Q9UGM6 (SYWM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan--tRNA ligase, mitochondrial
EC=6.1.1.2

Alternative name(s):
(Mt)TrpRS
Tryptophanyl-tRNA synthetase
Short name=TrpRS

Gene names

Name:

WARS2

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	360 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)

Catalytic activity	ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome tryptophanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro vasculogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tryptophan-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UGM6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UGM6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     212-220: TSMKKVKSL → SMCVLVFLT
     221-360: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 18	18	Mitochondrion
	Chain	19 – 360	342	Tryptophan--tRNA ligase, mitochondrial		PRO_0000035828
Natural variations
	Alternative sequence	212 – 220	9	TSMKKVKSL → SMCVLVFLT in isoform 2.		VSP_041414
	Alternative sequence	221 – 360	140	Missing in isoform 2.		VSP_041415
	Natural variant	50	1	G → S. Ref.6 Corresponds to variant rs11552864 [ dbSNP | Ensembl ].		VAR_028848
	Natural variant	267	1	A → P. Corresponds to variant rs3790549 [ dbSNP | Ensembl ].		VAR_020217
	Natural variant	360	1	L → P. Corresponds to variant rs17023101 [ dbSNP | Ensembl ].		VAR_052407
Experimental info
	Sequence conflict	151	1	H → R in BAD96917. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8C80DF6FCA214A91	FASTA	360	40,147
	10 20 30 40 50 60 MALHSMRKAR ERWSFIRALH KGSAAAPALQ KDSKKRVFSG IQPTGILHLG NYLGAIESWV 70 80 90 100 110 120 RLQDEYDSVL YSIVDLHSIT VPQDPAVLRQ SILDMTAVLL ACGINPEKSI LFQQSQVSEH 130 140 150 160 170 180 TQLSWILSCM VRLPRLQHLH QWKAKTTKQK HDGTVGLLTY PVLQAADILL YKSTHVPVGE 190 200 210 220 230 240 DQVQHMELVQ DLAQGFNKKY GEFFPVPESI LTSMKKVKSL RDPSAKMSKS DPDKLATVRI 250 260 270 280 290 300 TDSPEEIVQK FRKAVTDFTS EVTYDPAGRA GVSNIVAVHA AVTGLSVEEV VRRSAGMNTA 310 320 330 340 350 360 RYKLAVADAV IEKFAPIKRE IEKLKLDKDH LEKVLQIGSA KAKELAYTVC QEVKKLVGFL
	Isoform 2 [UniParc]. Checksum: 2535F75EDCD833F5	FASTA	220	24,813
	10 20 30 40 50 60 MALHSMRKAR ERWSFIRALH KGSAAAPALQ KDSKKRVFSG IQPTGILHLG NYLGAIESWV 70 80 90 100 110 120 RLQDEYDSVL YSIVDLHSIT VPQDPAVLRQ SILDMTAVLL ACGINPEKSI LFQQSQVSEH 130 140 150 160 170 180 TQLSWILSCM VRLPRLQHLH QWKAKTTKQK HDGTVGLLTY PVLQAADILL YKSTHVPVGE 190 200 210 220 DQVQHMELVQ DLAQGFNKKY GEFFPVPESI LSMCVLVFLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase." Jorgensen R., Soegaard T.M.M., Rossing A.B., Martensen P.M., Justesen J. J. Biol. Chem. 275:16820-16826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[2]	"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] (ISOFORM 1).
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney proximal tubule.
[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] (ISOFORMS 1 AND 2), VARIANT SER-50. Tissue: Brain.
[7]	"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	AJ242739 mRNA. Translation: CAB63107.1. AK223197 mRNA. Translation: BAD96917.1. AK313740 mRNA. Translation: BAG36481.1. AL359823, AL139420, AL590288 Genomic DNA. Translation: CAI21995.1. AL359823, AL139420, AL590288 Genomic DNA. Translation: CAI21996.1. AL139420, AL359823, AL590288 Genomic DNA. Translation: CAI22501.1. AL139420, AL359823, AL590288 Genomic DNA. Translation: CAI22502.1. AL590288, AL359823, AL139420 Genomic DNA. Translation: CAH71367.1. AL590288, AL139420, AL359823 Genomic DNA. Translation: CAH71368.1. CH471122 Genomic DNA. Translation: EAW56693.1. BC044575 mRNA. Translation: AAH44575.1. BC039889 mRNA. No translation available.
IPI	IPI00025050. IPI00397465.
RefSeq	NP_056651.1. NM_015836.3. NP_957715.1. NM_201263.2.
UniGene	Hs.523506.
3D structure databases
ProteinModelPortal	Q9UGM6.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000235521.
PTM databases
PhosphoSite	Q9UGM6.
Polymorphism databases
DMDM	21362967.
Proteomic databases
PaxDb	Q9UGM6.
PRIDE	Q9UGM6.
Protocols and materials databases
DNASU	10352.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000235521; ENSP00000235521; ENSG00000116874. ENST00000369426; ENSP00000358434; ENSG00000116874.
GeneID	10352.
KEGG	hsa:10352.
UCSC	uc001ehn.3. human.
Organism-specific databases
CTD	10352.
GeneCards	GC01M119573.
H-InvDB	HIX0023588.
HGNC	HGNC:12730. WARS2.
MIM	604733. gene.
neXtProt	NX_Q9UGM6.
PharmGKB	PA37341.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0180.
HOGENOM	HOG000059940.
HOVERGEN	HBG027444.
InParanoid	Q9UGM6.
KO	K01867.
OMA	KFAPIKS.
OrthoDB	EOG4TQM9F.
PhylomeDB	Q9UGM6.
Enzyme and pathway databases
BRENDA	6.1.1.2. 2681.
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9UGM6.
Bgee	Q9UGM6.
CleanEx	HS_WARS2.
Genevestigator	Q9UGM6.
GermOnline	ENSG00000116874. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002306. Trp-tRNA-ligase. IPR024109. Trp-tRNA-ligase_bac-type. [Graphical view]
PANTHER	PTHR10055. PTHR10055. 1 hit.
Pfam	PF00579. tRNA-synt_1b. 1 hit. [Graphical view]
PRINTS	PR01039. TRNASYNTHTRP.
TIGRFAMs	TIGR00233. trpS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	WARS2. human.
DrugBank	DB00150. L-Tryptophan.
GenomeRNAi	10352.
NextBio	39255.
SOURCE	Search...

Entry information

Entry name

SYWM_HUMAN

Accession

Primary (citable) accession number: Q9UGM6
Secondary accession number(s): B1ALR1 , B2R9D4, Q53FT4, Q5VUD2, Q86TQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 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.