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P49591

- SYSC_HUMAN

UniProt

P49591 - SYSC_HUMAN

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Protein

Serine--tRNA ligase, cytoplasmic

Gene
SARS, SERS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).1 Publication

Catalytic activityi

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).
ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei318 – 3181ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei325 – 3251Serine By similarity
Binding sitei429 – 4291Serine By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi302 – 3043ATP By similarity
Nucleotide bindingi391 – 3944ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: ProtInc
  3. serine-tRNA ligase activity Source: Reactome

GO - Biological processi

  1. gene expression Source: Reactome
  2. selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
  3. seryl-tRNA aminoacylation Source: InterPro
  4. translation Source: ProtInc
  5. tRNA aminoacylation for protein translation Source: Reactome
  6. tRNA processing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.
UniPathwayiUPA00906; UER00895.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--tRNA ligase, cytoplasmic (EC:6.1.1.11)
Alternative name(s):
Seryl-tRNA synthetase
Short name:
SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene namesi
Name:SARS
Synonyms:SERS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10537. SARS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Serine--tRNA ligase, cytoplasmicPRO_0000122191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei241 – 2411Phosphoserine1 Publication
Modified residuei323 – 3231N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49591.
PaxDbiP49591.
PRIDEiP49591.

PTM databases

PhosphoSiteiP49591.

Miscellaneous databases

PMAP-CutDBP49591.

Expressioni

Gene expression databases

ArrayExpressiP49591.
BgeeiP49591.
CleanExiHS_SARS.
GenevestigatoriP49591.

Organism-specific databases

HPAiHPA016939.

Interactioni

Subunit structurei

Homodimer. The tRNA molecule binds across the dimer By similarity.

Protein-protein interaction databases

BioGridi112208. 31 interactions.
DIPiDIP-38215N.
IntActiP49591. 4 interactions.
STRINGi9606.ENSP00000234677.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73
Helixi10 – 123
Helixi16 – 2510
Helixi31 – 7040
Helixi82 – 843
Beta strandi86 – 894
Helixi92 – 965
Beta strandi100 – 1023
Helixi103 – 11210
Helixi118 – 13114
Helixi132 – 1343
Helixi149 – 1524
Beta strandi154 – 1607
Helixi170 – 1767
Helixi183 – 1897
Beta strandi195 – 1973
Helixi199 – 21719
Beta strandi221 – 2244
Beta strandi227 – 2304
Helixi231 – 2377
Helixi240 – 2456
Beta strandi249 – 2513
Beta strandi254 – 2563
Beta strandi266 – 2683
Helixi273 – 2775
Turni278 – 2825
Beta strandi283 – 2853
Turni287 – 2893
Beta strandi292 – 30110
Beta strandi308 – 3114
Beta strandi315 – 3173
Beta strandi319 – 33012
Helixi336 – 35419
Beta strandi359 – 3635
Helixi366 – 3683
Beta strandi374 – 38310
Turni384 – 3874
Beta strandi388 – 39710
Helixi401 – 4066
Beta strandi409 – 4113
Beta strandi424 – 4329
Helixi433 – 44412
Beta strandi447 – 4515
Helixi454 – 4574
Beta strandi464 – 4696

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VBBX-ray2.89A/B/C/D/E/F1-514[»]
4L87X-ray2.90A2-477[»]
ProteinModelPortaliP49591.
SMRiP49591. Positions 2-477.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 2733Serine binding By similarity

Domaini

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0172.
HOGENOMiHOG000035937.
HOVERGENiHBG023172.
KOiK01875.
OrthoDBiEOG7Z95KZ.
PhylomeDBiP49591.
TreeFamiTF300762.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 2 hits.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49591-1 [UniParc]FASTAAdd to Basket

« Hide

MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA    50
DNLNKLKNLC SKTIGEKMKK KEPVGDDESV PENVLSFDDL TADALANLKV 100
SQIKKVRLLI DEAILKCDAE RIKLEAERFE NLREIGNLLH PSVPISNDED 150
VDNKVERIWG DCTVRKKYSH VDLVVMVDGF EGEKGAVVAG SRGYFLKGVL 200
VFLEQALIQY ALRTLGSRGY IPIYTPFFMR KEVMQEVAQL SQFDEELYKV 250
IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC 300
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE 350
FYQSLGIPYH IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD 400
YQARRLRIRY GQTKKMMDKV EFVHMLNATM CATTRTICAI LENYQTEKGI 450
TVPEKLKEFM PPGLQELIPF VKPAPIEQEP SKKQKKQHEG SKKKAAARDV 500
TLENRLQNME VTDA 514
Length:514
Mass (Da):58,777
Last modified:January 23, 2007 - v3
Checksum:iF59DA8E55F193ACB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541N → S in CAA62635. 1 Publication
Sequence conflicti435 – 4351R → C in AAH09390. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91257 mRNA. Translation: CAA62635.1.
D49914 mRNA. Translation: BAA95602.1.
AK312771 mRNA. Translation: BAG35636.1.
AL356389 Genomic DNA. Translation: CAI13599.1.
CH471122 Genomic DNA. Translation: EAW56369.1.
BC000716 mRNA. Translation: AAH00716.1.
BC009390 mRNA. Translation: AAH09390.1.
CCDSiCCDS795.1.
PIRiG01026.
RefSeqiNP_006504.2. NM_006513.3.
UniGeneiHs.531176.

Genome annotation databases

EnsembliENST00000234677; ENSP00000234677; ENSG00000031698.
GeneIDi6301.
KEGGihsa:6301.
UCSCiuc001dwu.2. human.

Polymorphism databases

DMDMi19860217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91257 mRNA. Translation: CAA62635.1 .
D49914 mRNA. Translation: BAA95602.1 .
AK312771 mRNA. Translation: BAG35636.1 .
AL356389 Genomic DNA. Translation: CAI13599.1 .
CH471122 Genomic DNA. Translation: EAW56369.1 .
BC000716 mRNA. Translation: AAH00716.1 .
BC009390 mRNA. Translation: AAH09390.1 .
CCDSi CCDS795.1.
PIRi G01026.
RefSeqi NP_006504.2. NM_006513.3.
UniGenei Hs.531176.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VBB X-ray 2.89 A/B/C/D/E/F 1-514 [» ]
4L87 X-ray 2.90 A 2-477 [» ]
ProteinModelPortali P49591.
SMRi P49591. Positions 2-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112208. 31 interactions.
DIPi DIP-38215N.
IntActi P49591. 4 interactions.
STRINGi 9606.ENSP00000234677.

Chemistry

DrugBanki DB00133. L-Serine.

PTM databases

PhosphoSitei P49591.

Polymorphism databases

DMDMi 19860217.

Proteomic databases

MaxQBi P49591.
PaxDbi P49591.
PRIDEi P49591.

Protocols and materials databases

DNASUi 6301.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234677 ; ENSP00000234677 ; ENSG00000031698 .
GeneIDi 6301.
KEGGi hsa:6301.
UCSCi uc001dwu.2. human.

Organism-specific databases

CTDi 6301.
GeneCardsi GC01P109756.
HGNCi HGNC:10537. SARS.
HPAi HPA016939.
MIMi 607529. gene.
neXtProti NX_P49591.
PharmGKBi PA34945.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0172.
HOGENOMi HOG000035937.
HOVERGENi HBG023172.
KOi K01875.
OrthoDBi EOG7Z95KZ.
PhylomeDBi P49591.
TreeFami TF300762.

Enzyme and pathway databases

UniPathwayi UPA00906 ; UER00895 .
Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi SARS. human.
GeneWikii SARS_(gene).
GenomeRNAii 6301.
NextBioi 24463.
PMAP-CutDB P49591.
PROi P49591.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49591.
Bgeei P49591.
CleanExi HS_SARS.
Genevestigatori P49591.

Family and domain databases

Gene3Di 1.10.287.40. 1 hit.
InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view ]
PANTHERi PTHR11778. PTHR11778. 1 hit.
Pfami PF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view ]
PIRSFi PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSi PR00981. TRNASYNTHSER.
SUPFAMi SSF46589. SSF46589. 2 hits.
TIGRFAMsi TIGR00414. serS. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase."
    Vincent C., Tarbouriech N., Haertlein M.
    Eur. J. Biochem. 250:77-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Brain.
  2. "Isolation and characterization of human seryl-tRNA synthetase cDNA."
    Shiba K., Yu R., Motegi H., Martinis S., Noda T.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain and Placenta.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYSC_HUMAN
AccessioniPrimary (citable) accession number: P49591
Secondary accession number(s): B2R6Y9, Q5T5C8, Q9NSE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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