Full text data of SARS
SARS
(SERS)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Serine--tRNA ligase, cytoplasmic; 6.1.1.11 (Seryl-tRNA synthetase; SerRS; Seryl-tRNA(Ser/Sec) synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine--tRNA ligase, cytoplasmic; 6.1.1.11 (Seryl-tRNA synthetase; SerRS; Seryl-tRNA(Ser/Sec) synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49591
ID SYSC_HUMAN Reviewed; 514 AA.
AC P49591; B2R6Y9; Q5T5C8; Q9NSE3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Serine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=SARS; Synonyms=SERS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9431993; DOI=10.1111/j.1432-1033.1997.00077.x;
RA Vincent C., Tarbouriech N., Haertlein M.;
RT "Genomic organization, cDNA sequence, bacterial expression, and
RT purification of human seryl-tRNA synthase.";
RL Eur. J. Biochem. 250:77-84(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shiba K., Yu R., Motegi H., Martinis S., Noda T.;
RT "Isolation and characterization of human seryl-tRNA synthetase cDNA.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-323, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC probably able to aminoacylate tRNA(Sec) with serine, to form the
CC misacylated tRNA L-seryl-tRNA(Sec), which will be further
CC converted into selenocysteinyl-tRNA(Sec).
CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC + L-seryl-tRNA(Ser).
CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC + L-seryl-tRNA(Sec).
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
CC 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC N-terminal extension that is involved in tRNA binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Type-1 seryl-tRNA synthetase subfamily.
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DR EMBL; X91257; CAA62635.1; -; mRNA.
DR EMBL; D49914; BAA95602.1; -; mRNA.
DR EMBL; AK312771; BAG35636.1; -; mRNA.
DR EMBL; AL356389; CAI13599.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56369.1; -; Genomic_DNA.
DR EMBL; BC000716; AAH00716.1; -; mRNA.
DR EMBL; BC009390; AAH09390.1; -; mRNA.
DR PIR; G01026; G01026.
DR RefSeq; NP_006504.2; NM_006513.3.
DR UniGene; Hs.531176; -.
DR PDB; 3VBB; X-ray; 2.89 A; A/B/C/D/E/F=1-514.
DR PDB; 4L87; X-ray; 2.90 A; A=2-477.
DR PDBsum; 3VBB; -.
DR PDBsum; 4L87; -.
DR ProteinModelPortal; P49591; -.
DR SMR; P49591; 2-475.
DR IntAct; P49591; 4.
DR STRING; 9606.ENSP00000234677; -.
DR DrugBank; DB00133; L-Serine.
DR PhosphoSite; P49591; -.
DR DMDM; 19860217; -.
DR PaxDb; P49591; -.
DR PRIDE; P49591; -.
DR DNASU; 6301; -.
DR Ensembl; ENST00000234677; ENSP00000234677; ENSG00000031698.
DR GeneID; 6301; -.
DR KEGG; hsa:6301; -.
DR UCSC; uc001dwu.2; human.
DR CTD; 6301; -.
DR GeneCards; GC01P109756; -.
DR HGNC; HGNC:10537; SARS.
DR HPA; HPA016939; -.
DR MIM; 607529; gene.
DR neXtProt; NX_P49591; -.
DR PharmGKB; PA34945; -.
DR eggNOG; COG0172; -.
DR HOGENOM; HOG000035937; -.
DR HOVERGEN; HBG023172; -.
DR KO; K01875; -.
DR OrthoDB; EOG7Z95KZ; -.
DR PhylomeDB; P49591; -.
DR Reactome; REACT_71; Gene Expression.
DR UniPathway; UPA00906; UER00895.
DR ChiTaRS; SARS; human.
DR GeneWiki; SARS_(gene); -.
DR GenomeRNAi; 6301; -.
DR NextBio; 24463; -.
DR PMAP-CutDB; P49591; -.
DR PRO; PR:P49591; -.
DR ArrayExpress; P49591; -.
DR Bgee; P49591; -.
DR CleanEx; HS_SARS; -.
DR Genevestigator; P49591; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0004828; F:serine-tRNA ligase activity; TAS:Reactome.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0008033; P:tRNA processing; TAS:ProtInc.
DR Gene3D; 1.10.287.40; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR11778; PTHR11778; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 2.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1 514 Serine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000122191.
FT NP_BIND 302 304 ATP (By similarity).
FT NP_BIND 391 394 ATP (By similarity).
FT REGION 271 273 Serine binding (By similarity).
FT BINDING 318 318 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 325 325 Serine (By similarity).
FT BINDING 429 429 Serine (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 241 241 Phosphoserine.
FT MOD_RES 323 323 N6-acetyllysine.
FT CONFLICT 54 54 N -> S (in Ref. 1; CAA62635).
FT CONFLICT 435 435 R -> C (in Ref. 6; AAH09390).
FT HELIX 5 7
FT HELIX 10 12
FT HELIX 16 25
FT HELIX 31 70
FT HELIX 82 84
FT STRAND 86 89
FT HELIX 92 96
FT STRAND 100 102
FT HELIX 103 112
FT HELIX 118 131
FT HELIX 132 134
FT HELIX 149 152
FT STRAND 154 160
FT HELIX 170 176
FT HELIX 183 189
FT STRAND 195 197
FT HELIX 199 217
FT STRAND 221 224
FT STRAND 227 230
FT HELIX 231 237
FT HELIX 240 245
FT STRAND 249 251
FT STRAND 254 256
FT STRAND 266 268
FT HELIX 273 277
FT TURN 278 282
FT STRAND 283 285
FT TURN 287 289
FT STRAND 292 301
FT STRAND 308 311
FT STRAND 315 317
FT STRAND 319 330
FT HELIX 336 354
FT STRAND 359 363
FT HELIX 366 368
FT STRAND 374 383
FT TURN 384 387
FT STRAND 388 397
FT HELIX 401 406
FT STRAND 409 411
FT STRAND 424 432
FT HELIX 433 444
FT STRAND 447 451
FT HELIX 454 457
FT STRAND 464 469
SQ SEQUENCE 514 AA; 58777 MW; F59DA8E55F193ACB CRC64;
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC
SKTIGEKMKK KEPVGDDESV PENVLSFDDL TADALANLKV SQIKKVRLLI DEAILKCDAE
RIKLEAERFE NLREIGNLLH PSVPISNDED VDNKVERIWG DCTVRKKYSH VDLVVMVDGF
EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY IPIYTPFFMR KEVMQEVAQL
SQFDEELYKV IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE FYQSLGIPYH
IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV
EFVHMLNATM CATTRTICAI LENYQTEKGI TVPEKLKEFM PPGLQELIPF VKPAPIEQEP
SKKQKKQHEG SKKKAAARDV TLENRLQNME VTDA
//
ID SYSC_HUMAN Reviewed; 514 AA.
AC P49591; B2R6Y9; Q5T5C8; Q9NSE3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Serine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=SARS; Synonyms=SERS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9431993; DOI=10.1111/j.1432-1033.1997.00077.x;
RA Vincent C., Tarbouriech N., Haertlein M.;
RT "Genomic organization, cDNA sequence, bacterial expression, and
RT purification of human seryl-tRNA synthase.";
RL Eur. J. Biochem. 250:77-84(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shiba K., Yu R., Motegi H., Martinis S., Noda T.;
RT "Isolation and characterization of human seryl-tRNA synthetase cDNA.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-323, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC probably able to aminoacylate tRNA(Sec) with serine, to form the
CC misacylated tRNA L-seryl-tRNA(Sec), which will be further
CC converted into selenocysteinyl-tRNA(Sec).
CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC + L-seryl-tRNA(Ser).
CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC + L-seryl-tRNA(Sec).
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
CC 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC N-terminal extension that is involved in tRNA binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Type-1 seryl-tRNA synthetase subfamily.
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DR EMBL; X91257; CAA62635.1; -; mRNA.
DR EMBL; D49914; BAA95602.1; -; mRNA.
DR EMBL; AK312771; BAG35636.1; -; mRNA.
DR EMBL; AL356389; CAI13599.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56369.1; -; Genomic_DNA.
DR EMBL; BC000716; AAH00716.1; -; mRNA.
DR EMBL; BC009390; AAH09390.1; -; mRNA.
DR PIR; G01026; G01026.
DR RefSeq; NP_006504.2; NM_006513.3.
DR UniGene; Hs.531176; -.
DR PDB; 3VBB; X-ray; 2.89 A; A/B/C/D/E/F=1-514.
DR PDB; 4L87; X-ray; 2.90 A; A=2-477.
DR PDBsum; 3VBB; -.
DR PDBsum; 4L87; -.
DR ProteinModelPortal; P49591; -.
DR SMR; P49591; 2-475.
DR IntAct; P49591; 4.
DR STRING; 9606.ENSP00000234677; -.
DR DrugBank; DB00133; L-Serine.
DR PhosphoSite; P49591; -.
DR DMDM; 19860217; -.
DR PaxDb; P49591; -.
DR PRIDE; P49591; -.
DR DNASU; 6301; -.
DR Ensembl; ENST00000234677; ENSP00000234677; ENSG00000031698.
DR GeneID; 6301; -.
DR KEGG; hsa:6301; -.
DR UCSC; uc001dwu.2; human.
DR CTD; 6301; -.
DR GeneCards; GC01P109756; -.
DR HGNC; HGNC:10537; SARS.
DR HPA; HPA016939; -.
DR MIM; 607529; gene.
DR neXtProt; NX_P49591; -.
DR PharmGKB; PA34945; -.
DR eggNOG; COG0172; -.
DR HOGENOM; HOG000035937; -.
DR HOVERGEN; HBG023172; -.
DR KO; K01875; -.
DR OrthoDB; EOG7Z95KZ; -.
DR PhylomeDB; P49591; -.
DR Reactome; REACT_71; Gene Expression.
DR UniPathway; UPA00906; UER00895.
DR ChiTaRS; SARS; human.
DR GeneWiki; SARS_(gene); -.
DR GenomeRNAi; 6301; -.
DR NextBio; 24463; -.
DR PMAP-CutDB; P49591; -.
DR PRO; PR:P49591; -.
DR ArrayExpress; P49591; -.
DR Bgee; P49591; -.
DR CleanEx; HS_SARS; -.
DR Genevestigator; P49591; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0004828; F:serine-tRNA ligase activity; TAS:Reactome.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0008033; P:tRNA processing; TAS:ProtInc.
DR Gene3D; 1.10.287.40; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR11778; PTHR11778; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 2.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1 514 Serine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000122191.
FT NP_BIND 302 304 ATP (By similarity).
FT NP_BIND 391 394 ATP (By similarity).
FT REGION 271 273 Serine binding (By similarity).
FT BINDING 318 318 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 325 325 Serine (By similarity).
FT BINDING 429 429 Serine (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 241 241 Phosphoserine.
FT MOD_RES 323 323 N6-acetyllysine.
FT CONFLICT 54 54 N -> S (in Ref. 1; CAA62635).
FT CONFLICT 435 435 R -> C (in Ref. 6; AAH09390).
FT HELIX 5 7
FT HELIX 10 12
FT HELIX 16 25
FT HELIX 31 70
FT HELIX 82 84
FT STRAND 86 89
FT HELIX 92 96
FT STRAND 100 102
FT HELIX 103 112
FT HELIX 118 131
FT HELIX 132 134
FT HELIX 149 152
FT STRAND 154 160
FT HELIX 170 176
FT HELIX 183 189
FT STRAND 195 197
FT HELIX 199 217
FT STRAND 221 224
FT STRAND 227 230
FT HELIX 231 237
FT HELIX 240 245
FT STRAND 249 251
FT STRAND 254 256
FT STRAND 266 268
FT HELIX 273 277
FT TURN 278 282
FT STRAND 283 285
FT TURN 287 289
FT STRAND 292 301
FT STRAND 308 311
FT STRAND 315 317
FT STRAND 319 330
FT HELIX 336 354
FT STRAND 359 363
FT HELIX 366 368
FT STRAND 374 383
FT TURN 384 387
FT STRAND 388 397
FT HELIX 401 406
FT STRAND 409 411
FT STRAND 424 432
FT HELIX 433 444
FT STRAND 447 451
FT HELIX 454 457
FT STRAND 464 469
SQ SEQUENCE 514 AA; 58777 MW; F59DA8E55F193ACB CRC64;
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC
SKTIGEKMKK KEPVGDDESV PENVLSFDDL TADALANLKV SQIKKVRLLI DEAILKCDAE
RIKLEAERFE NLREIGNLLH PSVPISNDED VDNKVERIWG DCTVRKKYSH VDLVVMVDGF
EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY IPIYTPFFMR KEVMQEVAQL
SQFDEELYKV IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE FYQSLGIPYH
IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV
EFVHMLNATM CATTRTICAI LENYQTEKGI TVPEKLKEFM PPGLQELIPF VKPAPIEQEP
SKKQKKQHEG SKKKAAARDV TLENRLQNME VTDA
//
MIM
607529
*RECORD*
*FIELD* NO
607529
*FIELD* TI
*607529 SERYL-tRNA SYNTHETASE; SARS
;;SERS
*FIELD* TX
CLONING
Vincent et al. (1997) assembled 2 overlapping clones of SARS, which they
read morecalled SERS, isolated from human fetal and infant brain cDNA libraries.
They obtained the full-length cDNA by 5-prime RACE of a brain cDNA
library. The deduced 514-amino acid protein has a calculated molecular
mass of about 59 kD. SARS has a 2-domain structure consisting of a
tRNA-binding domain and a catalytic domain, which contains the 3 motifs
shared by class II aminoacyl-tRNA synthetases. Motifs 2 and 3 share
sequence conservation between prokaryotic and eukaryotic seryl-tRNA
synthetases. SARS has no mitochondrial import signal sequence. Partial
Sars protein sequences from mouse and Chinese hamster share 94% and 92%
identity with human SARS.
GENE FUNCTION
Vincent et al. (1997) assayed bacterially expressed human SARS against
calf liver and E. coli tRNAs and found similar seryl-tRNA synthetase
activity against both substrates.
Using small interfering RNA, Herzog et al. (2009) found that depletion
of SARS from human umbilical vein endothelial cells (HUVECs) increased
cell death, presumably due to loss of the function of SARS in protein
synthesis. However, prior to cell death, SARS depletion caused abnormal
tube formation and increased branching behavior of HUVECs in a rapid
network formation assay. Herzog et al. (2009) concluded that SARS
functions in angiogenesis, in addition to its role in protein synthesis.
GENE STRUCTURE
Vincent et al. (1997) determined that the SARS gene contains 11 exons
and spans more than 15 kb.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SARS
gene to chromosome 1 (TMAP stSG9565).
ANIMAL MODEL
Independently, Fukui et al. (2009) and Herzog et al. (2009) identified
mutations in the zebrafish Sars gene that caused abnormal vascular
development. The function of Sars in vascular development was
independent of its canonical seryl-tRNA synthetase activity.
*FIELD* RF
1. Fukui, H.; Hanaoka, R.; Kawahara, A.: Noncanonical activity of
seryl-tRNA synthetase is involved in vascular development. Circ.
Res. 104: 1253-1259, 2009.
2. Herzog, W.; Muller, K.; Huisken, J.; Stainier, D. Y. R.: Genetic
evidence for a noncanonical function of seryl-tRNA synthetase in vascular
development. Circ. Res. 104: 1260-1266, 2009. Note: Erratum: Circ.
Res. 105: e54 only, 2009.
3. Vincent, C.; Tarbouriech, N.; Hartlein, M.: Genomic organization,
cDNA sequence, bacterial expression, and purification of human seryl-tRNA
synthase. Europ. J. Biochem. 250: 77-84, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 10/22/2010
*FIELD* CD
Patricia A. Hartz: 1/30/2003
*FIELD* ED
terry: 07/27/2012
mgross: 11/3/2010
terry: 10/22/2010
mgross: 1/30/2003
*RECORD*
*FIELD* NO
607529
*FIELD* TI
*607529 SERYL-tRNA SYNTHETASE; SARS
;;SERS
*FIELD* TX
CLONING
Vincent et al. (1997) assembled 2 overlapping clones of SARS, which they
read morecalled SERS, isolated from human fetal and infant brain cDNA libraries.
They obtained the full-length cDNA by 5-prime RACE of a brain cDNA
library. The deduced 514-amino acid protein has a calculated molecular
mass of about 59 kD. SARS has a 2-domain structure consisting of a
tRNA-binding domain and a catalytic domain, which contains the 3 motifs
shared by class II aminoacyl-tRNA synthetases. Motifs 2 and 3 share
sequence conservation between prokaryotic and eukaryotic seryl-tRNA
synthetases. SARS has no mitochondrial import signal sequence. Partial
Sars protein sequences from mouse and Chinese hamster share 94% and 92%
identity with human SARS.
GENE FUNCTION
Vincent et al. (1997) assayed bacterially expressed human SARS against
calf liver and E. coli tRNAs and found similar seryl-tRNA synthetase
activity against both substrates.
Using small interfering RNA, Herzog et al. (2009) found that depletion
of SARS from human umbilical vein endothelial cells (HUVECs) increased
cell death, presumably due to loss of the function of SARS in protein
synthesis. However, prior to cell death, SARS depletion caused abnormal
tube formation and increased branching behavior of HUVECs in a rapid
network formation assay. Herzog et al. (2009) concluded that SARS
functions in angiogenesis, in addition to its role in protein synthesis.
GENE STRUCTURE
Vincent et al. (1997) determined that the SARS gene contains 11 exons
and spans more than 15 kb.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SARS
gene to chromosome 1 (TMAP stSG9565).
ANIMAL MODEL
Independently, Fukui et al. (2009) and Herzog et al. (2009) identified
mutations in the zebrafish Sars gene that caused abnormal vascular
development. The function of Sars in vascular development was
independent of its canonical seryl-tRNA synthetase activity.
*FIELD* RF
1. Fukui, H.; Hanaoka, R.; Kawahara, A.: Noncanonical activity of
seryl-tRNA synthetase is involved in vascular development. Circ.
Res. 104: 1253-1259, 2009.
2. Herzog, W.; Muller, K.; Huisken, J.; Stainier, D. Y. R.: Genetic
evidence for a noncanonical function of seryl-tRNA synthetase in vascular
development. Circ. Res. 104: 1260-1266, 2009. Note: Erratum: Circ.
Res. 105: e54 only, 2009.
3. Vincent, C.; Tarbouriech, N.; Hartlein, M.: Genomic organization,
cDNA sequence, bacterial expression, and purification of human seryl-tRNA
synthase. Europ. J. Biochem. 250: 77-84, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 10/22/2010
*FIELD* CD
Patricia A. Hartz: 1/30/2003
*FIELD* ED
terry: 07/27/2012
mgross: 11/3/2010
terry: 10/22/2010
mgross: 1/30/2003