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Probable methyltransferase TARBP1 (EC 2.1.1.-) (TAR RNA-binding protein 1) (TAR RNA-binding protein of 185 kDa) (TRP-185)

 TARB1_HUMAN             Reviewed;        1621 AA.
Q13395; Q9H581;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 139.
RecName: Full=Probable methyltransferase TARBP1;
EC=2.1.1.-;
AltName: Full=TAR RNA-binding protein 1;
AltName: Full=TAR RNA-binding protein of 185 kDa;
Short=TRP-185;
Name=TARBP1; Synonyms=TRM3, TRP185;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1404-1427 AND
1535-1548, FUNCTION, SUBUNIT, AND RNA-BINDING.
PubMed=8846792;
Wu-Baer F., Lane W.S., Gaynor R.B.;
"The cellular factor TRP-185 regulates RNA polymerase II binding to
HIV-1 TAR RNA.";
EMBO J. 14:5995-6009(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
FUNCTION.
PubMed=7638159; DOI=10.1073/pnas.92.16.7153;
Wu-Baer F., Sigman D., Gaynor R.B.;
"Specific binding of RNA polymerase II to the human immunodeficiency
virus trans-activating region RNA is regulated by cellular cofactors
and Tat.";
Proc. Natl. Acad. Sci. U.S.A. 92:7153-7157(1995).
[4]
FUNCTION.
PubMed=8626763; DOI=10.1074/jbc.271.8.4201;
Wu-Baer F., Lane W.S., Gaynor R.B.;
"Identification of a group of cellular cofactors that stimulate the
binding of RNA polymerase II and TRP-185 to human immunodeficiency
virus 1 TAR RNA.";
J. Biol. Chem. 271:4201-4208(1996).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1442, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[8]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1438-1621 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE, AND SUBUNIT.
PubMed=18412263; DOI=10.1002/prot.22065;
Wu H., Min J., Zeng H., Plotnikov A.N.;
"Crystal structure of the methyltransferase domain of human TARBP1.";
Proteins 72:519-525(2008).
-!- FUNCTION: Probable S-adenosyl-L-methionine-dependent
methyltransferase which methylates RNA molecules such as tRNAs. In
case of infection by HIV-1, it binds to the loop region of TAR
RNA, a region also bound by RNA polymerase II. Binding of TARBP1
and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive,
suggesting that TARBP1 may function alone or in conjunction with
HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May
act by methylating HIV-1 TAR RNA. {ECO:0000269|PubMed:7638159,
ECO:0000269|PubMed:8626763, ECO:0000269|PubMed:8846792}.
-!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:18412263,
ECO:0000269|PubMed:8846792}.
-!- SIMILARITY: Belongs to the class IV-like SAM-binding
methyltransferase superfamily. RNA methyltransferase TrmH family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U38847; AAC50379.1; -; mRNA.
EMBL; AL136124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS1601.1; -.
PIR; S62356; S62356.
RefSeq; NP_005637.3; NM_005646.3.
UniGene; Hs.498115; -.
PDB; 2HA8; X-ray; 1.60 A; A/B=1438-1621.
PDBsum; 2HA8; -.
ProteinModelPortal; Q13395; -.
SMR; Q13395; -.
BioGrid; 112757; 42.
IntAct; Q13395; 8.
STRING; 9606.ENSP00000040877; -.
iPTMnet; Q13395; -.
PhosphoSitePlus; Q13395; -.
BioMuta; TARBP1; -.
DMDM; 74739787; -.
EPD; Q13395; -.
MaxQB; Q13395; -.
PaxDb; Q13395; -.
PeptideAtlas; Q13395; -.
PRIDE; Q13395; -.
ProteomicsDB; 59365; -.
DNASU; 6894; -.
Ensembl; ENST00000040877; ENSP00000040877; ENSG00000059588.
GeneID; 6894; -.
KEGG; hsa:6894; -.
UCSC; uc001hwd.3; human.
CTD; 6894; -.
DisGeNET; 6894; -.
EuPathDB; HostDB:ENSG00000059588.9; -.
GeneCards; TARBP1; -.
HGNC; HGNC:11568; TARBP1.
HPA; CAB020810; -.
HPA; HPA024632; -.
MIM; 605052; gene.
neXtProt; NX_Q13395; -.
OpenTargets; ENSG00000059588; -.
PharmGKB; PA36333; -.
eggNOG; KOG0839; Eukaryota.
eggNOG; COG0566; LUCA.
GeneTree; ENSGT00390000003939; -.
HOGENOM; HOG000154511; -.
HOVERGEN; HBG094026; -.
InParanoid; Q13395; -.
KO; K15333; -.
OMA; EGNQIHV; -.
OrthoDB; EOG091G0UYQ; -.
PhylomeDB; Q13395; -.
TreeFam; TF314976; -.
ChiTaRS; TARBP1; human.
EvolutionaryTrace; Q13395; -.
GeneWiki; TARBP1; -.
GenomeRNAi; 6894; -.
PRO; PR:Q13395; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000059588; Expressed in 227 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_TARBP1; -.
Genevisible; Q13395; HS.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; TAS:ProtInc.
GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IBA:GO_Central.
GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IBA:GO_Central.
GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
Gene3D; 3.40.1280.10; -; 1.
InterPro; IPR029028; Alpha/beta_knot_MTases.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR025806; Prob_MeTrfase_TARBP1.
InterPro; IPR001537; SpoU_MeTrfase.
InterPro; IPR029026; tRNA_m1G_MTases_N.
Pfam; PF00588; SpoU_methylase; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF75217; SSF75217; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Methyltransferase; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 1621 Probable methyltransferase TARBP1.
/FTId=PRO_0000273201.
REGION 1543 1545 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:18412263}.
REGION 1586 1595 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:18412263}.
COMPBIAS 99 219 Ala-rich.
BINDING 1566 1566 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000269|PubMed:18412263}.
BINDING 1600 1600 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:18412263}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 1442 1442 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VARIANT 221 221 L -> P (in dbSNP:rs12082990).
/FTId=VAR_030101.
VARIANT 425 425 A -> T (in dbSNP:rs10910439).
/FTId=VAR_030102.
VARIANT 513 513 D -> G (in dbSNP:rs35562024).
/FTId=VAR_061907.
VARIANT 678 678 S -> G (in dbSNP:rs4920246).
/FTId=VAR_030103.
VARIANT 743 743 N -> S (in dbSNP:rs2273872).
/FTId=VAR_030104.
VARIANT 864 864 H -> P (in dbSNP:rs4272658).
/FTId=VAR_030105.
VARIANT 997 997 F -> L (in dbSNP:rs12135427).
/FTId=VAR_030106.
VARIANT 1038 1038 T -> I (in dbSNP:rs3820602).
/FTId=VAR_030107.
VARIANT 1359 1359 I -> V (in dbSNP:rs3738616).
/FTId=VAR_030108.
VARIANT 1461 1461 I -> V (in dbSNP:rs2275654).
/FTId=VAR_030109.
STRAND 1465 1467 {ECO:0000244|PDB:2HA8}.
HELIX 1474 1486 {ECO:0000244|PDB:2HA8}.
STRAND 1490 1495 {ECO:0000244|PDB:2HA8}.
HELIX 1497 1501 {ECO:0000244|PDB:2HA8}.
HELIX 1503 1509 {ECO:0000244|PDB:2HA8}.
HELIX 1512 1514 {ECO:0000244|PDB:2HA8}.
STRAND 1518 1520 {ECO:0000244|PDB:2HA8}.
HELIX 1523 1525 {ECO:0000244|PDB:2HA8}.
HELIX 1526 1535 {ECO:0000244|PDB:2HA8}.
STRAND 1539 1543 {ECO:0000244|PDB:2HA8}.
HELIX 1552 1554 {ECO:0000244|PDB:2HA8}.
STRAND 1559 1565 {ECO:0000244|PDB:2HA8}.
TURN 1568 1570 {ECO:0000244|PDB:2HA8}.
HELIX 1574 1577 {ECO:0000244|PDB:2HA8}.
STRAND 1581 1585 {ECO:0000244|PDB:2HA8}.
STRAND 1590 1593 {ECO:0000244|PDB:2HA8}.
HELIX 1597 1613 {ECO:0000244|PDB:2HA8}.
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


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