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Protein

Lysine--tRNA ligase

Gene

KARS

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

Functioni

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA3(Lys), the primer for reverse transcription initiation.2 Publications

Catalytic activityi

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).

Cofactori

Ca2+1 Publication

Enzyme regulationi

Up-regulated by DARS and EEF1A1, but not by AIMP2.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei277Substrate; via carbonyl oxygen1 Publication1
Binding sitei301Substrate1 Publication1
Binding sitei339Substrate1 Publication1
Binding sitei341Substrate1 Publication1
Metal bindingi487Calcium1 Publication1
Metal bindingi494Calcium1 Publication1
Binding sitei497Substrate1 Publication1
Binding sitei501Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi323 – 325ATP1 Publication3
Nucleotide bindingi331 – 332ATP1 Publication2
Nucleotide bindingi494 – 495ATP1 Publication2
Nucleotide bindingi550 – 553ATP1 Publication4

GO - Molecular functioni

  • amino acid binding Source: Ensembl
  • ATP binding Source: UniProtKB-KW
  • lysine-tRNA ligase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • diadenosine tetraphosphate biosynthetic process Source: Ensembl
  • lysyl-tRNA aminoacylation Source: UniProtKB
  • tRNA aminoacylation for protein translation Source: Reactome
  • tRNA processing Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000065427-MONOMER.
BRENDAi6.1.1.6. 2681.
ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-379726. Mitochondrial tRNA aminoacylation.
SIGNORiQ15046.

Protein family/group databases

MoonProtiQ15046.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine--tRNA ligase (EC:6.1.1.6)
Alternative name(s):
Lysyl-tRNA synthetase
Short name:
LysRS
Gene namesi
Name:KARS
Synonyms:KIAA0070
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:6215. KARS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease, recessive, intermediate type, B (CMTRIB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.
See also OMIM:613641
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064911105L → H in CMTRIB; severely affects enzyme activity. 1 PublicationCorresponds to variant rs267607194dbSNPEnsembl.1
Natural variantiVAR_064912274I → M in CMTRIB. 1 PublicationCorresponds to variant rs146955132dbSNPEnsembl.1
Deafness, autosomal recessive, 89 (DFNB89)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic deafness characterized by bilateral, prelingual, moderate to severe hearing loss affecting all frequencies.
See also OMIM:613916
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070233145Y → H in DFNB89. 1 PublicationCorresponds to variant rs397514745dbSNPEnsembl.1
Natural variantiVAR_070234349D → N in DFNB89. 1 PublicationCorresponds to variant rs397514746dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 65Missing : Loss of nuclear localization, but no effect on packaging into HIV-1. 1 PublicationAdd BLAST65

Keywords - Diseasei

Charcot-Marie-Tooth disease, Deafness, Disease mutation, Neurodegeneration, Neuropathy, Non-syndromic deafness

Organism-specific databases

DisGeNETi3735.
MalaCardsiKARS.
MIMi613641. phenotype.
613916. phenotype.
OpenTargetsiENSG00000065427.
Orphaneti254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.
90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA30016.

Chemistry databases

ChEMBLiCHEMBL5575.
DrugBankiDB00123. L-Lysine.

Polymorphism and mutation databases

BioMutaiKARS.
DMDMi20178333.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001527652 – 597Lysine--tRNA ligaseAdd BLAST596

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei88N6-acetyllysineCombined sources1
Modified residuei141N6-acetyllysineCombined sources1
Modified residuei590PhosphoserineBy similarity1
Modified residuei591PhosphothreonineBy similarity1
Modified residuei596PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15046.
MaxQBiQ15046.
PaxDbiQ15046.
PeptideAtlasiQ15046.
PRIDEiQ15046.

PTM databases

iPTMnetiQ15046.
PhosphoSitePlusiQ15046.
SwissPalmiQ15046.

Expressioni

Gene expression databases

BgeeiENSG00000065427.
CleanExiHS_KARS.
ExpressionAtlasiQ15046. baseline and differential.
GenevisibleiQ15046. HS.

Organism-specific databases

HPAiHPA041345.
HPA041550.

Interactioni

Subunit structurei

Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with AIMP2 (via N-terminus) and MITF. Interacts directly with HIV-1 virus GAG protein.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131558EBI-356367,EBI-745226
RPSAP088655EBI-356367,EBI-354112

Protein-protein interaction databases

BioGridi109938. 76 interactors.
DIPiDIP-29725N.
IntActiQ15046. 26 interactors.
MINTiMINT-1154971.
STRINGi9606.ENSP00000325448.

Chemistry databases

BindingDBiQ15046.

Structurei

Secondary structure

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi73 – 89Combined sources17
Helixi105 – 112Combined sources8
Beta strandi126 – 137Combined sources12
Beta strandi139 – 149Combined sources11
Beta strandi152 – 159Combined sources8
Helixi160 – 162Combined sources3
Helixi166 – 175Combined sources10
Beta strandi181 – 190Combined sources10
Beta strandi196 – 207Combined sources12
Turni216 – 218Combined sources3
Helixi223 – 228Combined sources6
Helixi230 – 236Combined sources7
Helixi238 – 260Combined sources23
Beta strandi270 – 274Combined sources5
Beta strandi277 – 279Combined sources3
Beta strandi284 – 287Combined sources4
Turni288 – 291Combined sources4
Beta strandi292 – 296Combined sources5
Helixi301 – 309Combined sources9
Beta strandi314 – 322Combined sources9
Beta strandi328 – 330Combined sources3
Beta strandi333 – 343Combined sources11
Helixi347 – 366Combined sources20
Beta strandi367 – 373Combined sources7
Beta strandi383 – 386Combined sources4
Beta strandi392 – 395Combined sources4
Helixi396 – 404Combined sources9
Helixi411 – 413Combined sources3
Helixi417 – 429Combined sources13
Helixi440 – 451Combined sources12
Helixi453 – 455Combined sources3
Beta strandi460 – 463Combined sources4
Helixi467 – 469Combined sources3
Beta strandi477 – 479Combined sources3
Beta strandi482 – 490Combined sources9
Beta strandi493 – 501Combined sources9
Helixi505 – 519Combined sources15
Turni520 – 522Combined sources3
Beta strandi524 – 526Combined sources3
Helixi531 – 538Combined sources8
Beta strandi543 – 550Combined sources8
Helixi551 – 558Combined sources8
Helixi564 – 567Combined sources4
Beta strandi568 – 570Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BJUX-ray2.31A/B/C/D70-582[»]
4DPGX-ray2.84A/B/C/D/E/F/G/H70-581[»]
4YCUX-ray2.10A/B70-581[»]
4YCWX-ray2.90A/B/E/F70-581[»]
ProteinModelPortaliQ15046.
SMRiQ15046.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15046.

Family & Domainsi

Domaini

The N-terminal domain (1-65) of the cytoplasmic isoform is a functional tRNA-binding domain (By similarity), is required for nuclear localization, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization and is required for interaction with HIV-1 GAG and incorporation into virions. The C-terminal domain (452-597) is not required for interaction with AIMP2.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1885. Eukaryota.
COG1190. LUCA.
GeneTreeiENSGT00550000074841.
HOGENOMiHOG000236577.
HOVERGENiHBG002562.
InParanoidiQ15046.
KOiK04567.
OMAiHHNTLDI.
OrthoDBiEOG091G03SI.
PhylomeDBiQ15046.
TreeFamiTF300365.

Family and domain databases

CDDicd00775. LysRS_core. 1 hit.
HAMAPiMF_00252. Lys_tRNA_synth_class2. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR002313. Lys-tRNA-ligase_II.
IPR018149. Lys-tRNA-synth_II_C.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PIRSFiPIRSF039101. LysRS2. 1 hit.
PRINTSiPR00982. TRNASYNTHLYS.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 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. AlignAdd to basket

Isoform Cytoplasmic (identifier: Q15046-1) [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
MAAVQAAEVK VDGSEPKLSK NELKRRLKAE KKVAEKEAKQ KELSEKQLSQ
60 70 80 90 100
ATAAATNHTT DNGVGPEEES VDPNQYYKIR SQAIHQLKVN GEDPYPHKFH
110 120 130 140 150
VDISLTDFIQ KYSHLQPGDH LTDITLKVAG RIHAKRASGG KLIFYDLRGE
160 170 180 190 200
GVKLQVMANS RNYKSEEEFI HINNKLRRGD IIGVQGNPGK TKKGELSIIP
210 220 230 240 250
YEITLLSPCL HMLPHLHFGL KDKETRYRQR YLDLILNDFV RQKFIIRSKI
260 270 280 290 300
ITYIRSFLDE LGFLEIETPM MNIIPGGAVA KPFITYHNEL DMNLYMRIAP
310 320 330 340 350
ELYHKMLVVG GIDRVYEIGR QFRNEGIDLT HNPEFTTCEF YMAYADYHDL
360 370 380 390 400
MEITEKMVSG MVKHITGSYK VTYHPDGPEG QAYDVDFTPP FRRINMVEEL
410 420 430 440 450
EKALGMKLPE TNLFETEETR KILDDICVAK AVECPPPRTT ARLLDKLVGE
460 470 480 490 500
FLEVTCINPT FICDHPQIMS PLAKWHRSKE GLTERFELFV MKKEICNAYT
510 520 530 540 550
ELNDPMRQRQ LFEEQAKAKA AGDDEAMFID ENFCTALEYG LPPTAGWGMG
560 570 580 590
IDRVAMFLTD SNNIKEVLLF PAMKPEDKKE NVATTDTLES TTVGTSV
Length:597
Mass (Da):68,048
Last modified:April 16, 2002 - v3
Checksum:iE7770953332D905D
GO
Isoform Mitochondrial (identifier: Q15046-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MAAVQAAEVKVDGSEPKLSKN → MLTQAAVRLVRGSLRKTSWAEWGHRELRLGQLAPFTAPHKDKSFSDQRS

Note: Mitochondrial precursor. Contains a mitochondrial transit peptide at positions 1-16.Curated
Show »
Length:625
Mass (Da):71,497
Checksum:i294DA1CE5A137AD6
GO

Sequence cautioni

The sequence BAA06688 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform Mitochondrial (identifier: Q15046-2)
Sequence conflicti48R → G in AAG30114 (PubMed:10952987).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064911105L → H in CMTRIB; severely affects enzyme activity. 1 PublicationCorresponds to variant rs267607194dbSNPEnsembl.1
Natural variantiVAR_070233145Y → H in DFNB89. 1 PublicationCorresponds to variant rs397514745dbSNPEnsembl.1
Natural variantiVAR_052640179G → A.Corresponds to variant rs11557665dbSNPEnsembl.1
Natural variantiVAR_064912274I → M in CMTRIB. 1 PublicationCorresponds to variant rs146955132dbSNPEnsembl.1
Natural variantiVAR_070234349D → N in DFNB89. 1 PublicationCorresponds to variant rs397514746dbSNPEnsembl.1
Natural variantiVAR_016105595T → S.3 PublicationsCorresponds to variant rs6834dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0384811 – 21MAAVQ…KLSKN → MLTQAAVRLVRGSLRKTSWA EWGHRELRLGQLAPFTAPHK DKSFSDQRS in isoform Mitochondrial. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32053 mRNA. Translation: BAA22084.1.
AF285758 mRNA. Translation: AAG30114.1.
D31890 mRNA. Translation: BAA06688.1. Different initiation.
AC025287 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95622.1.
CH471114 Genomic DNA. Translation: EAW95624.1.
BC004132 mRNA. Translation: AAH04132.1.
CCDSiCCDS10923.1. [Q15046-1]
CCDS45532.1. [Q15046-2]
RefSeqiNP_001123561.1. NM_001130089.1. [Q15046-2]
NP_005539.1. NM_005548.2. [Q15046-1]
UniGeneiHs.3100.

Genome annotation databases

EnsembliENST00000302445; ENSP00000303043; ENSG00000065427. [Q15046-1]
ENST00000319410; ENSP00000325448; ENSG00000065427. [Q15046-2]
GeneIDi3735.
KEGGihsa:3735.
UCSCiuc002feq.4. human. [Q15046-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32053 mRNA. Translation: BAA22084.1.
AF285758 mRNA. Translation: AAG30114.1.
D31890 mRNA. Translation: BAA06688.1. Different initiation.
AC025287 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95622.1.
CH471114 Genomic DNA. Translation: EAW95624.1.
BC004132 mRNA. Translation: AAH04132.1.
CCDSiCCDS10923.1. [Q15046-1]
CCDS45532.1. [Q15046-2]
RefSeqiNP_001123561.1. NM_001130089.1. [Q15046-2]
NP_005539.1. NM_005548.2. [Q15046-1]
UniGeneiHs.3100.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BJUX-ray2.31A/B/C/D70-582[»]
4DPGX-ray2.84A/B/C/D/E/F/G/H70-581[»]
4YCUX-ray2.10A/B70-581[»]
4YCWX-ray2.90A/B/E/F70-581[»]
ProteinModelPortaliQ15046.
SMRiQ15046.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109938. 76 interactors.
DIPiDIP-29725N.
IntActiQ15046. 26 interactors.
MINTiMINT-1154971.
STRINGi9606.ENSP00000325448.

Chemistry databases

BindingDBiQ15046.
ChEMBLiCHEMBL5575.
DrugBankiDB00123. L-Lysine.

Protein family/group databases

MoonProtiQ15046.

PTM databases

iPTMnetiQ15046.
PhosphoSitePlusiQ15046.
SwissPalmiQ15046.

Polymorphism and mutation databases

BioMutaiKARS.
DMDMi20178333.

Proteomic databases

EPDiQ15046.
MaxQBiQ15046.
PaxDbiQ15046.
PeptideAtlasiQ15046.
PRIDEiQ15046.

Protocols and materials databases

DNASUi3735.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302445; ENSP00000303043; ENSG00000065427. [Q15046-1]
ENST00000319410; ENSP00000325448; ENSG00000065427. [Q15046-2]
GeneIDi3735.
KEGGihsa:3735.
UCSCiuc002feq.4. human. [Q15046-1]

Organism-specific databases

CTDi3735.
DisGeNETi3735.
GeneCardsiKARS.
HGNCiHGNC:6215. KARS.
HPAiHPA041345.
HPA041550.
MalaCardsiKARS.
MIMi601421. gene.
613641. phenotype.
613916. phenotype.
neXtProtiNX_Q15046.
OpenTargetsiENSG00000065427.
Orphaneti254334. Autosomal recessive intermediate Charcot-Marie-Tooth disease type B.
90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA30016.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1885. Eukaryota.
COG1190. LUCA.
GeneTreeiENSGT00550000074841.
HOGENOMiHOG000236577.
HOVERGENiHBG002562.
InParanoidiQ15046.
KOiK04567.
OMAiHHNTLDI.
OrthoDBiEOG091G03SI.
PhylomeDBiQ15046.
TreeFamiTF300365.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000065427-MONOMER.
BRENDAi6.1.1.6. 2681.
ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-379726. Mitochondrial tRNA aminoacylation.
SIGNORiQ15046.

Miscellaneous databases

ChiTaRSiKARS. human.
EvolutionaryTraceiQ15046.
GeneWikiiKARS_(gene).
GenomeRNAii3735.
PROiQ15046.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000065427.
CleanExiHS_KARS.
ExpressionAtlasiQ15046. baseline and differential.
GenevisibleiQ15046. HS.

Family and domain databases

CDDicd00775. LysRS_core. 1 hit.
HAMAPiMF_00252. Lys_tRNA_synth_class2. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR002313. Lys-tRNA-ligase_II.
IPR018149. Lys-tRNA-synth_II_C.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PIRSFiPIRSF039101. LysRS2. 1 hit.
PRINTSiPR00982. TRNASYNTHLYS.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00499. lysS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYK_HUMAN
AccessioniPrimary (citable) accession number: Q15046
Secondary accession number(s): A8MSK1
, D3DUK4, O14946, Q96J25, Q9HB23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 16, 2002
Last modified: November 30, 2016
This is version 161 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

Miscellaneous

Shares a bidirectional promoter with TERF2IP/RAP1.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 16
    Human chromosome 16: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.