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MT21E_MOUSE
ID   MT21E_MOUSE             Reviewed;         244 AA.
AC   Q8CDZ2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Protein-lysine methyltransferase METTL21E;
DE            EC=2.1.1.-;
DE   AltName: Full=Methyltransferase-like protein 21E;
GN   Name=Mettl21e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Jaw, and Limb;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Protein-lysine methyltransferase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC       family. {ECO:0000305}.
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DR   EMBL; AK029331; BAC26399.1; -; mRNA.
DR   EMBL; BC100531; AAI00532.1; -; mRNA.
DR   CCDS; CCDS14931.1; -.
DR   RefSeq; NP_997164.1; NM_207281.3.
DR   AlphaFoldDB; Q8CDZ2; -.
DR   SMR; Q8CDZ2; -.
DR   BioGRID; 240076; 260.
DR   STRING; 10090.ENSMUSP00000056481; -.
DR   PaxDb; Q8CDZ2; -.
DR   PRIDE; Q8CDZ2; -.
DR   DNASU; 403183; -.
DR   Ensembl; ENSMUST00000054801; ENSMUSP00000056481; ENSMUSG00000046828.
DR   GeneID; 403183; -.
DR   KEGG; mmu:403183; -.
DR   UCSC; uc007awk.1; mouse.
DR   CTD; 403183; -.
DR   MGI; MGI:2685837; Mettl21e.
DR   VEuPathDB; HostDB:ENSMUSG00000046828; -.
DR   eggNOG; KOG2793; Eukaryota.
DR   GeneTree; ENSGT00940000159229; -.
DR   HOGENOM; CLU_055721_0_0_1; -.
DR   InParanoid; Q8CDZ2; -.
DR   OMA; YLCQENT; -.
DR   OrthoDB; 1494909at2759; -.
DR   PhylomeDB; Q8CDZ2; -.
DR   TreeFam; TF354267; -.
DR   BioGRID-ORCS; 403183; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Mettl21e; mouse.
DR   PRO; PR:Q8CDZ2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8CDZ2; protein.
DR   Bgee; ENSMUSG00000046828; Expressed in knee joint and 35 other tissues.
DR   Genevisible; Q8CDZ2; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..244
FT                   /note="Protein-lysine methyltransferase METTL21E"
FT                   /id="PRO_0000329292"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  28067 MW;  BFBF32560A392D6C CRC64;
     MDLTVTHITH KETYKEPRDD DDDKQVVAEI MARSFIPTLI TTIPWEGFHF AGHEIQITEG
     KDCYGAFVWP SALVLCYFLE THAKQYNMVD KNVIEIGAGT GLVSIVASLL GARVIATDLP
     ELLGNLQYNI SRNTKMKCKH LPQVKELSWG VALDRNFPRS SNNFDYILAA DVVYAHPFLE
     ELLMTFDHLC KETTIILWAM RFRLEKENKF VDKFKELFDL EEISSFPSLN IKLYKAMKKN
     RRSA
 
 
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