Reviewed,
UniProtKB/Swiss-Prot P49591 (SYSC_HUMAN)
Last modified
February 9, 2010.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Seryl-tRNA synthetase, cytoplasmic EC=6.1.1.11 Alternative name(s): Seryl-tRNA(Ser/Sec) synthetase Serine--tRNA ligase Short name=SerRS | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 514 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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). Ref.1 |
| Catalytic activity | ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). |
| Pathway | |
| Subunit structure | Homodimer. The tRNA molecule binds across the dimer By similarity. |
| Subcellular location | |
| Domain | Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA processing Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | cytosol Ref.1 Inferred from Experiment. Source: Reactome |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Ref.1Traceable author statement. Source: ProtInc protein bindingInferred from physical interaction. Source: IntAct serine-tRNA ligase activity Ref.1Inferred from Experiment. Source: Reactome |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 514 | 513 | Seryl-tRNA synthetase, cytoplasmic | PRO_0000122191 | |||||
Regions | |||||||||
| Nucleotide binding | 302 – 304 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 391 – 394 | 4 | ATP By similarity | ||||||
| Region | 271 – 273 | 3 | Serine binding By similarity | ||||||
Sites | |||||||||
| Binding site | 318 | 1 | ATP; via carbonyl oxygen and amide nitrogen By similarity | ||||||
| Binding site | 325 | 1 | Serine By similarity | ||||||
| Binding site | 429 | 1 | Serine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 241 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 323 | 1 | N6-acetyllysine Ref.9 | ||||||
Experimental info | |||||||||
| Sequence conflict | 54 | 1 | N → S in CAA62635. Ref.1 | ||||||
| Sequence conflict | 435 | 1 | R → C in AAH09390. Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 9431993] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Placenta. |
| [7] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. |
| [8] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-323, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00220637. |
| PIR | G01026. |
| RefSeq | NP_006504.2. |
| UniGene | Hs.531176 |
3D structure databases | |
| SMR | P49591. Positions 2-470. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P49591. 6 interactions. |
| STRING | P49591. |
PTM databases | |
| PhosphoSite | P49591. |
Proteomic databases | |
| PRIDE | P49591. |
Genome annotation databases | |
| Ensembl | ENST00000234677; ENSP00000234677; ENSG00000031698; Homo sapiens. [Genome view] |
| GeneID | 6301. |
| KEGG | hsa:6301. |
| NMPDR | fig|9606.3.peg.1628. |
| UCSC | uc001dwu.1. human. |
Organism-specific databases | |
| CTD | 6301. |
| GeneCards | GC01P109468. |
| H-InvDB | HIX0000844. |
| HGNC | HGNC:10537. SARS. |
| HPA | HPA016939. |
| MIM | 607529. gene. |
| PharmGKB | PA34945. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG19225. |
| HOVERGEN | P49591. |
| OrthoDB | EOG9DFS7F. |
| PhylomeDB | P49591. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.11. 247. |
| Reactome | REACT_71. Gene Expression. |
Gene expression databases | |
| ArrayExpress | P49591. |
| Bgee | P49591. |
| CleanEx | HS_SARS. |
| Genevestigator | P49591. |
| GermOnline | ENSG00000031698. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. IPR010978. tRNA_bd_arm. [Graphical view] |
| PANTHER | PTHR11778. tRNA-synt_ser. 1 hit. |
| Pfam | PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view] |
| PIRSF | PIRSF001529. Ser-tRNA-synth_IIa. 1 hit. |
| PRINTS | PR00981. TRNASYNTHSER. |
| TIGRFAMs | TIGR00414. serS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00133. L-Serine. |
| NextBio | 24463. |
| PMAP-CutDB | P49591. |
| SOURCE | Search... |
Entry information
| Entry name | SYSC_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P49591 Secondary accession number(s): B2R6Y9, Q5T5C8, Q9NSE3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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