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Reviewed, UniProtKB/Swiss-Prot A6QPM3 (PRDM6_BOVIN)

Last modified November 3, 2009. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative histone-lysine N-methyltransferase PRDM6
    EC=2.1.1.43
Alternative name(s):
    PR domain zinc finger protein 6
    PR domain-containing protein 6
Gene names
Name: PRDM6
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Putative histone methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. Promotes the transition from differentiated to proliferative smooth muscle by suppressing differentiation and maintaining the proliferative potential of vascular smooth muscle cells. Also plays a role in endothelial cells by inhibiting endothelial cell proliferation, survival and differentiation. It is unclear whether it has histone methyltransferase activity in vivo. According to some authors, it does not act as a histone methyltransferase by itself and represses transcription by recruiting EHMT2/G9a. According to others, it possesses histone methyltransferase activity when associated with other proteins and specifically methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' methylation represents a specific tag for epigenetic transcriptional repression By similarity.

Catalytic activity

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine.

Subunit structure

Interacts with HDAC1, HDAC2, HDAC3, CBX1 and EP300 By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 4 C2H2-type zinc fingers.

Contains 1 SET domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Putative histone-lysine N-methyltransferase PRDM6
PRO_0000363958

Regions

Domain242 – 364123SET
Zinc finger468 – 49023C2H2-type 1; degenerate
Zinc finger496 – 51823C2H2-type 2
Zinc finger524 – 54623C2H2-type 3
Zinc finger552 – 57423C2H2-type 4; degenerate
Compositional bias30 – 334Poly-Gly
Compositional bias43 – 7028Pro-rich
Compositional bias94 – 10613Poly-Ala
Compositional bias223 – 2275Poly-Ala

Sequences

Sequence LengthMass (Da)Tools
A6QPM3-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: B7D55FF617059231

FASTA59063,989
        10         20         30         40         50         60 
MLKPGDPGGS AFLKVDPAYL QHWQQLFPHG GGGPLKGGGA AGPLGAPQPL QPPPPPERAE 

        70         80         90        100        110        120 
PQPDSLRPRP ASLSSASSTP ASSSTSASSA SSCAAAAAAA AAAALAGLSA LPVAQLPVFA 

       130        140        150        160        170        180 
PLATVAAEPL PPKDLCLGAT SGPGPSKCGG SGGDGRGVPR FRCSAEELDY YLYGQQRMEI 

       190        200        210        220        230        240 
IPLNQHTSDP NNRCDMCADN RNGECPMHGP LHSLRRLVGT SSAAAAAPPP ELPEWLRDLP 

       250        260        270        280        290        300 
REVCLCTSTV PGLAYGICAA QRIQQGTWIG PFQGVLLPPE KVQAGAVRNT QHLWEIYDQD 

       310        320        330        340        350        360 
GTLQHFIDGG EPSKSSWMRY IRCARHCGEQ NLTVVQYRSN IFYRACIDIP RGTELLVWYN 

       370        380        390        400        410        420 
DSYTSFFGIP LQCIAQDENL NVPSTVMEAM CRQDALQPFN KSSKLSQAPQ QRSVVFPQTP 

       430        440        450        460        470        480 
CGRNFSLLDK SGPLESGFNQ ISVKNQRVLA SPTSTSQLHS EFSDWHLWKC GQCFKTFTQR 

       490        500        510        520        530        540 
ILLQMHVCTQ NPDRPYQCGH CSQSFSQPSE LRNHVVTHSS DRPFKCGYCG RAFAGATTLN 

       550        560        570        580        590 
NHIRTHTGEK PFKCERCERS FTQATQLSRH QRMPNECKPI TESPESIEVD 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal spinal cord.

Cross-references

Sequence databases

BC149387 mRNA. Translation: AAI49388.1.
IPIIPI00715269.
RefSeqNP_001096725.1.
UniGeneBt.36375

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSBTAT00000027421; ENSBTAP00000027421; ENSBTAG00000020578; Bos taurus. [Genome view]
GeneID519857.
KEGGbta:519857.

Organism-specific databases

CTD519857.

Phylogenomic databases

OMALQPFSKS.

Family and domain databases

InterProIPR001214. SET.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 2 hits.
PfamPF00856. SET. 1 hit.
PF00096. zf-C2H2. 3 hits.
[Graphical view]
SMARTSM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEPS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRDM6_BOVIN
AccessionPrimary (citable) accession number: A6QPM3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: August 21, 2007
Last modified: November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents