P49591 (SYSC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SARS
Synonyms:	SERS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
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	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	selenocysteinyl-tRNA(Sec) biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome tRNA processing Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Traceable author statement Ref.1. Source: ProtInc serine-tRNA ligase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

Serine--tRNA ligase, 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 amide nitrogen and carbonyl oxygen 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.8

Experimental info

Sequence conflict

54

1

N → S in CAA62635. Ref.1

Sequence conflict

435

1

R → C in AAH09390. Ref.6

Secondary structure

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514

Helix Strand Turn

Details...

Helix

5 – 7

3

Helix

10 – 12

3

Helix

16 – 25

10

Helix

31 – 70

40

Helix

82 – 84

3

Beta strand

86 – 89

4

Helix

92 – 96

5

Beta strand

100 – 102

3

Helix

103 – 112

10

Helix

118 – 131

14

Helix

132 – 134

3

Helix

149 – 152

4

Beta strand

154 – 160

7

Helix

170 – 176

7

Helix

183 – 189

7

Beta strand

195 – 197

3

Helix

199 – 217

19

Beta strand

221 – 224

4

Beta strand

227 – 230

4

Helix

231 – 237

7

Beta strand

249 – 251

3

Beta strand

266 – 268

3

Helix

273 – 277

5

Turn

287 – 289

3

Beta strand

292 – 301

10

Beta strand

315 – 317

3

Beta strand

319 – 330

12

Helix

336 – 354

19

Beta strand

359 – 363

5

Helix

366 – 368

3

Beta strand

374 – 383

10

Turn

384 – 387

4

Beta strand

388 – 397

10

Helix

401 – 406

6

Beta strand

409 – 411

3

Beta strand

424 – 432

9

Helix

433 – 444

12

Beta strand

447 – 451

5

Helix

454 – 457

4

Beta strand

464 – 469

6

Sequences

	Sequence		Length	Mass (Da)
	P49591 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F59DA8E55F193ACB	FASTA	514	58,777
	10 20 30 40 50 60 MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC 70 80 90 100 110 120 SKTIGEKMKK KEPVGDDESV PENVLSFDDL TADALANLKV SQIKKVRLLI DEAILKCDAE 130 140 150 160 170 180 RIKLEAERFE NLREIGNLLH PSVPISNDED VDNKVERIWG DCTVRKKYSH VDLVVMVDGF 190 200 210 220 230 240 EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY IPIYTPFFMR KEVMQEVAQL 250 260 270 280 290 300 SQFDEELYKV IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC 310 320 330 340 350 360 FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE FYQSLGIPYH 370 380 390 400 410 420 IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV 430 440 450 460 470 480 EFVHMLNATM CATTRTICAI LENYQTEKGI TVPEKLKEFM PPGLQELIPF VKPAPIEQEP 490 500 510 SKKQKKQHEG SKKKAAARDV TLENRLQNME VTDA

References

	« Hide 'large scale' referencesShow '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] [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]	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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"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, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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. NM_006513.3.

UniGene

Hs.531176.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3VBB	X-ray	2.89	A/B/C/D/E/F	1-514	[»]

ProteinModelPortal

P49591.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49591. 4 interactions.

STRING

9606.ENSP00000234677.

PTM databases

PhosphoSite

P49591.

Polymorphism databases

DMDM

19860217.

Proteomic databases

PaxDb

P49591.

PRIDE

P49591.

Protocols and materials databases

DNASU

6301.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000234677; ENSP00000234677; ENSG00000031698.

GeneID

6301.

KEGG

hsa:6301.

UCSC

uc001dwu.2. human.

Organism-specific databases

CTD

6301.

GeneCards

GC01P109756.

HGNC

HGNC:10537. SARS.

HPA

HPA016939.

MIM

607529. gene.

neXtProt

NX_P49591.

PharmGKB

PA34945.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0172.

HOGENOM

HOG000035937.

HOVERGEN

HBG023172.

KO

K01875.

OrthoDB

EOG4320Z0.

PhylomeDB

P49591.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

UniPathway

UPA00906; UER00895.

Gene expression databases

ArrayExpress

P49591.

Bgee

P49591.

CleanEx

HS_SARS.

Genevestigator

P49591.

GermOnline

ENSG00000031698. Homo sapiens.

Family and domain databases

Gene3D

1.10.287.40. 1 hit.

InterPro

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]

PANTHER

PTHR11778. PTHR11778. 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.

SUPFAM

SSF46589. tRNA_binding_arm. 1 hit.

TIGRFAMs

TIGR00414. serS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SARS. human.

DrugBank

DB00133. L-Serine.

GenomeRNAi

6301.

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

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.