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Q2VPK5

- CTU2_HUMAN

UniProt

Q2VPK5 - CTU2_HUMAN

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Protein

Cytoplasmic tRNA 2-thiolation protein 2

Gene

CTU2

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 PublicationUniRule annotation

Pathwayi

GO - Molecular functioni

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

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 2UniRule annotation
Gene namesi
Name:CTU2UniRule annotation
Synonyms:C16orf84, NCS2UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:28005. CTU2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165449882.

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.
GenevestigatoriQ2VPK5.

Organism-specific databases

HPAiHPA041135.
HPA041894.

Interactioni

Subunit structurei

Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi131513. 15 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. Align

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]
UniGeneiHs.592074.

Genome annotation databases

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

Polymorphism databases

DMDMi121941955.

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 .
CCDSi CCDS32506.1. [Q2VPK5-5 ]
CCDS45545.1. [Q2VPK5-1 ]
RefSeqi NP_001012777.1. NM_001012759.1. [Q2VPK5-1 ]
NP_001012780.1. NM_001012762.1. [Q2VPK5-5 ]
UniGenei Hs.592074.

3D structure databases

ProteinModelPortali Q2VPK5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 131513. 15 interactions.
DIPi DIP-48633N.
STRINGi 9606.ENSP00000388320.

PTM databases

PhosphoSitei Q2VPK5.

Polymorphism databases

DMDMi 121941955.

Proteomic databases

MaxQBi Q2VPK5.
PaxDbi Q2VPK5.
PRIDEi Q2VPK5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312060 ; ENSP00000308617 ; ENSG00000174177 . [Q2VPK5-5 ]
ENST00000453996 ; ENSP00000388320 ; ENSG00000174177 . [Q2VPK5-1 ]
GeneIDi 348180.
KEGGi hsa:348180.
UCSCi uc002flm.3. human. [Q2VPK5-1 ]
uc002fln.3. human. [Q2VPK5-5 ]

Organism-specific databases

CTDi 348180.
GeneCardsi GC16P088773.
H-InvDB HIX0018098.
HGNCi HGNC:28005. CTU2.
HPAi HPA041135.
HPA041894.
neXtProti NX_Q2VPK5.
PharmGKBi PA165449882.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG308629.
GeneTreei ENSGT00390000008797.
HOGENOMi HOG000007287.
HOVERGENi HBG107783.
InParanoidi Q2VPK5.
KOi K14169.
PhylomeDBi Q2VPK5.
TreeFami TF313203.

Enzyme and pathway databases

UniPathwayi UPA00988 .

Miscellaneous databases

ChiTaRSi CTU2. human.
GeneWikii C16orf84.
GenomeRNAii 348180.
NextBioi 99363.
PROi Q2VPK5.

Gene expression databases

Bgeei Q2VPK5.
CleanExi HS_C16orf84.
ExpressionAtlasi Q2VPK5. baseline and differential.
Genevestigatori Q2VPK5.

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

« 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: October 29, 2014
This is version 79 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