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Q2VPK5 (CTU2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Cytoplasmic tRNA 2-thiolation protein 2
Gene names
Name:CTU2
Synonyms:C16orf84, NCS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Pathway

tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. HAMAP-Rule MF_03054

Subunit structure

Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. Ref.5

Subcellular location

Cytoplasm HAMAP-Rule MF_03054.

Sequence similarities

Belongs to the CTU2/NCS2 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein urmylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA thio-modification

Non-traceable author statement Ref.5. Source: UniProtKB

tRNA wobble uridine modification

Non-traceable author statement Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionnucleotidyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q2VPK5-1)

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: Q2VPK5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q2VPK5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     474-515: PSLDPLPPYILAEAQLRTQRAWGLQEIRDCLIEDSDDEAGQS → GLGLAGDPGLSD
Note: Incomplete sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 515514Cytoplasmic tRNA 2-thiolation protein 2 HAMAP-Rule MF_03054
PRO_0000289175

Amino acid modifications

Modified residue21N-acetylcysteine Ref.6
Modified residue4151Phosphoserine Ref.8
Modified residue4191Phosphoserine Ref.4 Ref.7
Modified residue5081Phosphoserine Ref.3 Ref.4

Natural variations

Alternative sequence1 – 8787Missing in isoform 2.
VSP_025950
Alternative sequence474 – 51542PSLDP…EAGQS → GLGLAGDPGLSD in isoform 3.
VSP_039378
Natural variant1861H → Y.
Corresponds to variant rs2290895 [ dbSNP | Ensembl ].
VAR_062244
Natural variant2531M → V. Ref.2
Corresponds to variant rs11549837 [ dbSNP | Ensembl ].
VAR_032595
Natural variant3321V → I.
Corresponds to variant rs4782321 [ dbSNP | Ensembl ].
VAR_032596
Natural variant4161Q → R. Ref.2
Corresponds to variant rs8059048 [ dbSNP | Ensembl ].
VAR_032597

Experimental info

Sequence conflict2971R → W in AAH80540. Ref.1

Sequences

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

Last modified January 10, 2006. Version 1.
Checksum: 200CE7129FC89E65

FASTA51556,107
        10         20         30         40         50         60 
MCQVGEDYGE PAPEEPPPAP RPSREQKCVK CKEAQPVVVI RAGDAFCRDC FKAFYVHKFR 

        70         80         90        100        110        120 
AMLGKNRLIF PGEKVLLAWS GGPSSSSMVW QVLEGLSQDS AKRLRFVAGV IFVDEGAACG 

       130        140        150        160        170        180 
QSLEERSKTL AEVKPILQAT GFPWHVVALE EVFSLPPSVL WCSAQELVGS EGAYKAAVDS 

       190        200        210        220        230        240 
FLQQQHVLGA GGGPGPTQGE EQPPQPPLDP QNLARPPAPA QTEALSQLFC SVRTLTAKEE 

       250        260        270        280        290        300 
LLQTLRTHLI LHMARAHGYS KVMTGDSCTR LAIKLMTNLA LGRGAFLAWD TGFSDERHGD 

       310        320        330        340        350        360 
VVVVRPMRDH TLKEVAFYNR LFSVPSVFTP AVDTKAPEKA SIHRLMEAFI LRLQTQFPST 

       370        380        390        400        410        420 
VSTVYRTSEK LVKGPRDGPA AGDSGPRCLL CMCALDVDAA DSATAFGAQT SSRLSQMQSP 

       430        440        450        460        470        480 
IPLTETRTPP GPCCSPGVGW AQRCGQGACR REDPQACIEE QLCYSCRVNM KDLPSLDPLP 

       490        500        510 
PYILAEAQLR TQRAWGLQEI RDCLIEDSDD EAGQS 

« Hide

Isoform 2 [UniParc].

Checksum: F964CA51F97BD822
Show »

FASTA42846,527
Isoform 3 [UniParc].

Checksum: F88DF9EE98405429
Show »

FASTA48552,467

References

« Hide 'large scale' references
[1]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-515 (ISOFORM 3), VARIANTS VAL-253 AND ARG-416.
Tissue: Brain, Choriocarcinoma and Skin.
[3]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway."
Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E., Ploegh H.L.
Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN 2-THIOLATION OF TRNA, IDENTIFICATION IN A COMPLEX WITH URM1 AND CTU1.
[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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC138028 Genomic DNA. No translation available.
BC021829 mRNA. No translation available.
BC080540 mRNA. Translation: AAH80540.1.
BC108659 mRNA. Translation: AAI08660.1.
BC121805 mRNA. Translation: AAI21806.1.
BC125269 mRNA. Translation: AAI25270.1.
BC157881 mRNA. Translation: AAI57882.1.
RefSeqNP_001012777.1. NM_001012759.1.
NP_001012780.1. NM_001012762.1.
UniGeneHs.592074.

3D structure databases

ProteinModelPortalQ2VPK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid131513. 3 interactions.
DIPDIP-48633N.
STRING9606.ENSP00000388320.

PTM databases

PhosphoSiteQ2VPK5.

Polymorphism databases

DMDM121941955.

Proteomic databases

PaxDbQ2VPK5.
PRIDEQ2VPK5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312060; ENSP00000308617; ENSG00000174177. [Q2VPK5-5]
ENST00000378384; ENSP00000367635; ENSG00000174177. [Q2VPK5-3]
ENST00000453996; ENSP00000388320; ENSG00000174177. [Q2VPK5-1]
GeneID348180.
KEGGhsa:348180.
UCSCuc002flm.3. human. [Q2VPK5-1]
uc002fln.3. human. [Q2VPK5-5]

Organism-specific databases

CTD348180.
GeneCardsGC16P088773.
H-InvDBHIX0018098.
HGNCHGNC:28005. CTU2.
HPAHPA041135.
HPA041894.
neXtProtNX_Q2VPK5.
PharmGKBPA165449882.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308629.
HOGENOMHOG000007287.
HOVERGENHBG107783.
KOK14169.
PhylomeDBQ2VPK5.
TreeFamTF313203.

Enzyme and pathway databases

UniPathwayUPA00988.

Gene expression databases

ArrayExpressQ2VPK5.
BgeeQ2VPK5.
CleanExHS_C16orf84.
GenevestigatorQ2VPK5.

Family and domain databases

HAMAPMF_03054. CTU2.
InterProIPR019407. Ncs2/Tuc2/Ctu2.
[Graphical view]
PfamPF10288. DUF2392. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTU2. human.
GeneWikiC16orf84.
GenomeRNAi348180.
NextBio99363.
PROQ2VPK5.

Entry information

Entry nameCTU2_HUMAN
AccessionPrimary (citable) accession number: Q2VPK5
Secondary accession number(s): B2RXK0 expand/collapse secondary AC list , Q0P511, Q66K78, Q6P4C8, Q86SV4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 74 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM