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Q92743

- HTRA1_HUMAN

UniProt

Q92743 - HTRA1_HUMAN

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Protein

Serine protease HTRA1

Gene

HTRA1

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

Functioni

Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei169 – 1691Involved in trimer stabilization
Sitei171 – 1711Involved in trimer stabilization
Active sitei220 – 2201Charge relay systemSequence Analysis
Active sitei250 – 2501Charge relay systemSequence Analysis
Sitei278 – 2781Involved in trimer stabilization
Active sitei328 – 3281Charge relay system

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: ProtInc
  2. serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of BMP signaling pathway Source: Ensembl
  2. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  3. proteolysis Source: UniProtKB
  4. regulation of cell growth Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Growth factor binding

Protein family/group databases

MEROPSiS01.277.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease HTRA1 (EC:3.4.21.-)
Alternative name(s):
High-temperature requirement A serine peptidase 1
L56
Serine protease 11
Gene namesi
Name:HTRA1
Synonyms:HTRA, PRSS11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9476. HTRA1.

Subcellular locationi

Secreted. Cytoplasmcytosol
Note: Predominantly secreted. Also found associated with the plasma membrane.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular space Source: ProtInc
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Involvement in diseasei

Macular degeneration, age-related, 7 (ARMD7) [MIM:610149]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Cerebral arteriopathy with subcortical infarcts and leukoencephalopathy, autosomal recessive (CARASIL) [MIM:600142]: A cerebrovascular disease characterized by non-hypertensive arteriopathy of cerebral small vessels with subcortical infarcts, alopecia, and spondylosis. Small cerebral arteries show arteriosclerotic changes, fibrous intimal proliferation, and hyaline degeneration with splitting of the intima and/or the internal elastic membrane. Neurologic features include progressive dementia, gait disturbances, extrapyramidal and pyramidal signs, and demyelination of the cerebral white matter with sparing of U fibers.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti252 – 2521A → T in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
Corresponds to variant rs113993968 [ dbSNP | Ensembl ].
VAR_063148
Natural varianti297 – 2971V → M in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
Corresponds to variant rs113993969 [ dbSNP | Ensembl ].
VAR_063149

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi328 – 3281S → A: Loss of activity. 2 Publications

Keywords - Diseasei

Age-related macular degeneration, Disease mutation

Organism-specific databases

MIMi600142. phenotype.
610149. phenotype.
Orphaneti279. Age-related macular degeneration.
199354. CARASIL.
PharmGKBiPA33829.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 480458Serine protease HTRA1PRO_0000026943Add
BLAST

Proteomic databases

PaxDbiQ92743.
PeptideAtlasiQ92743.
PRIDEiQ92743.

PTM databases

PhosphoSiteiQ92743.

Expressioni

Tissue specificityi

Widely expressed, with strongest expression in placenta (at protein level). Secreted by synovial fibroblasts. Up-regulated in osteoarthritis and rheumatoid arthritis synovial fluids and cartilage as compared with non-arthritic (at protein level).3 Publications

Developmental stagei

In the placenta, in the first trimester of gestation, low expression in the cells surrounding villi both in the inner layer of the cytotrophoblast and in the outer layer of the syncytiotrophoblast (at protein level). In the third trimester of gestation, very strong expression in the outer layer forming the syncytiotrophoblast and lower in the cytotrophoblast (at protein level).1 Publication

Gene expression databases

BgeeiQ92743.
CleanExiHS_HTRA1.
ExpressionAtlasiQ92743. baseline and differential.
GenevestigatoriQ92743.

Organism-specific databases

HPAiHPA036655.

Interactioni

Subunit structurei

Forms homotrimers. In the presence of substrate, may form higher-order multimers in a PDZ-independent manner. Interacts with TGF-beta family members, including BMP4, TGFB1, TGFB2, activin A and GDF5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi111635. 7 interactions.
DIPiDIP-33195N.
IntActiQ92743. 6 interactions.
MINTiMINT-1198897.
STRINGi9606.ENSP00000357980.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 453Combined sources
Beta strandi57 – 593Combined sources
Beta strandi65 – 684Combined sources
Beta strandi74 – 774Combined sources
Beta strandi87 – 904Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi125 – 1284Combined sources
Helixi129 – 14113Combined sources
Helixi165 – 1684Combined sources
Helixi171 – 1799Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1919Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi198 – 20811Combined sources
Turni211 – 2133Combined sources
Beta strandi214 – 2185Combined sources
Turni219 – 2213Combined sources
Beta strandi224 – 2318Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi237 – 24610Combined sources
Turni247 – 2504Combined sources
Beta strandi251 – 2555Combined sources
Helixi270 – 2723Combined sources
Beta strandi278 – 2869Combined sources
Beta strandi289 – 29911Combined sources
Helixi304 – 3063Combined sources
Beta strandi317 – 3215Combined sources
Turni325 – 3295Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi339 – 34810Combined sources
Beta strandi351 – 3566Combined sources
Helixi357 – 36812Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi384 – 3896Combined sources
Helixi392 – 40110Combined sources
Beta strandi411 – 4177Combined sources
Beta strandi419 – 4213Combined sources
Helixi422 – 4265Combined sources
Beta strandi433 – 4375Combined sources
Helixi445 – 45410Combined sources
Beta strandi456 – 4649Combined sources
Beta strandi467 – 4737Combined sources
Beta strandi476 – 4783Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JOANMR-A380-480[»]
2YTWNMR-A370-480[»]
3NUMX-ray2.75A158-480[»]
3NWUX-ray3.20A/B/C158-375[»]
3NZIX-ray2.75A158-480[»]
3TJNX-ray3.00A/B/D161-367[»]
3TJOX-ray2.30A/B/D161-370[»]
3TJQX-ray2.00A35-156[»]
ProteinModelPortaliQ92743.
SMRiQ92743. Positions 36-154, 160-370, 380-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 10068IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini98 – 15760Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini365 – 467103PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni204 – 364161Serine proteaseAdd
BLAST

Domaini

The IGFBP N-terminal domain mediates interaction with TSC2 substrate.

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated
Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
Contains 1 Kazal-like domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0265.
GeneTreeiENSGT00510000046315.
HOGENOMiHOG000223641.
HOVERGENiHBG052044.
InParanoidiQ92743.
KOiK08784.
OMAiQRGACGQ.
OrthoDBiEOG7V1FR7.
PhylomeDBiQ92743.
TreeFamiTF323480.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR000867. IGFBP-like.
IPR002350. Kazal_dom.
IPR001478. PDZ.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00219. IGFBP. 1 hit.
PF07648. Kazal_2. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00121. IB. 1 hit.
SM00280. KAZAL. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS51323. IGFBP_N_2. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92743-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQIPRAALLP LLLLLLAAPA SAQLSRAGRS APLAAGCPDR CEPARCPPQP
60 70 80 90 100
EHCEGGRARD ACGCCEVCGA PEGAACGLQE GPCGEGLQCV VPFGVPASAT
110 120 130 140 150
VRRRAQAGLC VCASSEPVCG SDANTYANLC QLRAASRRSE RLHRPPVIVL
160 170 180 190 200
QRGACGQGQE DPNSLRHKYN FIADVVEKIA PAVVHIELFR KLPFSKREVP
210 220 230 240 250
VASGSGFIVS EDGLIVTNAH VVTNKHRVKV ELKNGATYEA KIKDVDEKAD
260 270 280 290 300
IALIKIDHQG KLPVLLLGRS SELRPGEFVV AIGSPFSLQN TVTTGIVSTT
310 320 330 340 350
QRGGKELGLR NSDMDYIQTD AIINYGNSGG PLVNLDGEVI GINTLKVTAG
360 370 380 390 400
ISFAIPSDKI KKFLTESHDR QAKGKAITKK KYIGIRMMSL TSSKAKELKD
410 420 430 440 450
RHRDFPDVIS GAYIIEVIPD TPAEAGGLKE NDVIISINGQ SVVSANDVSD
460 470 480
VIKRESTLNM VVRRGNEDIM ITVIPEEIDP
Length:480
Mass (Da):51,287
Last modified:February 1, 1997 - v1
Checksum:iCA20A99480FB2330
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti323 – 3231I → T in AAC97211. (PubMed:9852107)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti252 – 2521A → T in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
Corresponds to variant rs113993968 [ dbSNP | Ensembl ].
VAR_063148
Natural varianti297 – 2971V → M in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
Corresponds to variant rs113993969 [ dbSNP | Ensembl ].
VAR_063149

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07921 mRNA. Translation: CAA69226.1.
AF157623 Genomic DNA. Translation: AAD41525.1.
CH471066 Genomic DNA. Translation: EAW49312.1.
CH471066 Genomic DNA. Translation: EAW49313.1.
AF097709 mRNA. Translation: AAC97211.1.
CCDSiCCDS7630.1.
RefSeqiNP_002766.1. NM_002775.4.
UniGeneiHs.501280.

Genome annotation databases

EnsembliENST00000368984; ENSP00000357980; ENSG00000166033.
GeneIDi5654.
KEGGihsa:5654.
UCSCiuc001lgj.2. human.

Polymorphism databases

DMDMi18202620.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07921 mRNA. Translation: CAA69226.1 .
AF157623 Genomic DNA. Translation: AAD41525.1 .
CH471066 Genomic DNA. Translation: EAW49312.1 .
CH471066 Genomic DNA. Translation: EAW49313.1 .
AF097709 mRNA. Translation: AAC97211.1 .
CCDSi CCDS7630.1.
RefSeqi NP_002766.1. NM_002775.4.
UniGenei Hs.501280.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JOA NMR - A 380-480 [» ]
2YTW NMR - A 370-480 [» ]
3NUM X-ray 2.75 A 158-480 [» ]
3NWU X-ray 3.20 A/B/C 158-375 [» ]
3NZI X-ray 2.75 A 158-480 [» ]
3TJN X-ray 3.00 A/B/D 161-367 [» ]
3TJO X-ray 2.30 A/B/D 161-370 [» ]
3TJQ X-ray 2.00 A 35-156 [» ]
ProteinModelPortali Q92743.
SMRi Q92743. Positions 36-154, 160-370, 380-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111635. 7 interactions.
DIPi DIP-33195N.
IntActi Q92743. 6 interactions.
MINTi MINT-1198897.
STRINGi 9606.ENSP00000357980.

Protein family/group databases

MEROPSi S01.277.

PTM databases

PhosphoSitei Q92743.

Polymorphism databases

DMDMi 18202620.

Proteomic databases

PaxDbi Q92743.
PeptideAtlasi Q92743.
PRIDEi Q92743.

Protocols and materials databases

DNASUi 5654.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368984 ; ENSP00000357980 ; ENSG00000166033 .
GeneIDi 5654.
KEGGi hsa:5654.
UCSCi uc001lgj.2. human.

Organism-specific databases

CTDi 5654.
GeneCardsi GC10P124221.
GeneReviewsi HTRA1.
HGNCi HGNC:9476. HTRA1.
HPAi HPA036655.
MIMi 600142. phenotype.
602194. gene.
610149. phenotype.
neXtProti NX_Q92743.
Orphaneti 279. Age-related macular degeneration.
199354. CARASIL.
PharmGKBi PA33829.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0265.
GeneTreei ENSGT00510000046315.
HOGENOMi HOG000223641.
HOVERGENi HBG052044.
InParanoidi Q92743.
KOi K08784.
OMAi QRGACGQ.
OrthoDBi EOG7V1FR7.
PhylomeDBi Q92743.
TreeFami TF323480.

Miscellaneous databases

ChiTaRSi HTRA1. human.
EvolutionaryTracei Q92743.
GeneWikii HTRA1.
GenomeRNAii 5654.
NextBioi 21974.
PROi Q92743.
SOURCEi Search...

Gene expression databases

Bgeei Q92743.
CleanExi HS_HTRA1.
ExpressionAtlasi Q92743. baseline and differential.
Genevestigatori Q92743.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
InterProi IPR009030. Growth_fac_rcpt_N_dom.
IPR000867. IGFBP-like.
IPR002350. Kazal_dom.
IPR001478. PDZ.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00219. IGFBP. 1 hit.
PF07648. Kazal_2. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view ]
PRINTSi PR00834. PROTEASES2C.
SMARTi SM00121. IB. 1 hit.
SM00280. KAZAL. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS51323. IGFBP_N_2. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of a putative serine protease specific for IGF-binding proteins."
    Zumbrunn J., Trueb B.
    FEBS Lett. 398:187-192(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Genomic organization and promoter characterization of the human HTRA (PRSS11) gene."
    Crowl R.M., Luk D., Milnamow M.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage."
    Hu S.I., Carozza M., Klein M., Nantermet P., Luk D., Crowl R.M.
    J. Biol. Chem. 273:34406-34412(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-480, PROTEIN SEQUENCE OF 33-44, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-328.
    Tissue: Cartilage.
  5. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  6. Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ARMD7.
  8. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ARMD7.
  9. "The serine protease HtrA1 specifically interacts and degrades the tuberous sclerosis complex 2 protein."
    Campioni M., Severino A., Manente L., Tuduce I.L., Toldo S., Caraglia M., Crispi S., Ehrmann M., He X., Maguire J., De Falco M., De Luca A., Shridhar V., Baldi A.
    Mol. Cancer Res. 8:1248-1260(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Solution structure of the PDZ-domain of human protease HTRA 1 precursor."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 367-480.
  11. "Substrate-induced remodeling of the active site regulates human HTRA1 activity."
    Truebestein L., Tennstaedt A., Monig T., Krojer T., Canellas F., Kaiser M., Clausen T., Ehrmann M.
    Nat. Struct. Mol. Biol. 18:386-388(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 158-480, HOMOTRIMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-328.
  12. Cited for: VARIANTS CARASIL THR-252 AND MET-297, CHARACTERIZATION OF VARIANTS CARASIL THR-252 AND MET-297.

Entry informationi

Entry nameiHTRA1_HUMAN
AccessioniPrimary (citable) accession number: Q92743
Secondary accession number(s): D3DRE4, Q9UNS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: February 1, 1997
Last modified: November 26, 2014
This is version 141 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3