Q13395 (TARB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TARBP1
Synonyms:	TRM3, TRP185

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1621 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.3 Ref.4
Subunit structure	Monomer and homodimer. Ref.1
Sequence similarities	Belongs to the RNA methyltransferase TrmH family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	nucleus Traceable author statement. Source: ProtInc
Molecular function	RNA binding Traceable author statement. Source: ProtInc RNA methyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1621

1621

Probable methyltransferase TARBP1

PRO_0000273201

Regions

Compositional bias

99 – 219

121

Ala-rich

Sites

Binding site

1566

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

1586

1

S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Binding site

1595

1

S-adenosyl-L-methionine; via amide nitrogen By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6

Modified residue

1442

1

Phosphoserine Ref.5

Natural variations

Natural variant

221

1

L → P.
Corresponds to variant rs12082990 [ dbSNP | Ensembl ].

VAR_030101

Natural variant

425

1

A → T.
Corresponds to variant rs10910439 [ dbSNP | Ensembl ].

VAR_030102

Natural variant

513

1

D → G.
Corresponds to variant rs35562024 [ dbSNP | Ensembl ].

VAR_061907

Natural variant

678

1

S → G.
Corresponds to variant rs4920246 [ dbSNP | Ensembl ].

VAR_030103

Natural variant

743

1

N → S.
Corresponds to variant rs2273872 [ dbSNP | Ensembl ].

VAR_030104

Natural variant

864

1

H → P.
Corresponds to variant rs4272658 [ dbSNP | Ensembl ].

VAR_030105

Natural variant

997

1

F → L.
Corresponds to variant rs12135427 [ dbSNP | Ensembl ].

VAR_030106

Natural variant

1038

1

T → I.
Corresponds to variant rs3820602 [ dbSNP | Ensembl ].

VAR_030107

Natural variant

1359

1

I → V.
Corresponds to variant rs3738616 [ dbSNP | Ensembl ].

VAR_030108

Natural variant

1461

1

I → V.
Corresponds to variant rs2275654 [ dbSNP | Ensembl ].

VAR_030109

Secondary structure

1

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1621

Helix Strand Turn

Details...

Beta strand

1465 – 1467

3

Helix

1474 – 1486

13

Beta strand

1490 – 1495

6

Helix

1497 – 1501

5

Helix

1503 – 1509

7

Helix

1512 – 1514

3

Beta strand

1518 – 1520

3

Helix

1523 – 1525

3

Helix

1526 – 1535

10

Beta strand

1539 – 1543

5

Helix

1552 – 1554

3

Beta strand

1559 – 1565

7

Turn

1568 – 1570

3

Helix

1574 – 1577

4

Beta strand

1581 – 1585

5

Beta strand

1590 – 1593

4

Helix

1597 – 1613

17

Sequences

	Sequence		Length	Mass (Da)
	Q13395 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A8C2BC62B7F1ADA8	FASTA	1,621	181,675
	10 20 30 40 50 60 MEWVLAEALL SQSRDPRALL GALCQGEASA ERVETLRFLL QRLEDEEARG SGGAGALPEA 70 80 90 100 110 120 AREVAAGYLV PLLRSLRGRP AGGPDPSLQP RHRRRVLRAA GAALRSCVRL AGRPQLAAAL 130 140 150 160 170 180 AEEALRDLLA GWRAPGAEAA VEVLAAVGPC LRPREDGPLL ERVAGTAVAL ALGGGGDGDE 190 200 210 220 230 240 AGPAEDAAAL VAGRLLPVLV QCGGAALRAV WGGLAAPGAS LGSGRVEEKL LVLSALAEKL 250 260 270 280 290 300 LPEPGGDRAR GAREAGPDAR RCWRFWRTVQ AGLGQADALT RKRARYLLQR AVEVSAELGA 310 320 330 340 350 360 DCTCGPQEGN GPSLFWWSER KKDELLKFWE NYILIMETLE GNQIHVIKPV LPKLNNLFEY 370 380 390 400 410 420 AVSEENGCWL FHPSWHMCIY KRMFESENKI LSKEGVIHFL ELYETKILPF SPEFSEFIIG 430 440 450 460 470 480 PLMDALSESS LYSRSPGQPI GSCSPLGLKL QKFLVTYISL LPEEIKSSFL LKFIRKMTSR 490 500 510 520 530 540 HWCAVPILFL SKALANVPRH KALGIDGLLA LRDVIHCTMI THQILLRGAA QCYLLQTAMN 550 560 570 580 590 600 LLDVEKVSLS DVSTFLMSLR QEESLGRGTS LWTELCDWLR VNESYFKPSP TCSSIGLHKT 610 620 630 640 650 660 SLNAYVKSIV QEYVKSSAWE TGENCFMPDW FEAKLVSLMV LLAVDVEGMK TQYSGKQRTE 670 680 690 700 710 720 NVLRIFLDPL LDVLMKFSTN AYMPLLKTDR CLQLLLKLLN TCRLKGSSAQ DDEVSTVLQN 730 740 750 760 770 780 FFMSTTESIS EFILRRLTMN ELNSVSDLDR CHLYLMVLTE LINLHLKVGW KRGNPIWRVI 790 800 810 820 830 840 SLLKNASIQH LQEMDSGQEP TVGSQIQRVV SMAALAMVCE AIDQKPELQL DSLHAGPLES 850 860 870 880 890 900 FLSSLQLNQT LQKPHAEEQS SYAHPLECSS VLEESSSSQG WGKIVAQYIH DQWVCLSFLL 910 920 930 940 950 960 KKYHTLIPTT GSEILEPFLP AVQMPIRTLQ SALEALTVLS SDQVLPVFHC LKVLVPKLLT 970 980 990 1000 1010 1020 SSESLCIESF DMAWKIISSL SNTQLIFWAN LKAFVQFVFD NKVLTIAAKI KGQAYFKIKE 1030 1040 1050 1060 1070 1080 IMYKIIEMSA IKTGVFNTLI SYCCQSWIVS ASNVSQGSLS SAKNYSELIL EACIFGTVFR 1090 1100 1110 1120 1130 1140 RDQRLVQDVQ TFIENLGHDC AANIVMENTK REDHYVRICA VKFLCLLDGS NMSHKLFIED 1150 1160 1170 1180 1190 1200 LAIKLLDKDE LVSKSKKRYY VNSLQHRVKN RVWQTLLVLF PRLDQNFLNG IIDRIFQAGF 1210 1220 1230 1240 1250 1260 TNNQASIKYF IEWIIILILH KFPQFLPKFW DCFSYGEENL KTSICTFLAV LSHLDIITQN 1270 1280 1290 1300 1310 1320 IPEKKLILKQ ALIVVLQWCF NHNFSVRLYA LVALKKLWTV CKVLSVEEFD ALTPVIESSL 1330 1340 1350 1360 1370 1380 HQVESMHGAG NAKKNWQRIQ EHFFFATFHP LKDYCLETIF YILPRLSGLI EDEWITIDKF 1390 1400 1410 1420 1430 1440 TRFTDVPLAA GFQWYLSQTQ LSKLKPGDWS QQDIGTNLVE ADNQAEWTDV QKKIIPWNSR 1450 1460 1470 1480 1490 1500 VSDLDLELLF QDRAARLGKS ISRLIVVASL IDKPTNLGGL CRTCEVFGAS VLVVGSLQCI 1510 1520 1530 1540 1550 1560 SDKQFQHLSV SAEQWLPLVE VKPPQLIDYL QQKKTEGYTI IGVEQTAKSL DLTQYCFPEK 1570 1580 1590 1600 1610 1620 SLLLLGNERE GIPANLIQQL DVCVEIPQQG IIRSLNVHVS GALLIWEYTR QQLLSHGDTK P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8846792] [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: 16710414] [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: 7638159] [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: 8626763] [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1442, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U38847 mRNA. Translation: AAC50379.1.
AL136124, AL355472 Genomic DNA. Translation: CAI22828.1.
AL355472, AL136124 Genomic DNA. Translation: CAI22931.1.

IPI

IPI00298447.

PIR

S62356.

RefSeq

NP_005637.3. NM_005646.3.

UniGene

Hs.498115.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HA8	X-ray	1.60	A/B	1438-1621	[»]

ProteinModelPortal

Q13395.

SMR

Q13395. Positions 1457-1615.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13395. 1 interaction.

STRING

Q13395.

PTM databases

PhosphoSite

Q13395.

Polymorphism databases

DMDM

74739787.

Proteomic databases

PRIDE

Q13395.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000040877; ENSP00000040877; ENSG00000059588.

GeneID

6894.

KEGG

hsa:6894.

UCSC

uc001hwd.1. human.

Organism-specific databases

CTD

6894.

GeneCards

GC01M234527.

HGNC

HGNC:11568. TARBP1.

HPA

CAB020810.
HPA024632.

MIM

605052. gene.

neXtProt

NX_Q13395.

PharmGKB

PA36333.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06333.

GeneTree

ENSGT00390000003939.

HOGENOM

HBG714207.

HOVERGEN

HBG094026.

InParanoid

Q13395.

OMA

TVFRRDQ.

OrthoDB

EOG4S7JP4.

PhylomeDB

Q13395.

Gene expression databases

ArrayExpress

Q13395.

Bgee

Q13395.

CleanEx

HS_TARBP1.

Genevestigator

Q13395.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR001537. SpoU_MeTrfase.
[Graphical view]

Pfam

PF00588. SpoU_methylase. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

ProtoNet

Search...

Other

NextBio

26945.

SOURCE

Search...

Entry information

Entry name

TARB1_HUMAN

Accession

Primary (citable) accession number: Q13395
Secondary accession number(s): Q9H581

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.