TARB1_HUMAN
ID TARB1_HUMAN Reviewed; 1621 AA.
AC Q13395; Q9H581;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable methyltransferase TARBP1;
DE EC=2.1.1.-;
DE AltName: Full=TAR RNA-binding protein 1;
DE AltName: Full=TAR RNA-binding protein of 185 kDa;
DE Short=TRP-185;
GN Name=TARBP1; Synonyms=TRM3, TRP185;
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], PROTEIN SEQUENCE OF 1404-1427 AND 1535-1548,
RP FUNCTION, SUBUNIT, AND RNA-BINDING.
RX PubMed=8846792; DOI=10.1002/j.1460-2075.1995.tb00288.x;
RA Wu-Baer F., Lane W.S., Gaynor R.B.;
RT "The cellular factor TRP-185 regulates RNA polymerase II binding to HIV-1
RT TAR RNA.";
RL EMBO J. 14:5995-6009(1995).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=7638159; DOI=10.1073/pnas.92.16.7153;
RA Wu-Baer F., Sigman D., Gaynor R.B.;
RT "Specific binding of RNA polymerase II to the human immunodeficiency virus
RT trans-activating region RNA is regulated by cellular cofactors and Tat.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7153-7157(1995).
RN [4]
RP FUNCTION.
RX PubMed=8626763; DOI=10.1074/jbc.271.8.4201;
RA Wu-Baer F., Lane W.S., Gaynor R.B.;
RT "Identification of a group of cellular cofactors that stimulate the binding
RT of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR
RT RNA.";
RL J. Biol. Chem. 271:4201-4208(1996).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1442, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1438-1621 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, AND SUBUNIT.
RX PubMed=18412263; DOI=10.1002/prot.22065;
RA Wu H., Min J., Zeng H., Plotnikov A.N.;
RT "Crystal structure of the methyltransferase domain of human TARBP1.";
RL Proteins 72:519-525(2008).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC which methylates RNA molecules such as tRNAs.
CC {ECO:0000305|PubMed:18412263}.
CC -!- FUNCTION: (Microbial infection) In case of infection by HIV-1, it binds
CC to the loop region of TAR RNA, a region also bound by RNA polymerase II
CC (PubMed:7638159, PubMed:8626763, PubMed:8846792). Binding of TARBP1 and
CC RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting
CC that TARBP1 may function alone or in conjunction with HIV-1 Tat to
CC disengage RNA polymerase II from HIV-1 TAR RNA (PubMed:7638159,
CC PubMed:8626763, PubMed:8846792). {ECO:0000269|PubMed:7638159,
CC ECO:0000269|PubMed:8626763, ECO:0000269|PubMed:8846792}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:18412263,
CC ECO:0000269|PubMed:8846792}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; U38847; AAC50379.1; -; mRNA.
DR EMBL; AL136124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1601.1; -.
DR PIR; S62356; S62356.
DR RefSeq; NP_005637.3; NM_005646.3.
DR PDB; 2HA8; X-ray; 1.60 A; A/B=1438-1621.
DR PDBsum; 2HA8; -.
DR AlphaFoldDB; Q13395; -.
DR SMR; Q13395; -.
DR BioGRID; 112757; 71.
DR IntAct; Q13395; 31.
DR STRING; 9606.ENSP00000040877; -.
DR ChEMBL; CHEMBL2807; -.
DR iPTMnet; Q13395; -.
DR PhosphoSitePlus; Q13395; -.
DR BioMuta; TARBP1; -.
DR DMDM; 74739787; -.
DR EPD; Q13395; -.
DR jPOST; Q13395; -.
DR MassIVE; Q13395; -.
DR MaxQB; Q13395; -.
DR PaxDb; Q13395; -.
DR PeptideAtlas; Q13395; -.
DR PRIDE; Q13395; -.
DR ProteomicsDB; 59365; -.
DR Antibodypedia; 20805; 74 antibodies from 24 providers.
DR DNASU; 6894; -.
DR Ensembl; ENST00000040877.2; ENSP00000040877.1; ENSG00000059588.10.
DR GeneID; 6894; -.
DR KEGG; hsa:6894; -.
DR MANE-Select; ENST00000040877.2; ENSP00000040877.1; NM_005646.4; NP_005637.3.
DR UCSC; uc001hwd.3; human.
DR CTD; 6894; -.
DR DisGeNET; 6894; -.
DR GeneCards; TARBP1; -.
DR HGNC; HGNC:11568; TARBP1.
DR HPA; ENSG00000059588; Low tissue specificity.
DR MIM; 605052; gene.
DR neXtProt; NX_Q13395; -.
DR OpenTargets; ENSG00000059588; -.
DR PharmGKB; PA36333; -.
DR VEuPathDB; HostDB:ENSG00000059588; -.
DR eggNOG; KOG0839; Eukaryota.
DR GeneTree; ENSGT00390000003939; -.
DR HOGENOM; CLU_002618_1_1_1; -.
DR InParanoid; Q13395; -.
DR OMA; YAHPSEC; -.
DR OrthoDB; 171334at2759; -.
DR PhylomeDB; Q13395; -.
DR TreeFam; TF314976; -.
DR BRENDA; 2.1.1.34; 2681.
DR PathwayCommons; Q13395; -.
DR SignaLink; Q13395; -.
DR BioGRID-ORCS; 6894; 22 hits in 1080 CRISPR screens.
DR ChiTaRS; TARBP1; human.
DR EvolutionaryTrace; Q13395; -.
DR GeneWiki; TARBP1; -.
DR GenomeRNAi; 6894; -.
DR Pharos; Q13395; Tbio.
DR PRO; PR:Q13395; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13395; protein.
DR Bgee; ENSG00000059588; Expressed in right hemisphere of cerebellum and 200 other tissues.
DR Genevisible; Q13395; HS.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR CDD; cd18091; SpoU-like_TRM3-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025806; Prob_MeTrfase_TARBP1.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR045330; Trm3/TARBP1.
DR InterPro; IPR044748; Trm3/TARBP1_C.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12029; PTHR12029; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Methyltransferase;
KW Phosphoprotein; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..1621
FT /note="Probable methyltransferase TARBP1"
FT /id="PRO_0000273201"
FT BINDING 1543..1545
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18412263"
FT BINDING 1566
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18412263"
FT BINDING 1586..1595
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18412263"
FT BINDING 1600
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18412263"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 1442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VARIANT 221
FT /note="L -> P (in dbSNP:rs12082990)"
FT /id="VAR_030101"
FT VARIANT 425
FT /note="A -> T (in dbSNP:rs10910439)"
FT /id="VAR_030102"
FT VARIANT 513
FT /note="D -> G (in dbSNP:rs35562024)"
FT /id="VAR_061907"
FT VARIANT 678
FT /note="S -> G (in dbSNP:rs4920246)"
FT /id="VAR_030103"
FT VARIANT 743
FT /note="N -> S (in dbSNP:rs2273872)"
FT /id="VAR_030104"
FT VARIANT 864
FT /note="H -> P (in dbSNP:rs4272658)"
FT /id="VAR_030105"
FT VARIANT 997
FT /note="F -> L (in dbSNP:rs12135427)"
FT /id="VAR_030106"
FT VARIANT 1038
FT /note="T -> I (in dbSNP:rs3820602)"
FT /id="VAR_030107"
FT VARIANT 1359
FT /note="I -> V (in dbSNP:rs3738616)"
FT /id="VAR_030108"
FT VARIANT 1461
FT /note="I -> V (in dbSNP:rs2275654)"
FT /id="VAR_030109"
FT STRAND 1465..1467
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1474..1486
FT /evidence="ECO:0007829|PDB:2HA8"
FT STRAND 1490..1495
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1497..1501
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1503..1509
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1512..1514
FT /evidence="ECO:0007829|PDB:2HA8"
FT STRAND 1518..1520
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1523..1525
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1526..1535
FT /evidence="ECO:0007829|PDB:2HA8"
FT STRAND 1539..1543
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1552..1554
FT /evidence="ECO:0007829|PDB:2HA8"
FT STRAND 1559..1565
FT /evidence="ECO:0007829|PDB:2HA8"
FT TURN 1568..1570
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1574..1577
FT /evidence="ECO:0007829|PDB:2HA8"
FT STRAND 1581..1585
FT /evidence="ECO:0007829|PDB:2HA8"
FT STRAND 1590..1593
FT /evidence="ECO:0007829|PDB:2HA8"
FT HELIX 1597..1613
FT /evidence="ECO:0007829|PDB:2HA8"
SQ SEQUENCE 1621 AA; 181675 MW; A8C2BC62B7F1ADA8 CRC64;
MEWVLAEALL SQSRDPRALL GALCQGEASA ERVETLRFLL QRLEDEEARG SGGAGALPEA
AREVAAGYLV PLLRSLRGRP AGGPDPSLQP RHRRRVLRAA GAALRSCVRL AGRPQLAAAL
AEEALRDLLA GWRAPGAEAA VEVLAAVGPC LRPREDGPLL ERVAGTAVAL ALGGGGDGDE
AGPAEDAAAL VAGRLLPVLV QCGGAALRAV WGGLAAPGAS LGSGRVEEKL LVLSALAEKL
LPEPGGDRAR GAREAGPDAR RCWRFWRTVQ AGLGQADALT RKRARYLLQR AVEVSAELGA
DCTCGPQEGN GPSLFWWSER KKDELLKFWE NYILIMETLE GNQIHVIKPV LPKLNNLFEY
AVSEENGCWL FHPSWHMCIY KRMFESENKI LSKEGVIHFL ELYETKILPF SPEFSEFIIG
PLMDALSESS LYSRSPGQPI GSCSPLGLKL QKFLVTYISL LPEEIKSSFL LKFIRKMTSR
HWCAVPILFL SKALANVPRH KALGIDGLLA LRDVIHCTMI THQILLRGAA QCYLLQTAMN
LLDVEKVSLS DVSTFLMSLR QEESLGRGTS LWTELCDWLR VNESYFKPSP TCSSIGLHKT
SLNAYVKSIV QEYVKSSAWE TGENCFMPDW FEAKLVSLMV LLAVDVEGMK TQYSGKQRTE
NVLRIFLDPL LDVLMKFSTN AYMPLLKTDR CLQLLLKLLN TCRLKGSSAQ DDEVSTVLQN
FFMSTTESIS EFILRRLTMN ELNSVSDLDR CHLYLMVLTE LINLHLKVGW KRGNPIWRVI
SLLKNASIQH LQEMDSGQEP TVGSQIQRVV SMAALAMVCE AIDQKPELQL DSLHAGPLES
FLSSLQLNQT LQKPHAEEQS SYAHPLECSS VLEESSSSQG WGKIVAQYIH DQWVCLSFLL
KKYHTLIPTT GSEILEPFLP AVQMPIRTLQ SALEALTVLS SDQVLPVFHC LKVLVPKLLT
SSESLCIESF DMAWKIISSL SNTQLIFWAN LKAFVQFVFD NKVLTIAAKI KGQAYFKIKE
IMYKIIEMSA IKTGVFNTLI SYCCQSWIVS ASNVSQGSLS SAKNYSELIL EACIFGTVFR
RDQRLVQDVQ TFIENLGHDC AANIVMENTK REDHYVRICA VKFLCLLDGS NMSHKLFIED
LAIKLLDKDE LVSKSKKRYY VNSLQHRVKN RVWQTLLVLF PRLDQNFLNG IIDRIFQAGF
TNNQASIKYF IEWIIILILH KFPQFLPKFW DCFSYGEENL KTSICTFLAV LSHLDIITQN
IPEKKLILKQ ALIVVLQWCF NHNFSVRLYA LVALKKLWTV CKVLSVEEFD ALTPVIESSL
HQVESMHGAG NAKKNWQRIQ EHFFFATFHP LKDYCLETIF YILPRLSGLI EDEWITIDKF
TRFTDVPLAA GFQWYLSQTQ LSKLKPGDWS QQDIGTNLVE ADNQAEWTDV QKKIIPWNSR
VSDLDLELLF QDRAARLGKS ISRLIVVASL IDKPTNLGGL CRTCEVFGAS VLVVGSLQCI
SDKQFQHLSV SAEQWLPLVE VKPPQLIDYL QQKKTEGYTI IGVEQTAKSL DLTQYCFPEK
SLLLLGNERE GIPANLIQQL DVCVEIPQQG IIRSLNVHVS GALLIWEYTR QQLLSHGDTK
P
