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A2RUC4 (TYW5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA wybutosine-synthesizing protein 5

Short name=hTYW5
EC=1.14.11.42
Alternative name(s):
tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase
Gene names
Name:TYW5
Synonyms:C2orf60
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

tRNA hydroxylase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW*). OHyW* being further transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of wybutosine found in higher eukaryotes. Ref.5

Catalytic activity

7-(3-amino-3-carboxypropyl)wyosine37 in tRNA(Phe) + 2-oxoglutarate + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNA(Phe) + succinate + CO2.

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.6

Pathway

tRNA modification; wybutosine-tRNA(Phe) biosynthesis. Ref.5 Ref.6

Subunit structure

Homodimer. Ref.6

Sequence similarities

Belongs to the TYW5 family.

Contains 1 JmjC domain.

Sequence caution

The sequence AAH63502.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A2RUC4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: A2RUC4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315tRNA wybutosine-synthesizing protein 5
PRO_0000309274

Regions

Domain102 – 267166JmjC

Sites

Metal binding1601Iron; catalytic
Metal binding1621Iron; catalytic
Metal binding2351Iron; catalytic
Binding site10612-oxoglutarate
Binding site16612-oxoglutarate
Binding site17512-oxoglutarate

Natural variations

Alternative sequence1 – 163163Missing in isoform 2.
VSP_029106
Natural variant501S → G.
Corresponds to variant rs10497844 [ dbSNP | Ensembl ].
VAR_036926

Experimental info

Mutagenesis1081R → A: Abolishes enzyme activity and ability to bind tRNA. Ref.6
Mutagenesis1491R → A: Abolishes enzyme activity and ability to bind tRNA. Ref.6

Secondary structure

............................................................. 315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: F291C48E8CA729FE

FASTA31536,548
        10         20         30         40         50         60 
MAGQHLPVPR LEGVSREQFM QHLYPQRKPL VLEGIDLGPC TSKWTVDYLS QVGGKKEVKI 

        70         80         90        100        110        120 
HVAAVAQMDF ISKNFVYRTL PFDQLVQRAA EEKHKEFFVS EDEKYYLRSL GEDPRKDVAD 

       130        140        150        160        170        180 
IRKQFPLLKG DIKFPEFFKE EQFFSSVFRI SSPGLQLWTH YDVMDNLLIQ VTGKKRVVLF 

       190        200        210        220        230        240 
SPRDAQYLYL KGTKSEVLNI DNPDLAKYPL FSKARRYECS LEAGDVLFIP ALWFHNVISE 

       250        260        270        280        290        300 
EFGVGVNIFW KHLPSECYDK TDTYGNKDPT AASRAAQILD RALKTLAELP EEYRDFYARR 

       310 
MVLHIQDKAY SKNSE 

« Hide

Isoform 2 [UniParc].

Checksum: 3FF012BC9E0CAED4
Show »

FASTA15217,526

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Tongue.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Retinoblastoma.
[5]"Expanding role of the jumonji C domain as an RNA hydroxylase."
Noma A., Ishitani R., Kato M., Nagao A., Nureki O., Suzuki T.
J. Biol. Chem. 285:34503-34507(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PATHWAY.
[6]"Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification."
Kato M., Araiso Y., Noma A., Nagao A., Suzuki T., Ishitani R., Nureki O.
Nucleic Acids Res. 39:1576-1585(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-311 IN COMPLEX WITH 2-OXOGLUTARATE AND NICKEL ION, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-108 AND ARG-149.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK095272 mRNA. Translation: BAC04517.1.
AK298977 mRNA. Translation: BAG61071.1.
AC097717 Genomic DNA. Translation: AAY24162.1.
CH471063 Genomic DNA. Translation: EAW70191.1.
BC063502 mRNA. Translation: AAH63502.1. Different initiation.
BC132835 mRNA. Translation: AAI32836.1.
BC136837 mRNA. Translation: AAI36838.1.
CCDSCCDS42795.1. [A2RUC4-1]
RefSeqNP_001034782.1. NM_001039693.2. [A2RUC4-1]
UniGeneHs.204619.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AL5X-ray2.50A/B/C/D1-315[»]
3AL6X-ray2.80A/B/C/D1-315[»]
ProteinModelPortalA2RUC4.
SMRA2RUC4. Positions 1-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000346627.

PTM databases

PhosphoSiteA2RUC4.

Proteomic databases

MaxQBA2RUC4.
PaxDbA2RUC4.
PRIDEA2RUC4.

Protocols and materials databases

DNASU129450.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354611; ENSP00000346627; ENSG00000162971. [A2RUC4-1]
GeneID129450.
KEGGhsa:129450.
UCSCuc002uvi.4. human. [A2RUC4-1]
uc002uvj.4. human. [A2RUC4-2]

Organism-specific databases

CTD129450.
GeneCardsGC02M200794.
H-InvDBHIX0002719.
HGNCHGNC:26754. TYW5.
HPAHPA045803.
neXtProtNX_A2RUC4.
PharmGKBPA162379298.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276154.
HOVERGENHBG096249.
InParanoidA2RUC4.
KOK18066.
OMARMVLRIQ.
OrthoDBEOG7X3QRF.
PhylomeDBA2RUC4.
TreeFamTF332364.

Enzyme and pathway databases

UniPathwayUPA00375.

Gene expression databases

ArrayExpressA2RUC4.
BgeeA2RUC4.
CleanExHS_C2orf60.
GenevestigatorA2RUC4.

Family and domain databases

InterProIPR003347. JmjC_dom.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEPS51184. JMJC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi129450.
NextBio82587.
PROA2RUC4.

Entry information

Entry nameTYW5_HUMAN
AccessionPrimary (citable) accession number: A2RUC4
Secondary accession number(s): B2RNE3, Q8N1R2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM