Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y3I0

- RTCB_HUMAN

UniProt

Q9Y3I0 - RTCB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

Mn2+By similarityNote: 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
Complete GO annotation...

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
  2. nucleus Source: UniProtKB
  3. tRNA-splicing ligase complex Source: UniProtKB
Complete GO annotation...

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

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.
DIPiDIP-46750N.
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.
GeneTreeiENSGT00390000015260.
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

        10         20         30         40         50
MSRSYNDELQ FLEKINKNCW RIKKGFVPNM QVEGVFYVND ALEKLMFEEL
60 70 80 90 100
RNACRGGGVG GFLPAMKQIG NVAALPGIVH RSIGLPDVHS GYGFAIGNMA
110 120 130 140 150
AFDMNDPEAV VSPGGVGFDI NCGVRLLRTN LDESDVQPVK EQLAQAMFDH
160 170 180 190 200
IPVGVGSKGV IPMNAKDLEE ALEMGVDWSL REGYAWAEDK EHCEEYGRML
210 220 230 240 250
QADPNKVSAR AKKRGLPQLG TLGAGNHYAE IQVVDEIFNE YAAKKMGIDH
260 270 280 290 300
KGQVCVMIHS GSRGLGHQVA TDALVAMEKA MKRDKIIVND RQLACARIAS
310 320 330 340 350
PEGQDYLKGM AAAGNYAWVN RSSMTFLTRQ AFAKVFNTTP DDLDLHVIYD
360 370 380 390 400
VSHNIAKVEQ HVVDGKERTL LVHRKGSTRA FPPHHPLIAV DYQLTGQPVL
410 420 430 440 450
IGGTMGTCSY VLTGTEQGMT ETFGTTCHGA GRALSRAKSR RNLDFQDVLD
460 470 480 490 500
KLADMGIAIR VASPKLVMEE APESYKNVTD VVNTCHDAGI SKKAIKLRPI

AVIKG
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. Curated
The sequence AAF67477.1 differs from that shown. Reason: Frameshift at positions 173 and 180. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
DIPi DIP-46750N.
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.
GeneTreei ENSGT00390000015260.
HOVERGENi HBG081383.
InParanoidi Q9Y3I0.
KOi K14415.
OMAi GRMLNAD.
OrthoDBi EOG7DRJ2Q.
PhylomeDBi Q9Y3I0.
TreeFami TF314404.

Miscellaneous databases

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

Gene expression databases

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 115 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