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P41252

- SYIC_HUMAN

UniProt

P41252 - SYIC_HUMAN

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Protein
Isoleucine--tRNA ligase, cytoplasmic
Gene
IARS
Organism
Homo sapiens (Human)
Status
Reviewed - 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).UniRule annotation

Sites

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. aminoacyl-tRNA editing activity Source: InterPro
  3. isoleucine-tRNA ligase activity Source: Reactome
  4. protein binding Source: IntAct

GO - Biological processi

  1. gene expression Source: Reactome
  2. isoleucyl-tRNA aminoacylation Source: InterPro
  3. osteoblast differentiation Source: UniProt
  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: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProt
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, cytoplasmicUniRule annotation
PRO_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

ArrayExpressiP41252.
BgeeiP41252.
CleanExiHS_IARS.
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. 65 interactions.
IntActiP41252. 8 interactions.
MINTiMINT-141153.
STRINGi9606.ENSP00000364794.

Structurei

3D structure databases

ProteinModelPortaliP41252.
SMRiP41252. Positions 1-841.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 5811"HIGH" regionUniRule annotation
Add
BLAST
Motifi600 – 6045"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246403.
HOVERGENiHBG013511.
InParanoidiP41252.
KOiK01870.
OMAiRVEHMVE.
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.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_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

MLQQVPENIN FPAEEEKILE FWTEFNCFQE CLKQSKHKPK FTFYDGPPFA     50
TGLPHYGHIL AGTIKDIVTR YAHQSGFHVD RRFGWDCHGL PVEYEIDKTL 100
GIRGPEDVAK MGITEYNNQC RAIVMRYSAE WKSTVSRLGR WIDFDNDYKT 150
LYPQFMESVW WVFKQLYDKG LVYRGVKVMP FSTACNTPLS NFESHQNYKD 200
VQDPSVFVTF PLEEDETVSL VAWTTTPWTL PSNLAVCVNP EMQYVKIKDV 250
ARGRLLILME ARLSALYKLE SDYEILERFP GAYLKGKKYR PLFDYFLKCK 300
ENGAFTVLVD NYVKEEEGTG VVHQAPYFGA EDYRVCMDFN IIRKDSLPVC 350
PVDASGCFTT EVTDFAGQYV KDADKSIIRT LKEQGRLLVA TTFTHSYPFC 400
WRSDTPLIYK AVPSWFVRVE NMVDQLLRNN DLCYWVPELV REKRFGNWLK 450
DARDWTISRN RYWGTPIPLW VSDDFEEVVC IGSVAELEEL SGAKISDLHR 500
ESVDHLTIPS RCGKGSLHRI SEVFDCWFES GSMPYAQVHY PFENKREFED 550
AFPADFIAEG IDQTRGWFYT LLVLATALFG QPPFKNVIVN GLVLASDGQK 600
MSKRKKNYPD PVSIIQKYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK 650
DVLLPWYNAY RFLIQNVLRL QKEEEIEFLY NENTVRESPN ITDRWILSFM 700
QSLIGFFETE MAAYRLYTVV PRLVKFVDIL TNWYVRMNRR RLKGENGMED 750
CVMALETLFS VLLSLCRLMA PYTPFLTELM YQNLKVLIDP VSVQDKDTLS 800
IHYLMLPRVR EELIDKKTES AVSQMQSVIE LGRVIRDRKT IPIKYPLKEI 850
VVIHQDPEAL KDIKSLEKYI IEELNVRKVT LSTDKNKYGI RLRAEPDHMV 900
LGKRLKGAFK AVMTSIKQLS SEELEQFQKT GTIVVEGHEL HDEDIRLMYT 950
FDQATGGTAQ FEAHSDAQAL VLLDVTPDQS MVDEGMAREV INRIQKLRKK 1000
CNLVPTDEIT VYYKAKSEGT YLNSVIESHT EFIFTTIKAP LKPYPVSPSD 1050
KVLIQEKTQL KGSELEITLT RGSSLPGPAC AYVNLNICAN GSEQGGVLLL 1100
ENPKGDNRLD LLKLKSVVTS IFGVKNTELA VFHDETEIQN QTDLLSLSGK 1150
TLCVTAGSAP SLINSSSTLL CQYINLQLLN AKPQECLMGT VGTLLLENPL 1200
GQNGLTHQGL LYEAAKVFGL RSRKLKLFLN ETQTQEITED IPVKTLNMKT 1250
VYVSVLPTTA DF 1262
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti658 – 6581N → S in CAD97671. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000443024; ENSP00000406448; ENSG00000196305.
GeneIDi3376.
KEGGihsa:3376.
UCSCiuc004art.2. human.

Polymorphism databases

DMDMi239938717.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6694.1.
PIRi I59314.
RefSeqi NP_002152.2. NM_002161.5.
NP_038203.2. NM_013417.3.
UniGenei Hs.445403.

3D structure databases

ProteinModelPortali P41252.
SMRi P41252. Positions 1-841.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109605. 65 interactions.
IntActi P41252. 8 interactions.
MINTi MINT-141153.
STRINGi 9606.ENSP00000364794.

Chemistry

BindingDBi P41252.
ChEMBLi CHEMBL3235.
DrugBanki DB00167. L-Isoleucine.

PTM databases

PhosphoSitei P41252.

Polymorphism databases

DMDMi 239938717.

Proteomic databases

MaxQBi P41252.
PaxDbi P41252.
PRIDEi P41252.

Protocols and materials databases

DNASUi 3376.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375643 ; ENSP00000364794 ; ENSG00000196305 .
ENST00000443024 ; ENSP00000406448 ; ENSG00000196305 .
GeneIDi 3376.
KEGGi hsa:3376.
UCSCi uc004art.2. human.

Organism-specific databases

CTDi 3376.
GeneCardsi GC09M094972.
HGNCi HGNC:5330. IARS.
HPAi HPA029806.
MIMi 600709. gene.
neXtProti NX_P41252.
PharmGKBi PA29580.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246403.
HOVERGENi HBG013511.
InParanoidi P41252.
KOi K01870.
OMAi RVEHMVE.
OrthoDBi EOG7M98FD.
PhylomeDBi P41252.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi IARS. human.
GeneWikii IARS.
GenomeRNAii 3376.
NextBioi 13356.
PMAP-CutDB P41252.
PROi P41252.
SOURCEi Search...

Gene expression databases

ArrayExpressi P41252.
Bgeei P41252.
CleanExi HS_IARS.
Genevestigatori P41252.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPi MF_02003. Ile_tRNA_synth_type2.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view ]
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view ]
PRINTSi PR00984. TRNASYNTHILE.
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsi TIGR00392. ileS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 143 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

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