI7-2]
XP_006713747.1. XM_006713684.1. [Q9HCI7-2]
UniGeneiHs.18631.

Genome annotation databases

EnsembliENST00000309993; ENSP00000311827; ENSG00000174579. [Q9HCI7-1]
ENST00000434835; ENSP00000387948; ENSG00000174579. [Q9HCI7-2]
GeneIDi55167.
KEGGihsa:55167.
UCSCiuc003eqx.1. human. [Q9HCI7-1]

Polymorphism databases

DMDMi158564022.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS33861.1. [Q9HCI7-1 ]
CCDS46922.1. [Q9HCI7-2 ]
RefSeqi NP_001138889.1. NM_001145417.1. [Q9HCI7-2 ]
NP_060603.2. NM_018133.3. [Q9HCI7-1 ]
XP_005247628.1. XM_005247571.1. [Q9HCI7-2 ]
XP_005247629.1. XM_005247572.1. [Q9HCI7-2 ]
XP_006713747.1. XM_006713684.1. [Q9HCI7-2 ]
UniGenei Hs.18631.

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 C/D 1-116 [» ]
4B86 X-ray 3.50 C/D/G/H/K/L 1-116 [» ]
ProteinModelPortali Q9HCI7.
SMRi Q9HCI7. Positions 1-115.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120467. 22 interactions.
IntActi Q9HCI7. 7 interactions.
STRINGi 9606.ENSP00000311827.

PTM databases

PhosphoSitei Q9HCI7.

Polymorphism databases

DMDMi 158564022.

Proteomic databases

MaxQBi Q9HCI7.
PaxDbi Q9HCI7.
PRIDEi Q9HCI7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309993 ; ENSP00000311827 ; ENSG00000174579 . [Q9HCI7-1 ]
ENST00000434835 ; ENSP00000387948 ; ENSG00000174579 . [Q9HCI7-2 ]
GeneIDi 55167.
KEGGi hsa:55167.
UCSCi uc003eqx.1. human. [Q9HCI7-1 ]

Organism-specific databases

CTDi 55167.
GeneCardsi GC03M135867.
HGNCi HGNC:25544. MSL2.
HPAi HPA003413.
MIMi 614802. gene.
neXtProti NX_Q9HCI7.
PharmGKBi PA164723152.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG86640.
GeneTreei ENSGT00390000016814.
HOGENOMi HOG000043091.
HOVERGENi HBG108149.
InParanoidi Q9HCI7.
KOi K13164.
OMAi NVMPGSP.
OrthoDBi EOG7JX33Z.
PhylomeDBi Q9HCI7.
TreeFami TF328848.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi MSL2. human.
GenomeRNAii 55167.
NextBioi 35476248.
PROi Q9HCI7.
SOURCEi Search...

Gene expression databases

Bgeei Q9HCI7.
CleanExi HS_MSL2.
ExpressionAtlasi Q9HCI7. baseline and differential.
Genevestigatori Q9HCI7.

Family and domain databases

InterProi IPR001841. Znf_RING.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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.

Entry informationi

Entry nameiMSL2_HUMAN
AccessioniPrimary (citable) accession number: Q9HCI7
Secondary accession number(s): B4DYL4
, G5E9I1, Q0D2P1, Q8NDB4, Q9NVS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: November 26, 2014
This is version 91 of the entry and version 2 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 3
    Human chromosome 3: 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