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Q8N5Y2

- MS3L1_HUMAN

UniProt

Q8N5Y2 - MS3L1_HUMAN

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Protein

Male-specific lethal 3 homolog

Gene

MSL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. methylated histone binding Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H4-K16 acetylation Source: UniProtKB
  3. multicellular organismal development Source: ProtInc
  4. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MSL3
Synonyms:MSL3L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7370. MSL3.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311Y → A: Diminishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1). 1 Publication
Mutagenesisi55 – 551H → A: Diminishes DNA-binding; when associated with A-65. 1 Publication
Mutagenesisi56 – 561F → A: Abolishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1).
Mutagenesisi59 – 591W → G: Diminishes DNA-binding. 1 Publication
Mutagenesisi65 – 651R → A: Diminishes DNA-binding; when associated with A-55. 1 Publication

Organism-specific databases

PharmGKBiPA164723161.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Male-specific lethal 3 homologPRO_0000080247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei311 – 3111Phosphoserine1 Publication
Modified residuei367 – 3671Phosphoserine2 Publications
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei405 – 4051Phosphothreonine1 Publication
Modified residuei407 – 4071Phosphoserine2 Publications
Modified residuei411 – 4111Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8N5Y2.
PaxDbiQ8N5Y2.
PRIDEiQ8N5Y2.

PTM databases

PhosphoSiteiQ8N5Y2.

Expressioni

Tissue specificityi

Expressed in many tissues including liver, pancreas, heart, lung, kidney, skeletal muscle, brain, and placenta, with highest expression in skeletal muscle and heart.

Gene expression databases

BgeeiQ8N5Y2.
CleanExiHS_MSL3.
ExpressionAtlasiQ8N5Y2. baseline and differential.
GenevestigatoriQ8N5Y2.

Organism-specific databases

HPAiHPA034535.
HPA034536.

Interactioni

Subunit structurei

Component the MSL histone acetyltransferase complex at least composed of the MOF/KAT8, MSL1/hampin, MSL2 and MSL3. Interacts (via the MRG domain) with MSL1.4 Publications

Protein-protein interaction databases

BioGridi116143. 17 interactions.
DIPiDIP-56857N.
IntActiQ8N5Y2. 5 interactions.
STRINGi9606.ENSP00000312244.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 205
Beta strandi30 – 4213
Beta strandi48 – 569
Helixi61 – 633
Beta strandi65 – 684
Helixi69 – 713
Beta strandi72 – 743
Helixi77 – 9115
Helixi178 – 19215
Helixi206 – 22217
Helixi251 – 27222
Helixi276 – 2783
Helixi279 – 2879
Helixi447 – 4493
Helixi453 – 46917
Helixi474 – 49320
Helixi495 – 4984
Helixi501 – 5033

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ8N5Y2.
SMRiQ8N5Y2. Positions 9-92, 171-293, 442-507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N5Y2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9059ChromoAdd
BLAST
Domaini168 – 517350MRGPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 440151Required for the histone acetyltransferase activity of the MSL complexAdd
BLAST

Sequence similaritiesi

Contains 1 chromo domain.Curated
Contains 1 MRG domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG293760.
GeneTreeiENSGT00730000111072.
HOGENOMiHOG000293161.
HOVERGENiHBG052511.
InParanoidiQ8N5Y2.
KOiK18403.
OMAiGMKFKFH.
OrthoDBiEOG7BCNBQ.
PhylomeDBiQ8N5Y2.
TreeFamiTF323400.

Family and domain databases

InterProiIPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERiPTHR10880. PTHR10880. 1 hit.
PfamiPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS51640. MRG. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N5Y2-1) [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
MSASEGMKFK FHSGEKVLCF EPDPTKARVL YDAKIVDVIV GKDEKGRKIP
60 70 80 90 100
EYLIHFNGWN RSWDRWAAED HVLRDTDENR RLQRKLARKA VARLRSTGRK
110 120 130 140 150
KKRCRLPGVD SVLKGLPTEE KDENDENSLS SSSDCSENKD EEISEESDIE
160 170 180 190 200
EKTEVKEEPE LQTRREMEER TITIEIPEVL KKQLEDDCYY INRRKRLVKL
210 220 230 240 250
PCQTNIITIL ESYVKHFAIN AAFSANERPR HHHVMPHANM NVHYIPAEKN
260 270 280 290 300
VDLCKEMVDG LRITFDYTLP LVLLYPYEQA QYKKVTSSKF FLPIKESATS
310 320 330 340 350
TNRSQEELSP SPPLLNPSTP QSTESQPTTG EPATPKRRKA EPEALQSLRR
360 370 380 390 400
STRHSANCDR LSESSASPQP KRRQQDTSAS MPKLFLHLEK KTPVHSRSSS
410 420 430 440 450
PIPLTPSKEG SAVFAGFEGR RTNEINEVLS WKLVPDNYPP GDQPPPPSYI
460 470 480 490 500
YGAQHLLRLF VKLPEILGKM SFSEKNLKAL LKHFDLFLRF LAEYHDDFFP
510 520
ESAYVAACEA HYSTKNPRAI Y
Length:521
Mass (Da):59,824
Last modified:October 1, 2002 - v1
Checksum:i6DFFB9E183D0CFB9
GO
Isoform 2 (identifier: Q8N5Y2-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:462
Mass (Da):53,043
Checksum:i88D09081DA2C7F1A
GO
Isoform 3 (identifier: Q8N5Y2-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:509
Mass (Da):58,249
Checksum:i50F8B10061D5E89E
GO
Isoform 4 (identifier: Q8N5Y2-4) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:355
Mass (Da):40,577
Checksum:i86211AD697FA2C88
GO
Isoform 5 (identifier: Q8N5Y2-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:416
Mass (Da):47,950
Checksum:i97B2DC9F80BE09BE
GO
Isoform 6 (identifier: Q8N5Y2-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MSASEG → MKMMKT
     7-155: Missing.

Note: No experimental confirmation available.

Show »
Length:372
Mass (Da):42,725
Checksum:iFD52D6BBAFA528D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371D → V in AAD38499. (PubMed:10395802)Curated
Sequence conflicti346 – 3461Q → R in AK025642. (PubMed:14702039)Curated
Sequence conflicti391 – 3911K → E in AK025642. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → T.1 Publication
Corresponds to variant rs150938844 [ dbSNP | Ensembl ].
VAR_069061
Natural varianti199 – 1991K → Q.
Corresponds to variant rs1051595 [ dbSNP | Ensembl ].
VAR_048732
Natural varianti251 – 2511V → I.
Corresponds to variant rs1051600 [ dbSNP | Ensembl ].
VAR_048733

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 166166Missing in isoform 4. 1 PublicationVSP_045652Add
BLAST
Alternative sequencei1 – 5959Missing in isoform 2. 1 PublicationVSP_007636Add
BLAST
Alternative sequencei1 – 3434MSASE…LYDAK → MSPSVRPGAGWAPVGRPGRP IQ in isoform 3. 1 PublicationVSP_043342Add
BLAST
Alternative sequencei1 – 66MSASEG → MKMMKT in isoform 6. 1 PublicationVSP_055376
Alternative sequencei7 – 155149Missing in isoform 6. 1 PublicationVSP_055377Add
BLAST
Alternative sequencei60 – 612NR → MP in isoform 2. 1 PublicationVSP_007637
Alternative sequencei391 – 41626KTPVH…AVFAG → SRFILGCPRPGRASVYFVFS QCQAWC in isoform 5. 1 PublicationVSP_045653Add
BLAST
Alternative sequencei417 – 521105Missing in isoform 5. 1 PublicationVSP_045654Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14147.1. [Q8N5Y2-1]
CCDS14148.1. [Q8N5Y2-5]
CCDS14149.1. [Q8N5Y2-4]
CCDS55369.1. [Q8N5Y2-3]
CCDS65213.1. [Q8N5Y2-6]
PIRiT08795.
RefSeqiNP_001180199.1. NM_001193270.2. [Q8N5Y2-3]
NP_001269103.1. NM_001282174.1. [Q8N5Y2-6]
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]
XP_006724524.1. XM_006724461.1. [Q8N5Y2-6]
UniGeneiHs.655288.

Genome annotation databases

EnsembliENST00000312196; ENSP00000312244; ENSG00000005302. [Q8N5Y2-1]
ENST00000337339; ENSP00000338078; ENSG00000005302. [Q8N5Y2-5]
ENST00000361672; ENSP00000354562; ENSG00000005302. [Q8N5Y2-6]
ENST00000380693; ENSP00000370069; ENSG00000005302. [Q8N5Y2-4]
ENST00000398527; ENSP00000381538; ENSG00000005302. [Q8N5Y2-3]
GeneIDi10943.
KEGGihsa:10943.
UCSCiuc004cuv.1. human.
uc004cuw.3. human. [Q8N5Y2-1]
uc011mig.2. human.
uc011mih.2. human. [Q8N5Y2-3]

Polymorphism databases

DMDMi32171482.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14147.1. [Q8N5Y2-1 ]
CCDS14148.1. [Q8N5Y2-5 ]
CCDS14149.1. [Q8N5Y2-4 ]
CCDS55369.1. [Q8N5Y2-3 ]
CCDS65213.1. [Q8N5Y2-6 ]
PIRi T08795.
RefSeqi NP_001180199.1. NM_001193270.2. [Q8N5Y2-3 ]
NP_001269103.1. NM_001282174.1. [Q8N5Y2-6 ]
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 ]
XP_006724524.1. XM_006724461.1. [Q8N5Y2-6 ]
UniGenei Hs.655288.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y0N X-ray 3.00 A/B/C/D 167-289 [» ]
A/B/C/D 442-518 [» ]
3OA6 X-ray 2.35 A/B 1-101 [» ]
3OB9 X-ray 2.50 A/B/C/D/E 2-93 [» ]
ProteinModelPortali Q8N5Y2.
SMRi Q8N5Y2. Positions 9-92, 171-293, 442-507.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116143. 17 interactions.
DIPi DIP-56857N.
IntActi Q8N5Y2. 5 interactions.
STRINGi 9606.ENSP00000312244.

PTM databases

PhosphoSitei Q8N5Y2.

Polymorphism databases

DMDMi 32171482.

Proteomic databases

MaxQBi Q8N5Y2.
PaxDbi Q8N5Y2.
PRIDEi Q8N5Y2.

Protocols and materials databases

DNASUi 10943.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312196 ; ENSP00000312244 ; ENSG00000005302 . [Q8N5Y2-1 ]
ENST00000337339 ; ENSP00000338078 ; ENSG00000005302 . [Q8N5Y2-5 ]
ENST00000361672 ; ENSP00000354562 ; ENSG00000005302 . [Q8N5Y2-6 ]
ENST00000380693 ; ENSP00000370069 ; ENSG00000005302 . [Q8N5Y2-4 ]
ENST00000398527 ; ENSP00000381538 ; ENSG00000005302 . [Q8N5Y2-3 ]
GeneIDi 10943.
KEGGi hsa:10943.
UCSCi uc004cuv.1. human.
uc004cuw.3. human. [Q8N5Y2-1 ]
uc011mig.2. human.
uc011mih.2. human. [Q8N5Y2-3 ]

Organism-specific databases

CTDi 10943.
GeneCardsi GC0XP011776.
HGNCi HGNC:7370. MSL3.
HPAi HPA034535.
HPA034536.
MIMi 300609. gene.
neXtProti NX_Q8N5Y2.
PharmGKBi PA164723161.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG293760.
GeneTreei ENSGT00730000111072.
HOGENOMi HOG000293161.
HOVERGENi HBG052511.
InParanoidi Q8N5Y2.
KOi K18403.
OMAi GMKFKFH.
OrthoDBi EOG7BCNBQ.
PhylomeDBi Q8N5Y2.
TreeFami TF323400.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi MSL3. human.
EvolutionaryTracei Q8N5Y2.
GenomeRNAii 10943.
NextBioi 35463804.
PROi Q8N5Y2.
SOURCEi Search...

Gene expression databases

Bgeei Q8N5Y2.
CleanExi HS_MSL3.
ExpressionAtlasi Q8N5Y2. baseline and differential.
Genevestigatori Q8N5Y2.

Family and domain databases

InterProi IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view ]
PANTHERi PTHR10880. PTHR10880. 1 hit.
Pfami PF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 2 hits.
PROSITEi PS51640. MRG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiMS3L1_HUMAN
AccessioniPrimary (citable) accession number: Q8N5Y2
Secondary accession number(s): A6NCU2
, A6NHW8, A8K165, B4DUV8, B7Z227, Q9UG70, Q9Y5Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 124 of the entry and version 1 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

Miscellaneous

MSL3L1 gene undergoes X inactivation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3