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Q8N5Y2 (MS3L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceEvidence 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 Ref.16 Ref.17

Subunit structure

Component the MSL histone acetyltransferase complex at least composed of the MOF/KAT8, MSL1/hampin, MSL2 and MSL3. Interacts (via the MRG domain) with MSL1. Ref.11 Ref.14 Ref.17

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.

Alternative products

This entry describes 6 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.
Isoform 6 (identifier: Q8N5Y2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MSASEG → MKMMKT
     7-155: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Male-specific lethal 3 homolog
PRO_0000080247

Regions

Domain32 – 9059Chromo
Domain168 – 517350MRG
Region290 – 440151Required for the histone acetyltransferase activity of the MSL complex

Amino acid modifications

Modified residue3111Phosphoserine Ref.10
Modified residue3671Phosphoserine Ref.9 Ref.12
Modified residue4001Phosphoserine Ref.13
Modified residue4051Phosphothreonine Ref.10
Modified residue4071Phosphoserine Ref.9 Ref.10
Modified residue4111Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 166166Missing in isoform 4.
VSP_045652
Alternative sequence1 – 5959Missing in isoform 2.
VSP_007636
Alternative sequence1 – 3434MSASE…LYDAK → MSPSVRPGAGWAPVGRPGRP IQ in isoform 3.
VSP_043342
Alternative sequence1 – 66MSASEG → MKMMKT in isoform 6.
VSP_055376
Alternative sequence7 – 155149Missing in isoform 6.
VSP_055377
Alternative sequence60 – 612NR → MP in isoform 2.
VSP_007637
Alternative sequence391 – 41626KTPVH…AVFAG → SRFILGCPRPGRASVYFVFS QCQAWC in isoform 5.
VSP_045653
Alternative sequence417 – 521105Missing in isoform 5.
VSP_045654
Natural variant21S → T. Ref.2
Corresponds to variant rs150938844 [ dbSNP | Ensembl ].
VAR_069061
Natural variant1991K → Q.
Corresponds to variant rs1051595 [ dbSNP | Ensembl ].
VAR_048732
Natural variant2511V → I.
Corresponds to variant rs1051600 [ dbSNP | Ensembl ].
VAR_048733

Experimental info

Mutagenesis311Y → A: Diminishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1). Ref.16
Mutagenesis551H → A: Diminishes DNA-binding; when associated with A-65. Ref.15
Mutagenesis561F → A: Abolishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1).
Mutagenesis591W → G: Diminishes DNA-binding. Ref.15
Mutagenesis651R → A: Diminishes DNA-binding; when associated with A-55. Ref.15
Sequence conflict371D → V in AAD38499. Ref.1
Sequence conflict3461Q → R in AK025642. Ref.2
Sequence conflict3911K → E in AK025642. Ref.2

Secondary structure

.................................. 521
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6DFFB9E183D0CFB9

FASTA52159,824
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 88D09081DA2C7F1A
Show »

FASTA46253,043
Isoform 3 [UniParc].

Checksum: 50F8B10061D5E89E
Show »

FASTA50958,249
Isoform 4 [UniParc].

Checksum: 86211AD697FA2C88
Show »

FASTA35540,577
Isoform 5 [UniParc].

Checksum: 97B2DC9F80BE09BE
Show »

FASTA41647,950
Isoform 6 [UniParc].

Checksum: FD52D6BBAFA528D9
Show »

FASTA37242,725

References

« Hide '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. expand/collapse author list , 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; 5 AND 6), VARIANT THR-2.
Tissue: Amygdala, 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. expand/collapse author list , 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. expand/collapse author list , 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: IDENTIFICATION OF MSL COMPLEX COMPONENTS, FUNCTION OF THE MSL COMPLEX, 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex."
Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
Cell Res. 22:1078-1081(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MSL COMPLEX, INTERACTION WITH MSL1.
[15]"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.
[16]"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.
[17]"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 167-517 IN COMPLEX WITH MSL1, FUNCTION IN MSL COMPLEX, INTERACTION WITH MSL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117065 mRNA. Translation: AAD38499.1.
AK025642 mRNA. No translation available.
AK289780 mRNA. Translation: BAF82469.1.
AK294255 mRNA. Translation: BAH11713.1.
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.
CCDSCCDS14147.1. [Q8N5Y2-1]
CCDS14148.1. [Q8N5Y2-5]
CCDS14149.1. [Q8N5Y2-4]
CCDS55369.1. [Q8N5Y2-3]
PIRT08795.
RefSeqNP_001180199.1. NM_001193270.2. [Q8N5Y2-3]
NP_001269103.1. NM_001282174.1.
NP_006791.2. NM_006800.3. [Q8N5Y2-4]
NP_523352.1. NM_078628.1. [Q8N5Y2-5]
NP_523353.2. NM_078629.3. [Q8N5Y2-1]
XP_005274497.1. XM_005274440.2. [Q8N5Y2-4]
UniGeneHs.655288.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y0NX-ray3.00A/B/C/D167-289[»]
A/B/C/D442-518[»]
3OA6X-ray2.35A/B1-101[»]
3OB9X-ray2.50A/B/C/D/E2-93[»]
ProteinModelPortalQ8N5Y2.
SMRQ8N5Y2. Positions 9-92, 171-293, 442-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116143. 14 interactions.
DIPDIP-56857N.
IntActQ8N5Y2. 5 interactions.
STRING9606.ENSP00000312244.

PTM databases

PhosphoSiteQ8N5Y2.

Polymorphism databases

DMDM32171482.

Proteomic databases

MaxQBQ8N5Y2.
PaxDbQ8N5Y2.
PRIDEQ8N5Y2.

Protocols and materials databases

DNASU10943.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312196; ENSP00000312244; ENSG00000005302. [Q8N5Y2-1]
ENST00000337339; ENSP00000338078; ENSG00000005302. [Q8N5Y2-5]
ENST00000361672; ENSP00000354562; ENSG00000005302.
ENST00000380693; ENSP00000370069; ENSG00000005302. [Q8N5Y2-4]
ENST00000398527; ENSP00000381538; ENSG00000005302. [Q8N5Y2-3]
GeneID10943.
KEGGhsa:10943.
UCSCuc004cuw.3. human. [Q8N5Y2-1]
uc011mih.2. human. [Q8N5Y2-3]

Organism-specific databases

CTD10943.
GeneCardsGC0XP011776.
HGNCHGNC:7370. MSL3.
HPAHPA034535.
HPA034536.
MIM300609. gene.
neXtProtNX_Q8N5Y2.
PharmGKBPA164723161.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293760.
HOGENOMHOG000293161.
HOVERGENHBG052511.
InParanoidQ8N5Y2.
OMAGMKFKFH.
OrthoDBEOG7BCNBQ.
PhylomeDBQ8N5Y2.
TreeFamTF323400.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ8N5Y2.
BgeeQ8N5Y2.
CleanExHS_MSL3.
GenevestigatorQ8N5Y2.

Family and domain databases

InterProIPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERPTHR10880. PTHR10880. 1 hit.
PfamPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 2 hits.
PROSITEPS51640. MRG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSL3. human.
EvolutionaryTraceQ8N5Y2.
GenomeRNAi10943.
NextBio35463804.
PROQ8N5Y2.
SOURCESearch...

Entry information

Entry nameMS3L1_HUMAN
AccessionPrimary (citable) accession number: Q8N5Y2
Secondary accession number(s): A6NCU2 expand/collapse secondary AC list , A6NHW8, A8K165, B4DUV8, B7Z227, Q9UG70, Q9Y5Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM