TRM1L_HUMAN
ID TRM1L_HUMAN Reviewed; 733 AA.
AC Q7Z2T5; Q5TEN0; Q6ZMX0; Q8IWH5; Q8NC68; Q9BZQ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=TRMT1-like protein;
DE EC=2.1.1.-;
GN Name=TRMT1L; Synonyms=C1orf25, TRM1L; ORFNames=MSTP070;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human RGS8
RT gene from the 1q25 region encompassing the hereditary prostate cancer
RT (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 423-733.
RC TISSUE=Aorta;
RA Hui R.T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
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., Buerckstuemmer T.,
RA 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-612 AND SER-707, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-585, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May play a role in motor coordination and exploratory
CC behavior. {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z2T5; Q00403: GTF2B; NbExp=3; IntAct=EBI-1237316, EBI-389564;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z2T5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2T5-2; Sequence=VSP_031042, VSP_031043;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11318611}.
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=AAH39738.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAQ13590.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF288399; AAG60618.1; -; mRNA.
DR EMBL; AK074936; BAC11302.1; -; mRNA.
DR EMBL; AK074993; BAC11341.1; -; mRNA.
DR EMBL; AK131460; BAD18605.1; -; mRNA.
DR EMBL; AL109865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91190.1; -; Genomic_DNA.
DR EMBL; BC039738; AAH39738.1; ALT_SEQ; mRNA.
DR EMBL; BC045535; AAH45535.1; -; mRNA.
DR EMBL; AF163261; AAQ13590.1; ALT_INIT; mRNA.
DR CCDS; CCDS1366.1; -. [Q7Z2T5-1]
DR RefSeq; NP_001189352.1; NM_001202423.1.
DR RefSeq; NP_112196.3; NM_030934.4. [Q7Z2T5-1]
DR AlphaFoldDB; Q7Z2T5; -.
DR SMR; Q7Z2T5; -.
DR BioGRID; 123562; 162.
DR IntAct; Q7Z2T5; 43.
DR MINT; Q7Z2T5; -.
DR STRING; 9606.ENSP00000356476; -.
DR GlyGen; Q7Z2T5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z2T5; -.
DR MetOSite; Q7Z2T5; -.
DR PhosphoSitePlus; Q7Z2T5; -.
DR SwissPalm; Q7Z2T5; -.
DR BioMuta; TRMT1L; -.
DR DMDM; 166988174; -.
DR EPD; Q7Z2T5; -.
DR jPOST; Q7Z2T5; -.
DR MassIVE; Q7Z2T5; -.
DR MaxQB; Q7Z2T5; -.
DR PaxDb; Q7Z2T5; -.
DR PeptideAtlas; Q7Z2T5; -.
DR PRIDE; Q7Z2T5; -.
DR ProteomicsDB; 68967; -. [Q7Z2T5-1]
DR ProteomicsDB; 68968; -. [Q7Z2T5-2]
DR Antibodypedia; 20610; 90 antibodies from 15 providers.
DR DNASU; 81627; -.
DR Ensembl; ENST00000367506.10; ENSP00000356476.5; ENSG00000121486.12. [Q7Z2T5-1]
DR GeneID; 81627; -.
DR KEGG; hsa:81627; -.
DR MANE-Select; ENST00000367506.10; ENSP00000356476.5; NM_030934.5; NP_112196.3.
DR UCSC; uc001grf.5; human. [Q7Z2T5-1]
DR CTD; 81627; -.
DR GeneCards; TRMT1L; -.
DR HGNC; HGNC:16782; TRMT1L.
DR HPA; ENSG00000121486; Low tissue specificity.
DR MIM; 611673; gene.
DR neXtProt; NX_Q7Z2T5; -.
DR OpenTargets; ENSG00000121486; -.
DR PharmGKB; PA25612; -.
DR VEuPathDB; HostDB:ENSG00000121486; -.
DR eggNOG; KOG1253; Eukaryota.
DR GeneTree; ENSGT00530000063646; -.
DR HOGENOM; CLU_010862_3_0_1; -.
DR InParanoid; Q7Z2T5; -.
DR OMA; MIRENCQ; -.
DR OrthoDB; 1414511at2759; -.
DR PhylomeDB; Q7Z2T5; -.
DR TreeFam; TF300851; -.
DR PathwayCommons; Q7Z2T5; -.
DR SignaLink; Q7Z2T5; -.
DR BioGRID-ORCS; 81627; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; TRMT1L; human.
DR GenomeRNAi; 81627; -.
DR Pharos; Q7Z2T5; Tdark.
DR PRO; PR:Q7Z2T5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z2T5; protein.
DR Bgee; ENSG00000121486; Expressed in bronchial epithelial cell and 198 other tissues.
DR ExpressionAtlas; Q7Z2T5; baseline and differential.
DR Genevisible; Q7Z2T5; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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:0007610; P:behavior; IEA:UniProtKB-KW.
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.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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..733
FT /note="TRMT1-like protein"
FT /id="PRO_0000317568"
FT DOMAIN 227..688
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT ZN_FING 184..206
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031042"
FT VAR_SEQ 505..733
FT /note="ENPYRQLPCNCHGSMPGKTAIELGPLWSSSLFNTGFLKRMLFESLHHGLDDI
FT QTLIKTLIFESECTPQSQFSIHASSNVNKQEENGVFIKTTDDTTTDNYIAQGKRKSNEM
FT ITNLGKKQKTDVSTEHPPFYYNIHRHSIKGMNMPKLKKFLCYLSQAGFRVSRTHFDPMG
FT VRTDAPLMQFKSILLKYSTPTYTGGQSESHVQSASEDTVTERVEMSVNDKAEASGCRRW
FT -> DYSANFVISYTGFPFVNRQDIRKTHIDSCLVTVMEACLERQQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031043"
FT CONFLICT 156
FT /note="R -> G (in Ref. 2; BAC11302)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="N -> S (in Ref. 2; BAD18605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 733 AA; 81747 MW; 364B6BD4F22D1B08 CRC64;
MENMAEEELL PLEKEEVEVA QVQVPTPARD SAGVPAPAPD SALDSAPTPA SAPAPAPALA
QAPALSPSLA SAPEEAKSKR HISIQRQLAD LENLAFVTDG NFDSASSLNS DNLDAGNRQA
CPLCPKEKFR ACNSHKLRRH LQNLHWKVSV EFEGYRMCIC HLPCRPVKPN IIGEQITSKM
GAHYHCIICS ATITRRTDML GHVRRHMNKG ETKSSYIAAS TAKPPKEILK EADTDVQVCP
NYSIPQKTDS YFNPKMKLNR QLIFCTLAAL AEERKPLECL DAFGATGIMG LQWAKHLGNA
VKVTINDLNE NSVTLIQENC HLNKLKVVVD SKEKEKSDDI LEEGEKNLGN IKVTKMDANV
LMHLRSFDFI HLDPFGTSVN YLDSAFRNIR NLGIVSVTST DISSLYAKAQ HVARRHYGCN
IVRTEYYKEL AARIVVAAVA RAAARCNKGI EVLFAVALEH FVLVVVRVLR GPTSADETAK
KIQYLIHCQW CEERIFQKDG NMVEENPYRQ LPCNCHGSMP GKTAIELGPL WSSSLFNTGF
LKRMLFESLH HGLDDIQTLI KTLIFESECT PQSQFSIHAS SNVNKQEENG VFIKTTDDTT
TDNYIAQGKR KSNEMITNLG KKQKTDVSTE HPPFYYNIHR HSIKGMNMPK LKKFLCYLSQ
AGFRVSRTHF DPMGVRTDAP LMQFKSILLK YSTPTYTGGQ SESHVQSASE DTVTERVEMS
VNDKAEASGC RRW
