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Protein

Histone-lysine N-methyltransferase KMT5C

Gene

Kmt5c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase KMT5CCurated (EC:2.1.1.43)
Alternative name(s):
Lysine-specific methyltransferase 5CImported
Suppressor of variegation 4-20 homolog 2
Short name:
Su(var)4-20 homolog 2
Short name:
Suv4-20h2
Gene namesi
Name:Kmt5cImported
Synonyms:Suv420h2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1305226. Kmt5c.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Histone-lysine N-methyltransferase KMT5CPRO_0000281795Add
BLAST

Proteomic databases

PaxDbiP0C2N6.
PRIDEiP0C2N6.

PTM databases

PhosphoSiteiP0C2N6.

Expressioni

Inductioni

Strongly down-regulated in various cancers such as hepatocarcinomas.2 Publications

Gene expression databases

GenevisibleiP0C2N6. RN.

Interactioni

Subunit structurei

Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023744.

Structurei

3D structure databases

ProteinModelPortaliP0C2N6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 218115SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni350 – 44394Required for heterochromatin localizationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2589. Eukaryota.
ENOG410XPH8. LUCA.
GeneTreeiENSGT00520000055640.
HOVERGENiHBG095676.
InParanoidiP0C2N6.
KOiK11429.
OMAiFCAACQP.
OrthoDBiEOG7MKW6P.
PhylomeDBiP0C2N6.
TreeFamiTF106433.

Family and domain databases

InterProiIPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C2N6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP TLRRQHHLRS
60 70 80 90 100
ALEAFLRQRD LEAAFRALTL GGWMAHYFQN RAPRQEAALK NHIFCYLRAF
110 120 130 140 150
LPESGFTILP CTRYSMETNG AKIVSTRAWK KNEKLELLVG CIAELREEDE
160 170 180 190 200
YLLRAGENDF SVMYSTRKRS AQLWLGPAAF INHDCKPNCK FVPSDGNTAC
210 220 230 240 250
VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CYTCERKGEG AFRLQPREPE
260 270 280 290 300
LRPRPLDKYE LRETKRRLQQ CLDSSQQNLL SLRACSHLSP LRPDPFCAAC
310 320 330 340 350
QPSCLLPVSP HMDYLPLWLQ WVPQPQPRVR PRKRRRRRRR RPRIPQASLS
360 370 380 390 400
PDLHTACVSL HRWGGCGPHC QLRAEAMVTL HLLPQTRWTP KQDWYWARRY
410 420 430 440 450
GLPSVVRVEL SPLAPALPAA PAPAGNLGPT PTPDLIPKQA LAFAPFCPPK
460 470
RLRLVVSHGS IDLDINSGEP
Length:470
Mass (Da):53,607
Last modified:April 3, 2007 - v1
Checksum:i060148E2FFFB49AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY724526 mRNA. No translation available.
RefSeqiNP_001100945.1. NM_001107475.1.
XP_006228321.1. XM_006228259.1.
XP_006228322.1. XM_006228260.1.
XP_006228323.1. XM_006228261.1.
XP_006228324.1. XM_006228262.2.
XP_006228325.1. XM_006228263.1.
XP_006228326.1. XM_006228264.1.
XP_006228327.1. XM_006228265.2.
XP_006228328.1. XM_006228266.1.
XP_008757145.1. XM_008758923.1.
XP_008757146.1. XM_008758924.1.
UniGeneiRn.105145.

Genome annotation databases

EnsembliENSRNOT00000023744; ENSRNOP00000023744; ENSRNOG00000017508.
GeneIDi308345.
KEGGirno:308345.
UCSCiRGD:1305226. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY724526 mRNA. No translation available.
RefSeqiNP_001100945.1. NM_001107475.1.
XP_006228321.1. XM_006228259.1.
XP_006228322.1. XM_006228260.1.
XP_006228323.1. XM_006228261.1.
XP_006228324.1. XM_006228262.2.
XP_006228325.1. XM_006228263.1.
XP_006228326.1. XM_006228264.1.
XP_006228327.1. XM_006228265.2.
XP_006228328.1. XM_006228266.1.
XP_008757145.1. XM_008758923.1.
XP_008757146.1. XM_008758924.1.
UniGeneiRn.105145.

3D structure databases

ProteinModelPortaliP0C2N6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023744.

PTM databases

PhosphoSiteiP0C2N6.

Proteomic databases

PaxDbiP0C2N6.
PRIDEiP0C2N6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023744; ENSRNOP00000023744; ENSRNOG00000017508.
GeneIDi308345.
KEGGirno:308345.
UCSCiRGD:1305226. rat.

Organism-specific databases

CTDi84787.
RGDi1305226. Kmt5c.

Phylogenomic databases

eggNOGiKOG2589. Eukaryota.
ENOG410XPH8. LUCA.
GeneTreeiENSGT00520000055640.
HOVERGENiHBG095676.
InParanoidiP0C2N6.
KOiK11429.
OMAiFCAACQP.
OrthoDBiEOG7MKW6P.
PhylomeDBiP0C2N6.
TreeFamiTF106433.

Miscellaneous databases

NextBioi658668.
PROiP0C2N6.

Gene expression databases

GenevisibleiP0C2N6. RN.

Family and domain databases

InterProiIPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Methyl deficiency, alterations in global histone modifications, and carcinogenesis."
    Pogribny I.P., Tryndyak V.P., Muskhelishvili L., Rusyn I., Ross S.A.
    J. Nutr. 137:216S-222S(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  3. "Histone H3 lysine 9 and H4 lysine 20 trimethylation and the expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in hepatocarcinogenesis induced by methyl deficiency in rats."
    Pogribny I.P., Ross S.A., Tryndyak V.P., Pogribna M., Poirier L.A., Karpinets T.V.
    Carcinogenesis 27:1180-1186(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiKMT5C_RAT
AccessioniPrimary (citable) accession number: P0C2N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: May 11, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.