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P54136

- SYRC_HUMAN

UniProt

P54136 - SYRC_HUMAN

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Protein
Arginine--tRNA ligase, cytoplasmic
Gene
RARS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.1 Publication

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).UniRule annotation

Kineticsi

  1. KM=3.9 µM for arginine (ATP-PPi exchange at 37 degrees Celsius)1 Publication
  2. KM=3.5 µM for arginine (arginylation at 37 degrees Celsius)
  3. KM=1183 µM for ATP (ATP-PPi exchange at 37 Celsius)
  4. KM=910 µM for ATP (arginylation at 37 Celsius)
  5. KM=0.05 µM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius)
  6. KM=0.41 µM for calf liver tRNA-Arg (arginylation at 37 Celsius)

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. arginine binding Source: Ensembl
  3. arginine-tRNA ligase activity Source: Reactome
  4. protein binding Source: IntAct
  5. tRNA binding Source: Ensembl

GO - Biological processi

  1. arginyl-tRNA aminoacylation Source: ProtInc
  2. gene expression Source: Reactome
  3. 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:
Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Name:RARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9870. RARS.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrion Source: Ensembl
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34231.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicUniRule annotation
PRO_0000035797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP54136.
PaxDbiP54136.
PeptideAtlasiP54136.
PRIDEiP54136.

PTM databases

PhosphoSiteiP54136.

Expressioni

Gene expression databases

ArrayExpressiP54136.
BgeeiP54136.
CleanExiHS_RARS.
GenevestigatoriP54136.

Organism-specific databases

HPAiHPA003979.
HPA004130.

Interactioni

Subunit structurei

Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LARSQ9P2J53EBI-355482,EBI-356077

Protein-protein interaction databases

BioGridi111852. 37 interactions.
IntActiP54136. 8 interactions.
MINTiMINT-5006018.
STRINGi9606.ENSP00000231572.

Structurei

3D structure databases

ProteinModelPortaliP54136.
SMRiP54136. Positions 74-659.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7272Could be involved in the assembly of the multisynthetase complexUniRule annotation
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 21212"HIGH" regionUniRule annotation
Add
BLAST

Domaini

The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0018.
HOGENOMiHOG000247212.
HOVERGENiHBG029238.
InParanoidiP54136.
KOiK01887.
OMAiIRNTIND.
OrthoDBiEOG764725.
PhylomeDBiP54136.
TreeFamiTF106111.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Complexed (identifier: P54136-1) [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

MDVLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK    50
LKYRLNILRK SLQAERNKPT KNMINIISRL QEVFGHAIKA AYPDLENPPL 100
LVTPSQQAKF GDYQCNSAMG ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC 150
IEKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPALGE NKKVIVDFSS 200
PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD WGTQFGMLIA 250
HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK 300
NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD RMNDIVKEFE 350
DRGFVQVDDG RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK 400
ADMIIYVVDN GQSVHFQTIF AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK 450
KFKTRSGETV RLMDLLGEGL KRSMDKLKEK ERDKVLTAEE LNAAQTSVAY 500
GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI 550
DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 600
IYELATAFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD 650
ILGIKPVQRM 660
Length:660
Mass (Da):75,379
Last modified:April 16, 2002 - v2
Checksum:iFE9FB5C910709956
GO
Isoform Monomeric (identifier: P54136-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:588
Mass (Da):67,140
Checksum:i857EA1F69F3B6A3B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31V → I.
Corresponds to variant rs244903 [ dbSNP | Ensembl ].
VAR_020106
Natural varianti135 – 1351R → G.
Corresponds to variant rs1059443 [ dbSNP | Ensembl ].
VAR_052635
Natural varianti397 – 3971F → Y.
Corresponds to variant rs2305734 [ dbSNP | Ensembl ].
VAR_020107

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform Monomeric.
VSP_018905Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391P → S in AAB35627. 1 Publication
Sequence conflicti130 – 1312QK → PE in AAB35627. 1 Publication
Sequence conflicti135 – 1373REI → GEF in AAB35627. 1 Publication
Sequence conflicti147 – 15610DNECIEKVEI → AMDVLKRVEF in AAB35627. 1 Publication
Sequence conflicti164 – 1641V → G in AAB35627. 1 Publication
Sequence conflicti278 – 2781K → N in BAG37326. 1 Publication
Sequence conflicti308 – 3125WKLIC → YLLMS in AAB35627. 1 Publication
Sequence conflicti341 – 3411R → G in BAD96517. 1 Publication
Sequence conflicti358 – 3581D → G in BAG37326. 1 Publication
Sequence conflicti487 – 4871T → A in BAD96517. 1 Publication
Sequence conflicti567 – 5671D → V in AAB35627. 1 Publication
Sequence conflicti635 – 6406MLLCEA → ILCET in AAB35627. 1 Publication
Sequence conflicti651 – 6511I → T in AAB35627. 1 Publication
Sequence conflicti657 – 6604VQRM → GPRV in AAB35627. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S80343 mRNA. Translation: AAB35627.1.
BT007394 mRNA. Translation: AAP36058.1.
AK314795 mRNA. Translation: BAG37326.1.
AK222797 mRNA. Translation: BAD96517.1.
BC000528 mRNA. Translation: AAH00528.1.
BC014619 mRNA. Translation: AAH14619.1.
CCDSiCCDS4367.1. [P54136-1]
PIRiJC4365.
RefSeqiNP_002878.2. NM_002887.3. [P54136-1]
UniGeneiHs.654907.

Genome annotation databases

EnsembliENST00000231572; ENSP00000231572; ENSG00000113643. [P54136-1]
GeneIDi5917.
KEGGihsa:5917.
UCSCiuc003lzx.3. human. [P54136-1]

Polymorphism databases

DMDMi20178331.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S80343 mRNA. Translation: AAB35627.1 .
BT007394 mRNA. Translation: AAP36058.1 .
AK314795 mRNA. Translation: BAG37326.1 .
AK222797 mRNA. Translation: BAD96517.1 .
BC000528 mRNA. Translation: AAH00528.1 .
BC014619 mRNA. Translation: AAH14619.1 .
CCDSi CCDS4367.1. [P54136-1 ]
PIRi JC4365.
RefSeqi NP_002878.2. NM_002887.3. [P54136-1 ]
UniGenei Hs.654907.

3D structure databases

ProteinModelPortali P54136.
SMRi P54136. Positions 74-659.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111852. 37 interactions.
IntActi P54136. 8 interactions.
MINTi MINT-5006018.
STRINGi 9606.ENSP00000231572.

Chemistry

BindingDBi P54136.
ChEMBLi CHEMBL2824.

PTM databases

PhosphoSitei P54136.

Polymorphism databases

DMDMi 20178331.

Proteomic databases

MaxQBi P54136.
PaxDbi P54136.
PeptideAtlasi P54136.
PRIDEi P54136.

Protocols and materials databases

DNASUi 5917.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000231572 ; ENSP00000231572 ; ENSG00000113643 . [P54136-1 ]
GeneIDi 5917.
KEGGi hsa:5917.
UCSCi uc003lzx.3. human. [P54136-1 ]

Organism-specific databases

CTDi 5917.
GeneCardsi GC05P167846.
HGNCi HGNC:9870. RARS.
HPAi HPA003979.
HPA004130.
MIMi 107820. gene.
neXtProti NX_P54136.
PharmGKBi PA34231.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0018.
HOGENOMi HOG000247212.
HOVERGENi HBG029238.
InParanoidi P54136.
KOi K01887.
OMAi IRNTIND.
OrthoDBi EOG764725.
PhylomeDBi P54136.
TreeFami TF106111.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

GeneWikii RARS_(gene).
GenomeRNAii 5917.
NextBioi 23038.
PROi P54136.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54136.
Bgeei P54136.
CleanExi HS_RARS.
Genevestigatori P54136.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPi MF_00123. Arg_tRNA_synth.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view ]
PANTHERi PTHR11956. PTHR11956. 1 hit.
Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view ]
PRINTSi PR01038. TRNASYNTHARG.
SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view ]
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsi TIGR00456. argS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase."
    Girjes A.A., Hobson K., Chen P., Lavin M.F.
    Gene 164:347-350(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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].
  4. 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].
    Tissue: Liver.
  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].
    Tissue: Muscle.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Tissue: Platelet.
  7. "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase."
    Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K.
    J. Biol. Chem. 274:16673-16676(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AIMP1.
  8. "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex."
    Ling C., Yao Y.N., Zheng Y.G., Wei H., Wang L., Wu X.F., Wang E.D.
    J. Biol. Chem. 280:34755-34763(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INTERACTION WITH LARS2.
  9. "Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA."
    Zheng Y.-G., Wei H., Ling C., Xu M.-G., Wang E.-D.
    Biochemistry 45:1338-1344(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION.
  10. "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines."
    Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., Uberti E.C.
    J. Cell. Physiol. 212:293-297(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AIMP1.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYRC_HUMAN
AccessioniPrimary (citable) accession number: P54136
Secondary accession number(s): B2RBS9, Q53GY4, Q9BWA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 16, 2002
Last modified: September 3, 2014
This is version 145 of the entry and version 2 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, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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