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Q9NRG4

- SMYD2_HUMAN

UniProt

Q9NRG4 - SMYD2_HUMAN

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Protein
N-lysine methyltransferase SMYD2
Gene
SMYD2, KMT3C
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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'.6 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371S-adenosyl-L-methionine
Binding sitei240 – 2401Peptide substrate; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9039MYND-type
Add
BLAST

GO - Molecular functioni

  1. RNA polymerase II core binding Source: UniProtKB
  2. histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. p53 binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. protein-lysine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of cell proliferation Source: UniProtKB
  2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. peptidyl-lysine dimethylation Source: UniProtKB
  4. peptidyl-lysine monomethylation Source: UniProtKB
  5. regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  6. transcription, DNA-templated Source: UniProtKB-KW
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

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:20982. SMYD2.

Subcellular locationi

Cytoplasmcytosol By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871E → K: Abolishes methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi189 – 1891E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi190 – 1901E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi207 – 2071H → A: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi240 – 2401Y → F: Abolishes methyltransferase activity. 2 Publications
Mutagenesisi245 – 2451Y → F: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi252 – 2521D → R: Slightly reduces methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi253 – 2531R → Q: No effect on methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi306 – 3061R → E: No effect on methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi374 – 3741Y → A: Abolishes methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi429 – 4291E → K: Reduces methyltransferase activity on p53/TP53. 1 Publication
Mutagenesisi431 – 4311E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication

Organism-specific databases

PharmGKBiPA134930268.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433N-lysine methyltransferase SMYD2
PRO_0000218309Add
BLAST

Proteomic databases

MaxQBiQ9NRG4.
PaxDbiQ9NRG4.
PRIDEiQ9NRG4.

PTM databases

PhosphoSiteiQ9NRG4.

Expressioni

Inductioni

Expression is repressed by CEBPA.1 Publication

Gene expression databases

ArrayExpressiQ9NRG4.
BgeeiQ9NRG4.
CleanExiHS_SMYD2.
GenevestigatoriQ9NRG4.

Organism-specific databases

HPAiHPA029023.

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 HSP90AA1.3 Publications

Protein-protein interaction databases

BioGridi121274. 11 interactions.
DIPiDIP-50202N.
STRINGi9606.ENSP00000355924.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135
Beta strandi17 – 259
Beta strandi32 – 376
Beta strandi39 – 435
Helixi45 – 473
Turni53 – 553
Turni66 – 683
Beta strandi72 – 754
Helixi76 – 9621
Helixi97 – 993
Helixi104 – 11815
Helixi124 – 1263
Beta strandi127 – 1293
Helixi131 – 1333
Helixi138 – 1403
Helixi143 – 16018
Turni161 – 1633
Helixi169 – 18214
Beta strandi184 – 1874
Beta strandi193 – 1986
Helixi200 – 2034
Beta strandi205 – 2073
Beta strandi212 – 2187
Beta strandi221 – 2288
Beta strandi235 – 2384
Helixi247 – 25812
Helixi265 – 2695
Helixi273 – 2764
Helixi288 – 30821
Turni309 – 3113
Helixi314 – 32815
Turni329 – 3313
Helixi337 – 35216
Helixi356 – 37318
Helixi379 – 39416
Helixi398 – 41518
Helixi421 – 43010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RIBX-ray2.79A/B1-433[»]
3S7BX-ray2.42A1-433[»]
3S7DX-ray2.30A1-433[»]
3S7FX-ray2.85A1-433[»]
3S7JX-ray3.04A1-433[»]
3TG4X-ray2.00A1-433[»]
3TG5X-ray2.30A1-433[»]
4O6FX-ray2.82A1-433[»]
ProteinModelPortaliQ9NRG4.
SMRiQ9NRG4. Positions 6-432.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 241235SET
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 SET domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
HOGENOMiHOG000007850.
HOVERGENiHBG098536.
InParanoidiQ9NRG4.
KOiK11426.
OMAiQPFQVGD.
OrthoDBiEOG74XS68.
PhylomeDBiQ9NRG4.
TreeFamiTF106487.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR001214. SET_dom.
IPR011990. TPR-like_helical.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS50280. SET. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NRG4-1 [UniParc]FASTAAdd to Basket

« Hide

MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN    50
HCEYCFTRKE GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW 100
NPSETVRLTA RILAKQKIHP ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ 150
SDIAALHHFY SKHLGFPDND SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP 200
DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY IDLLYPTEDR 250
NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN 300
VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC 350
LYMQDWEGAL QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA 400
GEKALKKAIA IMEVAHGKDH PYISEIKQEI ESH 433
Length:433
Mass (Da):49,688
Last modified:September 13, 2005 - v2
Checksum:i3EEA5B8417870F5D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651G → E.3 Publications
Corresponds to variant rs1134647 [ dbSNP | Ensembl ].
VAR_023442
Natural varianti430 – 4301I → M.
Corresponds to variant rs11120301 [ dbSNP | Ensembl ].
VAR_052991

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF226053 mRNA. Translation: AAF86953.1.
AK313868 mRNA. Translation: BAG36596.1.
AL929236 Genomic DNA. Translation: CAH70920.1.
BC017080 mRNA. Translation: AAH17080.2.
BC098276 mRNA. Translation: AAH98276.1.
BC098133 mRNA. Translation: AAH98133.1.
BC098335 mRNA. Translation: AAH98335.1.
CCDSiCCDS31022.1.
RefSeqiNP_064582.2. NM_020197.2.
UniGeneiHs.66170.

Genome annotation databases

EnsembliENST00000366957; ENSP00000355924; ENSG00000143499.
GeneIDi56950.
KEGGihsa:56950.
UCSCiuc021piw.1. human.

Polymorphism databases

DMDMi90185234.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF226053 mRNA. Translation: AAF86953.1 .
AK313868 mRNA. Translation: BAG36596.1 .
AL929236 Genomic DNA. Translation: CAH70920.1 .
BC017080 mRNA. Translation: AAH17080.2 .
BC098276 mRNA. Translation: AAH98276.1 .
BC098133 mRNA. Translation: AAH98133.1 .
BC098335 mRNA. Translation: AAH98335.1 .
CCDSi CCDS31022.1.
RefSeqi NP_064582.2. NM_020197.2.
UniGenei Hs.66170.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q9NRG4.
SMRi Q9NRG4. Positions 6-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121274. 11 interactions.
DIPi DIP-50202N.
STRINGi 9606.ENSP00000355924.

Chemistry

ChEMBLi CHEMBL2169716.
GuidetoPHARMACOLOGYi 2714.

PTM databases

PhosphoSitei Q9NRG4.

Polymorphism databases

DMDMi 90185234.

Proteomic databases

MaxQBi Q9NRG4.
PaxDbi Q9NRG4.
PRIDEi Q9NRG4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366957 ; ENSP00000355924 ; ENSG00000143499 .
GeneIDi 56950.
KEGGi hsa:56950.
UCSCi uc021piw.1. human.

Organism-specific databases

CTDi 56950.
GeneCardsi GC01P214454.
HGNCi HGNC:20982. SMYD2.
HPAi HPA029023.
MIMi 610663. gene.
neXtProti NX_Q9NRG4.
PharmGKBi PA134930268.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
HOGENOMi HOG000007850.
HOVERGENi HBG098536.
InParanoidi Q9NRG4.
KOi K11426.
OMAi QPFQVGD.
OrthoDBi EOG74XS68.
PhylomeDBi Q9NRG4.
TreeFami TF106487.

Miscellaneous databases

ChiTaRSi SMYD2. human.
GenomeRNAii 56950.
NextBioi 62549.
PROi Q9NRG4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRG4.
Bgeei Q9NRG4.
CleanExi HS_SMYD2.
Genevestigatori Q9NRG4.

Family and domain databases

Gene3Di 1.25.40.10. 1 hit.
InterProi IPR001214. SET_dom.
IPR011990. TPR-like_helical.
IPR002893. Znf_MYND.
[Graphical view ]
Pfami PF00856. SET. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view ]
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS50280. SET. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene expressed in human liver cancer tissue."
    Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-165.
    Tissue: Liver cancer.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-165.
    Tissue: Testis.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT GLU-165.
    Tissue: Colon.
  5. Cited for: FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF HIS-207.
  6. "C/EBPalphap30 plays transcriptional regulatory roles distinct from C/EBPalphap42."
    Wang C., Chen X., Wang Y., Gong J., Hu G.
    Cell Res. 17:374-383(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. Cited for: FUNCTION.
  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.
  9. Cited for: FUNCTION, INTERACTION WITH RB, MUTAGENESIS OF TYR-240.
  10. "Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins."
    Xu S., Zhong C., Zhang T., Ding J.
    J. Mol. Cell Biol. 3:293-300(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS.
  11. "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.
  12. 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.

Entry informationi

Entry nameiSMYD2_HUMAN
AccessioniPrimary (citable) accession number: Q9NRG4
Secondary accession number(s): B2R9P9
, Q4V765, Q5VSH9, Q96AI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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

External Data

Dasty 3

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