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Protein

Histone H2A deubiquitinase MYSM1

Gene

MYSM1

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

Functioni

Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi656 – 6561Zinc; catalyticBy similarity
Metal bindingi658 – 6581Zinc; catalyticBy similarity
Metal bindingi669 – 6691Zinc; catalyticCurated

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • histone binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • metallopeptidase activity Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • chromatin remodeling Source: UniProtKB
  • monoubiquitinated histone H2A deubiquitination Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of cell migration Source: Ensembl
  • regulation of hair follicle development Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Protein family/group databases

MEROPSiM67.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A deubiquitinase MYSM1 (EC:3.4.19.-)
Short name:
2A-DUB
Alternative name(s):
Myb-like, SWIRM and MPN domain-containing protein 1
Gene namesi
Name:MYSM1
Synonyms:KIAA1915
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29401. MYSM1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi669 – 6691D → N: Abolishes H2A deubiquitination. 1 Publication

Organism-specific databases

PharmGKBiPA142671301.

Polymorphism and mutation databases

BioMutaiMYSM1.
DMDMi74756898.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 828828Histone H2A deubiquitinase MYSM1PRO_0000234073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei236 – 2361PhosphothreonineCombined sources
Modified residuei340 – 3401PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5VVJ2.
MaxQBiQ5VVJ2.
PaxDbiQ5VVJ2.
PRIDEiQ5VVJ2.

PTM databases

iPTMnetiQ5VVJ2.
PhosphoSiteiQ5VVJ2.

Expressioni

Gene expression databases

BgeeiQ5VVJ2.
CleanExiHS_MYSM1.
GenevisibleiQ5VVJ2. HS.

Organism-specific databases

HPAiHPA054291.

Interactioni

Subunit structurei

Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Binds histones.1 Publication

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125363. 13 interactions.
DIPiDIP-58941N.
STRINGi9606.ENSP00000418734.

Structurei

Secondary structure

1
828
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 13513Combined sources
Helixi140 – 1478Combined sources
Beta strandi148 – 1503Combined sources
Helixi152 – 16615Combined sources
Helixi388 – 3914Combined sources
Helixi395 – 3984Combined sources
Helixi406 – 42318Combined sources
Helixi430 – 4323Combined sources
Turni433 – 4375Combined sources
Beta strandi438 – 4414Combined sources
Helixi443 – 45614Combined sources
Beta strandi457 – 4604Combined sources
Beta strandi466 – 4683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU7NMR-A117-181[»]
2DCENMR-A367-470[»]
ProteinModelPortaliQ5VVJ2.
SMRiQ5VVJ2. Positions 119-181, 367-470, 577-694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5VVJ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 16752SANTPROSITE-ProRule annotationAdd
BLAST
Domaini372 – 47099SWIRMPROSITE-ProRule annotationAdd
BLAST
Domaini572 – 682111MPNAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi656 – 66914JAMM motifAdd
BLAST
Motifi774 – 7785LXXLL motif

Domaini

Binds double-stranded DNA via the SANT domain. The SWIRM domain does not bind double-stranded DNA.

Sequence similaritiesi

Belongs to the peptidase M67A family. MYSM1 subfamily.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated
Contains 1 SANT domain.PROSITE-ProRule annotation
Contains 1 SWIRM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1279. Eukaryota.
KOG1555. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00530000063766.
HOVERGENiHBG079486.
InParanoidiQ5VVJ2.
KOiK11865.
OMAiIPWTLDN.
OrthoDBiEOG7P8P96.
PhylomeDBiQ5VVJ2.
TreeFamiTF324811.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR000555. JAMM/MPN+_dom.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VVJ2-1) [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
MAAEEADVDI EGDVVAAAGA QPGSGENTAS VLQKDHYLDS SWRTENGLIP
60 70 80 90 100
WTLDNTISEE NRAVIEKMLL EEEYYLSKKS QPEKVWLDQK EDDKKYMKSL
110 120 130 140 150
QKTAKIMVHS PTKPASYSVK WTIEEKELFE QGLAKFGRRW TKISKLIGSR
160 170 180 190 200
TVLQVKSYAR QYFKNKVKCG LDKETPNQKT GHNLQVKNED KGTKAWTPSC
210 220 230 240 250
LRGRADPNLN AVKIEKLSDD EEVDITDEVD ELSSQTPQKN SSSDLLLDFP
260 270 280 290 300
NSKMHETNQG EFITSDSQEA LFSKSSRGCL QNEKQDETLS SSEITLWTEK
310 320 330 340 350
QSNGDKKSIE LNDQKFNELI KNCNKHDGRG IIVDARQLPS PEPCEIQKNL
360 370 380 390 400
NDNEMLFHSC QMVEESHEEE ELKPPEQEIE IDRNIIQEEE KQAIPEFFEG
410 420 430 440 450
RQAKTPERYL KIRNYILDQW EICKPKYLNK TSVRPGLKNC GDVNCIGRIH
460 470 480 490 500
TYLELIGAIN FGCEQAVYNR PQTVDKVRIR DRKDAVEAYQ LAQRLQSMRT
510 520 530 540 550
RRRRVRDPWG NWCDAKDLEG QTFEHLSAEE LAKRREEEKG RPVKSLKVPR
560 570 580 590 600
PTKSSFDPFQ LIPCNFFSEE KQEPFQVKVA SEALLIMDLH AHVSMAEVIG
610 620 630 640 650
LLGGRYSEVD KVVEVCAAEP CNSLSTGLQC EMDPVSQTQA SETLAVRGFS
660 670 680 690 700
VIGWYHSHPA FDPNPSLRDI DTQAKYQSYF SRGGAKFIGM IVSPYNRNNP
710 720 730 740 750
LPYSQITCLV ISEEISPDGS YRLPYKFEVQ QMLEEPQWGL VFEKTRWIIE
760 770 780 790 800
KYRLSHSSVP MDKIFRRDSD LTCLQKLLEC MRKTLSKVTN CFMAEEFLTE
810 820
IENLFLSNYK SNQENGVTEE NCTKELLM
Note: No experimental confirmation available.
Length:828
Mass (Da):95,032
Last modified:December 7, 2004 - v1
Checksum:i9EE635A30AF3B089
GO
Isoform 2 (identifier: Q5VVJ2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-253: Missing.

Note: No experimental confirmation available.
Show »
Length:575
Mass (Da):66,421
Checksum:iEC1B07CACB78B111
GO
Isoform 3 (identifier: Q5VVJ2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-594: Missing.

Show »
Length:234
Mass (Da):26,716
Checksum:iB9F47C517543A052
GO

Sequence cautioni

The sequence BAB67808.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG54377.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311E → G in BAG54377 (PubMed:14702039).Curated
Sequence conflicti540 – 5401G → D in BAG54377 (PubMed:14702039).Curated
Sequence conflicti782 – 7821R → G in CAH18287 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001C → S.
Corresponds to variant rs17118103 [ dbSNP | Ensembl ].
VAR_051814
Natural varianti264 – 2641T → A.2 Publications
Corresponds to variant rs12139511 [ dbSNP | Ensembl ].
VAR_051815
Natural varianti825 – 8251E → K.
Corresponds to variant rs232777 [ dbSNP | Ensembl ].
VAR_051816

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 594594Missing in isoform 3. 2 PublicationsVSP_018210Add
BLAST
Alternative sequencei1 – 253253Missing in isoform 2. 1 PublicationVSP_018211Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067502 mRNA. Translation: BAB67808.1. Different initiation.
AK126835 mRNA. Translation: BAG54377.1. Different initiation.
AK292919 mRNA. Translation: BAF85608.1.
BX537912 mRNA. Translation: CAD97896.1.
CR627323 mRNA. Translation: CAH10370.1.
CR749450 mRNA. Translation: CAH18287.1.
AL450024, AL035411 Genomic DNA. Translation: CAH70737.1.
AL035411, AL450024 Genomic DNA. Translation: CAI21908.1.
CCDSiCCDS41343.1. [Q5VVJ2-1]
RefSeqiNP_001078956.1. NM_001085487.2. [Q5VVJ2-1]
UniGeneiHs.744921.

Genome annotation databases

EnsembliENST00000472487; ENSP00000418734; ENSG00000162601. [Q5VVJ2-1]
ENST00000622766; ENSP00000478391; ENSG00000162601. [Q5VVJ2-3]
GeneIDi114803.
KEGGihsa:114803.
UCSCiuc001cza.4. human. [Q5VVJ2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067502 mRNA. Translation: BAB67808.1. Different initiation.
AK126835 mRNA. Translation: BAG54377.1. Different initiation.
AK292919 mRNA. Translation: BAF85608.1.
BX537912 mRNA. Translation: CAD97896.1.
CR627323 mRNA. Translation: CAH10370.1.
CR749450 mRNA. Translation: CAH18287.1.
AL450024, AL035411 Genomic DNA. Translation: CAH70737.1.
AL035411, AL450024 Genomic DNA. Translation: CAI21908.1.
CCDSiCCDS41343.1. [Q5VVJ2-1]
RefSeqiNP_001078956.1. NM_001085487.2. [Q5VVJ2-1]
UniGeneiHs.744921.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU7NMR-A117-181[»]
2DCENMR-A367-470[»]
ProteinModelPortaliQ5VVJ2.
SMRiQ5VVJ2. Positions 119-181, 367-470, 577-694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125363. 13 interactions.
DIPiDIP-58941N.
STRINGi9606.ENSP00000418734.

Protein family/group databases

MEROPSiM67.005.

PTM databases

iPTMnetiQ5VVJ2.
PhosphoSiteiQ5VVJ2.

Polymorphism and mutation databases

BioMutaiMYSM1.
DMDMi74756898.

Proteomic databases

EPDiQ5VVJ2.
MaxQBiQ5VVJ2.
PaxDbiQ5VVJ2.
PRIDEiQ5VVJ2.

Protocols and materials databases

DNASUi114803.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000472487; ENSP00000418734; ENSG00000162601. [Q5VVJ2-1]
ENST00000622766; ENSP00000478391; ENSG00000162601. [Q5VVJ2-3]
GeneIDi114803.
KEGGihsa:114803.
UCSCiuc001cza.4. human. [Q5VVJ2-1]

Organism-specific databases

CTDi114803.
GeneCardsiMYSM1.
H-InvDBHIX0000634.
HGNCiHGNC:29401. MYSM1.
HPAiHPA054291.
MIMi612176. gene.
neXtProtiNX_Q5VVJ2.
PharmGKBiPA142671301.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1279. Eukaryota.
KOG1555. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00530000063766.
HOVERGENiHBG079486.
InParanoidiQ5VVJ2.
KOiK11865.
OMAiIPWTLDN.
OrthoDBiEOG7P8P96.
PhylomeDBiQ5VVJ2.
TreeFamiTF324811.

Miscellaneous databases

EvolutionaryTraceiQ5VVJ2.
GenomeRNAii114803.
PROiQ5VVJ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VVJ2.
CleanExiHS_MYSM1.
GenevisibleiQ5VVJ2. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR000555. JAMM/MPN+_dom.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-264.
    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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-828 (ISOFORM 1), VARIANT ALA-264.
    Tissue: Trachea.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133 (ISOFORM 1).
    Tissue: Fetal skin and Liver.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
    Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
    Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN COMPLEX, MUTAGENESIS OF ASP-669.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-218 AND THR-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: STRUCTURE BY NMR OF 117-181 AND OF 367-470, INTERACTION WITH DNA.

Entry informationi

Entry nameiMYSM1_HUMAN
AccessioniPrimary (citable) accession number: Q5VVJ2
Secondary accession number(s): A8KA54
, B3KX65, Q68DD3, Q6AI53, Q7Z3G8, Q96PX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 7, 2004
Last modified: June 8, 2016
This is version 129 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.