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Q9Y3I0

- RTCB_HUMAN

UniProt

Q9Y3I0 - RTCB_HUMAN

Protein

tRNA-splicing ligase RtcB homolog

Gene

RTCB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.2 Publications

    Catalytic activityi

    ATP + (ribonucleotide)(n) + (ribonucleotide)(m) = AMP + diphosphate + (ribonucleotide)(n+m).1 PublicationUniRule annotation

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi119 – 1191Manganese 1By similarity
    Metal bindingi122 – 1221Manganese 1By similarity
    Metal bindingi122 – 1221Manganese 2By similarity
    Metal bindingi227 – 2271Manganese 1By similarity
    Binding sitei230 – 2301GMPBy similarity
    Metal bindingi259 – 2591Manganese 2By similarity
    Metal bindingi353 – 3531Manganese 2By similarity
    Binding sitei409 – 4091GMPBy similarity
    Active sitei428 – 4281GMP-histidine intermediateBy similarity
    Binding sitei504 – 5041GMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi353 – 3542GMPBy similarity
    Nucleotide bindingi400 – 4034GMPBy similarity
    Nucleotide bindingi428 – 4314GMPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. RNA ligase (ATP) activity Source: UniProtKB
    5. vinculin binding Source: UniProtKB

    GO - Biological processi

    1. in utero embryonic development Source: Ensembl
    2. placenta development Source: Ensembl
    3. tRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    ATP-binding, Manganese, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA-splicing ligase RtcB homologUniRule annotation (EC:6.5.1.3UniRule annotation)
    Gene namesi
    Name:RTCBUniRule annotation
    Synonyms:C22orf28
    ORF Names:HSPC117
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:26935. RTCB.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 PublicationUniRule annotation
    Note: Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low.1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. tRNA-splicing ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1221C → A: Abolishes tRNA ligase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA145149387.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505tRNA-splicing ligase RtcB homologPRO_0000255241Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y3I0.
    PaxDbiQ9Y3I0.
    PeptideAtlasiQ9Y3I0.
    PRIDEiQ9Y3I0.

    2D gel databases

    UCD-2DPAGEQ9Y3I0.

    PTM databases

    PhosphoSiteiQ9Y3I0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y3I0.
    BgeeiQ9Y3I0.
    CleanExiHS_C22orf28.
    GenevestigatoriQ9Y3I0.

    Organism-specific databases

    HPAiHPA001103.

    Interactioni

    Subunit structurei

    Catalytic component of the tRNA-splicing ligase complex.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi119569. 44 interactions.
    IntActiQ9Y3I0. 14 interactions.
    MINTiMINT-4654730.
    STRINGi9606.ENSP00000216038.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y3I0.
    SMRiQ9Y3I0. Positions 12-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RtcB family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1690.
    HOVERGENiHBG081383.
    InParanoidiQ9Y3I0.
    KOiK14415.
    OMAiGRMLNAD.
    OrthoDBiEOG7DRJ2Q.
    PhylomeDBiQ9Y3I0.
    TreeFamiTF314404.

    Family and domain databases

    HAMAPiMF_03144. RtcB_euk.
    InterProiIPR001233. RtcB.
    IPR027513. RtcB_euk.
    [Graphical view]
    PANTHERiPTHR11118. PTHR11118. 1 hit.
    PfamiPF01139. RtcB. 1 hit.
    [Graphical view]
    SUPFAMiSSF103365. SSF103365. 1 hit.
    PROSITEiPS01288. UPF0027. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y3I0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRSYNDELQ FLEKINKNCW RIKKGFVPNM QVEGVFYVND ALEKLMFEEL    50
    RNACRGGGVG GFLPAMKQIG NVAALPGIVH RSIGLPDVHS GYGFAIGNMA 100
    AFDMNDPEAV VSPGGVGFDI NCGVRLLRTN LDESDVQPVK EQLAQAMFDH 150
    IPVGVGSKGV IPMNAKDLEE ALEMGVDWSL REGYAWAEDK EHCEEYGRML 200
    QADPNKVSAR AKKRGLPQLG TLGAGNHYAE IQVVDEIFNE YAAKKMGIDH 250
    KGQVCVMIHS GSRGLGHQVA TDALVAMEKA MKRDKIIVND RQLACARIAS 300
    PEGQDYLKGM AAAGNYAWVN RSSMTFLTRQ AFAKVFNTTP DDLDLHVIYD 350
    VSHNIAKVEQ HVVDGKERTL LVHRKGSTRA FPPHHPLIAV DYQLTGQPVL 400
    IGGTMGTCSY VLTGTEQGMT ETFGTTCHGA GRALSRAKSR RNLDFQDVLD 450
    KLADMGIAIR VASPKLVMEE APESYKNVTD VVNTCHDAGI SKKAIKLRPI 500
    AVIKG 505
    Length:505
    Mass (Da):55,210
    Last modified:November 1, 1999 - v1
    Checksum:iC7C0CC2C95BDD27B
    GO

    Sequence cautioni

    The sequence AAF29081.1 differs from that shown. Reason: Frameshift at positions 295 and 298.
    The sequence AAF67477.1 differs from that shown. Reason: Frameshift at positions 173 and 180.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti296 – 2961A → P in AAF29081. (PubMed:11042152)Curated
    Sequence conflicti303 – 3031G → V in AAF29081. (PubMed:11042152)Curated
    Sequence conflicti303 – 3031G → V in AAF67477. (PubMed:10931946)Curated
    Sequence conflicti427 – 4271C → R in CAG33456. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti153 – 1531V → A.
    Corresponds to variant rs11545747 [ dbSNP | Ensembl ].
    VAR_052485
    Natural varianti343 – 3431L → F.1 Publication
    Corresponds to variant rs17849275 [ dbSNP | Ensembl ].
    VAR_028853

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL050255 mRNA. Translation: CAB43357.1.
    AF161466 mRNA. Translation: AAF29081.1. Frameshift.
    AF155658 mRNA. Translation: AAF67477.1. Frameshift.
    CR457175 mRNA. Translation: CAG33456.1.
    CR456450 mRNA. Translation: CAG30336.1.
    AK312503 mRNA. Translation: BAG35405.1.
    AL021937 Genomic DNA. Translation: CAB38260.1.
    CH471095 Genomic DNA. Translation: EAW60021.1.
    BC000151 mRNA. Translation: AAH00151.1.
    BC002970 mRNA. Translation: AAH02970.1.
    BC010308 mRNA. Translation: AAH10308.1.
    BC016707 mRNA. Translation: AAH16707.1.
    AL137272 mRNA. Translation: CAB70670.1.
    CCDSiCCDS13905.1.
    PIRiT46344.
    RefSeqiNP_055121.1. NM_014306.4.
    UniGeneiHs.474643.

    Genome annotation databases

    EnsembliENST00000216038; ENSP00000216038; ENSG00000100220.
    GeneIDi51493.
    KEGGihsa:51493.
    UCSCiuc003amm.2. human.

    Polymorphism databases

    DMDMi74753486.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL050255 mRNA. Translation: CAB43357.1 .
    AF161466 mRNA. Translation: AAF29081.1 . Frameshift.
    AF155658 mRNA. Translation: AAF67477.1 . Frameshift.
    CR457175 mRNA. Translation: CAG33456.1 .
    CR456450 mRNA. Translation: CAG30336.1 .
    AK312503 mRNA. Translation: BAG35405.1 .
    AL021937 Genomic DNA. Translation: CAB38260.1 .
    CH471095 Genomic DNA. Translation: EAW60021.1 .
    BC000151 mRNA. Translation: AAH00151.1 .
    BC002970 mRNA. Translation: AAH02970.1 .
    BC010308 mRNA. Translation: AAH10308.1 .
    BC016707 mRNA. Translation: AAH16707.1 .
    AL137272 mRNA. Translation: CAB70670.1 .
    CCDSi CCDS13905.1.
    PIRi T46344.
    RefSeqi NP_055121.1. NM_014306.4.
    UniGenei Hs.474643.

    3D structure databases

    ProteinModelPortali Q9Y3I0.
    SMRi Q9Y3I0. Positions 12-505.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119569. 44 interactions.
    IntActi Q9Y3I0. 14 interactions.
    MINTi MINT-4654730.
    STRINGi 9606.ENSP00000216038.

    PTM databases

    PhosphoSitei Q9Y3I0.

    Polymorphism databases

    DMDMi 74753486.

    2D gel databases

    UCD-2DPAGE Q9Y3I0.

    Proteomic databases

    MaxQBi Q9Y3I0.
    PaxDbi Q9Y3I0.
    PeptideAtlasi Q9Y3I0.
    PRIDEi Q9Y3I0.

    Protocols and materials databases

    DNASUi 51493.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216038 ; ENSP00000216038 ; ENSG00000100220 .
    GeneIDi 51493.
    KEGGi hsa:51493.
    UCSCi uc003amm.2. human.

    Organism-specific databases

    CTDi 51493.
    GeneCardsi GC22M032784.
    HGNCi HGNC:26935. RTCB.
    HPAi HPA001103.
    MIMi 613901. gene.
    neXtProti NX_Q9Y3I0.
    PharmGKBi PA145149387.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1690.
    HOVERGENi HBG081383.
    InParanoidi Q9Y3I0.
    KOi K14415.
    OMAi GRMLNAD.
    OrthoDBi EOG7DRJ2Q.
    PhylomeDBi Q9Y3I0.
    TreeFami TF314404.

    Miscellaneous databases

    ChiTaRSi C22orf28. human.
    GenomeRNAii 51493.
    NextBioi 55157.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3I0.
    Bgeei Q9Y3I0.
    CleanExi HS_C22orf28.
    Genevestigatori Q9Y3I0.

    Family and domain databases

    HAMAPi MF_03144. RtcB_euk.
    InterProi IPR001233. RtcB.
    IPR027513. RtcB_euk.
    [Graphical view ]
    PANTHERi PTHR11118. PTHR11118. 1 hit.
    Pfami PF01139. RtcB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103365. SSF103365. 1 hit.
    PROSITEi PS01288. UPF0027. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
      Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
      Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adrenal gland.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thalamus.
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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], VARIANT PHE-343.
      Tissue: Choriocarcinoma and Lung carcinoma.
    10. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 4-14; 45-51; 56-81; 141-158; 199-206; 264-279; 298-308; 442-460 AND 466-476, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-505.
      Tissue: Testis.
    12. "Kinesin transports RNA: isolation and characterization of an RNA-transporting granule."
      Kanai Y., Dohmae N., Hirokawa N.
      Neuron 43:513-525(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A RNA TRANSPORT COMPLEX.
    13. "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress."
      Guo D., Han J., Adam B.-L., Colburn N.H., Wang M.-H., Dong Z., Eizirik D.L., She J.-X., Wang C.-Y.
      Biochem. Biophys. Res. Commun. 337:1308-1318(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX, MUTAGENESIS OF CYS-122.
    16. "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors."
      Popow J., Jurkin J., Schleiffer A., Martinez J.
      Nature 511:104-107(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
    17. "hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel transcription-dependent shuttling RNA-transporting complex."
      Perez-Gonzalez A., Pazo A., Navajas R., Ciordia S., Rodriguez-Frandsen A., Nieto A.
      PLoS ONE 9:E90957-E90957(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiRTCB_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3I0
    Secondary accession number(s): B2R6A8
    , Q6IAI0, Q9BWL4, Q9NTH1, Q9P037, Q9P0J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 113 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

    Miscellaneous

    Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP (PubMed:24870230).1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families
    6. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3