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Database: UniProt
Entry: Q9Y5N5
LinkDB: Q9Y5N5
Original site: Q9Y5N5 
ID   HEMK2_HUMAN             Reviewed;         214 AA.
AC   Q9Y5N5; Q96F73;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   09-JUL-2014, entry version 115.
DE   RecName: Full=HemK methyltransferase family member 2;
DE            EC=2.1.1.-;
DE   AltName: Full=M.HsaHemK2P;
DE   AltName: Full=N(6)-adenine-specific DNA methyltransferase 1;
GN   Name=N6AMT1; Synonyms=C21orf127, HEMK2; ORFNames=PRED28;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASP-34; ARG-146
RP   AND ARG-166.
RA   Reboul J., Misseri Y., Bonnerot C., Mogensen E., Lutfalla G.;
RT   "Identification of a novel putative eukaryotic DNA-
RT   methyltransferase.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-34.
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ASP-34;
RP   ARG-146 AND ARG-166.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
RP   ASP-34; ARG-146 AND ARG-166.
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH TRMT112.
RX   PubMed=18539146; DOI=10.1016/j.febslet.2008.05.045;
RA   Figaro S., Scrima N., Buckingham R.H., Heurgue-Hamard V.;
RT   "HemK2 protein, encoded on human chromosome 21, methylates translation
RT   termination factor eRF1.";
RL   FEBS Lett. 582:2352-2356(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21193388; DOI=10.1289/ehp.1002733;
RA   Ren X., Aleshin M., Jo W.J., Dills R., Kalman D.A., Vulpe C.D.,
RA   Smith M.T., Zhang L.;
RT   "Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1)
RT   in arsenic biomethylation and its role in arsenic-induced toxicity.";
RL   Environ. Health Perspect. 119:771-777(2011).
CC   -!- FUNCTION: Heterodimeric methyltransferase that catalyzes N5-
CC       methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as
CC       methyl donor. ETF1 needs to be complexed to ERF3 in its GTP-bound
CC       form to be efficiently methylated. May play a role in the
CC       modulation of arsenic-induced toxicity. May be involved in the
CC       conversion of monomethylarsonous acid (3+) into the less toxic
CC       dimethylarsonic acid.
CC   -!- SUBUNIT: Heterodimer with TRMT112.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y5N5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y5N5-2; Sequence=VSP_040294;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC       parathyroid and pituitary glands, followed by adrenal gland and
CC       kidney, and lowest expression in leukocytes and mammary gland.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related
CC       family.
CC   -!- CAUTION: Was originally (Ref.1) proposed to be a DNA
CC       methyltransferase, but was then shown to be a protein
CC       methyltransferase (PubMed:18539146).
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DR   EMBL; AF139682; AAD38520.1; -; mRNA.
DR   EMBL; AF227510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL163248; CAB90428.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09941.1; -; Genomic_DNA.
DR   EMBL; BC011554; AAH11554.1; -; mRNA.
DR   CCDS; CCDS33525.1; -. [Q9Y5N5-2]
DR   CCDS; CCDS33526.1; -. [Q9Y5N5-1]
DR   RefSeq; NP_037372.3; NM_013240.4.
DR   RefSeq; NP_877426.3; NM_182749.3.
DR   UniGene; Hs.163846; -.
DR   ProteinModelPortal; Q9Y5N5; -.
DR   SMR; Q9Y5N5; 21-214.
DR   BioGrid; 118872; 3.
DR   IntAct; Q9Y5N5; 1.
DR   MINT; MINT-3087317; -.
DR   STRING; 9606.ENSP00000303584; -.
DR   DMDM; 313104228; -.
DR   MaxQB; Q9Y5N5; -.
DR   PaxDb; Q9Y5N5; -.
DR   PRIDE; Q9Y5N5; -.
DR   DNASU; 29104; -.
DR   Ensembl; ENST00000303775; ENSP00000303584; ENSG00000156239. [Q9Y5N5-1]
DR   Ensembl; ENST00000351429; ENSP00000286764; ENSG00000156239. [Q9Y5N5-2]
DR   Ensembl; ENST00000460212; ENSP00000436490; ENSG00000156239. [Q9Y5N5-1]
DR   GeneID; 29104; -.
DR   KEGG; hsa:29104; -.
DR   UCSC; uc002ymp.2; human. [Q9Y5N5-2]
DR   CTD; 29104; -.
DR   GeneCards; GC21M030244; -.
DR   H-InvDB; HIX0020675; -.
DR   HGNC; HGNC:16021; N6AMT1.
DR   HPA; CAB034133; -.
DR   HPA; CAB034135; -.
DR   HPA; HPA059242; -.
DR   MIM; 614553; gene.
DR   neXtProt; NX_Q9Y5N5; -.
DR   PharmGKB; PA162396656; -.
DR   eggNOG; COG2890; -.
DR   HOGENOM; HOG000219949; -.
DR   HOVERGEN; HBG052569; -.
DR   InParanoid; Q9Y5N5; -.
DR   KO; K00571; -.
DR   OMA; EHVYEPA; -.
DR   OrthoDB; EOG738066; -.
DR   PhylomeDB; Q9Y5N5; -.
DR   TreeFam; TF314919; -.
DR   GenomeRNAi; 29104; -.
DR   NextBio; 52151; -.
DR   PRO; PR:Q9Y5N5; -.
DR   Bgee; Q9Y5N5; -.
DR   CleanEx; HS_N6AMT1; -.
DR   Genevestigator; Q9Y5N5; -.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; IDA:MGI.
DR   GO; GO:0006479; P:protein methylation; IDA:GOC.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004557; PrmC_related.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00537; hemK_rel_arch; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Methyltransferase;
KW   Polymorphism; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    214       HemK methyltransferase family member 2.
FT                                /FTId=PRO_0000088049.
FT   REGION       53     57       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      122    125       Substrate binding (By similarity).
FT   BINDING      77     77       S-adenosyl-L-methionine (By similarity).
FT   BINDING     122    122       S-adenosyl-L-methionine (By similarity).
FT   VAR_SEQ     105    132       Missing (in isoform 2).
FT                                /FTId=VSP_040294.
FT   VARIANT      34     34       N -> D (in dbSNP:rs1997607).
FT                                /FTId=VAR_060445.
FT   VARIANT     146    146       K -> R (in dbSNP:rs2205447).
FT                                /FTId=VAR_060446.
FT   VARIANT     166    166       K -> R (in dbSNP:rs2205446).
FT                                /FTId=VAR_060447.
SQ   SEQUENCE   214 AA;  22900 MW;  401B9A533C19F7C6 CRC64;
     MAGENFATPF HGHVGRGAFS DVYEPAEDTF LLLNALEAAA AELAGVEICL EVGSGSGVVS
     AFLASMIGPQ ALYMCTDINP EAAACTLETA RCNKVHIQPV ITDLVKGLLP RLTEKVDLLV
     FNPPYVVTPP QEVGSHGIEA AWAGGKNGRE VMDRFFPLVP DLLSPKGLFY LVTIKENNPE
     EILKIMKTKG LQGTTALSRQ AGQETLSVLK FTKS
//
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