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Q9H324

- ATS10_HUMAN

UniProt

Q9H324 - ATS10_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 10

Gene

ADAMTS10

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

Functioni

Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi392 – 3921Zinc; catalyticBy similarity
Active sitei393 – 3931PROSITE-ProRule annotation
Metal bindingi396 – 3961Zinc; catalyticBy similarity
Metal bindingi402 – 4021Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.235.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 10 (EC:3.4.24.-)
Short name:
ADAM-TS 10
Short name:
ADAM-TS10
Short name:
ADAMTS-10
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:13201. ADAMTS10.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

  1. extracellular matrix Source: UniProtKB
  2. microfibril Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Weill-Marchesani syndrome 1 (WMS1) [MIM:277600]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251A → T in WMS1; shows consistent and significantly diminished protein secretion. 1 Publication
VAR_054439

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi277600. phenotype.
Orphaneti3449. Weill-Marchesani syndrome.
PharmGKBiPA24537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 233208By similarityPRO_0000029184Add
BLAST
Chaini234 – 1103870A disintegrin and metalloproteinase with thrombospondin motifs 10PRO_0000029185Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi315 ↔ 376By similarity
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi351 ↔ 358By similarity
Disulfide bondi370 ↔ 452By similarity
Disulfide bondi409 ↔ 436By similarity
Disulfide bondi479 ↔ 501By similarity
Disulfide bondi490 ↔ 508By similarity
Disulfide bondi496 ↔ 531By similarity
Disulfide bondi521 ↔ 536By similarity
Disulfide bondi559 ↔ 596By similarity
Disulfide bondi563 ↔ 601By similarity
Disulfide bondi574 ↔ 586By similarity
Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi892 – 8921N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9H324.
PRIDEiQ9H324.

PTM databases

PhosphoSiteiQ9H324.

Expressioni

Tissue specificityi

Widely expressed in adult tissues.1 Publication

Gene expression databases

BgeeiQ9H324.
CleanExiHS_ADAMTS10.
ExpressionAtlasiQ9H324. baseline and differential.
GenevestigatoriQ9H324.

Organism-specific databases

HPAiHPA040223.

Interactioni

Subunit structurei

Interacts with FBN1; this interaction promotes microfibrils assembly.1 Publication

Protein-protein interaction databases

BioGridi123586. 7 interactions.
IntActiQ9H324. 7 interactions.
MINTiMINT-8247349.
STRINGi9606.ENSP00000270328.

Structurei

3D structure databases

ProteinModelPortaliQ9H324.
SMRiQ9H324. Positions 236-805.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini239 – 457219Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini460 – 54687DisintegrinAdd
BLAST
Domaini547 – 60256TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini825 – 88359TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini884 – 94562TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini947 – 100155TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1003 – 105856TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1065 – 110339PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni706 – 828123SpacerAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 614Poly-Pro
Compositional biasi568 – 5714Poly-Ser
Compositional biasi604 – 705102Cys-richAdd
BLAST

Domaini

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.By similarity

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG288089.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiQ9H324.
KOiK08625.
OMAiLENYEIA.
OrthoDBiEOG78WKQV.
PhylomeDBiQ9H324.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H324-1) [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

        10         20         30         40         50
MAPACQILRW ALALGLGLMF EVTHAFRSQD EFLSSLESYE IAFPTRVDHN
60 70 80 90 100
GALLAFSPPP PRRQRRGTGA TAESRLFYKV ASPSTHFLLN LTRSSRLLAG
110 120 130 140 150
HVSVEYWTRE GLAWQRAARP HCLYAGHLQG QASTSHVAIS TCGGLHGLIV
160 170 180 190 200
ADEEEYLIEP LHGGPKGSRS PEESGPHVVY KRSSLRHPHL DTACGVRDEK
210 220 230 240 250
PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY VETLVVADKM
260 270 280 290 300
MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GSTVNILVTR LILLTEDQPT
310 320 330 340 350
LEITHHAGKS LDSFCKWQKS IVNHSGHGNA IPENGVANHD TAVLITRYDI
360 370 380 390 400
CIYKNKPCGT LGLAPVGGMC ERERSCSVNE DIGLATAFTI AHEIGHTFGM
410 420 430 440 450
NHDGVGNSCG ARGQDPAKLM AAHITMKTNP FVWSSCSRDY ITSFLDSGLG
460 470 480 490 500
LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR FQHGVKSRQC KYGEVCSELW
510 520 530 540 550
CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG SRPEGVDGAW
560 570 580 590 600
GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD
610 620 630 640 650
CPPGSQDFRE VQCSEFDSIP FRGKFYKWKT YRGGGVKACS LTCLAEGFNF
660 670 680 690 700
YTERAAAVVD GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG
710 720 730 740 750
DGSACETIEG VFSPASPGAG YEDVVWIPKG SVHIFIQDLN LSLSHLALKG
760 770 780 790 800
DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ GPDQVQSLEA LGPINASLIV
810 820 830 840 850
MVLARTELPA LRYRFNAPIA RDSLPPYSWH YAPWTKCSAQ CAGGSQVQAV
860 870 880 890 900
ECRNQLDSSA VAPHYCSAHS KLPKRQRACN TEPCPPDWVV GNWSLCSRSC
910 920 930 940 950
DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACH GPTCPPEWAA
960 970 980 990 1000
LDWSECTPSC GPGLRHRVVL CKSADHRATL PPAHCSPAAK PPATMRCNLR
1010 1020 1030 1040 1050
RCPPARWVAG EWGECSAQCG VGQRQRSVRC TSHTGQASHE CTEALRPPTT
1060 1070 1080 1090 1100
QQCEAKCDSP TPGDGPEECK DVNKVAYCPL VLKFQFCSRA YFRQMCCKTC

HGH
Length:1,103
Mass (Da):120,874
Last modified:June 12, 2007 - v2
Checksum:iD7558271C303A87C
GO
Isoform 2 (identifier: Q9H324-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-637: MAPACQILRW...WKTYRGGGVK → MGPTSVLRAG...NSTSGKRTGE

Note: No experimental confirmation available. Gene prediction based on partial mRNA and EST data.

Show »
Length:590
Mass (Da):62,530
Checksum:i346AE6537FB016C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3862AT → PQ in AAG35563. (PubMed:15355968)Curated
Sequence conflicti437 – 4371S → N in AAG35563. (PubMed:15355968)Curated
Sequence conflicti643 – 6431C → S in AAG35563. (PubMed:15355968)Curated
Sequence conflicti1101 – 11011H → Q in AAG35563. (PubMed:15355968)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251A → T in WMS1; shows consistent and significantly diminished protein secretion. 1 Publication
VAR_054439
Natural varianti119 – 1191R → Q.
Corresponds to variant rs3814291 [ dbSNP | Ensembl ].
VAR_054440
Natural varianti134 – 1341T → S.1 Publication
Corresponds to variant rs7255721 [ dbSNP | Ensembl ].
VAR_054441

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 637637MAPAC…GGGVK → MGPTSVLRAGLTPSCLPPPS GATNGSVSPLGRAQRVWTEP GGRGLHGATAAGPVAAACPL LAVTATAPGQPSGASTVWVR EGGTAPATRMTVPLAPRTSE KCSVLNLTASLSVGNSTSGK RTGE in isoform 2. CuratedVSP_054707Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC092315 Genomic DNA. No translation available.
AC130469 Genomic DNA. No translation available.
AF163762 mRNA. Translation: AAG35563.1.
CCDSiCCDS12206.1. [Q9H324-1]
CCDS62529.1. [Q9H324-2]
RefSeqiNP_001269281.1. NM_001282352.1. [Q9H324-2]
NP_112219.3. NM_030957.3.
UniGeneiHs.657508.

Genome annotation databases

EnsembliENST00000595838; ENSP00000470501; ENSG00000142303. [Q9H324-2]
GeneIDi81794.
KEGGihsa:81794.
UCSCiuc002mkj.1. human. [Q9H324-1]

Polymorphism databases

DMDMi148887344.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC092315 Genomic DNA. No translation available.
AC130469 Genomic DNA. No translation available.
AF163762 mRNA. Translation: AAG35563.1 .
CCDSi CCDS12206.1. [Q9H324-1 ]
CCDS62529.1. [Q9H324-2 ]
RefSeqi NP_001269281.1. NM_001282352.1. [Q9H324-2 ]
NP_112219.3. NM_030957.3.
UniGenei Hs.657508.

3D structure databases

ProteinModelPortali Q9H324.
SMRi Q9H324. Positions 236-805.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123586. 7 interactions.
IntActi Q9H324. 7 interactions.
MINTi MINT-8247349.
STRINGi 9606.ENSP00000270328.

Protein family/group databases

MEROPSi M12.235.

PTM databases

PhosphoSitei Q9H324.

Polymorphism databases

DMDMi 148887344.

Proteomic databases

PaxDbi Q9H324.
PRIDEi Q9H324.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000595838 ; ENSP00000470501 ; ENSG00000142303 . [Q9H324-2 ]
GeneIDi 81794.
KEGGi hsa:81794.
UCSCi uc002mkj.1. human. [Q9H324-1 ]

Organism-specific databases

CTDi 81794.
GeneCardsi GC19M008645.
GeneReviewsi ADAMTS10.
HGNCi HGNC:13201. ADAMTS10.
HPAi HPA040223.
MIMi 277600. phenotype.
608990. gene.
neXtProti NX_Q9H324.
Orphaneti 3449. Weill-Marchesani syndrome.
PharmGKBi PA24537.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG288089.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004800.
HOVERGENi HBG004315.
InParanoidi Q9H324.
KOi K08625.
OMAi LENYEIA.
OrthoDBi EOG78WKQV.
PhylomeDBi Q9H324.
TreeFami TF313537.

Enzyme and pathway databases

Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GeneWikii ADAMTS10.
GenomeRNAii 81794.
NextBioi 72110.
PROi Q9H324.
SOURCEi Search...

Gene expression databases

Bgeei Q9H324.
CleanExi HS_ADAMTS10.
ExpressionAtlasi Q9H324. baseline and differential.
Genevestigatori Q9H324.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 5 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 5 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation."
    Somerville R.P.T., Jungers K.A., Apte S.S.
    J. Biol. Chem. 279:51208-51217(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-1103 (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-134.
  3. Cited for: INVOLVEMENT IN WMS1.
  4. "ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts."
    Kutz W.E., Wang L.W., Bader H.L., Majors A.K., Iwata K., Traboulsi E.I., Sakai L.Y., Keene D.R., Apte S.S.
    J. Biol. Chem. 286:17156-17167(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBN1.
  5. "Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme."
    Kutz W.E., Wang L.W., Dagoneau N., Odrcic K.J., Cormier-Daire V., Traboulsi E.I., Apte S.S.
    Hum. Mutat. 29:1425-1434(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WMS1 THR-25, CHARACTERIZATION OF VARIANT WMS1 THR-25.

Entry informationi

Entry nameiATS10_HUMAN
AccessioniPrimary (citable) accession number: Q9H324
Secondary accession number(s): M0QZE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: June 12, 2007
Last modified: November 26, 2014
This is version 132 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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3