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Protein

N-lysine methyltransferase SMYD2

Gene

Smyd2

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

Functioni

Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860' (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei240 – 2401Peptide substrate; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9039MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-3214841. PKMTs methylate histone lysines.
R-RNO-6804760. Regulation of TP53 Activity through Methylation.

Names & Taxonomyi

Protein namesi
Recommended name:
N-lysine methyltransferase SMYD2 (EC:2.1.1.-)
Alternative name(s):
Histone methyltransferase SMYD2 (EC:2.1.1.43)
SET and MYND domain-containing protein 2
Gene namesi
Name:Smyd2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi727785. Smyd2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433N-lysine methyltransferase SMYD2PRO_0000218311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7M6Z3.

PTM databases

iPTMnetiQ7M6Z3.
PhosphoSiteiQ7M6Z3.

Expressioni

Gene expression databases

GenevisibleiQ7M6Z3. RN.

Interactioni

Subunit structurei

Interacts with RNA polymerase II and HELZ. Interacts with SIN3A and HDAC1. Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004783.

Structurei

3D structure databases

ProteinModelPortaliQ7M6Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 241235SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 193S-adenosyl-L-methionine bindingBy similarity
Regioni183 – 1853Peptide substrate bindingBy similarity
Regioni206 – 2072S-adenosyl-L-methionine bindingBy similarity
Regioni258 – 2603S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9039MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2084. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00530000063077.
HOGENOMiHOG000007850.
HOVERGENiHBG098536.
InParanoidiQ7M6Z3.
KOiK11426.
OMAiHPERTQS.
OrthoDBiEOG74XS68.
PhylomeDBiQ7M6Z3.
TreeFamiTF106487.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR001214. SET_dom.
IPR011990. TPR-like_helical_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50280. SET. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7M6Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAEARGGLE RFCSAGKGRG LRALRPFHVG DLLFSCPAYA CVLTVGERGH
60 70 80 90 100
HCECCFARKE GLSKCGRCKQ AFYCDVECQK EDWPLHKLEC SSMVVFGENW
110 120 130 140 150
NPSETVRLTA RILAKQKMHP ERTPSEKLLA VREFESHLDK LDNEKKDLIQ
160 170 180 190 200
SDIAALHQFY SKHLEFPDHS SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP
210 220 230 240 250
DVALMNHSCC PNVIVTYKGT LAEVRAVQEI HPGDEVFTSY IDLLYPTEDR
260 270 280 290 300
NDRLRDSYFF TCECRECTTK DKDKAKVEIR KLSNPPQAEA IRDMVRYARN
310 320 330 340 350
VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC
360 370 380 390 400
LYMQDWEGAL KYGQKIIKPY SKHYPVYSLN VASMWLKLGR LYMGLENKAA
410 420 430
GEKALKKAIA IMEIAHGKDH PYISEIKQEI ESH
Length:433
Mass (Da):49,648
Last modified:December 15, 2003 - v1
Checksum:i7CE05492B8CA1578
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BK001057 mRNA. Translation: DAA01315.1.
RefSeqiNP_996733.1. NM_206851.1.
UniGeneiRn.7052.

Genome annotation databases

EnsembliENSRNOT00000004783; ENSRNOP00000004783; ENSRNOG00000003583.
GeneIDi289372.
KEGGirno:289372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BK001057 mRNA. Translation: DAA01315.1.
RefSeqiNP_996733.1. NM_206851.1.
UniGeneiRn.7052.

3D structure databases

ProteinModelPortaliQ7M6Z3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004783.

PTM databases

iPTMnetiQ7M6Z3.
PhosphoSiteiQ7M6Z3.

Proteomic databases

PaxDbiQ7M6Z3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004783; ENSRNOP00000004783; ENSRNOG00000003583.
GeneIDi289372.
KEGGirno:289372.

Organism-specific databases

CTDi56950.
RGDi727785. Smyd2.

Phylogenomic databases

eggNOGiKOG2084. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00530000063077.
HOGENOMiHOG000007850.
HOVERGENiHBG098536.
InParanoidiQ7M6Z3.
KOiK11426.
OMAiHPERTQS.
OrthoDBiEOG74XS68.
PhylomeDBiQ7M6Z3.
TreeFamiTF106487.

Enzyme and pathway databases

ReactomeiR-RNO-3214841. PKMTs methylate histone lysines.
R-RNO-6804760. Regulation of TP53 Activity through Methylation.

Miscellaneous databases

PROiQ7M6Z3.

Gene expression databases

GenevisibleiQ7M6Z3. RN.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR001214. SET_dom.
IPR011990. TPR-like_helical_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50280. SET. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene discovery in the hamster: a comparative genomics approach for gene annotation by sequencing of hamster testis cDNAs."
    Oduru S., Campbell J.L., Karri S., Hendry W.J., Khan S.A., Williams S.C.
    BMC Genomics 4:22-22(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMYD2_RAT
AccessioniPrimary (citable) accession number: Q7M6Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: June 8, 2016
This is version 86 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.