YRDC_HUMAN
ID YRDC_HUMAN Reviewed; 279 AA.
AC Q86U90; Q4W4X8; Q6NVW3; Q7L4E4; Q7Z2I4; Q9H5F8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000305};
DE EC=2.7.7.87 {ECO:0000305|PubMed:29760464};
DE AltName: Full=Dopamine receptor-interacting protein 3 {ECO:0000303|Ref.6};
DE AltName: Full=Ischemia/reperfusion-inducible protein homolog {ECO:0000303|PubMed:16024787};
DE Short=hIRIP {ECO:0000303|PubMed:16024787};
DE Flags: Precursor;
GN Name=YRDC {ECO:0000303|PubMed:12730717, ECO:0000312|HGNC:HGNC:28905};
GN Synonyms=DRIP3 {ECO:0000303|Ref.6}, IRIP {ECO:0000303|PubMed:16024787};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12730717; DOI=10.1007/s10038-002-0001-3;
RA Chen J., Ji C., Gu S., Zhao E., Dai J., Huang L., Qian J., Ying K., Xie Y.,
RA Mao Y.;
RT "Isolation and identification of a novel cDNA that encodes human yrdC
RT protein.";
RL J. Hum. Genet. 48:164-169(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-279.
RX PubMed=16024787; DOI=10.1128/mcb.25.15.6496-6508.2005;
RA Jiang W., Prokopenko O., Wong L., Inouye M., Mirochnitchenko O.;
RT "IRIP, a new ischemia/reperfusion-inducible protein that participates in
RT the regulation of transporter activity.";
RL Mol. Cell. Biol. 25:6496-6508(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-279.
RA Lafuente M.J., Nasir J.;
RT "Cloning and characterization of DRIP3, a new protein that specifically
RT interacts with the D1 dopamine receptor.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-279.
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF 15-ALA--SER-17 AND SER-17.
RX PubMed=29760464; DOI=10.1038/s41467-018-04250-4;
RA Lin H., Miyauchi K., Harada T., Okita R., Takeshita E., Komaki H.,
RA Fujioka K., Yagasaki H., Goto Y.I., Yanaka K., Nakagawa S., Sakaguchi Y.,
RA Suzuki T.;
RT "CO2-sensitive tRNA modification associated with human mitochondrial
RT disease.";
RL Nat. Commun. 9:1875-1875(2018).
RN [21]
RP FUNCTION, INVOLVEMENT IN GAMOS10, VARIANTS GAMOS10 VAL-84 AND LEU-265 DEL,
RP AND CHARACTERIZATION OF VARIANTS GAMOS10 VAL-84 AND LEU-265 DEL.
RX PubMed=31481669; DOI=10.1038/s41467-019-11951-x;
RA Arrondel C., Missoury S., Snoek R., Patat J., Menara G., Collinet B.,
RA Liger D., Durand D., Gribouval O., Boyer O., Buscara L., Martin G.,
RA Machuca E., Nevo F., Lescop E., Braun D.A., Boschat A.C., Sanquer S.,
RA Guerrera I.C., Revy P., Parisot M., Masson C., Boddaert N., Charbit M.,
RA Decramer S., Novo R., Macher M.A., Ranchin B., Bacchetta J., Laurent A.,
RA Collardeau-Frachon S., van Eerde A.M., Hildebrandt F., Magen D.,
RA Antignac C., van Tilbeurgh H., Mollet G.;
RT "Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to
RT Galloway-Mowat syndrome.";
RL Nat. Commun. 10:3967-3967(2019).
RN [22]
RP VARIANT GAMOS10 THR-221, CHARACTERIZATION OF VARIANT GAMOS10 THR-221, AND
RP FUNCTION.
RX PubMed=34545459; DOI=10.1007/s00439-021-02347-3;
RA Schmidt J., Goergens J., Pochechueva T., Kotter A., Schwenzer N., Sitte M.,
RA Werner G., Altmueller J., Thiele H., Nuernberg P., Isensee J., Li Y.,
RA Mueller C., Leube B., Reinhardt H.C., Hucho T., Salinas G., Helm M.,
RA Jachimowicz R.D., Wieczorek D., Kohl T., Lehnart S.E., Yigit G.,
RA Wollnik B.;
RT "Biallelic variants in YRDC cause a developmental disorder with progeroid
RT features.";
RL Hum. Genet. 140:1679-1693(2021).
CC -!- FUNCTION: Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase
CC required for the formation of a threonylcarbamoyl group on adenosine at
CC position 37 (t(6)A37) in tRNAs that read codons beginning with adenine
CC (PubMed:29760464, PubMed:31481669, PubMed:34545459). Catalyzes the
CC conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give
CC threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with
CC the release of diphosphate (PubMed:29760464). Participates in t(6)A37
CC formation in cytoplasmic and mitochondrial tRNAs (PubMed:29760464). May
CC regulate the activity of some transporters (By similarity).
CC {ECO:0000250|UniProtKB:Q3U5F4, ECO:0000269|PubMed:29760464,
CC ECO:0000269|PubMed:31481669, ECO:0000269|PubMed:34545459}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC Evidence={ECO:0000305|PubMed:29760464};
CC -!- SUBUNIT: Interacts with RSC1A1. {ECO:0000250|UniProtKB:Q3U5F4}.
CC -!- INTERACTION:
CC Q86U90; P46379-2: BAG6; NbExp=3; IntAct=EBI-21659356, EBI-10988864;
CC Q86U90; O14645: DNALI1; NbExp=3; IntAct=EBI-21659356, EBI-395638;
CC Q86U90; O14901: KLF11; NbExp=3; IntAct=EBI-21659356, EBI-948266;
CC Q86U90; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-21659356, EBI-2811583;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29760464}.
CC Mitochondrion {ECO:0000269|PubMed:29760464}. Cell membrane
CC {ECO:0000250|UniProtKB:Q3U5F4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q3U5F4}. Note=A large fraction localizes in the
CC cytoplasm, whereas a smaller fraction is imported to mitochondria.
CC {ECO:0000269|PubMed:29760464}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12730717}.
CC -!- DOMAIN: The mitochondrial targeting sequence (MTS) is weak and only
CC mediates import of a small fraction of YRDC in mitochondria.
CC {ECO:0000269|PubMed:29760464}.
CC -!- DISEASE: Galloway-Mowat syndrome 10 (GAMOS10) [MIM:619609]: A form of
CC Galloway-Mowat syndrome, a severe renal-neurological disease
CC characterized by early-onset nephrotic syndrome associated with
CC microcephaly, central nervous system abnormalities, developmental
CC delays, and a propensity for seizures. Brain anomalies include gyration
CC defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC and cerebellar hypoplasia. Most patients show facial dysmorphism
CC characterized by a small, narrow forehead, large/floppy ears, deep-set
CC eyes, and micrognathia. Additional variable features are visual
CC impairment and arachnodactyly. Most patients die in early childhood.
CC GAMOS10 is an autosomal recessive form with fatal outcome. Patients
CC manifest congenital hypothyroidism in addition to neurologic, renal and
CC dysmorphic features. {ECO:0000269|PubMed:31481669,
CC ECO:0000269|PubMed:34545459}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08984.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP37053.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP37054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY172561; AAO41711.1; -; mRNA.
DR EMBL; AL929472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07317.1; -; Genomic_DNA.
DR EMBL; BC008984; AAH08984.3; ALT_INIT; mRNA.
DR EMBL; BC067857; AAH67857.2; -; mRNA.
DR EMBL; BC068057; AAH68057.1; -; mRNA.
DR EMBL; BC080186; AAH80186.2; -; mRNA.
DR EMBL; AY286019; AAP37053.1; ALT_INIT; mRNA.
DR EMBL; AY286020; AAP37054.1; ALT_INIT; mRNA.
DR EMBL; AF250397; AAQ14263.1; -; mRNA.
DR EMBL; AK027129; BAB15668.1; ALT_INIT; mRNA.
DR CCDS; CCDS30675.1; -.
DR RefSeq; NP_078916.3; NM_024640.3.
DR AlphaFoldDB; Q86U90; -.
DR SMR; Q86U90; -.
DR BioGRID; 122814; 19.
DR IntAct; Q86U90; 7.
DR STRING; 9606.ENSP00000362135; -.
DR GlyGen; Q86U90; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q86U90; -.
DR PhosphoSitePlus; Q86U90; -.
DR BioMuta; YRDC; -.
DR DMDM; 74750410; -.
DR EPD; Q86U90; -.
DR jPOST; Q86U90; -.
DR MassIVE; Q86U90; -.
DR MaxQB; Q86U90; -.
DR PaxDb; Q86U90; -.
DR PeptideAtlas; Q86U90; -.
DR PRIDE; Q86U90; -.
DR ProteomicsDB; 69783; -.
DR Antibodypedia; 31792; 26 antibodies from 13 providers.
DR DNASU; 79693; -.
DR Ensembl; ENST00000373044.3; ENSP00000362135.2; ENSG00000196449.4.
DR GeneID; 79693; -.
DR KEGG; hsa:79693; -.
DR MANE-Select; ENST00000373044.3; ENSP00000362135.2; NM_024640.4; NP_078916.3.
DR UCSC; uc001cca.2; human.
DR CTD; 79693; -.
DR DisGeNET; 79693; -.
DR GeneCards; YRDC; -.
DR HGNC; HGNC:28905; YRDC.
DR HPA; ENSG00000196449; Tissue enhanced (bone).
DR MIM; 612276; gene.
DR MIM; 619609; phenotype.
DR neXtProt; NX_Q86U90; -.
DR OpenTargets; ENSG00000196449; -.
DR PharmGKB; PA142670553; -.
DR VEuPathDB; HostDB:ENSG00000196449; -.
DR eggNOG; KOG3051; Eukaryota.
DR GeneTree; ENSGT00390000015364; -.
DR HOGENOM; CLU_031397_5_0_1; -.
DR InParanoid; Q86U90; -.
DR OMA; LVDAFWP; -.
DR OrthoDB; 1027994at2759; -.
DR PhylomeDB; Q86U90; -.
DR TreeFam; TF314358; -.
DR PathwayCommons; Q86U90; -.
DR SignaLink; Q86U90; -.
DR BioGRID-ORCS; 79693; 700 hits in 1076 CRISPR screens.
DR ChiTaRS; YRDC; human.
DR GenomeRNAi; 79693; -.
DR Pharos; Q86U90; Tdark.
DR PRO; PR:Q86U90; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86U90; protein.
DR Bgee; ENSG00000196449; Expressed in gingival epithelium and 169 other tissues.
DR Genevisible; Q86U90; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0051051; P:negative regulation of transport; IDA:MGI.
DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR006070; YrdC-like_dom.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR SUPFAM; SSF55821; SSF55821; 1.
DR TIGRFAMs; TIGR00057; TIGR00057; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disease variant; Epilepsy;
KW Intellectual disability; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 56..279
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000341402"
FT DOMAIN 67..257
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VARIANT 84
FT /note="A -> V (in GAMOS10; slightly decreased formation of
FT tRNA threonylcarbamoyladenosine modification)"
FT /evidence="ECO:0000269|PubMed:31481669"
FT /id="VAR_085771"
FT VARIANT 221
FT /note="I -> T (in GAMOS10; decreased formation of tRNA
FT threonylcarbamoyladenosine modification)"
FT /evidence="ECO:0000269|PubMed:34545459"
FT /id="VAR_085772"
FT VARIANT 265
FT /note="Missing (in GAMOS10; slightly decreased formation of
FT tRNA threonylcarbamoyladenosine modification)"
FT /evidence="ECO:0000269|PubMed:31481669"
FT /id="VAR_085773"
FT MUTAGEN 15..17
FT /note="AAS->FAF: Improved mitochondrial targeting sequence
FT (MTS), leading to increased import into mitochondria."
FT /evidence="ECO:0000269|PubMed:29760464"
FT MUTAGEN 17
FT /note="S->F: Improved mitochondrial targeting sequence
FT (MTS), leading to increased import into mitochondria."
FT /evidence="ECO:0000269|PubMed:29760464"
SQ SEQUENCE 279 AA; 29328 MW; F8F5C30274E2BB12 CRC64;
MSPARRCRGM RAAVAASVGL SEGPAGSRSG RLFRPPSPAP AAPGARLLRL PGSGAVQAAS
PERAGWTEAL RAAVAELRAG AVVAVPTDTL YGLACAASCS AALRAVYRLK GRSEAKPLAV
CLGRVADVYR YCRVRVPEGL LKDLLPGPVT LVMERSEELN KDLNPFTPLV GIRIPDHAFM
QDLAQMFEGP LALTSANLSS QASSLNVEEF QDLWPQLSLV IDGGQIGDGQ SPECRLGSTV
VDLSVPGKFG IIRPGCALES TTAILQQKYG LLPSHASYL
