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Q9CWR2 (SMYD3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase SMYD3

EC=2.1.1.43
Alternative name(s):
SET and MYND domain-containing protein 3
Zinc finger MYND domain-containing protein 1
Gene names
Name:Smyd3
Synonyms:Zmynd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences By similarity.

Catalytic activity

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

Enzyme regulation

Histone methyltransferase activity strongly stimulated by HSPCA By similarity.

Subunit structure

Interacts with HSPCA. Interacts with HELZ. Interacts with POLR2A; the interaction may be indirect and may be mediated by HELZ By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Mainly cytoplasmic when cells are arrested at G0/G1 By similarity. Accumulates in the nucleus at S phase and G2/M By similarity.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family.

Contains 1 MYND-type zinc finger.

Contains 1 SET domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainZinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to dexamethasone stimulus

Inferred from direct assay PubMed 23752591. Source: MGI

establishment of protein localization

Inferred from mutant phenotype PubMed 23752591. Source: MGI

myotube cell development

Inferred from mutant phenotype PubMed 23752591. Source: MGI

negative regulation of protein kinase activity

Inferred from mutant phenotype PubMed 23752591. Source: MGI

nucleosome assembly

Inferred from mutant phenotype PubMed 23752591. Source: MGI

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 23752591. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23752591. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 23752591. Source: MGI

   Molecular_functionRNA polymerase II core binding

Inferred from direct assay PubMed 23752591. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 23752591. Source: MGI

RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 23752591. Source: MGI

histone-lysine N-methyltransferase activity

Inferred from direct assay PubMed 16805913. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23752591. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Histone-lysine N-methyltransferase SMYD3
PRO_0000218313

Regions

Domain4 – 240237SET
Zinc finger49 – 8739MYND-type
Region14 – 163S-adenosyl-L-methionine binding By similarity
Region205 – 2062S-adenosyl-L-methionine binding By similarity

Sites

Binding site1241S-adenosyl-L-methionine By similarity
Binding site1321S-adenosyl-L-methionine By similarity
Binding site2391S-adenosyl-L-methionine By similarity
Binding site2591S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict3181N → D in AAH61485. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9CWR2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1EC765044E1FB0DA

FASTA42849,126
        10         20         30         40         50         60 
MEALKVEKFT TANRGNGLRA VAPLRPGELL FRSDPLAYTV CKGSRGVVCD RCLLGKEKLM 

        70         80         90        100        110        120 
RCSQCRIAKY CSAKCQKKAW PDHRRECSCL KSCKPRYPPD SVRLLGRVIV KLMDEKPSES 

       130        140        150        160        170        180 
EKLYSFYDLE SNISKLTEDK KEGLRQLAMT FQHFMREEIQ DASQLPPSFD LFEAFAKVIC 

       190        200        210        220        230        240 
NSFTICNAEM QEVGVGLYPS MSLLNHSCDP NCSIVFNGPH LLLRAVREIE AGEELTICYL 

       250        260        270        280        290        300 
DMLMTSEERR KQLRDQYCFE CDCIRCQTQD KDADMLTGDE QIWKEVQESL KKIEELKAHW 

       310        320        330        340        350        360 
KWEQVLALCQ AIINSNSNRL PDINIYQLKV LDCAMDACIN LGMLEEALFY AMRTMEPYRI 

       370        380        390        400        410        420 
FFPGSHPVRG VQVMKVGKLQ LHQGMFPQAM KNLRLAFDIM KVTHGREHSL IEDLILLLEE 


CDANIRAS 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain cortex, Embryonic stem cell and Medulla oblongata.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N-3.
Tissue: Brain and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010447 mRNA. Translation: BAB26947.1.
AK044168 mRNA. Translation: BAC31804.1.
AK046829 mRNA. Translation: BAC32887.1.
BC052431 mRNA. Translation: AAH52431.1.
BC061485 mRNA. Translation: AAH61485.1.
CCDSCCDS15560.1.
RefSeqNP_081464.1. NM_027188.3.
XP_006497043.1. XM_006496980.1.
XP_006497044.1. XM_006496981.1.
XP_006497045.1. XM_006496982.1.
UniGeneMm.222338.

3D structure databases

ProteinModelPortalQ9CWR2.
SMRQ9CWR2. Positions 4-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213640. 1 interaction.

PTM databases

PhosphoSiteQ9CWR2.

Proteomic databases

MaxQBQ9CWR2.
PaxDbQ9CWR2.
PRIDEQ9CWR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000128302; ENSMUSP00000117410; ENSMUSG00000055067.
GeneID69726.
KEGGmmu:69726.
UCSCuc007dvj.1. mouse.

Organism-specific databases

CTD64754.
MGIMGI:1916976. Smyd3.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00530000063077.
HOGENOMHOG000007850.
HOVERGENHBG105004.
InParanoidQ9CWR2.
KOK11426.
OMAKVEKFAT.
OrthoDBEOG74XS68.
PhylomeDBQ9CWR2.
TreeFamTF106487.

Enzyme and pathway databases

BRENDA2.1.1.43. 3474.

Gene expression databases

ArrayExpressQ9CWR2.
BgeeQ9CWR2.
CleanExMM_SMYD3.
GenevestigatorQ9CWR2.

Family and domain databases

InterProIPR025805. Hist-Lys_N-MeTrfase_Smyd3.
IPR001214. SET_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamPF00856. SET. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTSM00317. SET. 1 hit.
[Graphical view]
PROSITEPS51574. SAM_MT43_2. 1 hit.
PS50280. SET. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMYD3. mouse.
NextBio330194.
PROQ9CWR2.
SOURCESearch...

Entry information

Entry nameSMYD3_MOUSE
AccessionPrimary (citable) accession number: Q9CWR2
Secondary accession number(s): Q6P7V6, Q8BG90
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot