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Q3U308

- CTU2_MOUSE

UniProt

Q3U308 - CTU2_MOUSE

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Protein
Cytoplasmic tRNA 2-thiolation protein 2
Gene
Ctu2, Ncs2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position By similarity.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. nucleotidyltransferase activity Source: UniProtKB-HAMAP
  2. tRNA binding Source: UniProtKB

GO - Biological processi

  1. protein urmylation Source: UniProtKB-HAMAP
  2. tRNA thio-modification Source: UniProtKB
  3. tRNA wobble uridine modification Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

UniPathwayiUPA00988.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic tRNA 2-thiolation protein 2
Gene namesi
Name:Ctu2
Synonyms:Ncs2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1914215. Ctu2.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: Ensembl
  3. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 514513Cytoplasmic tRNA 2-thiolation protein 2UniRule annotation
PRO_0000289176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteine By similarity
Modified residuei421 – 4211Phosphoserine By similarity
Modified residuei425 – 4251Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3U308.
PRIDEiQ3U308.

PTM databases

PhosphoSiteiQ3U308.

Expressioni

Gene expression databases

BgeeiQ3U308.
CleanExiMM_2310061F22RIK.
GenevestigatoriQ3U308.

Interactioni

Subunit structurei

Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ3U308.

Family & Domainsi

Sequence similaritiesi

Belongs to the CTU2/NCS2 family.

Phylogenomic databases

eggNOGiNOG308629.
GeneTreeiENSGT00390000008797.
HOGENOMiHOG000007287.
HOVERGENiHBG107783.
InParanoidiQ3U308.
KOiK14169.
OMAiCRDCFKA.
OrthoDBiEOG7C2R1T.
PhylomeDBiQ3U308.
TreeFamiTF313203.

Family and domain databases

HAMAPiMF_03054. CTU2.
InterProiIPR019407. Ncs2/Tuc2/Ctu2.
[Graphical view]
PfamiPF10288. DUF2392. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U308-1 [UniParc]FASTAAdd to Basket

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MCQAGEDYAG PARREPPPVP RPSREQKCVK CAEGLPVVVI RAGDAFCRVC    50
FKAFYVHKFR AMLGKNRVIF PGEKVLLSWS GGPSSSSMVW QVLEGLSQDS 100
AKRLRFVPGV IYVDEGAACG QSLEDRQKTV AEVKRILENT GFPWHVVALE 150
EVFSLPPSVL CCTSQESAGT EEAYKAAVDR FLQQQQQQQQ RVLGAEAGAS 200
PAQGEARLHP SHGREPSGTA GYPTAAQTEA LSRLFSSIKT LTAKEELLQT 250
LRTHLIVHIA RVHGYCKVMT GETCTRLAIK LMTNLALGRG AFLAWDTGFS 300
DERHGDVVLV RPMRDHTLKE VAFYNHLFRV PSVFTPAIDT KAPEKASIHR 350
LMEAFILRLQ TLFPSTVSTV YRTSEKLVKA PREGCAAGPS GPSCLLCMCA 400
LDIDTADSAT AFGAQSSSHL SQMPSAEAGM PTQPCCAAGE GQAQSCHREV 450
GKRGDARACI TEQLCYSCRV NMKDLPSLDP LPPYVLAEAQ LRSQRGSVSE 500
EIQEYLITDE EEDS 514
Length:514
Mass (Da):56,105
Last modified:October 11, 2005 - v1
Checksum:i88A531D4F3BD3532
GO

Sequence cautioni

The sequence BAC41181.1 differs from that shown. Reason: Frameshift at position 250.
The sequence AAH36332.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK090349 mRNA. Translation: BAC41181.1. Frameshift.
AK154995 mRNA. Translation: BAE32982.1.
BC036332 mRNA. Translation: AAH36332.1. Different initiation.
CCDSiCCDS52694.1.
RefSeqiNP_722470.2. NM_153775.2.
UniGeneiMm.482288.

Genome annotation databases

EnsembliENSMUST00000116412; ENSMUSP00000112113; ENSMUSG00000049482.
GeneIDi66965.
KEGGimmu:66965.
UCSCiuc009nsz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK090349 mRNA. Translation: BAC41181.1 . Frameshift.
AK154995 mRNA. Translation: BAE32982.1 .
BC036332 mRNA. Translation: AAH36332.1 . Different initiation.
CCDSi CCDS52694.1.
RefSeqi NP_722470.2. NM_153775.2.
UniGenei Mm.482288.

3D structure databases

ProteinModelPortali Q3U308.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q3U308.

Proteomic databases

PaxDbi Q3U308.
PRIDEi Q3U308.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000116412 ; ENSMUSP00000112113 ; ENSMUSG00000049482 .
GeneIDi 66965.
KEGGi mmu:66965.
UCSCi uc009nsz.2. mouse.

Organism-specific databases

CTDi 348180.
MGIi MGI:1914215. Ctu2.

Phylogenomic databases

eggNOGi NOG308629.
GeneTreei ENSGT00390000008797.
HOGENOMi HOG000007287.
HOVERGENi HBG107783.
InParanoidi Q3U308.
KOi K14169.
OMAi CRDCFKA.
OrthoDBi EOG7C2R1T.
PhylomeDBi Q3U308.
TreeFami TF313203.

Enzyme and pathway databases

UniPathwayi UPA00988 .

Miscellaneous databases

NextBioi 323147.
PROi Q3U308.
SOURCEi Search...

Gene expression databases

Bgeei Q3U308.
CleanExi MM_2310061F22RIK.
Genevestigatori Q3U308.

Family and domain databases

HAMAPi MF_03054. CTU2.
InterProi IPR019407. Ncs2/Tuc2/Ctu2.
[Graphical view ]
Pfami PF10288. DUF2392. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Diencephalon.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCTU2_MOUSE
AccessioniPrimary (citable) accession number: Q3U308
Secondary accession number(s): Q8BTG9, Q8CI68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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