Q8N5Y2 (MS3L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Male-specific lethal 3 homolog

Alternative name(s):
Male-specific lethal-3 homolog 1
Male-specific lethal-3 protein-like 1
Short name=MSL3-like 1

Gene names

Name:	MSL3
Synonyms:	MSL3L1

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	521 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex. Ref.7 Ref.11 Ref.14 Ref.15
Subunit structure	Component the MSL histone acetyltransferase complex at least composed of the MOF/KAT8, MSL1/hampin, MSL2 and MSL3. Ref.11
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed in many tissues including liver, pancreas, heart, lung, kidney, skeletal muscle, brain, and placenta, with highest expression in skeletal muscle and heart.
Miscellaneous	MSL3L1 gene undergoes X inactivation.
Sequence similarities	Contains 1 chromo domain. Contains 1 MRG domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H4-K16 acetylation Inferred from direct assay Ref.11. Source: UniProtKB multicellular organismal development Traceable author statement Ref.1. Source: ProtInc transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	MSL complex Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay Ref.14. Source: UniProtKB methylated histone residue binding Inferred from direct assay Ref.14. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N5Y2-1)

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: Q8N5Y2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.
     60-61: NR → MP

Isoform 3 (identifier: Q8N5Y2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAK → MSPSVRPGAGWAPVGRPGRPIQ

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8N5Y2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-166: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q8N5Y2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     391-416: KTPVHSRSSSPIPLTPSKEGSAVFAG → SRFILGCPRPGRASVYFVFSQCQAWC
     417-521: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 521

521

Male-specific lethal 3 homolog

PRO_0000080247

Regions

Domain

32 – 90

59

Chromo

Domain

168 – 517

350

MRG

Amino acid modifications

Modified residue

311

1

Phosphoserine Ref.10

Modified residue

367

1

Phosphoserine Ref.9 Ref.12

Modified residue

400

1

Phosphoserine Ref.13

Modified residue

405

1

Phosphothreonine Ref.10

Modified residue

407

1

Phosphoserine Ref.9 Ref.10

Modified residue

411

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1 – 166

166

Missing in isoform 4.

VSP_045652

Alternative sequence

1 – 59

59

Missing in isoform 2.

VSP_007636

Alternative sequence

1 – 34

34

MSASE…LYDAK → MSPSVRPGAGWAPVGRPGRP IQ in isoform 3.

VSP_043342

Alternative sequence

60 – 61

2

NR → MP in isoform 2.

VSP_007637

Alternative sequence

391 – 416

26

KTPVH…AVFAG → SRFILGCPRPGRASVYFVFS QCQAWC in isoform 5.

VSP_045653

Alternative sequence

417 – 521

105

Missing in isoform 5.

VSP_045654

Natural variant

2

1

S → T. Ref.2
Corresponds to variant rs150938844 [ dbSNP | Ensembl ].

VAR_069061

Natural variant

199

1

K → Q.
Corresponds to variant rs1051595 [ dbSNP | Ensembl ].

VAR_048732

Natural variant

251

1

V → I.
Corresponds to variant rs1051600 [ dbSNP | Ensembl ].

VAR_048733

Experimental info

Mutagenesis

31

1

Y → A: Diminishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1). Ref.15

Mutagenesis

55

1

H → A: Diminishes DNA-bindig; when associated with A-65. Ref.14

Mutagenesis

56

1

F → A: Abolishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1).

Mutagenesis

59

1

W → G: Diminishes DNA-binding. Ref.14

Mutagenesis

65

1

R → A: Diminishes DNA-bindig; when associated with A-55. Ref.14

Sequence conflict

37

1

D → V in AAD38499. Ref.1

Sequence conflict

346

1

Q → R in AK025642. Ref.2

Sequence conflict

391

1

K → E in AK025642. Ref.2

Secondary structure

1

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521

Helix Strand Turn

Details...

Beta strand

16 – 20

5

Beta strand

30 – 42

13

Beta strand

48 – 56

9

Helix

61 – 63

3

Beta strand

65 – 68

4

Helix

69 – 71

3

Beta strand

72 – 74

3

Helix

77 – 91

15

Helix

178 – 192

15

Helix

206 – 222

17

Helix

251 – 272

22

Helix

276 – 278

3

Helix

279 – 287

9

Helix

447 – 449

3

Helix

453 – 469

17

Helix

474 – 493

20

Helix

495 – 498

4

Helix

501 – 503

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 6DFFB9E183D0CFB9	FASTA	521	59,824
	10 20 30 40 50 60 MSASEGMKFK FHSGEKVLCF EPDPTKARVL YDAKIVDVIV GKDEKGRKIP EYLIHFNGWN 70 80 90 100 110 120 RSWDRWAAED HVLRDTDENR RLQRKLARKA VARLRSTGRK KKRCRLPGVD SVLKGLPTEE 130 140 150 160 170 180 KDENDENSLS SSSDCSENKD EEISEESDIE EKTEVKEEPE LQTRREMEER TITIEIPEVL 190 200 210 220 230 240 KKQLEDDCYY INRRKRLVKL PCQTNIITIL ESYVKHFAIN AAFSANERPR HHHVMPHANM 250 260 270 280 290 300 NVHYIPAEKN VDLCKEMVDG LRITFDYTLP LVLLYPYEQA QYKKVTSSKF FLPIKESATS 310 320 330 340 350 360 TNRSQEELSP SPPLLNPSTP QSTESQPTTG EPATPKRRKA EPEALQSLRR STRHSANCDR 370 380 390 400 410 420 LSESSASPQP KRRQQDTSAS MPKLFLHLEK KTPVHSRSSS PIPLTPSKEG SAVFAGFEGR 430 440 450 460 470 480 RTNEINEVLS WKLVPDNYPP GDQPPPPSYI YGAQHLLRLF VKLPEILGKM SFSEKNLKAL 490 500 510 520 LKHFDLFLRF LAEYHDDFFP ESAYVAACEA HYSTKNPRAI Y
	Isoform 2 [UniParc]. Checksum: 88D09081DA2C7F1A	FASTA	462	53,043
	10 20 30 40 50 60 MPSWDRWAAE DHVLRDTDEN RRLQRKLARK AVARLRSTGR KKKRCRLPGV DSVLKGLPTE 70 80 90 100 110 120 EKDENDENSL SSSSDCSENK DEEISEESDI EEKTEVKEEP ELQTRREMEE RTITIEIPEV 130 140 150 160 170 180 LKKQLEDDCY YINRRKRLVK LPCQTNIITI LESYVKHFAI NAAFSANERP RHHHVMPHAN 190 200 210 220 230 240 MNVHYIPAEK NVDLCKEMVD GLRITFDYTL PLVLLYPYEQ AQYKKVTSSK FFLPIKESAT 250 260 270 280 290 300 STNRSQEELS PSPPLLNPST PQSTESQPTT GEPATPKRRK AEPEALQSLR RSTRHSANCD 310 320 330 340 350 360 RLSESSASPQ PKRRQQDTSA SMPKLFLHLE KKTPVHSRSS SPIPLTPSKE GSAVFAGFEG 370 380 390 400 410 420 RRTNEINEVL SWKLVPDNYP PGDQPPPPSY IYGAQHLLRL FVKLPEILGK MSFSEKNLKA 430 440 450 460 LLKHFDLFLR FLAEYHDDFF PESAYVAACE AHYSTKNPRA IY
	Isoform 3 [UniParc]. Checksum: 50F8B10061D5E89E	FASTA	509	58,249
	10 20 30 40 50 60 MSPSVRPGAG WAPVGRPGRP IQIVDVIVGK DEKGRKIPEY LIHFNGWNRS WDRWAAEDHV 70 80 90 100 110 120 LRDTDENRRL QRKLARKAVA RLRSTGRKKK RCRLPGVDSV LKGLPTEEKD ENDENSLSSS 130 140 150 160 170 180 SDCSENKDEE ISEESDIEEK TEVKEEPELQ TRREMEERTI TIEIPEVLKK QLEDDCYYIN 190 200 210 220 230 240 RRKRLVKLPC QTNIITILES YVKHFAINAA FSANERPRHH HVMPHANMNV HYIPAEKNVD 250 260 270 280 290 300 LCKEMVDGLR ITFDYTLPLV LLYPYEQAQY KKVTSSKFFL PIKESATSTN RSQEELSPSP 310 320 330 340 350 360 PLLNPSTPQS TESQPTTGEP ATPKRRKAEP EALQSLRRST RHSANCDRLS ESSASPQPKR 370 380 390 400 410 420 RQQDTSASMP KLFLHLEKKT PVHSRSSSPI PLTPSKEGSA VFAGFEGRRT NEINEVLSWK 430 440 450 460 470 480 LVPDNYPPGD QPPPPSYIYG AQHLLRLFVK LPEILGKMSF SEKNLKALLK HFDLFLRFLA 490 500 EYHDDFFPES AYVAACEAHY STKNPRAIY
	Isoform 4 [UniParc]. Checksum: 86211AD697FA2C88	FASTA	355	40,577
	10 20 30 40 50 60 MEERTITIEI PEVLKKQLED DCYYINRRKR LVKLPCQTNI ITILESYVKH FAINAAFSAN 70 80 90 100 110 120 ERPRHHHVMP HANMNVHYIP AEKNVDLCKE MVDGLRITFD YTLPLVLLYP YEQAQYKKVT 130 140 150 160 170 180 SSKFFLPIKE SATSTNRSQE ELSPSPPLLN PSTPQSTESQ PTTGEPATPK RRKAEPEALQ 190 200 210 220 230 240 SLRRSTRHSA NCDRLSESSA SPQPKRRQQD TSASMPKLFL HLEKKTPVHS RSSSPIPLTP 250 260 270 280 290 300 SKEGSAVFAG FEGRRTNEIN EVLSWKLVPD NYPPGDQPPP PSYIYGAQHL LRLFVKLPEI 310 320 330 340 350 LGKMSFSEKN LKALLKHFDL FLRFLAEYHD DFFPESAYVA ACEAHYSTKN PRAIY
	Isoform 5 [UniParc]. Checksum: 97B2DC9F80BE09BE	FASTA	416	47,950
	10 20 30 40 50 60 MSASEGMKFK FHSGEKVLCF EPDPTKARVL YDAKIVDVIV GKDEKGRKIP EYLIHFNGWN 70 80 90 100 110 120 RSWDRWAAED HVLRDTDENR RLQRKLARKA VARLRSTGRK KKRCRLPGVD SVLKGLPTEE 130 140 150 160 170 180 KDENDENSLS SSSDCSENKD EEISEESDIE EKTEVKEEPE LQTRREMEER TITIEIPEVL 190 200 210 220 230 240 KKQLEDDCYY INRRKRLVKL PCQTNIITIL ESYVKHFAIN AAFSANERPR HHHVMPHANM 250 260 270 280 290 300 NVHYIPAEKN VDLCKEMVDG LRITFDYTLP LVLLYPYEQA QYKKVTSSKF FLPIKESATS 310 320 330 340 350 360 TNRSQEELSP SPPLLNPSTP QSTESQPTTG EPATPKRRKA EPEALQSLRR STRHSANCDR 370 380 390 400 410 LSESSASPQP KRRQQDTSAS MPKLFLHLEK SRFILGCPRP GRASVYFVFS QCQAWC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel chromo domain gene in Xp22.3 with homology to Drosophila msl-3." Prakash S.K., Van den Veyver I.B., Franco B., Volta M., Ballabio A., Zoghbi H.Y. Genomics 59:77-84(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[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] (ISOFORMS 3; 4 AND 5), VARIANT THR-2. Tissue: Brain and Hepatoma.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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] OF 283-521. Tissue: 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, FUNCTION OF THE MSL COMPLEX.
[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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-407 AND SER-411, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; THR-405 AND SER-407, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex." Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C. J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MSL COMPLEX, FUNCTION OF THE MSL COMPLEX.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, MASS SPECTROMETRY.
[14]	"Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain." Kim D., Blus B.J., Chandra V., Huang P., Rastinejad F., Khorasanizadeh S. Nat. Struct. Mol. Biol. 17:1027-1029(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-101 IN COMPLEX WITH DNA AND HISTONE H4, MUTAGENESIS OF HIS-55; TRP-59 AND ARG-65, FUNCTION.
[15]	"Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4." Moore S.A., Ferhatoglu Y., Jia Y., Al-Jiab R.A., Scott M.J. J. Biol. Chem. 285:40879-40890(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-93, MUTAGENESIS OF TYR-31, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF117065 mRNA. Translation: AAD38499.1.
AK025642 mRNA. No translation available.
AK289780 mRNA. Translation: BAF82469.1.
AK300814 mRNA. Translation: BAG62470.1.
AC004554 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98799.1.
CH471074 Genomic DNA. Translation: EAW98801.1.
BC031210 mRNA. Translation: AAH31210.1.
AL050178 mRNA. Translation: CAB43308.1.
AL713667 mRNA. Translation: CAD28473.1.

IPI

IPI00297145.
IPI00375604.
IPI00377170.
IPI00641297.

PIR

T08795.

RefSeq

NP_001180199.1. NM_001193270.1.
NP_006791.2. NM_006800.3.
NP_523352.1. NM_078628.1.
NP_523353.2. NM_078629.3.

UniGene

Hs.655288.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Y0N	X-ray	3.00	A/B/C/D	167-518	[»]
3OA6	X-ray	2.35	A/B	1-101	[»]
3OB9	X-ray	2.50	A/B/C/D/E	2-93	[»]

ProteinModelPortal

Q8N5Y2.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-56857N.

IntAct

Q8N5Y2. 3 interactions.

STRING

9606.ENSP00000312244.

PTM databases

PhosphoSite

Q8N5Y2.

Polymorphism databases

DMDM

32171482.

Proteomic databases

PaxDb

Q8N5Y2.

PRIDE

Q8N5Y2.

Protocols and materials databases

DNASU

10943.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312196; ENSP00000312244; ENSG00000005302.
ENST00000337339; ENSP00000338078; ENSG00000005302.
ENST00000380693; ENSP00000370069; ENSG00000005302.
ENST00000398527; ENSP00000381538; ENSG00000005302.

GeneID

10943.

KEGG

hsa:10943.

UCSC

uc004cuw.3. human.

Organism-specific databases

CTD

10943.

GeneCards

GC0XP011776.

HGNC

HGNC:7370. MSL3.

HPA

HPA034535.
HPA034536.

MIM

300609. gene.

neXtProt

NX_Q8N5Y2.

PharmGKB

PA164723161.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG293760.

HOGENOM

HOG000293161.

HOVERGEN

HBG052511.

InParanoid

Q8N5Y2.

OMA

GMKFKFH.

OrthoDB

EOG4X0MS9.

PhylomeDB

Q8N5Y2.

Gene expression databases

ArrayExpress

Q8N5Y2.

Bgee

Q8N5Y2.

CleanEx

HS_MSL3.

Genevestigator

Q8N5Y2.

GermOnline

ENSG00000005302. Homo sapiens.

Family and domain databases

InterPro

IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]

PANTHER

PTHR10880. PTHR10880. 1 hit.

Pfam

PF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS00598. CHROMO_1. False negative.
PS50013. CHROMO_2. False negative.
PS51640. MRG. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MSL3. human.

EvolutionaryTrace

Q8N5Y2.

GenomeRNAi

10943.

NextBio

35463804.

SOURCE

Search...

Entry information

Entry name

MS3L1_HUMAN

Accession

Primary (citable) accession number: Q8N5Y2
Secondary accession number(s): A6NCU2 , A6NHW8, A8K165, B4DUV8, Q9UG70, Q9Y5Z8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 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.