Histone H2A deubiquitinase MYSM1 - Branchiostoma floridae (Florida lancelet)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Histone H2A deubiquitinase MYSM1
Short name=2A-DUB
EC=3.4.19.-

Alternative name(s):
Myb-like, SWIRM and MPN domain-containing protein 1

Gene names

Name:	MYSM1
ORF Names:	BRAFLDRAFT_86936

Organism

Branchiostoma floridae (Florida lancelet) (Amphioxus)

Taxonomic identifier

7739 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Cephalochordata › Branchiostomidae › Branchiostoma

Protein attributes

Sequence length	809 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity.
Subcellular location	Nucleus By similarity.
Domain	Binds double-stranded DNA via the SANT domain. The SWIRM domain does not bind double-stranded DNA By similarity.
Sequence similarities	Belongs to the peptidase M67A family. MYSM1 subfamily. Contains 1 MPN (JAB/Mov34) domain. Contains 1 SANT domain. Contains 1 SWIRM domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histone deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin remodeling complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone binding Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 809

809

Histone H2A deubiquitinase MYSM1

PRO_0000373927

Regions

Domain

33 – 78

46

SANT

Domain

410 – 508

99

SWIRM

Domain

587 – 692

106

MPN

Motif

671 – 684

14

JAMM motif

Sites

Metal binding

671

1

Zinc; catalytic By similarity

Metal binding

673

1

Zinc; catalytic By similarity

Metal binding

684

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

B6MUN4 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 2A061E4A36A0893E
Show »

FASTA

809

90,132

        10         20         30         40         50         60 
MADDEEIDIE GDDDAPLLFD HKDDALALPD LPGYEPNWMF DHGQEIYGRS WTSISQFVQT 

        70         80         90        100        110        120 
RTPLQVKNYA RHFFKTKVVQ KVEEGEDEDV DIEGEESGEE AVMELRSTCG LNPAQPAVVT 

       130        140        150        160        170        180 
SDDTSTGENV MEETEAVTED HPSLDNLVQD DREMPQQETT GDGEQYPMDE HFLPVFPWQP 

       190        200        210        220        230        240 
DDTQNRVIVE RIEGSVGLGS VRGDKDVRPV PGVEQNTYGP HTDMFQVQNT LLAFEKQVGA 

       250        260        270        280        290        300 
DRIFEGPSXS KNEATDTQTE VSETKTEVIE RQTESQVDAT HMHTYGDGLM GSIERLTESV 

       310        320        330        340        350        360 
SSSELKEDLK TGIEYVEKDD ATDSSSTAKG YDNYTLDHPE DRSKPDSVVS EKWSCEEAMS 

       370        380        390        400        410        420 
SHTDGRTFSD SDSGKETYDL PRYNTTIFQG HSEDETSDAG QAEEETFFTF KKPTEEVVLD 

       430        440        450        460        470        480 
RSVITEEEKE VHKEFFDGRQ TKTPERYLKI RNHLLDCWER TKPEYLRKTV ARAGLRNCGD 

       490        500        510        520        530        540 
VNCIGRIHGY LERIGAINFG CEEANRGEFP VAKVGVKRNP QGHGEQLALQ AARLESMHVT 

       550        560        570        580        590        600 
SDELEKQDGG VSQIRPNRSR AARTNLNSFS YDPFKLVPCK RFSEESPAPF SVKIHATALV 

       610        620        630        640        650        660 
TIDMHAHIST AEVIGLLGGV FHRDPGALEV ASAEPCNSLS TGMQCEMDPV SQTQASEALS 

       670        680        690        700        710        720 
QAGYSVVGWY HSHPTFAPNP SVRDIETQTK FQEWFAQGGS PFIGIIVNPY SSTRISPLSR 

       730        740        750        760        770        780 
VTCLTISSEW NPPAIQRVKL LSRYAGHTDT TYMDKMLYSL SGHLCRGNAD SDEDGNSESL 

       790        800 
TLLTDIRDIF ANSWTSSLGT TPRSSIASL

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References

[1]

"The amphioxus genome and the evolution of the chordate karyotype."
Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J.

Rokhsar D.S.
Nature 453:1064-1071(2008) [PubMed: 18563158] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S238N-H82.
Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ABEP02030881 Genomic DNA. No translation available. ABEP02030882 Genomic DNA. No translation available. ABEP02030884 Genomic DNA. No translation available.
3D structure databases
ProteinModelPortal	B6MUN4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR009057. Homeodomain-like. IPR000555. Mov34_MPN_PAD1. IPR001005. SANT_DNA-bd. IPR007526. SWIRM. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF01398. Mov34. 1 hit. PF04433. SWIRM. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. SM00717. SANT. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 2 hits.
PROSITE	PS51293. SANT. False negative. PS50934. SWIRM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MYSM1_BRAFL

Accession

Primary (citable) accession number: B6MUN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	December 16, 2008
Last modified:	November 16, 2011
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents