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Protein

Cytoplasmic tRNA 2-thiolation protein 2

Gene

CTU2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.UniRule annotation1 Publication

Pathway:i5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis

This protein is involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis and in tRNA modification.

GO - Molecular functioni

GO - Biological processi

  • protein urmylation Source: UniProtKB-HAMAP
  • tRNA thio-modification Source: UniProtKB
  • 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 2UniRule annotation
Gene namesi
Name:CTU2UniRule annotation
Synonyms:C16orf84, NCS2UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:28005. CTU2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • mitochondrion Source: HPA
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165449882.

Polymorphism and mutation databases

BioMutaiCTU2.
DMDMi121941955.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 515514Cytoplasmic tRNA 2-thiolation protein 2PRO_0000289175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteine1 Publication
Modified residuei415 – 4151Phosphoserine1 Publication
Modified residuei419 – 4191Phosphoserine2 Publications
Modified residuei508 – 5081Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ2VPK5.
PaxDbiQ2VPK5.
PRIDEiQ2VPK5.

PTM databases

PhosphoSiteiQ2VPK5.

Expressioni

Gene expression databases

BgeeiQ2VPK5.
CleanExiHS_C16orf84.
ExpressionAtlasiQ2VPK5. baseline and differential.
GenevisibleiQ2VPK5. HS.

Organism-specific databases

HPAiHPA041135.
HPA041894.

Interactioni

Subunit structurei

Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi131513. 17 interactions.
DIPiDIP-48633N.
STRINGi9606.ENSP00000388320.

Structurei

3D structure databases

ProteinModelPortaliQ2VPK5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CTU2/NCS2 family.UniRule annotation

Phylogenomic databases

eggNOGiNOG308629.
GeneTreeiENSGT00390000008797.
HOGENOMiHOG000007287.
HOVERGENiHBG107783.
InParanoidiQ2VPK5.
KOiK14169.
PhylomeDBiQ2VPK5.
TreeFamiTF313203.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2VPK5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MCQVGEDYGE PAPEEPPPAP RPSREQKCVK CKEAQPVVVI RAGDAFCRDC
60 70 80 90 100
FKAFYVHKFR AMLGKNRLIF PGEKVLLAWS GGPSSSSMVW QVLEGLSQDS
110 120 130 140 150
AKRLRFVAGV IFVDEGAACG QSLEERSKTL AEVKPILQAT GFPWHVVALE
160 170 180 190 200
EVFSLPPSVL WCSAQELVGS EGAYKAAVDS FLQQQHVLGA GGGPGPTQGE
210 220 230 240 250
EQPPQPPLDP QNLARPPAPA QTEALSQLFC SVRTLTAKEE LLQTLRTHLI
260 270 280 290 300
LHMARAHGYS KVMTGDSCTR LAIKLMTNLA LGRGAFLAWD TGFSDERHGD
310 320 330 340 350
VVVVRPMRDH TLKEVAFYNR LFSVPSVFTP AVDTKAPEKA SIHRLMEAFI
360 370 380 390 400
LRLQTQFPST VSTVYRTSEK LVKGPRDGPA AGDSGPRCLL CMCALDVDAA
410 420 430 440 450
DSATAFGAQT SSRLSQMQSP IPLTETRTPP GPCCSPGVGW AQRCGQGACR
460 470 480 490 500
REDPQACIEE QLCYSCRVNM KDLPSLDPLP PYILAEAQLR TQRAWGLQEI
510
RDCLIEDSDD EAGQS
Length:515
Mass (Da):56,107
Last modified:January 10, 2006 - v1
Checksum:i200CE7129FC89E65
GO
Isoform 2 (identifier: Q2VPK5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.

Note: No experimental confirmation available.
Show »
Length:428
Mass (Da):46,527
Checksum:iF964CA51F97BD822
GO
Isoform 3 (identifier: Q2VPK5-5) [UniParc]FASTAAdd to basket

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

Note: Incomplete sequence.
Show »
Length:485
Mass (Da):52,467
Checksum:iF88DF9EE98405429
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971R → W in AAH80540 (PubMed:15616553).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861H → Y.
Corresponds to variant rs2290895 [ dbSNP | Ensembl ].
VAR_062244
Natural varianti253 – 2531M → V.1 Publication
Corresponds to variant rs11549837 [ dbSNP | Ensembl ].
VAR_032595
Natural varianti332 – 3321V → I.
Corresponds to variant rs4782321 [ dbSNP | Ensembl ].
VAR_032596
Natural varianti416 – 4161Q → R.1 Publication
Corresponds to variant rs8059048 [ dbSNP | Ensembl ].
VAR_032597

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787Missing in isoform 2. 1 PublicationVSP_025950Add
BLAST
Alternative sequencei474 – 51542PSLDP…EAGQS → GLGLAGDPGLSD in isoform 3. 1 PublicationVSP_039378Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32506.1. [Q2VPK5-5]
CCDS45545.1. [Q2VPK5-1]
RefSeqiNP_001012777.1. NM_001012759.1. [Q2VPK5-1]
NP_001012780.1. NM_001012762.1. [Q2VPK5-5]
XP_011521370.1. XM_011523068.1. [Q2VPK5-3]
UniGeneiHs.592074.

Genome annotation databases

EnsembliENST00000312060; ENSP00000308617; ENSG00000174177. [Q2VPK5-5]
ENST00000453996; ENSP00000388320; ENSG00000174177.
GeneIDi348180.
KEGGihsa:348180.
UCSCiuc002flm.3. human. [Q2VPK5-1]
uc002fln.3. human. [Q2VPK5-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32506.1. [Q2VPK5-5]
CCDS45545.1. [Q2VPK5-1]
RefSeqiNP_001012777.1. NM_001012759.1. [Q2VPK5-1]
NP_001012780.1. NM_001012762.1. [Q2VPK5-5]
XP_011521370.1. XM_011523068.1. [Q2VPK5-3]
UniGeneiHs.592074.

3D structure databases

ProteinModelPortaliQ2VPK5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131513. 17 interactions.
DIPiDIP-48633N.
STRINGi9606.ENSP00000388320.

PTM databases

PhosphoSiteiQ2VPK5.

Polymorphism and mutation databases

BioMutaiCTU2.
DMDMi121941955.

Proteomic databases

MaxQBiQ2VPK5.
PaxDbiQ2VPK5.
PRIDEiQ2VPK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312060; ENSP00000308617; ENSG00000174177. [Q2VPK5-5]
ENST00000453996; ENSP00000388320; ENSG00000174177.
GeneIDi348180.
KEGGihsa:348180.
UCSCiuc002flm.3. human. [Q2VPK5-1]
uc002fln.3. human. [Q2VPK5-5]

Organism-specific databases

CTDi348180.
GeneCardsiGC16P088773.
H-InvDBHIX0018098.
HGNCiHGNC:28005. CTU2.
HPAiHPA041135.
HPA041894.
neXtProtiNX_Q2VPK5.
PharmGKBiPA165449882.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG308629.
GeneTreeiENSGT00390000008797.
HOGENOMiHOG000007287.
HOVERGENiHBG107783.
InParanoidiQ2VPK5.
KOiK14169.
PhylomeDBiQ2VPK5.
TreeFamiTF313203.

Enzyme and pathway databases

UniPathwayiUPA00988.

Miscellaneous databases

ChiTaRSiCTU2. human.
GeneWikiiC16orf84.
GenomeRNAii348180.
NextBioi99363.
PROiQ2VPK5.

Gene expression databases

BgeeiQ2VPK5.
CleanExiHS_C16orf84.
ExpressionAtlasiQ2VPK5. baseline and differential.
GenevisibleiQ2VPK5. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCTU2_HUMAN
AccessioniPrimary (citable) accession number: Q2VPK5
Secondary accession number(s): B2RXK0
, Q0P511, Q66K78, Q6P4C8, Q86SV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 10, 2006
Last modified: July 22, 2015
This is version 84 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.