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P26639

- SYTC_HUMAN

UniProt

P26639 - SYTC_HUMAN

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Protein

Threonine--tRNA ligase, cytoplasmic

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

Functioni

Catalytic activityi

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).UniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein homodimerization activity Source: UniProtKB
  3. threonine-tRNA ligase activity Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. threonyl-tRNA aminoacylation Source: UniProtKB
  3. translation Source: UniProtKB
  4. tRNA aminoacylation for protein translation Source: Reactome
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligase, cytoplasmic (EC:6.1.1.3)
Alternative name(s):
Threonyl-tRNA synthetase
Short name:
ThrRS
Gene namesi
Name:TARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:11572. TARS.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723Threonine--tRNA ligase, cytoplasmicUniRule annotationPRO_0000101119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei243 – 2431N6-acetyllysine1 Publication
Modified residuei298 – 2981Phosphotyrosine By similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26639.
PaxDbiP26639.
PeptideAtlasiP26639.
PRIDEiP26639.

PTM databases

PhosphoSiteiP26639.

Expressioni

Gene expression databases

ArrayExpressiP26639.
BgeeiP26639.
CleanExiHS_TARS.
GenevestigatoriP26639.

Organism-specific databases

HPAiHPA037425.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi112760. 53 interactions.
IntActiP26639. 12 interactions.
MINTiMINT-3010570.
STRINGi9606.ENSP00000265112.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi82 – 865
Beta strandi92 – 965
Turni97 – 993
Helixi102 – 1087
Turni111 – 1133
Helixi114 – 1163
Beta strandi120 – 1278
Beta strandi129 – 1313
Beta strandi135 – 1417
Helixi323 – 3297
Beta strandi332 – 3343
Helixi347 – 36620
Beta strandi376 – 3794
Helixi380 – 3856
Helixi388 – 3914
Helixi393 – 3953
Beta strandi398 – 4014
Beta strandi404 – 4085
Helixi413 – 4219
Helixi427 – 4293
Beta strandi431 – 4366
Beta strandi439 – 4413
Helixi446 – 4483
Turni451 – 4533
Beta strandi456 – 4594
Beta strandi462 – 4676
Helixi469 – 4713
Helixi472 – 49019
Beta strandi493 – 4997
Helixi509 – 52517
Beta strandi530 – 5334
Beta strandi543 – 5497
Beta strandi555 – 56511
Helixi566 – 5705
Beta strandi587 – 5959
Helixi597 – 60711
Turni608 – 6103
Helixi614 – 6163
Beta strandi621 – 6277
Helixi628 – 6303
Helixi631 – 64212
Turni643 – 6453
Beta strandi648 – 6503
Helixi658 – 66710
Beta strandi671 – 6766
Helixi678 – 6836
Beta strandi685 – 6906
Beta strandi695 – 7006
Helixi701 – 71313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWTNMR-A79-153[»]
4HWTX-ray2.30A/B321-723[»]
ProteinModelPortaliP26639.
SMRiP26639. Positions 81-722.

Miscellaneous databases

EvolutionaryTraceiP26639.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0441.
HOGENOMiHOG000003878.
HOVERGENiHBG059513.
InParanoidiP26639.
KOiK01868.
OMAiYNSKLWQ.
OrthoDBiEOG7JDQX3.
PhylomeDBiP26639.
TreeFamiTF300858.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26639-1) [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

MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW    50
PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT 100
TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ 150
AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS 200
SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT 250
VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI 300
SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA 350
YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE 400
VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT 450
GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST 500
RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD 550
AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM 600
IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI 650
DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT 700
ISETIERLQQ LKEFRSKQAE EEF 723
Length:723
Mass (Da):83,435
Last modified:February 15, 2005 - v3
Checksum:i885745118972C5A9
GO
Isoform 2 (identifier: P26639-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-110: S → SHTASCKNLSSLASLLASVAIPSSGMPWPPLFFL

Show »
Length:756
Mass (Da):86,861
Checksum:iE3516F3A14CBC746
GO

Sequence cautioni

The sequence AAB04939.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211G → D.
Corresponds to variant rs34334786 [ dbSNP | Ensembl ].
VAR_034533

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei110 – 1101S → SHTASCKNLSSLASLLASVA IPSSGMPWPPLFFL in isoform 2. VSP_045114

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641A → G in AAB04939. 1 Publication
Sequence conflicti350 – 3501A → V in AAB04939. 1 Publication
Sequence conflicti417 – 4171C → S in AAB04939. 1 Publication
Sequence conflicti439 – 4391V → G in AAB04939. 1 Publication
Sequence conflicti453 – 4531T → I in AAH10578. 1 Publication
Sequence conflicti581 – 5811D → E in AAB04939. 1 Publication
Sequence conflicti612 – 6121W → LA in AAB04939. 1 Publication
Sequence conflicti636 – 6361K → N in AAB04939. 1 Publication
Sequence conflicti683 – 6831S → T in AAB04939. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63180 mRNA. Translation: AAB04939.1. Different initiation.
AK292346 mRNA. Translation: BAF85035.1.
AK293620 mRNA. Translation: BAG57079.1.
AC025441 Genomic DNA. No translation available.
AC034231 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10804.1.
BC000517 mRNA. Translation: AAH00517.2.
BC010578 mRNA. Translation: AAH10578.2.
CCDSiCCDS3899.1. [P26639-1]
CCDS58943.1. [P26639-2]
PIRiA38867. YSHUT.
RefSeqiNP_001245366.1. NM_001258437.1. [P26639-1]
NP_001245367.1. NM_001258438.1. [P26639-2]
NP_689508.3. NM_152295.4. [P26639-1]
UniGeneiHs.481860.

Genome annotation databases

EnsembliENST00000265112; ENSP00000265112; ENSG00000113407. [P26639-1]
ENST00000455217; ENSP00000387710; ENSG00000113407. [P26639-2]
ENST00000502553; ENSP00000424387; ENSG00000113407. [P26639-1]
GeneIDi6897.
KEGGihsa:6897.
UCSCiuc003jhy.4. human. [P26639-1]
uc011coc.3. human.

Polymorphism databases

DMDMi60267755.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63180 mRNA. Translation: AAB04939.1 . Different initiation.
AK292346 mRNA. Translation: BAF85035.1 .
AK293620 mRNA. Translation: BAG57079.1 .
AC025441 Genomic DNA. No translation available.
AC034231 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10804.1 .
BC000517 mRNA. Translation: AAH00517.2 .
BC010578 mRNA. Translation: AAH10578.2 .
CCDSi CCDS3899.1. [P26639-1 ]
CCDS58943.1. [P26639-2 ]
PIRi A38867. YSHUT.
RefSeqi NP_001245366.1. NM_001258437.1. [P26639-1 ]
NP_001245367.1. NM_001258438.1. [P26639-2 ]
NP_689508.3. NM_152295.4. [P26639-1 ]
UniGenei Hs.481860.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WWT NMR - A 79-153 [» ]
4HWT X-ray 2.30 A/B 321-723 [» ]
ProteinModelPortali P26639.
SMRi P26639. Positions 81-722.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112760. 53 interactions.
IntActi P26639. 12 interactions.
MINTi MINT-3010570.
STRINGi 9606.ENSP00000265112.

Chemistry

BindingDBi P26639.
ChEMBLi CHEMBL3391.
DrugBanki DB00156. L-Threonine.

PTM databases

PhosphoSitei P26639.

Polymorphism databases

DMDMi 60267755.

Proteomic databases

MaxQBi P26639.
PaxDbi P26639.
PeptideAtlasi P26639.
PRIDEi P26639.

Protocols and materials databases

DNASUi 6897.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265112 ; ENSP00000265112 ; ENSG00000113407 . [P26639-1 ]
ENST00000455217 ; ENSP00000387710 ; ENSG00000113407 . [P26639-2 ]
ENST00000502553 ; ENSP00000424387 ; ENSG00000113407 . [P26639-1 ]
GeneIDi 6897.
KEGGi hsa:6897.
UCSCi uc003jhy.4. human. [P26639-1 ]
uc011coc.3. human.

Organism-specific databases

CTDi 6897.
GeneCardsi GC05P033476.
H-InvDB HIX0004790.
HGNCi HGNC:11572. TARS.
HPAi HPA037425.
MIMi 187790. gene.
neXtProti NX_P26639.
PharmGKBi PA36337.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0441.
HOGENOMi HOG000003878.
HOVERGENi HBG059513.
InParanoidi P26639.
KOi K01868.
OMAi YNSKLWQ.
OrthoDBi EOG7JDQX3.
PhylomeDBi P26639.
TreeFami TF300858.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

EvolutionaryTracei P26639.
GeneWikii TARS_(gene).
GenomeRNAii 6897.
NextBioi 26959.
PROi P26639.
SOURCEi Search...

Gene expression databases

ArrayExpressi P26639.
Bgeei P26639.
CleanExi HS_TARS.
Genevestigatori P26639.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPi MF_00184. Thr_tRNA_synth.
InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view ]
Pfami PF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view ]
PRINTSi PR01047. TRNASYNTHTHR.
SMARTi SM00863. tRNA_SAD. 1 hit.
[Graphical view ]
SUPFAMi SSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsi TIGR00418. thrS. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes."
    Cruzen M.E., Arfin S.M.
    J. Biol. Chem. 266:9919-9923(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum and Testis.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Cervix and Lung.
  6. Cited for: ISGYLATION.
  7. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
    Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
    J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-222.
    Tissue: Lung adenocarcinoma.
  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-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Solution structure of the TGS domain from human threonyl-tRNA synthetase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 79-153.

Entry informationi

Entry nameiSYTC_HUMAN
AccessioniPrimary (citable) accession number: P26639
Secondary accession number(s): A8K8I1
, B4DEG8, Q96FP5, Q9BWA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 15, 2005
Last modified: September 3, 2014
This is version 159 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 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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