SMYD2

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'.6 Publications

Catalytic activityⁱ

L-lysyl-[histone]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁶-methyl-L-lysyl-[histone]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase."
  Abu-Farha M., Lambert J.P., Al-Madhoun A.S., Elisma F., Skerjanc I.S., Figeys D.
  Mol. Cell. Proteomics 7:560-572(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EPB41L3; HSP90AA1 AND TP53.
- Ref.12
  "Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation."
  Wang L., Li L., Zhang H., Luo X., Dai J., Zhou S., Gu J., Zhu J., Atadja P., Lu C., Li E., Zhao K.
  J. Biol. Chem. 286:38725-38737(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH TP53/P53 PEPTIDE; S-ADENOSYL-L-METHIONINE AND ZINC IONS, FUNCTION IN P53/TP53 METHYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-187; GLU-189; GLU-190; TYR-245; ASP-252; ARG-253; ARG-306; TYR-374; GLU-429 AND GLU-431.
- Ref.13
  "Structural basis of substrate methylation and inhibition of SMYD2."
  Ferguson A.D., Larsen N.A., Howard T., Pollard H., Green I., Grande C., Cheung T., Garcia-Arenas R., Cowen S., Wu J., Godin R., Chen H., Keen N.
  Structure 19:1262-1273(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH P53/TP53 PEPTIDE; S-ADENOSYL-L-METHIONINE; SYNTHETIC INHIBITOR AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-240.
EC:
2.1.1.43
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase."
  Abu-Farha M., Lambert J.P., Al-Madhoun A.S., Elisma F., Skerjanc I.S., Figeys D.
  Mol. Cell. Proteomics 7:560-572(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EPB41L3; HSP90AA1 AND TP53.
- Ref.12
  "Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation."
  Wang L., Li L., Zhang H., Luo X., Dai J., Zhou S., Gu J., Zhu J., Atadja P., Lu C., Li E., Zhao K.
  J. Biol. Chem. 286:38725-38737(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH TP53/P53 PEPTIDE; S-ADENOSYL-L-METHIONINE AND ZINC IONS, FUNCTION IN P53/TP53 METHYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-187; GLU-189; GLU-190; TYR-245; ASP-252; ARG-253; ARG-306; TYR-374; GLU-429 AND GLU-431.
- Ref.13
  "Structural basis of substrate methylation and inhibition of SMYD2."
  Ferguson A.D., Larsen N.A., Howard T., Pollard H., Green I., Grande C., Cheung T., Garcia-Arenas R., Cowen S., Wu J., Godin R., Chen H., Keen N.
  Structure 19:1262-1273(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH P53/TP53 PEPTIDE; S-ADENOSYL-L-METHIONINE; SYNTHETIC INHIBITOR AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-240.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
L-lysyl-[histone]
L-lysine residue
zoom
+
S-adenosyl-L-methionine
zoom
=
H⁺
+
N⁶-methyl-L-lysyl-[histone]
N⁶-methyl-L-lysine residue
zoom
+
S-adenosyl-L-homocysteine
zoom

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	137	S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication		1
Binding siteⁱ	240	Peptide substrate; via carbonyl oxygen		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	52 – 90	MYND-typePROSITE-ProRule annotationAdd BLAST		39

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, Methyltransferase, Transferase
Biological process	Transcription, Transcription regulation
Ligand	Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3214841 PKMTs methylate histone lysines R-HSA-6804760 Regulation of TP53 Activity through Methylation

Reactomeⁱ

R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-6804760 Regulation of TP53 Activity through Methylation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: N-lysine methyltransferase SMYD2 (EC:2.1.1.-) Alternative name(s): HSKM-B Histone methyltransferase SMYD2 (EC:2.1.1.43) Lysine N-methyltransferase 3C SET and MYND domain-containing protein 2
Gene namesⁱ	Name:SMYD2 Synonyms:KMT3C
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000143499.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:20982 SMYD2
MIMⁱ	610663 gene
neXtProtⁱ	NX_Q9NRG4

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	187	E → K: Abolishes methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	189	E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	190	E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	207	H → A: Abolishes methyltransferase activity. 1 Publication	1
Mutagenesisⁱ	240	Y → F: Abolishes methyltransferase activity. 2 Publications	1
Mutagenesisⁱ	245	Y → F: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	252	D → R: Slightly reduces methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	253	R → Q: No effect on methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	306	R → E: No effect on methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	374	Y → A: Abolishes methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	429	E → K: Reduces methyltransferase activity on p53/TP53. 1 Publication	1
Mutagenesisⁱ	431	E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	56950
Open Targets More...OpenTargetsⁱ	ENSG00000143499
PharmGKBⁱ	PA134930268

Chemistry databases

ChEMBLⁱ	CHEMBL2169716
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2714

Polymorphism and mutation databases

BioMutaⁱ	SMYD2
DMDMⁱ	90185234

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000218309	1 – 433	N-lysine methyltransferase SMYD2Add BLAST		433

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	283	PhosphoserineCombined sources		1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q9NRG4
jPOSTⁱ	Q9NRG4
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9NRG4
PaxDbⁱ	Q9NRG4
PeptideAtlas More...PeptideAtlasⁱ	Q9NRG4
PRIDEⁱ	Q9NRG4
ProteomicsDBⁱ	82355

PTM databases

iPTMnetⁱ	Q9NRG4
PhosphoSitePlusⁱ	Q9NRG4

Expressionⁱ

Inductionⁱ

Expression is repressed by CEBPA.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000143499 Expressed in 227 organ(s), highest expression level in left ventricle myocardium
ExpressionAtlasⁱ	Q9NRG4 baseline and differential
Genevisibleⁱ	Q9NRG4 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA029023

HPAⁱ

HPA029023

Interactionⁱ

Subunit structureⁱ

Interacts with RNA polymerase II and HELZ. Interacts with SIN3A and HDAC1 (By similarity). Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1.By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
TP53	P04637	6	EBI-1055671,EBI-366083

With

Entry

#Exp.

IntAct

Notes

TP53

P04637

6

EBI-1055671,EBI-366083

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	121274, 27 interactors
Database of interacting proteins More...DIPⁱ	DIP-50202N
IntActⁱ	Q9NRG4, 6 interactors
Molecular INTeraction database More...MINTⁱ	Q9NRG4
STRINGⁱ	9606.ENSP00000355924

Chemistry databases

BindingDBⁱ

Q9NRG4

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	1 – 4	Combined sources	4
Turnⁱ	5 – 8	Combined sources	4
Beta strandⁱ	9 – 14	Combined sources	6
Turnⁱ	15 – 17	Combined sources	3
Beta strandⁱ	18 – 25	Combined sources	8
Beta strandⁱ	32 – 37	Combined sources	6
Beta strandⁱ	39 – 43	Combined sources	5
Helixⁱ	45 – 47	Combined sources	3
Turnⁱ	48 – 50	Combined sources	3
Turnⁱ	53 – 55	Combined sources	3
Turnⁱ	66 – 68	Combined sources	3
Beta strandⁱ	72 – 75	Combined sources	4
Helixⁱ	76 – 86	Combined sources	11
Turnⁱ	87 – 89	Combined sources	3
Helixⁱ	90 – 96	Combined sources	7
Helixⁱ	97 – 99	Combined sources	3
Helixⁱ	104 – 118	Combined sources	15
Helixⁱ	124 – 126	Combined sources	3
Beta strandⁱ	127 – 129	Combined sources	3
Helixⁱ	131 – 133	Combined sources	3
Helixⁱ	138 – 140	Combined sources	3
Helixⁱ	143 – 164	Combined sources	22
Helixⁱ	169 – 182	Combined sources	14
Beta strandⁱ	184 – 187	Combined sources	4
Beta strandⁱ	193 – 198	Combined sources	6
Helixⁱ	200 – 203	Combined sources	4
Beta strandⁱ	205 – 207	Combined sources	3
Beta strandⁱ	212 – 218	Combined sources	7
Beta strandⁱ	221 – 228	Combined sources	8
Beta strandⁱ	235 – 238	Combined sources	4
Beta strandⁱ	243 – 245	Combined sources	3
Helixⁱ	247 – 258	Combined sources	12
Helixⁱ	265 – 269	Combined sources	5
Helixⁱ	273 – 276	Combined sources	4
Helixⁱ	288 – 305	Combined sources	18
Turnⁱ	309 – 311	Combined sources	3
Helixⁱ	318 – 329	Combined sources	12
Helixⁱ	337 – 353	Combined sources	17
Helixⁱ	356 – 373	Combined sources	18
Helixⁱ	379 – 394	Combined sources	16
Helixⁱ	398 – 415	Combined sources	18
Turnⁱ	416 – 419	Combined sources	4
Helixⁱ	421 – 432	Combined sources	12

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3RIB	X-ray	2.79	A/B	1-433	[»]
	3S7B	X-ray	2.42	A	1-433	[»]
	3S7D	X-ray	2.30	A	1-433	[»]
	3S7F	X-ray	2.85	A	1-433	[»]
	3S7J	X-ray	3.04	A	1-433	[»]
	3TG4	X-ray	2.00	A	1-433	[»]
	3TG5	X-ray	2.30	A	1-433	[»]
	4O6F	X-ray	2.82	A	1-433	[»]
	4WUY	X-ray	1.63	A	1-433	[»]
	4YND	X-ray	2.79	A	1-433	[»]
	5ARF	X-ray	1.92	A	2-433	[»]
	5ARG	X-ray	1.99	A	2-433	[»]
	5KJK	X-ray	1.93	A	5-433	[»]
	5KJL	X-ray	2.70	A	5-433	[»]
	5KJM	X-ray	2.19	A	5-433	[»]
	5KJN	X-ray	2.72	A	5-433	[»]
	5V3H	X-ray	2.69	A	1-433	[»]
	5WCG	X-ray	2.02	A	1-433	[»]
	6CBX	X-ray	1.94	A/B	1-433	[»]
	6CBY	X-ray	2.55	A/B	1-433	[»]
	6MON	X-ray	2.71	A/B	5-433	[»]
ProteinModelPortalⁱ	Q9NRG4
SMRⁱ	Q9NRG4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	7 – 241	SETPROSITE-ProRule annotationAdd BLAST		235

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	17 – 19	S-adenosyl-L-methionine binding	3
Regionⁱ	183 – 185	Peptide substrate binding	3
Regionⁱ	206 – 207	S-adenosyl-L-methionine binding	2
Regionⁱ	258 – 260	S-adenosyl-L-methionine binding	3

Sequence similaritiesⁱ

Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	52 – 90	MYND-typePROSITE-ProRule annotationAdd BLAST		39

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG2084 Eukaryota COG2940 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000157082
HOGENOMⁱ	HOG000007850
HOVERGENⁱ	HBG098536
InParanoidⁱ	Q9NRG4
KEGG Orthology (KO) More...KOⁱ	K11426
OMAⁱ	AVQEIHP
Database of Orthologous Groups More...OrthoDBⁱ	981799at2759
PhylomeDBⁱ	Q9NRG4
TreeFamⁱ	TF106487

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR001214 SET_dom IPR011990 TPR-like_helical_dom_sf IPR002893 Znf_MYND
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00856 SET, 1 hit PF01753 zf-MYND, 1 hit
SMARTⁱ	View protein in SMART SM00317 SET, 1 hit
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
PROSITEⁱ	View protein in PROSITE PS50280 SET, 1 hit PS01360 ZF_MYND_1, 1 hit PS50865 ZF_MYND_2, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: Q9NRG4-1) [UniParc]FASTA Add 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
MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN 
        60         70         80         90        100
HCEYCFTRKE GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW 
       110        120        130        140        150
NPSETVRLTA RILAKQKIHP ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ 
       160        170        180        190        200
SDIAALHHFY SKHLGFPDND SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP 
       210        220        230        240        250
DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY IDLLYPTEDR 
       260        270        280        290        300
NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN 
       310        320        330        340        350
VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC 
       360        370        380        390        400
LYMQDWEGAL QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA 
       410        420        430 
GEKALKKAIA IMEVAHGKDH PYISEIKQEI ESH

Length:433

Mass (Da):49,688

Last modified:September 13, 2005 - v2

Checksum:ⁱ3EEA5B8417870F5D

GO

Isoform 2 (identifier: Q9NRG4-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
273-433: Missing.

« Hide

        10         20         30         40         50
MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN 
        60         70         80         90        100
HCEYCFTRKE GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW 
       110        120        130        140        150
NPSETVRLTA RILAKQKIHP ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ 
       160        170        180        190        200
SDIAALHHFY SKHLGFPDND SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP 
       210        220        230        240        250
DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY IDLLYPTEDR 
       260        270 
NDRLRDSYFF TCECQECTTK DK

Note: No experimental confirmation available.

Show »

Length:272

Mass (Da):30,964

Checksum:ⁱF6A2B20624CED9C4

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	B0R0U3	B0R0U3_HUMAN		N-lysine methyltransferase SMYD2 N-lysine methyltransferase SMYD2	SMYD2	98	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_023442	165	G → E3 PublicationsCorresponds to variant dbSNP:rs1134647Ensembl.		1
Natural variantⁱVAR_052991	430	I → M. Corresponds to variant dbSNP:rs11120301Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_056005	273 – 433	Missing in isoform 2. 1 PublicationAdd BLAST		161

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF226053 mRNA Translation: AAF86953.1 AK313868 mRNA Translation: BAG36596.1 AL929236 Genomic DNA No translation available. BC017080 mRNA Translation: AAH17080.2 BC098276 mRNA Translation: AAH98276.1 BC098133 mRNA Translation: AAH98133.1 BC098305 mRNA Translation: AAH98305.1 BC098335 mRNA Translation: AAH98335.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS31022.1 [Q9NRG4-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_064582.2, NM_020197.2 [Q9NRG4-1]
UniGeneⁱ	Hs.66170

Genome annotation databases

Ensemblⁱ	ENST00000366957; ENSP00000355924; ENSG00000143499 [Q9NRG4-1]
GeneIDⁱ	56950
KEGGⁱ	hsa:56950
UCSC genome browser More...UCSCⁱ	uc057pjy.1 human [Q9NRG4-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
Q9NRG4	Isoform 2 of N-lysine methyltransferase SMYD2		HUMAN		272	UniRef100_Q9NRG4
UPI00062CAFFF		HUMAN		461

Protein	Similar proteins		Species	Score	Length	Source
Q9NRG4	Isoform 2 of N-lysine methyltransferase SMYD2		HUMAN		272	UniRef90_Q9NRG4
UPI0005F44378		COLAP		566
UPI00062CAFFF		HUMAN		461

Protein	Similar proteins		Species	Score	Length	Source
Q9NRG4	Isoform 2 of N-lysine methyltransferase SMYD2		HUMAN		272	UniRef50_Q9NRG4
Uncharacterized protein		COLAP		429
Uncharacterized protein		POEFO		436
Uncharacterized protein		POERE		499
Uncharacterized protein		sailfin molly		435
+206

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF226053 mRNA Translation: AAF86953.1 AK313868 mRNA Translation: BAG36596.1 AL929236 Genomic DNA No translation available. BC017080 mRNA Translation: AAH17080.2 BC098276 mRNA Translation: AAH98276.1 BC098133 mRNA Translation: AAH98133.1 BC098305 mRNA Translation: AAH98305.1 BC098335 mRNA Translation: AAH98335.1
CCDSⁱ	CCDS31022.1 [Q9NRG4-1]
RefSeqⁱ	NP_064582.2, NM_020197.2 [Q9NRG4-1]
UniGeneⁱ	Hs.66170

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3RIB	X-ray	2.79	A/B	1-433	[»]
	3S7B	X-ray	2.42	A	1-433	[»]
	3S7D	X-ray	2.30	A	1-433	[»]
	3S7F	X-ray	2.85	A	1-433	[»]
	3S7J	X-ray	3.04	A	1-433	[»]
	3TG4	X-ray	2.00	A	1-433	[»]
	3TG5	X-ray	2.30	A	1-433	[»]
	4O6F	X-ray	2.82	A	1-433	[»]
	4WUY	X-ray	1.63	A	1-433	[»]
	4YND	X-ray	2.79	A	1-433	[»]
	5ARF	X-ray	1.92	A	2-433	[»]
	5ARG	X-ray	1.99	A	2-433	[»]
	5KJK	X-ray	1.93	A	5-433	[»]
	5KJL	X-ray	2.70	A	5-433	[»]
	5KJM	X-ray	2.19	A	5-433	[»]
	5KJN	X-ray	2.72	A	5-433	[»]
	5V3H	X-ray	2.69	A	1-433	[»]
	5WCG	X-ray	2.02	A	1-433	[»]
	6CBX	X-ray	1.94	A/B	1-433	[»]
	6CBY	X-ray	2.55	A/B	1-433	[»]
	6MON	X-ray	2.71	A/B	5-433	[»]
ProteinModelPortalⁱ	Q9NRG4
SMRⁱ	Q9NRG4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	121274, 27 interactors
DIPⁱ	DIP-50202N
IntActⁱ	Q9NRG4, 6 interactors
MINTⁱ	Q9NRG4
STRINGⁱ	9606.ENSP00000355924

Chemistry databases

BindingDBⁱ	Q9NRG4
ChEMBLⁱ	CHEMBL2169716
GuidetoPHARMACOLOGYⁱ	2714

PTM databases

iPTMnetⁱ	Q9NRG4
PhosphoSitePlusⁱ	Q9NRG4

Polymorphism and mutation databases

BioMutaⁱ	SMYD2
DMDMⁱ	90185234

Proteomic databases

EPDⁱ	Q9NRG4
jPOSTⁱ	Q9NRG4
MaxQBⁱ	Q9NRG4
PaxDbⁱ	Q9NRG4
PeptideAtlasⁱ	Q9NRG4
PRIDEⁱ	Q9NRG4
ProteomicsDBⁱ	82355

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000366957; ENSP00000355924; ENSG00000143499 [Q9NRG4-1]
GeneIDⁱ	56950
KEGGⁱ	hsa:56950
UCSCⁱ	uc057pjy.1 human [Q9NRG4-1]

Organism-specific databases

CTDⁱ	56950
DisGeNETⁱ	56950
EuPathDBⁱ	HostDB:ENSG00000143499.13
GeneCardsⁱ	SMYD2
HGNCⁱ	HGNC:20982 SMYD2
HPAⁱ	HPA029023
MIMⁱ	610663 gene
neXtProtⁱ	NX_Q9NRG4
OpenTargetsⁱ	ENSG00000143499
PharmGKBⁱ	PA134930268
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2084 Eukaryota COG2940 LUCA
GeneTreeⁱ	ENSGT00940000157082
HOGENOMⁱ	HOG000007850
HOVERGENⁱ	HBG098536
InParanoidⁱ	Q9NRG4
KOⁱ	K11426
OMAⁱ	AVQEIHP
OrthoDBⁱ	981799at2759
PhylomeDBⁱ	Q9NRG4
TreeFamⁱ	TF106487

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3214841 PKMTs methylate histone lysines R-HSA-6804760 Regulation of TP53 Activity through Methylation

Reactomeⁱ

R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-6804760 Regulation of TP53 Activity through Methylation

Miscellaneous databases

ChiTaRSⁱ	SMYD2 human
GenomeRNAiⁱ	56950
Protein Ontology More...PROⁱ	PR:Q9NRG4
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000143499 Expressed in 227 organ(s), highest expression level in left ventricle myocardium
ExpressionAtlasⁱ	Q9NRG4 baseline and differential
Genevisibleⁱ	Q9NRG4 HS

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR001214 SET_dom IPR011990 TPR-like_helical_dom_sf IPR002893 Znf_MYND
Pfamⁱ	View protein in Pfam PF00856 SET, 1 hit PF01753 zf-MYND, 1 hit
SMARTⁱ	View protein in SMART SM00317 SET, 1 hit
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
PROSITEⁱ	View protein in PROSITE PS50280 SET, 1 hit PS01360 ZF_MYND_1, 1 hit PS50865 ZF_MYND_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SMYD2_HUMAN
Accessionⁱ	Q9NRG4Primary (citable) accession number: Q9NRG4 Secondary accession number(s): B2R9P9 , I6L9H7, Q4V765, Q5VSH9, Q96AI4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
	Last sequence update:	September 13, 2005
	Last modified:	February 13, 2019
	This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

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UniProtKB - Q9NRG4 (SMYD2_HUMAN)

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N-lysine methyltransferase SMYD2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Enzyme and pathway databases

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

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Phylogenomic databases

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Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

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Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ