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Q75ZY9

- MET_CANFA

UniProt

Q75ZY9 - MET_CANFA

Protein

Hepatocyte growth factor receptor

Gene

MET

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells By similarity.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    In its inactive state, the C-terminal tail interacts with the catalytic domain and inhibits the kinase activity. Upon ligand binding, the C-terminal tail is displaced and becomes phosphorylated, thus increasing the kinase activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei308 – 3092CleavageSequence Analysis
    Binding sitei1111 – 11111ATPPROSITE-ProRule annotation
    Active sitei1205 – 12051Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1085 – 10939ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hepatocyte growth factor-activated receptor activity Source: Ensembl

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. adult behavior Source: Ensembl
    3. brain development Source: Ensembl
    4. branching morphogenesis of an epithelial tube Source: Ensembl
    5. glucose homeostasis Source: Ensembl
    6. liver development Source: Ensembl
    7. muscle cell migration Source: Ensembl
    8. myoblast proliferation Source: Ensembl
    9. myotube differentiation Source: Ensembl
    10. negative regulation of hydrogen peroxide-mediated programmed cell death Source: Ensembl
    11. placenta development Source: Ensembl
    12. positive chemotaxis Source: UniProtKB
    13. positive regulation of endothelial cell chemotaxis Source: UniProtKB
    14. positive regulation of glucose transport Source: Ensembl
    15. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    16. protein autophosphorylation Source: Ensembl
    17. regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Source: Ensembl
    18. semaphorin-plexin signaling pathway Source: UniProtKB
    19. skeletal muscle tissue development Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hepatocyte growth factor receptor (EC:2.7.10.1)
    Short name:
    HGF receptor
    Alternative name(s):
    HGF/SF receptor
    Proto-oncogene c-Met
    Scatter factor receptor
    Short name:
    SF receptor
    Tyrosine-protein kinase Met
    Gene namesi
    Name:MET
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Membrane By similarity; Single-pass type I membrane protein By similarity

    GO - Cellular componenti

    1. basal plasma membrane Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 13821358Hepatocyte growth factor receptorPRO_0000024439Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi95 ↔ 101PROSITE-ProRule annotation
    Disulfide bondi98 ↔ 160PROSITE-ProRule annotation
    Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi133 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi173 ↔ 176PROSITE-ProRule annotation
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi299 ↔ 364PROSITE-ProRule annotation
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi386 ↔ 398PROSITE-ProRule annotation
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi521 ↔ 539PROSITE-ProRule annotation
    Disulfide bondi527 ↔ 562PROSITE-ProRule annotation
    Disulfide bondi530 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi542 ↔ 552PROSITE-ProRule annotation
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi636 – 6361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi880 – 8801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence Analysis
    Modified residuei978 – 9781PhosphothreonineBy similarity
    Modified residuei991 – 9911PhosphoserineBy similarity
    Modified residuei998 – 9981PhosphoserineBy similarity
    Modified residuei1001 – 10011PhosphoserineBy similarity
    Modified residuei1004 – 10041PhosphotyrosineBy similarity
    Modified residuei1231 – 12311PhosphotyrosineBy similarity
    Modified residuei1235 – 12351Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1236 – 12361Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1290 – 12901PhosphothreonineBy similarity
    Modified residuei1350 – 13501Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1357 – 13571Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1366 – 13661PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylated in response to ligand binding on Tyr-1235 and Tyr-1236 in the kinase domain leading to further phosphorylation of Tyr-1350 and Tyr-1357 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1350 and Tyr-1366. Dephosphorylated by PTPN1 and PTPN2 By similarity.By similarity
    Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Interactioni

    Subunit structurei

    Heterodimer made of an alpha chain (50 kDa) and a beta chain (145 kDa) which are disulfide linked. Binds PLXNB1. Interacts when phosphorylated with downstream effectors including STAT3, PIK3R1, SRC, PCLG1, GRB2 and GAB1. Interacts with SPSB1, SPSB2 and SPSB4. Interacts with INPP5D/SHIP1. When phosphorylated at Tyr-1357, interacts with INPPL1/SHIP2. Interacts with RANBP9 and RANBP10, as well as SPSB1, SPSB2, SPSB3 and SPSB4. SPSB1 binding occurs in the presence and in the absence of HGF, however HGF treatment has a positive effect on this interaction. Interacts with MUC20; prevents interaction with GRB2 and suppresses hepatocyte growth factor-induced cell proliferation. Interacts with GRB10 By similarity. Interacts with PTPN1 and PTPN2 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000005067.

    Structurei

    3D structure databases

    ProteinModelPortaliQ75ZY9.
    SMRiQ75ZY9. Positions 40-742, 1047-1347.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 935911ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini957 – 1379423CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei936 – 95621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 516490SemaPROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 65693IPT/TIG 1Add
    BLAST
    Domaini658 – 74083IPT/TIG 2Add
    BLAST
    Domaini743 – 83795IPT/TIG 3Add
    BLAST
    Domaini1079 – 1346268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1213 – 1382170Interaction with RANBP9By similarityAdd
    BLAST
    Regioni1321 – 136040Interaction with MUC20By similarityAdd
    BLAST

    Domaini

    The kinase domain is involved in SPSB1 binding.By similarity
    The beta-propeller Sema domain mediates binding to HGF.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 3 IPT/TIG domains.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 Sema domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000220900.
    HOVERGENiHBG006348.
    InParanoidiQ75ZY9.
    KOiK05099.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProiIPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR011009. Kinase-like_dom.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001627. Semap_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016244. Tyr_kinase_HGF/MSP_rcpt.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view]
    PIRSFiPIRSF000617. TyrPK_HGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00429. IPT. 4 hits.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF81296. SSF81296. 3 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q75ZY9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAPAVLAPG ILVLLFTLVQ KSYGECKEAL VKSEMNVNMK YQLPNFTAET     50
    PIQNVVLHKH HIYLGAVNYI YVLNDKDLQK VAEYKTGPVL EHPDCSPCQD 100
    CSHKANLSGG VWEDNINMAL LVDTYYDDQL ISCGSVHRGT CQRHILPPSN 150
    IADIQSEVHC MYSSQADEEP SQCPDCVVSA LGTKVLISEK DRFINFFVGN 200
    TINSSDHPDH SLHSISVRRL KETQDGFKFL TDQSYIDVLP EFRDSYPIKY 250
    VHAFESNHFI YFLTVQRETL DAQTFHTRII RFCSVDSGLH SYMEMPLECI 300
    LTEKRRKRST REEVFNILQA AYVSKPGAHL AKQIGANLND DILYGVFAQS 350
    KPDSAEPMNR SAVCAFPIKY VNEFFNKIVN KNNVRCLQHF YGPNHEHCFN 400
    RTLLRNSSGC EARNDEYRTE FTTALQRVDL FMGQFNQVLL TSISTFIKGD 450
    LTIANLGTSE GRFMQVVVSR SGLSTPHVNF RLDSHPVSPE AIVEHPLNQN 500
    GYTLVVTGKK ITRIPLNGLG CEHFQSCSQC LSAPPFVQCG WCHDRCVHLE 550
    ECPTGAWTQE VCLPAIYEVF PTSAPLEGGT VLTVCGWDFG FRRNNKFDLK 600
    KTKVFLGNES CTLTLSESTT NMLKCTVGPA VNEHFNISII ISNGRGTAQY 650
    STFSYVDPII TSISPSYGPK NGGTLLTLTG KYLNSGNSRH ISMGGKTCTL 700
    KSVSDSILEC YTPAQATATE FPIKLKIDLA NREMNSFSYQ EDPIVYAIHP 750
    TKSFISGGST ITAVGKNLNS VSVLRMVIDV HETRRNFTVA CQHRSNSEII 800
    CCTTPSLQQL NLQLPLKTKA FFMLDGIHSK YFDLIYVHNP VFKPFEKPVM 850
    ISIGNENVLE IKGNDIDPEA VKGEVLKVGN KSCETIYSDS KAVLCKVPND 900
    LLKLNNELNI EWKQAVSSTV LGKVIVQPDQ NFTGLIAGVI SISTIVLLLL 950
    GLFLWLKRKK QIKDLGSELV RYDARVHTPH LDRLVSARSV SPTTEMVSNE 1000
    SVDYRATFPE DQFPNSSQNG SCRQVQYPLT DLSPMLTSGD SDISSPLLQN 1050
    TVHIDLSALN PELVQAVQHV VIGPSSLIVH FNEVIGRGHF GCVYHGTLLD 1100
    NDDKKIHCAV KSLNRITDIG EVSQFLTEGI IMKDFSHPNV LSLLGICLRS 1150
    EGSPLVVLPY MKHGDLRNFI RNETHNPTVK DLIGFGLQVA KGMKYLASKK 1200
    FVHRDLAARN CMLDEKFTVK VADFGLARDM YDKEYYSVHN KTGAKLPVKW 1250
    MALESLQTQK FTTKSDVWSF GVLLWELMTR GAPPYPDVNT FDITVYLLQG 1300
    RRLLQPEYCP DPLYEVMLKC WHPRAELRPS FSELVSRISA IFSTFIGEHY 1350
    VHVNATYVNV KCVAPYPSLL SSQDNIDGEG DT 1382
    Length:1,382
    Mass (Da):154,637
    Last modified:July 5, 2004 - v1
    Checksum:i12BCF8E83821B2F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB118945 mRNA. Translation: BAC84966.1.
    AY543631 mRNA. Translation: AAS48569.1.
    DP000236 Genomic DNA. Translation: AAR16267.1.
    RefSeqiNP_001002963.1. NM_001002963.1.
    UniGeneiCfa.144.

    Genome annotation databases

    GeneIDi403438.
    KEGGicfa:403438.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB118945 mRNA. Translation: BAC84966.1 .
    AY543631 mRNA. Translation: AAS48569.1 .
    DP000236 Genomic DNA. Translation: AAR16267.1 .
    RefSeqi NP_001002963.1. NM_001002963.1.
    UniGenei Cfa.144.

    3D structure databases

    ProteinModelPortali Q75ZY9.
    SMRi Q75ZY9. Positions 40-742, 1047-1347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000005067.

    Chemistry

    ChEMBLi CHEMBL2046265.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403438.
    KEGGi cfa:403438.

    Organism-specific databases

    CTDi 4233.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220900.
    HOVERGENi HBG006348.
    InParanoidi Q75ZY9.
    KOi K05099.

    Miscellaneous databases

    NextBioi 20816956.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProi IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR011009. Kinase-like_dom.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001627. Semap_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016244. Tyr_kinase_HGF/MSP_rcpt.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF000617. TyrPK_HGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00429. IPT. 4 hits.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF81296. SSF81296. 3 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Morecular cloning of the canine c-Met/HGF receptor and it's expression in normal canine tissues."
      Neo S., Furuichi M., Watanabe M., Hisasue M., Tsuchiya R., Hisamatsu S., Kansaku N., Yamada T.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of the receptor tyrosine kinase Met and its autocrine loop in canine osteosarcoma cell lines."
      Liao A.T., Chien M.B., London C.A.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Comparative analyses of multi-species sequences from targeted genomic regions."
      Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G., Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C., Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S., Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R.
      , Cutler D.J., Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q., Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N., Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S., Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E., Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A., Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E., Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D., Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B., Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A., Haussler D., Green P., Miller W., Green E.D.
      Nature 424:788-793(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Involvement of hepatocyte growth factor in kidney development."
      Santos O.F., Barros E.J., Yang X.M., Matsumoto K., Nakamura T., Park M., Nigam S.K.
      Dev. Biol. 163:525-529(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN KIDNEY DEVELOPMENT.

    Entry informationi

    Entry nameiMET_CANFA
    AccessioniPrimary (citable) accession number: Q75ZY9
    Secondary accession number(s): A0M8U9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3