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Q9UNA0

- ATS5_HUMAN

UniProt

Q9UNA0 - ATS5_HUMAN

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Protein
A disintegrin and metalloproteinase with thrombospondin motifs 5
Gene
ADAMTS5, ADAMTS11, ADMP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.

Catalytic activityi

Cleaves aggrecan at the 392-Glu-|-Ala-393 site.

Cofactori

Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi209 – 2091Zinc; in inhibited form By similarity
Metal bindingi410 – 4101Zinc; catalytic
Active sitei411 – 41111 Publication
Metal bindingi414 – 4141Zinc; catalytic
Metal bindingi420 – 4201Zinc; catalytic

GO - Molecular functioni

  1. integrin binding Source: ProtInc
  2. metalloendopeptidase activity Source: InterPro
  3. metallopeptidase activity Source: ProtInc
  4. protein binding Source: IntAct
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. extracellular matrix disassembly Source: Reactome
  2. extracellular matrix organization Source: Reactome
  3. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.
REACT_201925. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM12.225.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 5 (EC:3.4.24.-)
Short name:
ADAM-TS 5
Short name:
ADAM-TS5
Short name:
ADAMTS-5
Alternative name(s):
A disintegrin and metalloproteinase with thrombospondin motifs 11
Short name:
ADAM-TS 11
Short name:
ADAMTS-11
ADMP-2
Aggrecanase-2
Gene namesi
Name:ADAMTS5
Synonyms:ADAMTS11, ADMP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:221. ADAMTS5.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Propeptidei17 – 261245 Reviewed prediction
PRO_0000029170Add
BLAST
Chaini262 – 930669A disintegrin and metalloproteinase with thrombospondin motifs 5
PRO_0000029171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi342 ↔ 3941 Publication
Disulfide bondi371 ↔ 3761 Publication
Disulfide bondi388 ↔ 4711 Publication
Disulfide bondi426 ↔ 4551 Publication
Disulfide bondi497 ↔ 5191 Publication
Glycosylationi498 – 4981N-linked (GlcNAc...)1 Publication
Disulfide bondi508 ↔ 5291 Publication
Disulfide bondi514 ↔ 5481 Publication
Disulfide bondi542 ↔ 5531 Publication
Glycosylationi570 – 5701C-linked (Man)1 Publication
Glycosylationi573 – 5731C-linked (Man)1 Publication
Disulfide bondi579 ↔ 616 By similarity
Glycosylationi582 – 5821O-linked (Fuc...)1 Publication
Disulfide bondi583 ↔ 621 By similarity
Disulfide bondi594 ↔ 606 By similarity
Glycosylationi728 – 7281N-linked (GlcNAc...) Reviewed prediction
Glycosylationi802 – 8021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi807 – 8071N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase By similarity.
C- and O-glycosylated. 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 can mediate the efficient secretion of ADAMTS family members. 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.2 Publications
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.2 Publications

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9UNA0.
PRIDEiQ9UNA0.

PTM databases

PhosphoSiteiQ9UNA0.

Miscellaneous databases

PMAP-CutDBQ9UNA0.

Expressioni

Tissue specificityi

Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.

Gene expression databases

BgeeiQ9UNA0.
CleanExiHS_ADAMTS5.
GenevestigatoriQ9UNA0.

Organism-specific databases

HPAiCAB025996.
HPA005661.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ACANP136082EBI-2808663,EBI-6259246From a different organism.

Protein-protein interaction databases

BioGridi116277. 1 interaction.
IntActiQ9UNA0. 3 interactions.
STRINGi9606.ENSP00000284987.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi267 – 2759
Helixi277 – 2837
Helixi284 – 2863
Helixi287 – 30216
Helixi305 – 3073
Beta strandi311 – 32010
Turni323 – 3264
Helixi334 – 34815
Beta strandi353 – 3564
Beta strandi360 – 3689
Beta strandi380 – 3823
Helixi390 – 3923
Beta strandi394 – 3985
Beta strandi401 – 4033
Helixi404 – 41512
Helixi424 – 4307
Beta strandi435 – 4373
Beta strandi440 – 4423
Helixi443 – 4453
Helixi454 – 46512
Turni466 – 4694
Helixi470 – 4723
Helixi487 – 4904
Helixi493 – 5019
Beta strandi509 – 5113
Turni513 – 5153
Beta strandi519 – 5235
Beta strandi526 – 5305
Beta strandi543 – 5453
Beta strandi547 – 5493
Beta strandi552 – 5543

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RJQX-ray2.60A262-628[»]
3B8ZX-ray1.40A/B264-480[»]
3HY7X-ray1.69A/B262-480[»]
3HY9X-ray2.02A/B262-480[»]
3HYGX-ray1.40A/B262-480[»]
3LJTX-ray1.60A264-480[»]
ProteinModelPortaliQ9UNA0.
SMRiQ9UNA0. Positions 259-797.

Miscellaneous databases

EvolutionaryTraceiQ9UNA0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 476210Peptidase M12B
Add
BLAST
Domaini485 – 56682Disintegrin
Add
BLAST
Domaini567 – 62256TSP type-1 1
Add
BLAST
Domaini875 – 92955TSP type-1 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni732 – 874143Spacer
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2148Cysteine switch By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi37 – 415Poly-Ala
Compositional biasi257 – 2615Poly-Arg
Compositional biasi624 – 731108Cys-rich
Add
BLAST

Domaini

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similaritiesi

Contains 1 disintegrin domain.
Contains 2 TSP type-1 domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG302522.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9UNA0.
KOiK08620.
OMAiRASCETP.
OrthoDBiEOG7WDN1M.
PhylomeDBiQ9UNA0.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013276. Pept_M12B_ADAM-TS5.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR01860. ADAMTS5.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 2 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UNA0-1 [UniParc]FASTAAdd to Basket

« Hide

MLLGWASLLL CAFRLPLAAV GPAATPAQDK AGQPPTAAAA AQPRRRQGEE    50
VQERAEPPGH PHPLAQRRRS KGLVQNIDQL YSGGGKVGYL VYAGGRRFLL 100
DLERDGSVGI AGFVPAGGGT SAPWRHRSHC FYRGTVDGSP RSLAVFDLCG 150
GLDGFFAVKH ARYTLKPLLR GPWAEEEKGR VYGDGSARIL HVYTREGFSF 200
EALPPRASCE TPASTPEAHE HAPAHSNPSG RAALASQLLD QSALSPAGGS 250
GPQTWWRRRR RSISRARQVE LLLVADASMA RLYGRGLQHY LLTLASIANR 300
LYSHASIENH IRLAVVKVVV LGDKDKSLEV SKNAATTLKN FCKWQHQHNQ 350
LGDDHEEHYD AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD 400
GLHAAFTVAH EIGHLLGLSH DDSKFCEETF GSTEDKRLMS SILTSIDASK 450
PWSKCTSATI TEFLDDGHGN CLLDLPRKQI LGPEELPGQT YDATQQCNLT 500
FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT PCGKGRICLQ 550
GKCVDKTKKK YYSTSSHGNW GSWGSWGQCS RSCGGGVQFA YRHCNNPAPR 600
NNGRYCTGKR AIYRSCSLMP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV 650
EWVPKYAGVL PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RLYSNSVCVR 700
GKCVRTGCDG IIGSKLQYDK CGVCGGDNSS CTKIVGTFNK KSKGYTDVVR 750
IPEGATHIKV RQFKAKDQTR FTAYLALKKK NGEYLINGKY MISTSETIID 800
INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT KPLDVRYSFF 850
VPKKSTPKVN SVTSHGSNKV GSHTSQPQWV TGPWLACSRT CDTGWHTRTV 900
QCQDGNRKLA KGCPLSQRPS AFKQCLLKKC 930
Length:930
Mass (Da):101,718
Last modified:January 11, 2011 - v2
Checksum:i8CCE448A15A29CE8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381G → A.2 Publications
Corresponds to variant rs457947 [ dbSNP | Ensembl ].
VAR_028199
Natural varianti614 – 6141R → H.1 Publication
Corresponds to variant rs2830585 [ dbSNP | Ensembl ].
VAR_021849
Natural varianti692 – 6921L → P.3 Publications
Corresponds to variant rs226794 [ dbSNP | Ensembl ].
VAR_028200

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142099 mRNA. Translation: AAD49577.1.
AP001698 Genomic DNA. Translation: BAA95504.1.
AP001697 Genomic DNA. Translation: BAA95503.1.
BC093775 mRNA. Translation: AAH93775.1.
BC093777 mRNA. Translation: AAH93777.1.
AF141293 mRNA. Translation: AAF02493.1.
CCDSiCCDS13579.1.
RefSeqiNP_008969.2. NM_007038.3.
UniGeneiHs.58324.

Genome annotation databases

EnsembliENST00000284987; ENSP00000284987; ENSG00000154736.
GeneIDi11096.
KEGGihsa:11096.
UCSCiuc002ymg.3. human.

Polymorphism databases

DMDMi317373326.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142099 mRNA. Translation: AAD49577.1 .
AP001698 Genomic DNA. Translation: BAA95504.1 .
AP001697 Genomic DNA. Translation: BAA95503.1 .
BC093775 mRNA. Translation: AAH93775.1 .
BC093777 mRNA. Translation: AAH93777.1 .
AF141293 mRNA. Translation: AAF02493.1 .
CCDSi CCDS13579.1.
RefSeqi NP_008969.2. NM_007038.3.
UniGenei Hs.58324.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RJQ X-ray 2.60 A 262-628 [» ]
3B8Z X-ray 1.40 A/B 264-480 [» ]
3HY7 X-ray 1.69 A/B 262-480 [» ]
3HY9 X-ray 2.02 A/B 262-480 [» ]
3HYG X-ray 1.40 A/B 262-480 [» ]
3LJT X-ray 1.60 A 264-480 [» ]
ProteinModelPortali Q9UNA0.
SMRi Q9UNA0. Positions 259-797.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116277. 1 interaction.
IntActi Q9UNA0. 3 interactions.
STRINGi 9606.ENSP00000284987.

Chemistry

BindingDBi Q9UNA0.
ChEMBLi CHEMBL2285.

Protein family/group databases

MEROPSi M12.225.

PTM databases

PhosphoSitei Q9UNA0.

Polymorphism databases

DMDMi 317373326.

Proteomic databases

PaxDbi Q9UNA0.
PRIDEi Q9UNA0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284987 ; ENSP00000284987 ; ENSG00000154736 .
GeneIDi 11096.
KEGGi hsa:11096.
UCSCi uc002ymg.3. human.

Organism-specific databases

CTDi 11096.
GeneCardsi GC21M028290.
H-InvDB HIX0016044.
HGNCi HGNC:221. ADAMTS5.
HPAi CAB025996.
HPA005661.
MIMi 605007. gene.
neXtProti NX_Q9UNA0.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG302522.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi Q9UNA0.
KOi K08620.
OMAi RASCETP.
OrthoDBi EOG7WDN1M.
PhylomeDBi Q9UNA0.
TreeFami TF331949.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.
REACT_201925. Degradation of the extracellular matrix.

Miscellaneous databases

EvolutionaryTracei Q9UNA0.
GeneWikii ADAMTS5.
GenomeRNAii 11096.
NextBioi 42182.
PMAP-CutDB Q9UNA0.
PROi Q9UNA0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UNA0.
CleanExi HS_ADAMTS5.
Genevestigatori Q9UNA0.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013276. Pept_M12B_ADAM-TS5.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view ]
PRINTSi PR01860. ADAMTS5.
PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 2 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 2 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-138 AND PRO-692.
    Tissue: Liver.
  2. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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], VARIANTS ALA-138 AND PRO-692.
    Tissue: Colon.
  4. "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
    Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
    J. Biol. Chem. 274:25555-25563(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-930, VARIANTS HIS-614 AND PRO-692.
    Tissue: Fetal brain.
  5. "Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan."
    Wang L.W., Leonhard-Melief C., Haltiwanger R.S., Apte S.S.
    J. Biol. Chem. 284:30004-30015(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-570; TRP-573 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 262-628 IN COMPLEX WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, DISULFIDE BONDS, GLYCOSYLATION AT ASN-498.

Entry informationi

Entry nameiATS5_HUMAN
AccessioniPrimary (citable) accession number: Q9UNA0
Secondary accession number(s): Q52LV4, Q9UKP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 145 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: 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

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