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TRM1L_MOUSE
ID   TRM1L_MOUSE             Reviewed;         728 AA.
AC   A2RSY6; Q0VGB9; Q3UFG1; Q3UKB0; Q8C2S4; Q8CI50; Q8R203; Q9CT68;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=TRMT1-like protein;
DE            EC=2.1.1.-;
GN   Name=Trmt1l;
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] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Pancreas, Placenta, and Thymus;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 202-728 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Brain, Eye, Kidney, and Mammary tumor;
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).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17198746; DOI=10.1016/j.gene.2006.11.004;
RA   Vauti F., Goller T., Beine R., Becker L., Klopstock T., Hoelter S.M.,
RA   Wurst W., Fuchs H., Gailus-Durner V., de Angelis M.H., Arnold H.-H.;
RT   "The mouse Trm1-like gene is expressed in neural tissues and plays a role
RT   in motor coordination and exploratory behaviour.";
RL   Gene 389:174-185(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play a role in motor coordination and exploratory
CC       behavior. {ECO:0000269|PubMed:17198746}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A2RSY6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2RSY6-2; Sequence=VSP_031047;
CC       Name=3;
CC         IsoId=A2RSY6-3; Sequence=VSP_031045, VSP_031046;
CC       Name=4;
CC         IsoId=A2RSY6-4; Sequence=VSP_031044;
CC   -!- TISSUE SPECIFICITY: Expressed in various neuronal structures during
CC       embryonic development, including spinal ganglia, trigeminal nerve and
CC       ganglion, olfactory and nasopharyngeal epithelium, nuclei of the
CC       metencephalon, thalamus and medulla oblongata. Also expressed in lung,
CC       esophagus, epiglottis, ependyma, vertebral column, spinal cord and
CC       brown adipose tissue. Expression persists in the adult brain with
CC       dynamically changing patterns in cortex and cerebellum.
CC       {ECO:0000269|PubMed:17198746}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and show no apparent anatomical
CC       defects. However, they display significantly altered motor coordination
CC       and aberrant exploratory behavior. {ECO:0000269|PubMed:17198746}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37478.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK004493; BAB23331.1; -; mRNA.
DR   EMBL; AK088077; BAC40131.1; -; mRNA.
DR   EMBL; AK146088; BAE26891.1; -; mRNA.
DR   EMBL; AK148524; BAE28600.1; -; mRNA.
DR   EMBL; BC022682; AAH22682.1; -; mRNA.
DR   EMBL; BC037478; AAH37478.1; ALT_INIT; mRNA.
DR   EMBL; BC110425; AAI10426.1; -; mRNA.
DR   EMBL; BC132299; AAI32300.1; -; mRNA.
DR   CCDS; CCDS15361.1; -. [A2RSY6-1]
DR   RefSeq; NP_081152.2; NM_026876.3.
DR   AlphaFoldDB; A2RSY6; -.
DR   SMR; A2RSY6; -.
DR   BioGRID; 221107; 3.
DR   IntAct; A2RSY6; 1.
DR   MINT; A2RSY6; -.
DR   STRING; 10090.ENSMUSP00000068309; -.
DR   iPTMnet; A2RSY6; -.
DR   PhosphoSitePlus; A2RSY6; -.
DR   EPD; A2RSY6; -.
DR   MaxQB; A2RSY6; -.
DR   PaxDb; A2RSY6; -.
DR   PeptideAtlas; A2RSY6; -.
DR   PRIDE; A2RSY6; -.
DR   ProteomicsDB; 300120; -. [A2RSY6-1]
DR   ProteomicsDB; 300121; -. [A2RSY6-2]
DR   ProteomicsDB; 300122; -. [A2RSY6-3]
DR   ProteomicsDB; 300123; -. [A2RSY6-4]
DR   DNASU; 98685; -.
DR   GeneID; 98685; -.
DR   KEGG; mmu:98685; -.
DR   UCSC; uc007cyr.1; mouse. [A2RSY6-4]
DR   UCSC; uc007cyt.1; mouse. [A2RSY6-3]
DR   UCSC; uc007cyu.1; mouse. [A2RSY6-1]
DR   UCSC; uc029qua.1; mouse. [A2RSY6-2]
DR   CTD; 81627; -.
DR   MGI; MGI:1916185; Trmt1l.
DR   eggNOG; KOG1253; Eukaryota.
DR   InParanoid; A2RSY6; -.
DR   OrthoDB; 1414511at2759; -.
DR   PhylomeDB; A2RSY6; -.
DR   TreeFam; TF300851; -.
DR   BioGRID-ORCS; 98685; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Trmt1l; mouse.
DR   PRO; PR:A2RSY6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; A2RSY6; protein.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR   Gene3D; 3.30.56.70; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR042296; tRNA_met_Trm1_C.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR10631; PTHR10631; 1.
DR   Pfam; PF02005; TRM; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Behavior; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Phosphoprotein; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..728
FT                   /note="TRMT1-like protein"
FT                   /id="PRO_0000317570"
FT   DOMAIN          224..683
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT   ZN_FING         181..203
FT                   /note="C2H2-type"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT   MOD_RES         607
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT   CROSSLNK        580
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT   VAR_SEQ         152..728
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031044"
FT   VAR_SEQ         285
FT                   /note="I -> K (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031045"
FT   VAR_SEQ         286..728
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031046"
FT   VAR_SEQ         645..728
FT                   /note="KLKKFLCCLSQAGFRVSRTHFDPMGIRTDAPLMQFKSILLKYSTPTYTGAQS
FT                   EGQMPPAAEDTVTDRVEMSVSDKAEASGCRRW -> NFLSLLQVKKIFVLSFASRLSSK
FT                   PNSL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031047"
FT   CONFLICT        24
FT                   /note="P -> R (in Ref. 1; BAE26891/BAE28600 and 2;
FT                   AAI10426)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="H -> D (in Ref. 1; BAC40131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="K -> Q (in Ref. 1; BAC40131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        436
FT                   /note="R -> I (in Ref. 1; BAB23331)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        614
FT                   /note="L -> V (in Ref. 1; BAE26891)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   728 AA;  80861 MW;  E39AE788EE72D903 CRC64;
     MENMAEEELL PQEKEEAQVR VPTPAPDSAP VPAPAADTAL DSAPTPDSDP APALAPAPAP
     ALSPSLASVP EEAESKRHIS IQRRLADLEK LAFGTEGDVD SASSLNSDNP GTENSQTCPL
     CPKEKFRAYS SHKLRRHLQN LHWKISVEFE GYRMCICHLA CRPVKPTIVG EQISSKLGAH
     YHCIICSATI TRRTDMLGHV KRHVNKGETK SRYIAASTAK SSNEILKETD TDIQVFPNYS
     IPQKTDSYFN PKMKLNRQII FCTLAALAKE RKPLECLDAF GATGIMGLQW AKHLGNAVKV
     TINDLNENSV TLIQKNCHLN KLKVVVDSEE KEEGDALEDD GTLGDIQVTR MDANVLMHLR
     SFDFIHLDPF GTSVNYLDSA FRNVRNLGIV SVTSTDISSL YAKAQHVARR HYGCNIVRTE
     YYKELAARIV VAAVARAAAR CNKGIEVLFA VALEHFVLVV VRVLRGPTSA DETAKKIQYL
     IHCQWCEERI FQKDGNMVEE NPYRQLPCNC HGSMPGKTAI ELGPLWSSSL FNTGFLKRML
     FESIHHGLDD IQPLIKTLIF ESECTPQSQC STHAPSNTNK QEENGVFVKT TDDTTIDIYS
     AQGKRKSNEM AINLAKKQKT DASTAHPPFY YNIHRHSIKG MNMPKLKKFL CCLSQAGFRV
     SRTHFDPMGI RTDAPLMQFK SILLKYSTPT YTGAQSEGQM PPAAEDTVTD RVEMSVSDKA
     EASGCRRW
 
 
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