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Q2VPK5

- CTU2_HUMAN

UniProt

Q2VPK5 - CTU2_HUMAN

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
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (10 Jan 2006)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. 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

    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-SubCell
    2. protein complex Source: UniProtKB

    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

    ArrayExpressiQ2VPK5.
    BgeeiQ2VPK5.
    CleanExiHS_C16orf84.
    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. 3 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.
    HOGENOMiHOG000007287.
    HOVERGENiHBG107783.
    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

    MCQVGEDYGE PAPEEPPPAP RPSREQKCVK CKEAQPVVVI RAGDAFCRDC    50
    FKAFYVHKFR AMLGKNRLIF PGEKVLLAWS GGPSSSSMVW QVLEGLSQDS 100
    AKRLRFVAGV IFVDEGAACG QSLEERSKTL AEVKPILQAT GFPWHVVALE 150
    EVFSLPPSVL WCSAQELVGS EGAYKAAVDS FLQQQHVLGA GGGPGPTQGE 200
    EQPPQPPLDP QNLARPPAPA QTEALSQLFC SVRTLTAKEE LLQTLRTHLI 250
    LHMARAHGYS KVMTGDSCTR LAIKLMTNLA LGRGAFLAWD TGFSDERHGD 300
    VVVVRPMRDH TLKEVAFYNR LFSVPSVFTP AVDTKAPEKA SIHRLMEAFI 350
    LRLQTQFPST VSTVYRTSEK LVKGPRDGPA AGDSGPRCLL CMCALDVDAA 400
    DSATAFGAQT SSRLSQMQSP IPLTETRTPP GPCCSPGVGW AQRCGQGACR 450
    REDPQACIEE QLCYSCRVNM KDLPSLDPLP PYILAEAQLR TQRAWGLQEI 500
    RDCLIEDSDD EAGQS 515
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 3 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.
    HOGENOMi HOG000007287.
    HOVERGENi HBG107783.
    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

    ArrayExpressi Q2VPK5.
    Bgeei Q2VPK5.
    CleanExi HS_C16orf84.
    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

    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 1, 2014
    This is version 78 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