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Protein

Probable methyltransferase TARBP1

Gene

TARBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1566 – 15661S-adenosyl-L-methionine; via amide nitrogen1 Publication
Binding sitei1600 – 16001S-adenosyl-L-methionine1 Publication

GO - Molecular functioni

  • RNA binding Source: ProtInc
  • tRNA (guanine) methyltransferase activity Source: GO_Central

GO - Biological processi

  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • tRNA methylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Probable methyltransferase TARBP1 (EC:2.1.1.-)
Alternative name(s):
TAR RNA-binding protein 1
TAR RNA-binding protein of 185 kDa
Short name:
TRP-185
Gene namesi
Name:TARBP1
Synonyms:TRM3, TRP185
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11568. TARBP1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36333.

Polymorphism and mutation databases

BioMutaiTARBP1.
DMDMi74739787.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16211621Probable methyltransferase TARBP1PRO_0000273201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei1442 – 14421PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13395.
MaxQBiQ13395.
PaxDbiQ13395.
PRIDEiQ13395.

PTM databases

iPTMnetiQ13395.
PhosphoSiteiQ13395.

Expressioni

Gene expression databases

BgeeiQ13395.
CleanExiHS_TARBP1.
GenevisibleiQ13395. HS.

Organism-specific databases

HPAiCAB020810.
HPA024632.

Interactioni

Subunit structurei

Monomer and homodimer.2 Publications

Protein-protein interaction databases

BioGridi112757. 32 interactions.
IntActiQ13395. 8 interactions.
STRINGi9606.ENSP00000040877.

Structurei

Secondary structure

1
1621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1465 – 14673Combined sources
Helixi1474 – 148613Combined sources
Beta strandi1490 – 14956Combined sources
Helixi1497 – 15015Combined sources
Helixi1503 – 15097Combined sources
Helixi1512 – 15143Combined sources
Beta strandi1518 – 15203Combined sources
Helixi1523 – 15253Combined sources
Helixi1526 – 153510Combined sources
Beta strandi1539 – 15435Combined sources
Helixi1552 – 15543Combined sources
Beta strandi1559 – 15657Combined sources
Turni1568 – 15703Combined sources
Helixi1574 – 15774Combined sources
Beta strandi1581 – 15855Combined sources
Beta strandi1590 – 15934Combined sources
Helixi1597 – 161317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HA8X-ray1.60A/B1438-1621[»]
ProteinModelPortaliQ13395.
SMRiQ13395. Positions 1457-1615.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13395.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1543 – 15453S-adenosyl-L-methionine binding1 Publication
Regioni1586 – 159510S-adenosyl-L-methionine binding1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi99 – 219121Ala-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0839. Eukaryota.
COG0566. LUCA.
GeneTreeiENSGT00390000003939.
HOGENOMiHOG000154511.
HOVERGENiHBG094026.
InParanoidiQ13395.
OMAiFGTVFRR.
OrthoDBiEOG7QNVK6.
PhylomeDBiQ13395.
TreeFamiTF314976.

Family and domain databases

Gene3Di3.40.1280.10. 1 hit.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR016024. ARM-type_fold.
IPR025806. Prob_MeTrfase_TARBP1.
IPR001537. SpoU_MeTrfase.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF00588. SpoU_methylase. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF75217. SSF75217. 1 hit.

Sequencei

Sequence statusi: Complete.

Q13395-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEWVLAEALL SQSRDPRALL GALCQGEASA ERVETLRFLL QRLEDEEARG
60 70 80 90 100
SGGAGALPEA AREVAAGYLV PLLRSLRGRP AGGPDPSLQP RHRRRVLRAA
110 120 130 140 150
GAALRSCVRL AGRPQLAAAL AEEALRDLLA GWRAPGAEAA VEVLAAVGPC
160 170 180 190 200
LRPREDGPLL ERVAGTAVAL ALGGGGDGDE AGPAEDAAAL VAGRLLPVLV
210 220 230 240 250
QCGGAALRAV WGGLAAPGAS LGSGRVEEKL LVLSALAEKL LPEPGGDRAR
260 270 280 290 300
GAREAGPDAR RCWRFWRTVQ AGLGQADALT RKRARYLLQR AVEVSAELGA
310 320 330 340 350
DCTCGPQEGN GPSLFWWSER KKDELLKFWE NYILIMETLE GNQIHVIKPV
360 370 380 390 400
LPKLNNLFEY AVSEENGCWL FHPSWHMCIY KRMFESENKI LSKEGVIHFL
410 420 430 440 450
ELYETKILPF SPEFSEFIIG PLMDALSESS LYSRSPGQPI GSCSPLGLKL
460 470 480 490 500
QKFLVTYISL LPEEIKSSFL LKFIRKMTSR HWCAVPILFL SKALANVPRH
510 520 530 540 550
KALGIDGLLA LRDVIHCTMI THQILLRGAA QCYLLQTAMN LLDVEKVSLS
560 570 580 590 600
DVSTFLMSLR QEESLGRGTS LWTELCDWLR VNESYFKPSP TCSSIGLHKT
610 620 630 640 650
SLNAYVKSIV QEYVKSSAWE TGENCFMPDW FEAKLVSLMV LLAVDVEGMK
660 670 680 690 700
TQYSGKQRTE NVLRIFLDPL LDVLMKFSTN AYMPLLKTDR CLQLLLKLLN
710 720 730 740 750
TCRLKGSSAQ DDEVSTVLQN FFMSTTESIS EFILRRLTMN ELNSVSDLDR
760 770 780 790 800
CHLYLMVLTE LINLHLKVGW KRGNPIWRVI SLLKNASIQH LQEMDSGQEP
810 820 830 840 850
TVGSQIQRVV SMAALAMVCE AIDQKPELQL DSLHAGPLES FLSSLQLNQT
860 870 880 890 900
LQKPHAEEQS SYAHPLECSS VLEESSSSQG WGKIVAQYIH DQWVCLSFLL
910 920 930 940 950
KKYHTLIPTT GSEILEPFLP AVQMPIRTLQ SALEALTVLS SDQVLPVFHC
960 970 980 990 1000
LKVLVPKLLT SSESLCIESF DMAWKIISSL SNTQLIFWAN LKAFVQFVFD
1010 1020 1030 1040 1050
NKVLTIAAKI KGQAYFKIKE IMYKIIEMSA IKTGVFNTLI SYCCQSWIVS
1060 1070 1080 1090 1100
ASNVSQGSLS SAKNYSELIL EACIFGTVFR RDQRLVQDVQ TFIENLGHDC
1110 1120 1130 1140 1150
AANIVMENTK REDHYVRICA VKFLCLLDGS NMSHKLFIED LAIKLLDKDE
1160 1170 1180 1190 1200
LVSKSKKRYY VNSLQHRVKN RVWQTLLVLF PRLDQNFLNG IIDRIFQAGF
1210 1220 1230 1240 1250
TNNQASIKYF IEWIIILILH KFPQFLPKFW DCFSYGEENL KTSICTFLAV
1260 1270 1280 1290 1300
LSHLDIITQN IPEKKLILKQ ALIVVLQWCF NHNFSVRLYA LVALKKLWTV
1310 1320 1330 1340 1350
CKVLSVEEFD ALTPVIESSL HQVESMHGAG NAKKNWQRIQ EHFFFATFHP
1360 1370 1380 1390 1400
LKDYCLETIF YILPRLSGLI EDEWITIDKF TRFTDVPLAA GFQWYLSQTQ
1410 1420 1430 1440 1450
LSKLKPGDWS QQDIGTNLVE ADNQAEWTDV QKKIIPWNSR VSDLDLELLF
1460 1470 1480 1490 1500
QDRAARLGKS ISRLIVVASL IDKPTNLGGL CRTCEVFGAS VLVVGSLQCI
1510 1520 1530 1540 1550
SDKQFQHLSV SAEQWLPLVE VKPPQLIDYL QQKKTEGYTI IGVEQTAKSL
1560 1570 1580 1590 1600
DLTQYCFPEK SLLLLGNERE GIPANLIQQL DVCVEIPQQG IIRSLNVHVS
1610 1620
GALLIWEYTR QQLLSHGDTK P
Length:1,621
Mass (Da):181,675
Last modified:November 1, 1996 - v1
Checksum:iA8C2BC62B7F1ADA8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211L → P.
Corresponds to variant rs12082990 [ dbSNP | Ensembl ].
VAR_030101
Natural varianti425 – 4251A → T.
Corresponds to variant rs10910439 [ dbSNP | Ensembl ].
VAR_030102
Natural varianti513 – 5131D → G.
Corresponds to variant rs35562024 [ dbSNP | Ensembl ].
VAR_061907
Natural varianti678 – 6781S → G.
Corresponds to variant rs4920246 [ dbSNP | Ensembl ].
VAR_030103
Natural varianti743 – 7431N → S.
Corresponds to variant rs2273872 [ dbSNP | Ensembl ].
VAR_030104
Natural varianti864 – 8641H → P.
Corresponds to variant rs4272658 [ dbSNP | Ensembl ].
VAR_030105
Natural varianti997 – 9971F → L.
Corresponds to variant rs12135427 [ dbSNP | Ensembl ].
VAR_030106
Natural varianti1038 – 10381T → I.
Corresponds to variant rs3820602 [ dbSNP | Ensembl ].
VAR_030107
Natural varianti1359 – 13591I → V.
Corresponds to variant rs3738616 [ dbSNP | Ensembl ].
VAR_030108
Natural varianti1461 – 14611I → V.
Corresponds to variant rs2275654 [ dbSNP | Ensembl ].
VAR_030109

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38847 mRNA. Translation: AAC50379.1.
AL136124, AL355472 Genomic DNA. Translation: CAI22828.1.
AL355472, AL136124 Genomic DNA. Translation: CAI22931.1.
CCDSiCCDS1601.1.
PIRiS62356.
RefSeqiNP_005637.3. NM_005646.3.
UniGeneiHs.498115.

Genome annotation databases

EnsembliENST00000040877; ENSP00000040877; ENSG00000059588.
GeneIDi6894.
KEGGihsa:6894.
UCSCiuc001hwd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38847 mRNA. Translation: AAC50379.1.
AL136124, AL355472 Genomic DNA. Translation: CAI22828.1.
AL355472, AL136124 Genomic DNA. Translation: CAI22931.1.
CCDSiCCDS1601.1.
PIRiS62356.
RefSeqiNP_005637.3. NM_005646.3.
UniGeneiHs.498115.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HA8X-ray1.60A/B1438-1621[»]
ProteinModelPortaliQ13395.
SMRiQ13395. Positions 1457-1615.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112757. 32 interactions.
IntActiQ13395. 8 interactions.
STRINGi9606.ENSP00000040877.

PTM databases

iPTMnetiQ13395.
PhosphoSiteiQ13395.

Polymorphism and mutation databases

BioMutaiTARBP1.
DMDMi74739787.

Proteomic databases

EPDiQ13395.
MaxQBiQ13395.
PaxDbiQ13395.
PRIDEiQ13395.

Protocols and materials databases

DNASUi6894.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000040877; ENSP00000040877; ENSG00000059588.
GeneIDi6894.
KEGGihsa:6894.
UCSCiuc001hwd.3. human.

Organism-specific databases

CTDi6894.
GeneCardsiTARBP1.
HGNCiHGNC:11568. TARBP1.
HPAiCAB020810.
HPA024632.
MIMi605052. gene.
neXtProtiNX_Q13395.
PharmGKBiPA36333.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0839. Eukaryota.
COG0566. LUCA.
GeneTreeiENSGT00390000003939.
HOGENOMiHOG000154511.
HOVERGENiHBG094026.
InParanoidiQ13395.
OMAiFGTVFRR.
OrthoDBiEOG7QNVK6.
PhylomeDBiQ13395.
TreeFamiTF314976.

Miscellaneous databases

ChiTaRSiTARBP1. human.
EvolutionaryTraceiQ13395.
GeneWikiiTARBP1.
GenomeRNAii6894.
NextBioi26945.
PROiQ13395.
SOURCEiSearch...

Gene expression databases

BgeeiQ13395.
CleanExiHS_TARBP1.
GenevisibleiQ13395. HS.

Family and domain databases

Gene3Di3.40.1280.10. 1 hit.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR016024. ARM-type_fold.
IPR025806. Prob_MeTrfase_TARBP1.
IPR001537. SpoU_MeTrfase.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF00588. SpoU_methylase. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF75217. SSF75217. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cellular factor TRP-185 regulates RNA polymerase II binding to HIV-1 TAR RNA."
    Wu-Baer F., Lane W.S., Gaynor R.B.
    EMBO J. 14:5995-6009(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1404-1427 AND 1535-1548, FUNCTION, SUBUNIT, RNA-BINDING.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat."
    Wu-Baer F., Sigman D., Gaynor R.B.
    Proc. Natl. Acad. Sci. U.S.A. 92:7153-7157(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "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."
    Wu-Baer F., Lane W.S., Gaynor R.B.
    J. Biol. Chem. 271:4201-4208(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure of the methyltransferase domain of human TARBP1."
    Wu H., Min J., Zeng H., Plotnikov A.N.
    Proteins 72:519-525(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1438-1621 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, SUBUNIT.

Entry informationi

Entry nameiTARB1_HUMAN
AccessioniPrimary (citable) accession number: Q13395
Secondary accession number(s): Q9H581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.