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Q9UGM6

- SYWM_HUMAN

UniProt

Q9UGM6 - SYWM_HUMAN

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Protein

Tryptophan--tRNA ligase, mitochondrial

Gene

WARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. tryptophan-tRNA ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. gene expression Source: Reactome
  2. tRNA aminoacylation for protein translation Source: Reactome
  3. tryptophanyl-tRNA aminoacylation Source: InterPro
  4. vasculogenesis Source: Ensembl
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

BRENDAi6.1.1.2. 2681.
ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligase, mitochondrial (EC:6.1.1.2)
Alternative name(s):
(Mt)TrpRS
Tryptophanyl-tRNA synthetase
Short name:
TrpRS
Gene namesi
Name:WARS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12730. WARS2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37341.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818MitochondrionAdd
BLAST
Chaini19 – 360342Tryptophan--tRNA ligase, mitochondrialPRO_0000035828Add
BLAST

Proteomic databases

MaxQBiQ9UGM6.
PaxDbiQ9UGM6.
PRIDEiQ9UGM6.

PTM databases

PhosphoSiteiQ9UGM6.

Expressioni

Gene expression databases

BgeeiQ9UGM6.
CleanExiHS_WARS2.
ExpressionAtlasiQ9UGM6. baseline and differential.
GenevestigatoriQ9UGM6.

Interactioni

Protein-protein interaction databases

BioGridi115633. 4 interactions.
STRINGi9606.ENSP00000235521.

Structurei

3D structure databases

ProteinModelPortaliQ9UGM6.
SMRiQ9UGM6. Positions 35-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0180.
GeneTreeiENSGT00510000047425.
HOGENOMiHOG000059940.
HOVERGENiHBG027444.
InParanoidiQ9UGM6.
KOiK01867.
OMAiSHILHRP.
OrthoDBiEOG7J447N.
PhylomeDBiQ9UGM6.
TreeFamiTF314321.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00140_B. Trp_tRNA_synth_B.
InterProiIPR001412. 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]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UGM6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MALHSMRKAR ERWSFIRALH KGSAAAPALQ KDSKKRVFSG IQPTGILHLG
60 70 80 90 100
NYLGAIESWV RLQDEYDSVL YSIVDLHSIT VPQDPAVLRQ SILDMTAVLL
110 120 130 140 150
ACGINPEKSI LFQQSQVSEH TQLSWILSCM VRLPRLQHLH QWKAKTTKQK
160 170 180 190 200
HDGTVGLLTY PVLQAADILL YKSTHVPVGE DQVQHMELVQ DLAQGFNKKY
210 220 230 240 250
GEFFPVPESI LTSMKKVKSL RDPSAKMSKS DPDKLATVRI TDSPEEIVQK
260 270 280 290 300
FRKAVTDFTS EVTYDPAGRA GVSNIVAVHA AVTGLSVEEV VRRSAGMNTA
310 320 330 340 350
RYKLAVADAV IEKFAPIKRE IEKLKLDKDH LEKVLQIGSA KAKELAYTVC
360
QEVKKLVGFL
Length:360
Mass (Da):40,147
Last modified:May 1, 2000 - v1
Checksum:i8C80DF6FCA214A91
GO
Isoform 2 (identifier: Q9UGM6-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:220
Mass (Da):24,813
Checksum:i2535F75EDCD833F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511H → R in BAD96917. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501G → S.1 Publication
Corresponds to variant rs11552864 [ dbSNP | Ensembl ].
VAR_028848
Natural varianti267 – 2671A → P.
Corresponds to variant rs3790549 [ dbSNP | Ensembl ].
VAR_020217
Natural varianti360 – 3601L → P.
Corresponds to variant rs17023101 [ dbSNP | Ensembl ].
VAR_052407

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei212 – 2209TSMKKVKSL → SMCVLVFLT in isoform 2. 1 PublicationVSP_041414
Alternative sequencei221 – 360140Missing in isoform 2. 1 PublicationVSP_041415Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30817.1. [Q9UGM6-2]
CCDS900.1. [Q9UGM6-1]
RefSeqiNP_056651.1. NM_015836.3. [Q9UGM6-1]
NP_957715.1. NM_201263.2. [Q9UGM6-2]
UniGeneiHs.523506.

Genome annotation databases

EnsembliENST00000235521; ENSP00000235521; ENSG00000116874. [Q9UGM6-1]
ENST00000369426; ENSP00000358434; ENSG00000116874. [Q9UGM6-2]
GeneIDi10352.
KEGGihsa:10352.
UCSCiuc001ehm.3. human. [Q9UGM6-2]
uc001ehn.3. human. [Q9UGM6-1]

Polymorphism databases

DMDMi21362967.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS30817.1. [Q9UGM6-2 ]
CCDS900.1. [Q9UGM6-1 ]
RefSeqi NP_056651.1. NM_015836.3. [Q9UGM6-1 ]
NP_957715.1. NM_201263.2. [Q9UGM6-2 ]
UniGenei Hs.523506.

3D structure databases

ProteinModelPortali Q9UGM6.
SMRi Q9UGM6. Positions 35-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115633. 4 interactions.
STRINGi 9606.ENSP00000235521.

Chemistry

DrugBanki DB00150. L-Tryptophan.

PTM databases

PhosphoSitei Q9UGM6.

Polymorphism databases

DMDMi 21362967.

Proteomic databases

MaxQBi Q9UGM6.
PaxDbi Q9UGM6.
PRIDEi Q9UGM6.

Protocols and materials databases

DNASUi 10352.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000235521 ; ENSP00000235521 ; ENSG00000116874 . [Q9UGM6-1 ]
ENST00000369426 ; ENSP00000358434 ; ENSG00000116874 . [Q9UGM6-2 ]
GeneIDi 10352.
KEGGi hsa:10352.
UCSCi uc001ehm.3. human. [Q9UGM6-2 ]
uc001ehn.3. human. [Q9UGM6-1 ]

Organism-specific databases

CTDi 10352.
GeneCardsi GC01M119573.
H-InvDB HIX0023588.
HGNCi HGNC:12730. WARS2.
MIMi 604733. gene.
neXtProti NX_Q9UGM6.
PharmGKBi PA37341.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0180.
GeneTreei ENSGT00510000047425.
HOGENOMi HOG000059940.
HOVERGENi HBG027444.
InParanoidi Q9UGM6.
KOi K01867.
OMAi SHILHRP.
OrthoDBi EOG7J447N.
PhylomeDBi Q9UGM6.
TreeFami TF314321.

Enzyme and pathway databases

BRENDAi 6.1.1.2. 2681.
Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi WARS2. human.
GeneWikii WARS2.
GenomeRNAii 10352.
NextBioi 39255.
PROi Q9UGM6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UGM6.
CleanExi HS_WARS2.
ExpressionAtlasi Q9UGM6. baseline and differential.
Genevestigatori Q9UGM6.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00140_B. Trp_tRNA_synth_B.
InterProi 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 ]
PANTHERi PTHR10055. PTHR10055. 1 hit.
Pfami PF00579. tRNA-synt_1b. 1 hit.
[Graphical view ]
PRINTSi PR01039. TRNASYNTHTRP.
TIGRFAMsi TIGR00233. trpS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYWM_HUMAN
AccessioniPrimary (citable) accession number: Q9UGM6
Secondary accession number(s): B1ALR1
, B2R9D4, Q53FT4, Q5VUD2, Q86TQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 119 of the entry and version 1 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

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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3