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Protein

Isoleucine--tRNA ligase, cytoplasmic

Gene

IARS

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

Functioni

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei603 – 6031ATPBy similarity

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. isoleucine-tRNA ligase activity Source: GO_Central

GO - Biological processi

  1. gene expression Source: Reactome
  2. isoleucyl-tRNA aminoacylation Source: GO_Central
  3. osteoblast differentiation 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:
Isoleucine--tRNA ligase, cytoplasmic (EC:6.1.1.5)
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name:
IRS
Short name:
IleRS
Gene namesi
Name:IARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:5330. IARS.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: GO_Central
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29580.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12621262Isoleucine--tRNA ligase, cytoplasmicPRO_0000098597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei1047 – 10471Phosphoserine3 Publications
Modified residuei1049 – 10491Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41252.
PaxDbiP41252.
PRIDEiP41252.

PTM databases

PhosphoSiteiP41252.

Miscellaneous databases

PMAP-CutDBP41252.

Expressioni

Gene expression databases

BgeeiP41252.
CleanExiHS_IARS.
ExpressionAtlasiP41252. baseline and differential.
GenevestigatoriP41252.

Organism-specific databases

HPAiHPA029806.

Interactioni

Subunit structurei

Part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro.

Binary interactionsi

WithEntry#Exp.IntActNotes
EPRSP078145EBI-355303,EBI-355315

Protein-protein interaction databases

BioGridi109605. 75 interactions.
IntActiP41252. 9 interactions.
MINTiMINT-141153.
STRINGi9606.ENSP00000364794.

Structurei

3D structure databases

ProteinModelPortaliP41252.
SMRiP41252. Positions 1-841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 5811"HIGH" regionAdd
BLAST
Motifi600 – 6045"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0060.
GeneTreeiENSGT00550000074921.
HOGENOMiHOG000246403.
HOVERGENiHBG013511.
InParanoidiP41252.
KOiK01870.
OMAiIPLPIWR.
OrthoDBiEOG7M98FD.
PhylomeDBiP41252.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQQVPENIN FPAEEEKILE FWTEFNCFQE CLKQSKHKPK FTFYDGPPFA
60 70 80 90 100
TGLPHYGHIL AGTIKDIVTR YAHQSGFHVD RRFGWDCHGL PVEYEIDKTL
110 120 130 140 150
GIRGPEDVAK MGITEYNNQC RAIVMRYSAE WKSTVSRLGR WIDFDNDYKT
160 170 180 190 200
LYPQFMESVW WVFKQLYDKG LVYRGVKVMP FSTACNTPLS NFESHQNYKD
210 220 230 240 250
VQDPSVFVTF PLEEDETVSL VAWTTTPWTL PSNLAVCVNP EMQYVKIKDV
260 270 280 290 300
ARGRLLILME ARLSALYKLE SDYEILERFP GAYLKGKKYR PLFDYFLKCK
310 320 330 340 350
ENGAFTVLVD NYVKEEEGTG VVHQAPYFGA EDYRVCMDFN IIRKDSLPVC
360 370 380 390 400
PVDASGCFTT EVTDFAGQYV KDADKSIIRT LKEQGRLLVA TTFTHSYPFC
410 420 430 440 450
WRSDTPLIYK AVPSWFVRVE NMVDQLLRNN DLCYWVPELV REKRFGNWLK
460 470 480 490 500
DARDWTISRN RYWGTPIPLW VSDDFEEVVC IGSVAELEEL SGAKISDLHR
510 520 530 540 550
ESVDHLTIPS RCGKGSLHRI SEVFDCWFES GSMPYAQVHY PFENKREFED
560 570 580 590 600
AFPADFIAEG IDQTRGWFYT LLVLATALFG QPPFKNVIVN GLVLASDGQK
610 620 630 640 650
MSKRKKNYPD PVSIIQKYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK
660 670 680 690 700
DVLLPWYNAY RFLIQNVLRL QKEEEIEFLY NENTVRESPN ITDRWILSFM
710 720 730 740 750
QSLIGFFETE MAAYRLYTVV PRLVKFVDIL TNWYVRMNRR RLKGENGMED
760 770 780 790 800
CVMALETLFS VLLSLCRLMA PYTPFLTELM YQNLKVLIDP VSVQDKDTLS
810 820 830 840 850
IHYLMLPRVR EELIDKKTES AVSQMQSVIE LGRVIRDRKT IPIKYPLKEI
860 870 880 890 900
VVIHQDPEAL KDIKSLEKYI IEELNVRKVT LSTDKNKYGI RLRAEPDHMV
910 920 930 940 950
LGKRLKGAFK AVMTSIKQLS SEELEQFQKT GTIVVEGHEL HDEDIRLMYT
960 970 980 990 1000
FDQATGGTAQ FEAHSDAQAL VLLDVTPDQS MVDEGMAREV INRIQKLRKK
1010 1020 1030 1040 1050
CNLVPTDEIT VYYKAKSEGT YLNSVIESHT EFIFTTIKAP LKPYPVSPSD
1060 1070 1080 1090 1100
KVLIQEKTQL KGSELEITLT RGSSLPGPAC AYVNLNICAN GSEQGGVLLL
1110 1120 1130 1140 1150
ENPKGDNRLD LLKLKSVVTS IFGVKNTELA VFHDETEIQN QTDLLSLSGK
1160 1170 1180 1190 1200
TLCVTAGSAP SLINSSSTLL CQYINLQLLN AKPQECLMGT VGTLLLENPL
1210 1220 1230 1240 1250
GQNGLTHQGL LYEAAKVFGL RSRKLKLFLN ETQTQEITED IPVKTLNMKT
1260
VYVSVLPTTA DF
Length:1,262
Mass (Da):144,498
Last modified:June 16, 2009 - v2
Checksum:i73CB3967A6868005
GO

Sequence cautioni

The sequence BAA05835.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti658 – 6581N → S in CAD97671 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021N → Y.1 Publication
VAR_071387
Natural varianti684 – 6841T → M.
Corresponds to variant rs2070053 [ dbSNP | Ensembl ].
VAR_058300
Natural varianti769 – 7691M → I.1 Publication
Corresponds to variant rs1136054 [ dbSNP | Ensembl ].
VAR_057951
Natural varianti1182 – 11821K → E.1 Publication
Corresponds to variant rs556155 [ dbSNP | Ensembl ].
VAR_057952
Natural varianti1188 – 11881M → T.1 Publication
VAR_071388

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28473 mRNA. Translation: BAA05835.1. Different initiation.
U04953 mRNA. Translation: AAA80153.1.
AK293014 mRNA. Translation: BAF85703.1.
BX537429 mRNA. Translation: CAD97671.1.
AL136097 Genomic DNA. Translation: CAI16202.2.
CH471089 Genomic DNA. Translation: EAW62813.1.
CCDSiCCDS6694.1.
PIRiI59314.
RefSeqiNP_002152.2. NM_002161.5.
NP_038203.2. NM_013417.3.
UniGeneiHs.445403.

Genome annotation databases

EnsembliENST00000375643; ENSP00000364794; ENSG00000196305.
GeneIDi3376.
KEGGihsa:3376.
UCSCiuc004art.2. human.

Polymorphism databases

DMDMi239938717.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28473 mRNA. Translation: BAA05835.1. Different initiation.
U04953 mRNA. Translation: AAA80153.1.
AK293014 mRNA. Translation: BAF85703.1.
BX537429 mRNA. Translation: CAD97671.1.
AL136097 Genomic DNA. Translation: CAI16202.2.
CH471089 Genomic DNA. Translation: EAW62813.1.
CCDSiCCDS6694.1.
PIRiI59314.
RefSeqiNP_002152.2. NM_002161.5.
NP_038203.2. NM_013417.3.
UniGeneiHs.445403.

3D structure databases

ProteinModelPortaliP41252.
SMRiP41252. Positions 1-841.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109605. 75 interactions.
IntActiP41252. 9 interactions.
MINTiMINT-141153.
STRINGi9606.ENSP00000364794.

Chemistry

BindingDBiP41252.
ChEMBLiCHEMBL3235.
DrugBankiDB00167. L-Isoleucine.

PTM databases

PhosphoSiteiP41252.

Polymorphism databases

DMDMi239938717.

Proteomic databases

MaxQBiP41252.
PaxDbiP41252.
PRIDEiP41252.

Protocols and materials databases

DNASUi3376.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375643; ENSP00000364794; ENSG00000196305.
GeneIDi3376.
KEGGihsa:3376.
UCSCiuc004art.2. human.

Organism-specific databases

CTDi3376.
GeneCardsiGC09M094972.
HGNCiHGNC:5330. IARS.
HPAiHPA029806.
MIMi600709. gene.
neXtProtiNX_P41252.
PharmGKBiPA29580.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0060.
GeneTreeiENSGT00550000074921.
HOGENOMiHOG000246403.
HOVERGENiHBG013511.
InParanoidiP41252.
KOiK01870.
OMAiIPLPIWR.
OrthoDBiEOG7M98FD.
PhylomeDBiP41252.

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiIARS. human.
GeneWikiiIARS.
GenomeRNAii3376.
NextBioi13356.
PMAP-CutDBP41252.
PROiP41252.
SOURCEiSearch...

Gene expression databases

BgeeiP41252.
CleanExiHS_IARS.
ExpressionAtlasiP41252. baseline and differential.
GenevestigatoriP41252.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit."
    Shiba K., Suzuki N., Shigesada K., Schimmel P., Noda T.
    Proc. Natl. Acad. Sci. U.S.A. 91:7435-7439(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension."
    Nichols R.C., Raben N., Boerkoel C.F., Plotz P.H.
    Gene 155:299-304(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, VARIANT ILE-769.
    Tissue: Liver.
  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].
    Tissue: Trachea.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-1182.
    Tissue: Colon endothelium.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1047 AND SER-1049, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANTS TYR-302 AND THR-1188.

Entry informationi

Entry nameiSYIC_HUMAN
AccessioniPrimary (citable) accession number: P41252
Secondary accession number(s): A8KAE9
, Q5TCD0, Q7Z3T4, Q9H588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: March 4, 2015
This is version 148 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 9
    Human chromosome 9: 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

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 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.