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Q9NSE4

- SYIM_HUMAN

UniProt

Q9NSE4 - SYIM_HUMAN

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Protein
Isoleucine--tRNA ligase, mitochondrial
Gene
IARS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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 sitei667 – 6671ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. aminoacyl-tRNA editing activity Source: InterPro
  3. isoleucine-tRNA ligase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. gene expression Source: Reactome
  2. isoleucyl-tRNA aminoacylation Source: InterPro
  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_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoleucine--tRNA ligase, mitochondrial (EC:6.1.1.5)
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name:
IleRS
Gene namesi
Name:IARS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29685. IARS2.

Subcellular locationi

Mitochondrion matrix By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671670.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848Mitochondrion Reviewed prediction
Add
BLAST
Chaini49 – 1012964Isoleucine--tRNA ligase, mitochondrialUniRule annotation
PRO_0000233335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysine; alternate By similarity
Modified residuei74 – 741N6-succinyllysine; alternate By similarity
Modified residuei189 – 1891N6-acetyllysine1 Publication
Modified residuei194 – 1941N6-succinyllysine By similarity
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
Modified residuei241 – 2411N6-succinyllysine; alternate By similarity
Modified residuei479 – 4791N6-succinyllysine By similarity
Modified residuei500 – 5001N6-succinyllysine By similarity
Modified residuei725 – 7251N6-acetyllysine By similarity
Modified residuei775 – 7751N6-acetyllysine; alternate1 Publication
Modified residuei775 – 7751N6-succinyllysine; alternate By similarity
Modified residuei781 – 7811N6-acetyllysine; alternate1 Publication
Modified residuei781 – 7811N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NSE4.
PaxDbiQ9NSE4.
PRIDEiQ9NSE4.

PTM databases

PhosphoSiteiQ9NSE4.

Expressioni

Gene expression databases

ArrayExpressiQ9NSE4.
BgeeiQ9NSE4.
CleanExiHS_IARS2.
GenevestigatoriQ9NSE4.

Organism-specific databases

HPAiHPA024212.
HPA024594.
HPA024596.

Interactioni

Protein-protein interaction databases

BioGridi120824. 19 interactions.
MINTiMINT-1490144.

Structurei

3D structure databases

ProteinModelPortaliQ9NSE4.
SMRiQ9NSE4. Positions 60-1009.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi116 – 12611"HIGH" region By similarity
Add
BLAST
Motifi664 – 6685"KMSKS" region By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0060.
HOVERGENiHBG059862.
InParanoidiQ9NSE4.
KOiK01870.
OMAiEYPEGHI.
PhylomeDBiQ9NSE4.
TreeFamiTF300518.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NSE4-1 [UniParc]FASTAAdd to Basket

« Hide

MRWGLRPRGP GAAALATARS LWGTPRLPCS PGWQGATKRL LVRSVSGASN     50
HQPNSNSGRY RDTVLLPQTS FPMKLLGRQQ PDTELEIQQK CGFSELYSWQ 100
RERKVKTEFC LHDGPPYANG DPHVGHALNK ILKDIANRFH MMNGSKIHFV 150
PGWDCHGLPI EIKVLSELGR EAQNLSAMEI RKKARSFAKA AIEKQKSAFI 200
RWGIMADWNN CYYTFDGKYE AKQLRTFYQM YDKGLVYRSY KPVFWSPSSR 250
TALAEAELEY NPEHVSRSIY VKFPLLKPSP KLASLIDGSS PVSILVWTTQ 300
PWTIPANEAV CYMPESKYAV VKCSKSGDLY VLAADKVASV ASTLETTFET 350
ISTLSGVDLE NGTCSHPLIP DKASPLLPAN HVTMAKGTGL VHTAPAHGME 400
DYGVASQHNL PMDCLVDEDG VFTDVAGPEL QNKAVLEEGT DVVIKMLQTA 450
KNLLKEEKLV HSYPYDWRTK KPVVIRASKQ WFINITDIKT AAKELLKKVK 500
FIPGSALNGM VEMMDRRPYW CISRQRVWGV PIPVFHHKTK DEYLINSQTT 550
EHIVKLVEQH GSDIWWTLPP EQLLPKEVLS EVGGPDALEY VPGQDILDIW 600
FDSGTSWSYV LPGPDQRADL YLEGKDQLGG WFQSSLLTSV AARKRAPYKT 650
VIVHGFTLGE KGEKMSKSLG NVIHPDVVVN GGQDQSKEPP YGADVLRWWV 700
ADSNVFTEVA IGPSVLNAAR DDISKLRNTL RFLLGNVADF NPETDSIPVN 750
DMYVIDQYML HLLQDLANKI TELYKQYDFG KVVRLLRTFY TRELSNFYFS 800
IIKDRLYCEK ENDPKRRSCQ TALVEILDVI VRSFAPILPH LAEEVFQHIP 850
YIKEPKSVFR TGWISTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 900
YKVITVIEPG LLFEIIEMLQ SEETSSTSQL NELMMASEST LLAQEPREMT 950
ADVIELKGKF LINLEGGDIR EESSYKVIVM PTTKEKCPRC WKYTAESSDT 1000
LCPRCAEVVS GK 1012
Length:1,012
Mass (Da):113,792
Last modified:May 2, 2006 - v2
Checksum:i7AAAC0C9DAD7A8C7
GO

Sequence cautioni

The sequence BAA91544.1 differs from that shown. Reason: Frameshift at position 879.
The sequence BAB14164.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141A → V.
Corresponds to variant rs2577154 [ dbSNP | Ensembl ].
VAR_059862
Natural varianti522 – 5221I → V.
Corresponds to variant rs11800305 [ dbSNP | Ensembl ].
VAR_034526

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti647 – 6471P → L in BAB14164. 1 Publication
Sequence conflicti907 – 9071I → T in BAB14164. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY267462 mRNA. Translation: AAP94033.1.
AC103590 Genomic DNA. No translation available.
D28500 mRNA. Translation: BAA95147.1.
CH471100 Genomic DNA. Translation: EAW93305.1.
BC010218 mRNA. Translation: AAH10218.2.
BC040376 mRNA. Translation: AAH40376.2.
BC047880 mRNA. Translation: AAH47880.3.
BC137438 mRNA. Translation: AAI37439.1.
AK001188 mRNA. Translation: BAA91544.1. Frameshift.
AK022665 mRNA. Translation: BAB14164.1. Different initiation.
CCDSiCCDS1523.1.
RefSeqiNP_060530.3. NM_018060.3.
UniGeneiHs.262823.

Genome annotation databases

EnsembliENST00000302637; ENSP00000303279; ENSG00000067704.
GeneIDi55699.
KEGGihsa:55699.
UCSCiuc001hmc.3. human.

Polymorphism databases

DMDMi94730583.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY267462 mRNA. Translation: AAP94033.1 .
AC103590 Genomic DNA. No translation available.
D28500 mRNA. Translation: BAA95147.1 .
CH471100 Genomic DNA. Translation: EAW93305.1 .
BC010218 mRNA. Translation: AAH10218.2 .
BC040376 mRNA. Translation: AAH40376.2 .
BC047880 mRNA. Translation: AAH47880.3 .
BC137438 mRNA. Translation: AAI37439.1 .
AK001188 mRNA. Translation: BAA91544.1 . Frameshift.
AK022665 mRNA. Translation: BAB14164.1 . Different initiation.
CCDSi CCDS1523.1.
RefSeqi NP_060530.3. NM_018060.3.
UniGenei Hs.262823.

3D structure databases

ProteinModelPortali Q9NSE4.
SMRi Q9NSE4. Positions 60-1009.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120824. 19 interactions.
MINTi MINT-1490144.

Chemistry

DrugBanki DB00167. L-Isoleucine.

PTM databases

PhosphoSitei Q9NSE4.

Polymorphism databases

DMDMi 94730583.

Proteomic databases

MaxQBi Q9NSE4.
PaxDbi Q9NSE4.
PRIDEi Q9NSE4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302637 ; ENSP00000303279 ; ENSG00000067704 .
GeneIDi 55699.
KEGGi hsa:55699.
UCSCi uc001hmc.3. human.

Organism-specific databases

CTDi 55699.
GeneCardsi GC01P220267.
HGNCi HGNC:29685. IARS2.
HPAi HPA024212.
HPA024594.
HPA024596.
MIMi 612801. gene.
neXtProti NX_Q9NSE4.
PharmGKBi PA142671670.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0060.
HOVERGENi HBG059862.
InParanoidi Q9NSE4.
KOi K01870.
OMAi EYPEGHI.
PhylomeDBi Q9NSE4.
TreeFami TF300518.

Enzyme and pathway databases

Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

GenomeRNAii 55699.
NextBioi 60534.
PROi Q9NSE4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NSE4.
Bgeei Q9NSE4.
CleanExi HS_IARS2.
Genevestigatori Q9NSE4.

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_02002. Ile_tRNA_synth_type1.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view ]
PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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. "Cloning and characterization of human mitochondrial isoleucine tRNA synthetase gene."
    Shan Y.X., Guo Z.K., Huang C.Q., Ye G.M., Tang W.W., Yu L.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Structure and evolution of two human isoleucyl-tRNA synthetases."
    Shiba K., Suzuki N., Shigesada K., Schimmel P., Noda T.
    Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-1012.
    Tissue: Brain.
  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: Brain, Liver, Placenta and Skin.
  6. "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] OF 142-1012.
  7. "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-189; LYS-233; LYS-241; LYS-775 AND LYS-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYIM_HUMAN
AccessioniPrimary (citable) accession number: Q9NSE4
Secondary accession number(s): B2RPG8
, Q1M2P9, Q6PI85, Q7L439, Q86WU9, Q96D91, Q9H9Q8, Q9NW42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: September 3, 2014
This is version 108 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, Reference proteome

Documents

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