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Q9H7B4

- SMYD3_HUMAN

UniProt

Q9H7B4 - SMYD3_HUMAN

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Protein

Histone-lysine N-methyltransferase SMYD3

Gene

SMYD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Histone methyltransferase activity strongly stimulated by HSPCA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
Binding sitei132 – 1321S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
Binding sitei181 – 1811S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
Binding sitei239 – 2391S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
Binding sitei259 – 2591S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri49 – 8739MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone-lysine N-methyltransferase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  4. RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  1. cellular response to dexamethasone stimulus Source: Ensembl
  2. establishment of protein localization Source: Ensembl
  3. myotube cell development Source: Ensembl
  4. negative regulation of protein kinase activity Source: Ensembl
  5. nucleosome assembly Source: Ensembl
  6. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  7. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SMYD3
Synonyms:ZMYND1, ZNFN3A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:15513. SMYD3.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37972.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Histone-lysine N-methyltransferase SMYD3PRO_0000218312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H7B4.
PaxDbiQ9H7B4.
PRIDEiQ9H7B4.

PTM databases

PhosphoSiteiQ9H7B4.

Expressioni

Tissue specificityi

Expressed in skeletal muscles and testis. Overexpressed in a majority of colorectal and hepatocellular carcinomas.1 Publication

Gene expression databases

BgeeiQ9H7B4.
CleanExiHS_SMYD3.
ExpressionAtlasiQ9H7B4. baseline and differential.
GenevestigatoriQ9H7B4.

Organism-specific databases

HPAiCAB012229.

Interactioni

Subunit structurei

Interacts with HSPCA. Interacts with HELZ. Interacts with POLR2A; the interaction may be indirect and may be mediated by HELZ.2 Publications

Protein-protein interaction databases

BioGridi122268. 30 interactions.
IntActiQ9H7B4. 12 interactions.
MINTiMINT-1033215.
STRINGi9606.ENSP00000373637.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Beta strandi12 – 2211
Beta strandi29 – 335
Beta strandi36 – 405
Helixi42 – 443
Turni50 – 523
Turni63 – 653
Beta strandi69 – 724
Helixi73 – 786
Helixi80 – 9213
Turni93 – 953
Helixi100 – 11415
Helixi119 – 1213
Beta strandi122 – 1243
Helixi126 – 1283
Helixi133 – 1353
Helixi138 – 15417
Turni155 – 1584
Helixi162 – 1643
Helixi171 – 18111
Beta strandi183 – 1864
Beta strandi192 – 1976
Helixi201 – 2033
Beta strandi211 – 2177
Beta strandi220 – 2256
Beta strandi234 – 2374
Helixi246 – 25712
Helixi264 – 2685
Turni269 – 2713
Helixi272 – 2754
Helixi280 – 29819
Helixi302 – 31312
Turni317 – 3193
Helixi325 – 34117
Helixi344 – 36118
Helixi367 – 38216
Helixi386 – 40318
Turni404 – 4074
Helixi409 – 42618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MEKX-ray2.10A1-428[»]
3OXFX-ray2.82A/B1-428[»]
3OXGX-ray3.41A1-428[»]
3OXLX-ray3.60A1-428[»]
3PDNX-ray1.70A1-428[»]
3QWPX-ray1.53A1-428[»]
3RU0X-ray1.85A/B2-428[»]
ProteinModelPortaliQ9H7B4.
SMRiQ9H7B4. Positions 4-428.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H7B4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 240237SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 163S-adenosyl-L-methionine binding
Regioni205 – 2062S-adenosyl-L-methionine binding

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family.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 fingeri49 – 8739MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00530000063077.
HOGENOMiHOG000007850.
HOVERGENiHBG105004.
InParanoidiQ9H7B4.
KOiK11426.
OMAiKVEKFAT.
OrthoDBiEOG74XS68.
PhylomeDBiQ9H7B4.
TreeFamiTF106487.

Family and domain databases

InterProiIPR025805. Hist-Lys_N-MeTrfase_Smyd3.
IPR001214. SET_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51574. SAM_MT43_2. 1 hit.
PS50280. SET. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H7B4-1) [UniParc]FASTAAdd 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
MEPLKVEKFA TAKRGNGLRA VTPLRPGELL FRSDPLAYTV CKGSRGVVCD
60 70 80 90 100
RCLLGKEKLM RCSQCRVAKY CSAKCQKKAW PDHKRECKCL KSCKPRYPPD
110 120 130 140 150
SVRLLGRVVF KLMDGAPSES EKLYSFYDLE SNINKLTEDK KEGLRQLVMT
160 170 180 190 200
FQHFMREEIQ DASQLPPAFD LFEAFAKVIC NSFTICNAEM QEVGVGLYPS
210 220 230 240 250
ISLLNHSCDP NCSIVFNGPH LLLRAVRDIE VGEELTICYL DMLMTSEERR
260 270 280 290 300
KQLRDQYCFE CDCFRCQTQD KDADMLTGDE QVWKEVQESL KKIEELKAHW
310 320 330 340 350
KWEQVLAMCQ AIISSNSERL PDINIYQLKV LDCAMDACIN LGLLEEALFY
360 370 380 390 400
GTRTMEPYRI FFPGSHPVRG VQVMKVGKLQ LHQGMFPQAM KNLRLAFDIM
410 420
RVTHGREHSL IEDLILLLEE CDANIRAS
Length:428
Mass (Da):49,097
Last modified:November 4, 2008 - v4
Checksum:i2079357016F200AC
GO
Isoform 2 (identifier: Q9H7B4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-170: Missing.
     171-176: LFEAFA → MEEEEE

Note: No experimental confirmation available.

Show »
Length:258
Mass (Da):29,759
Checksum:iC9A509C511BA28C4
GO
Isoform 3 (identifier: Q9H7B4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.

Show »
Length:369
Mass (Da):42,625
Checksum:iB5A3DC1D5C8AA743
GO

Sequence cautioni

The sequence CAI14744.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAI16628.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131K → N in BAB86333. (PubMed:15235609)Curated
Sequence conflicti13 – 131K → N in AAH31010. (PubMed:15489334)Curated
Sequence conflicti140 – 1401K → R in AAH31010. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 170170Missing in isoform 2. 1 PublicationVSP_012416Add
BLAST
Alternative sequencei1 – 5959Missing in isoform 3. 1 PublicationVSP_035601Add
BLAST
Alternative sequencei171 – 1766LFEAFA → MEEEEE in isoform 2. 1 PublicationVSP_012417

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB057595 mRNA. Translation: BAB86333.1.
AY186742 mRNA. Translation: AAO31695.1.
AK024733 mRNA. Translation: BAB14981.1.
AK289605 mRNA. Translation: BAF82294.1.
AL512412, AL445468 Genomic DNA. Translation: CAI14744.1. Different initiation.
AL512412, AL445468 Genomic DNA. Translation: CAI14745.1.
AL512412
, AL356583, AL358859, AL445468 Genomic DNA. Translation: CAI14746.1.
AL358859
, AL356583, AL445468, AL512412 Genomic DNA. Translation: CAI15419.1.
AL356583
, AL358859, AL445468, AL512412 Genomic DNA. Translation: CAI16395.1.
AL445468, AL512412 Genomic DNA. Translation: CAI16628.1. Different initiation.
AL445468, AL512412 Genomic DNA. Translation: CAI16629.1.
AL445468
, AL356583, AL358859, AL512412 Genomic DNA. Translation: CAI16630.1.
CH471148 Genomic DNA. Translation: EAW77142.1.
BC017079 mRNA. Translation: AAH17079.2.
BC031010 mRNA. Translation: AAH31010.1.
CCDSiCCDS31083.1. [Q9H7B4-3]
RefSeqiNP_001161212.1. NM_001167740.1. [Q9H7B4-1]
NP_073580.1. NM_022743.2. [Q9H7B4-3]
XP_005273286.1. XM_005273229.1. [Q9H7B4-2]
UniGeneiHs.567571.

Genome annotation databases

EnsembliENST00000490107; ENSP00000419184; ENSG00000185420. [Q9H7B4-3]
GeneIDi64754.
KEGGihsa:64754.
UCSCiuc001ibj.3. human. [Q9H7B4-1]

Polymorphism databases

DMDMi212276523.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB057595 mRNA. Translation: BAB86333.1 .
AY186742 mRNA. Translation: AAO31695.1 .
AK024733 mRNA. Translation: BAB14981.1 .
AK289605 mRNA. Translation: BAF82294.1 .
AL512412 , AL445468 Genomic DNA. Translation: CAI14744.1 . Different initiation.
AL512412 , AL445468 Genomic DNA. Translation: CAI14745.1 .
AL512412
, AL356583 , AL358859 , AL445468 Genomic DNA. Translation: CAI14746.1 .
AL358859
, AL356583 , AL445468 , AL512412 Genomic DNA. Translation: CAI15419.1 .
AL356583
, AL358859 , AL445468 , AL512412 Genomic DNA. Translation: CAI16395.1 .
AL445468 , AL512412 Genomic DNA. Translation: CAI16628.1 . Different initiation.
AL445468 , AL512412 Genomic DNA. Translation: CAI16629.1 .
AL445468
, AL356583 , AL358859 , AL512412 Genomic DNA. Translation: CAI16630.1 .
CH471148 Genomic DNA. Translation: EAW77142.1 .
BC017079 mRNA. Translation: AAH17079.2 .
BC031010 mRNA. Translation: AAH31010.1 .
CCDSi CCDS31083.1. [Q9H7B4-3 ]
RefSeqi NP_001161212.1. NM_001167740.1. [Q9H7B4-1 ]
NP_073580.1. NM_022743.2. [Q9H7B4-3 ]
XP_005273286.1. XM_005273229.1. [Q9H7B4-2 ]
UniGenei Hs.567571.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MEK X-ray 2.10 A 1-428 [» ]
3OXF X-ray 2.82 A/B 1-428 [» ]
3OXG X-ray 3.41 A 1-428 [» ]
3OXL X-ray 3.60 A 1-428 [» ]
3PDN X-ray 1.70 A 1-428 [» ]
3QWP X-ray 1.53 A 1-428 [» ]
3RU0 X-ray 1.85 A/B 2-428 [» ]
ProteinModelPortali Q9H7B4.
SMRi Q9H7B4. Positions 4-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122268. 30 interactions.
IntActi Q9H7B4. 12 interactions.
MINTi MINT-1033215.
STRINGi 9606.ENSP00000373637.

Chemistry

ChEMBLi CHEMBL2321643.

PTM databases

PhosphoSitei Q9H7B4.

Polymorphism databases

DMDMi 212276523.

Proteomic databases

MaxQBi Q9H7B4.
PaxDbi Q9H7B4.
PRIDEi Q9H7B4.

Protocols and materials databases

DNASUi 64754.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000490107 ; ENSP00000419184 ; ENSG00000185420 . [Q9H7B4-3 ]
GeneIDi 64754.
KEGGi hsa:64754.
UCSCi uc001ibj.3. human. [Q9H7B4-1 ]

Organism-specific databases

CTDi 64754.
GeneCardsi GC01M245912.
HGNCi HGNC:15513. SMYD3.
HPAi CAB012229.
MIMi 608783. gene.
neXtProti NX_Q9H7B4.
PharmGKBi PA37972.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00530000063077.
HOGENOMi HOG000007850.
HOVERGENi HBG105004.
InParanoidi Q9H7B4.
KOi K11426.
OMAi KVEKFAT.
OrthoDBi EOG74XS68.
PhylomeDBi Q9H7B4.
TreeFami TF106487.

Miscellaneous databases

ChiTaRSi SMYD3. human.
EvolutionaryTracei Q9H7B4.
GeneWikii SMYD3.
GenomeRNAii 64754.
NextBioi 66717.
PROi Q9H7B4.
SOURCEi Search...

Gene expression databases

Bgeei Q9H7B4.
CleanExi HS_SMYD3.
ExpressionAtlasi Q9H7B4. baseline and differential.
Genevestigatori Q9H7B4.

Family and domain databases

InterProi IPR025805. Hist-Lys_N-MeTrfase_Smyd3.
IPR001214. SET_dom.
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 PS51574. SAM_MT43_2. 1 hit.
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. "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells."
    Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., Nakamura Y.
    Nat. Cell Biol. 6:731-740(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HSPCA; HELZ AND POLR2A, DNA-BINDING.
  2. Sha J.H., Zhou Z.M., Xu M.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "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] (ISOFORMS 1 AND 3).
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Colon and Melanoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: CATALYTIC ACTIVITY, FUNCTION.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human histone-lysine n-methyltransferase SMYD3 in complex with S-adenosyl-L-methionine."
    Structural genomics consortium (SGC)
    Submitted (APR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS.

Entry informationi

Entry nameiSMYD3_HUMAN
AccessioniPrimary (citable) accession number: Q9H7B4
Secondary accession number(s): A8K0P0
, B1AN38, Q86TL8, Q8N5Z6, Q96AI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: November 4, 2008
Last modified: October 29, 2014
This is version 120 of the entry and version 4 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3