Q9HCI7 (MSL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MSL2
Synonyms:	KIAA1585, MSL2L1, RNF184

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	577 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 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.
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. The sequence BAA91673.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB13411.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
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
Molecular_function	ligase 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 577

577

E3 ubiquitin-protein ligase MSL2

PRO_0000299536

Regions

Zinc finger

44 – 85

42

RING-type

Compositional bias

396 – 463

68

Lys-rich

Natural variations

Alternative sequence

1 – 74

74

Missing in isoform 2.

VSP_046200

Experimental info

Mutagenesis

64

1

H → Y: Great redution in H2B ubiquitination. No effect on MSL1-binding. Ref.9

Sequence conflict

348

1

D → E in BAG63776. Ref.2

Sequence conflict

411

1

S → G in BAA91673. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

577

Helix Strand Turn

Details...

Helix

4 – 18

15

Helix

25 – 40

16

Turn

45 – 47

3

Beta strand

48 – 50

3

Helix

68 – 70

3

Beta strand

77 – 79

3

Turn

82 – 84

3

Helix

94 – 114

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 756C7625E0AF1CA6	FASTA	577	62,541
	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
	Isoform 2 [UniParc]. Checksum: F591F7182AA9937D	FASTA	503	54,339
	10 20 30 40 50 60 MMMKPSCSWC KDYEQFEENK QLSILVNCYK KLCEYITQTT LARDIIEAVD CSSDILALLN 70 80 90 100 110 120 DGSLFCEETE KPSDSSFTLC LTHSPLPSTS EPTTDPQASL SPMSESTLSI AIGSSVINGL 130 140 150 160 170 180 PTYNGLSIDR FGINIPSPEH SNTIDVCNTV DIKTEDLSDS LPPVCDTVAT DLCSTGIDIC 190 200 210 220 230 240 SFSEDIKPGD SLLLSVEEVL RSLETVSNTE VCCPNLQPNL EATVSNGPFL QLSSQSLSHN 250 260 270 280 290 300 VFMSTSPALH GLSCTAATPK IAKLNRKRSR SESDSEKVQP LPISTIIRGP TLGASAPVTV 310 320 330 340 350 360 KRESKISLQP IATVPNGGTT PKISKTVLLS TKSMKKSHEH GSKKSHSKTK PGILKKDKAV 370 380 390 400 410 420 KEKIPSHHFM PGSPTKTVYK KPQEKKGCKC GRATQNPSVL TCRGQRCPCY SNRKACLDCI 430 440 450 460 470 480 CRGCQNSYMA NGEKKLEAFA VPEKALEQTR LTLGINVTSI AVRNASTSTS VINVTGSPVT 490 500 TFLAASTHDD KSLDEAIDMR FDC

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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: MASS SPECTROMETRY, IDENTIFICATION OF MSL COMPLEX COMPONENTS.
[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.
+	Additional computationally mapped references.

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.

IPI

IPI00030554.

RefSeq

NP_001138889.1. NM_001145417.1.
NP_060603.2. NM_018133.3.

UniGene

Hs.18631.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9HCI7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HCI7. 7 interactions.

STRING

9606.ENSP00000311827.

PTM databases

PhosphoSite

Q9HCI7.

Polymorphism databases

DMDM

158564022.

Proteomic databases

PaxDb

Q9HCI7.

PRIDE

Q9HCI7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309993; ENSP00000311827; ENSG00000174579.
ENST00000434835; ENSP00000387948; ENSG00000174579.

GeneID

55167.

KEGG

hsa:55167.

UCSC

uc003eqx.1. human.

Organism-specific databases

CTD

55167.

GeneCards

GC03M135867.

HGNC

HGNC:25544. MSL2.

HPA

HPA003413.

MIM

614802. gene.

neXtProt

NX_Q9HCI7.

PharmGKB

PA164723152.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG86640.

HOGENOM

HOG000043091.

HOVERGEN

HBG108149.

InParanoid

Q9HCI7.

KO

K13164.

OMA

NVMPGSP.

OrthoDB

EOG4JQ3XD.

Gene expression databases

ArrayExpress

Q9HCI7.

Bgee

Q9HCI7.

CleanEx

HS_MSL2.

Genevestigator

Q9HCI7.

Family and domain databases

InterPro

IPR001841. Znf_RING.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MSL2. human.

GenomeRNAi

55167.

NextBio

35476248.

SOURCE

Search...

Entry information

Entry name

MSL2_HUMAN

Accession

Primary (citable) accession number: Q9HCI7
Secondary accession number(s): B4DYL4 , G5E9I1, Q0D2P1, Q8NDB4, Q9NVS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 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.