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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene

ADAMTS4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.

Catalytic activityi

Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi194Zinc; in inhibited formBy similarity1
Metal bindingi361Zinc; catalytic1 Publication1
Active sitei362PROSITE-ProRule annotation1 Publication1
Metal bindingi365Zinc; catalytic1 Publication1
Metal bindingi371Zinc; catalytic1 Publication1

GO - Molecular functioni

  • metalloendopeptidase activity Source: Reactome
  • metallopeptidase activity Source: ProtInc
  • peptidase activity Source: ProtInc
  • protease binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • extracellular matrix disassembly Source: Reactome
  • proteolysis Source: ProtInc
  • skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000158859-MONOMER.
ZFISH:ENSG00000158859-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.221.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
Short name:
ADAM-TS 4
Short name:
ADAM-TS4
Short name:
ADAMTS-4
Alternative name(s):
ADMP-1
Aggrecanase-1
Gene namesi
Name:ADAMTS4
Synonyms:KIAA0688
ORF Names:UNQ769/PRO1563
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:220. ADAMTS4.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi9507.
OpenTargetsiENSG00000158859.
PharmGKBiPA24548.

Chemistry databases

ChEMBLiCHEMBL2318.
DrugBankiDB06822. Tinzaparin.
GuidetoPHARMACOLOGYi1677.

Polymorphism and mutation databases

BioMutaiADAMTS4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 51Sequence analysisAdd BLAST51
PropeptideiPRO_000002916452 – 212Add BLAST161
ChainiPRO_0000029165213 – 837A disintegrin and metalloproteinase with thrombospondin motifs 4Add BLAST625

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi68N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi293 ↔ 3451 Publication
Disulfide bondi322 ↔ 3271 Publication
Disulfide bondi339 ↔ 4231 Publication
Disulfide bondi377 ↔ 4071 Publication
Disulfide bondi449 ↔ 4721 Publication
Disulfide bondi460 ↔ 4821 Publication
Disulfide bondi467 ↔ 5011 Publication
Disulfide bondi495 ↔ 5061 Publication
Disulfide bondi532 ↔ 569By similarity
Disulfide bondi536 ↔ 574By similarity
Disulfide bondi547 ↔ 559By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.
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

PaxDbiO75173.
PeptideAtlasiO75173.
PRIDEiO75173.

PTM databases

iPTMnetiO75173.
PhosphoSitePlusiO75173.

Miscellaneous databases

PMAP-CutDBO75173.

Expressioni

Tissue specificityi

Expressed in brain, lung and heart (PubMed:23897278). Expressed at very low level in placenta and skeletal muscles (PubMed:23897278). Isoform 2: Detected in osteoarthritic synovium (PubMed:16723216, PubMed:23897278).2 Publications

Inductioni

By IL1/interleukin-1.

Gene expression databases

BgeeiENSG00000158859.
CleanExiHS_ADAMTS4.
ExpressionAtlasiO75173. baseline and differential.
GenevisibleiO75173. HS.

Organism-specific databases

HPAiCAB025876.

Interactioni

Subunit structurei

Interacts with SRPX2.2 Publications

GO - Molecular functioni

  • protease binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114885. 26 interactors.
IntActiO75173. 2 interactors.
STRINGi9606.ENSP00000356975.

Chemistry databases

BindingDBiO75173.

Structurei

Secondary structure

1837
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi219 – 226Combined sources8
Helixi228 – 234Combined sources7
Helixi235 – 237Combined sources3
Helixi238 – 254Combined sources17
Helixi256 – 258Combined sources3
Beta strandi263 – 271Combined sources9
Beta strandi274 – 276Combined sources3
Helixi285 – 297Combined sources13
Beta strandi304 – 306Combined sources3
Beta strandi311 – 317Combined sources7
Turni322 – 324Combined sources3
Beta strandi331 – 333Combined sources3
Turni341 – 343Combined sources3
Beta strandi345 – 349Combined sources5
Beta strandi352 – 354Combined sources3
Helixi355 – 366Combined sources12
Helixi375 – 381Combined sources7
Beta strandi392 – 394Combined sources3
Helixi406 – 417Combined sources12
Turni418 – 423Combined sources6
Helixi439 – 442Combined sources4
Helixi445 – 453Combined sources9
Beta strandi463 – 465Combined sources3
Turni466 – 468Combined sources3
Beta strandi472 – 476Combined sources5
Beta strandi479 – 483Combined sources5
Beta strandi494 – 496Combined sources3
Beta strandi499 – 502Combined sources4
Beta strandi505 – 507Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RJPX-ray2.80A/B/C/D213-520[»]
3B2ZX-ray2.80A/B/C/D/E/F/G/H213-520[»]
4WK7X-ray1.24A213-439[»]
4WKEX-ray1.62A213-439[»]
4WKIX-ray1.60A213-439[»]
ProteinModelPortaliO75173.
SMRiO75173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75173.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini218 – 428Peptidase M12BPROSITE-ProRule annotationAdd BLAST211
Domaini437 – 519DisintegrinAdd BLAST83
Domaini520 – 575TSP type-1PROSITE-ProRule annotationAdd BLAST56

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni686 – 837SpacerAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi192 – 199Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi247 – 252Poly-Ala6
Compositional biasi577 – 685Cys-richAdd BLAST109

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.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiO75173.
KOiK07764.
OMAiKFRYGYN.
OrthoDBiEOG091G00AX.
PhylomeDBiO75173.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
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. AlignAdd to basket

Isoform 1 (identifier: O75173-1) [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
MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR
60 70 80 90 100
LASPLPREEE IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEQDS
110 120 130 140 150
GVQVEGLTVQ YLGQAPELLG GAEPGTYLTG TINGDPESVA SLHWDGGALL
160 170 180 190 200
GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI LRRKSPASGQ GPMCNVKAPL
210 220 230 240 250
GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR YLLTVMAAAA
260 270 280 290 300
KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN
310 320 330 340 350
TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED
360 370 380 390 400
DGLQSAFTAA HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP
410 420 430 440 450
EEPWSPCSAR FITDFLDNGY GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ
460 470 480 490 500
LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA MCQTKHSPWA DGTPCGPAQA
510 520 530 540 550
CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV QFSSRDCTRP
560 570 580 590 600
VPRNGGKYCE GRRTRFRSCN TEDCPTGSAL TFREEQCAAY NHRTDLFKSF
610 620 630 640 650
PGPMDWVPRY TGVAPQDQCK LTCQAQALGY YYVLEPRVVD GTPCSPDSSS
660 670 680 690 700
VCVQGRCIHA GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN
710 720 730 740 750
NVVTIPAGAT HILVRQQGNP GHRSIYLALK LPDGSYALNG EYTLMPSPTD
760 770 780 790 800
VVLPGAVSLR YSGATAASET LSGHGPLAQP LTLQVLVAGN PQDTRLRYSF
810 820 830
FVPRPTPSTP RPTPQDWLHR RAQILEILRR RPWAGRK
Length:837
Mass (Da):90,197
Last modified:January 11, 2011 - v3
Checksum:i0C05299D7FB23A8D
GO
Isoform 2 (identifier: O75173-2) [UniParc]FASTAAdd to basket
Also known as: ADAMTS4_v1

The sequence of this isoform differs from the canonical sequence as follows:
     697-837: YGYNNVVTIP...LRRRPWAGRK → CGTAWGSQLA...PALVSCPGRQ

Note: Functional aggrecanase.1 Publication
Show »
Length:846
Mass (Da):90,065
Checksum:iEE5ABC89BD0556D5
GO

Sequence cautioni

The sequence ABC88384 differs from that shown. Reason: Frameshift at position 697.Curated
The sequence BAA31663 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti306D → G in AAQ89245 (PubMed:12975309).Curated1
Sequence conflicti682G → R in AAL02262 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0306364T → I.1 PublicationCorresponds to variant rs17855814dbSNPEnsembl.1
Natural variantiVAR_05707377A → T.1 PublicationCorresponds to variant rs34448954dbSNPEnsembl.1
Natural variantiVAR_030637304D → N.1 PublicationCorresponds to variant rs17855813dbSNPEnsembl.1
Natural variantiVAR_030638369M → V.1 PublicationCorresponds to variant rs17855812dbSNPEnsembl.1
Natural variantiVAR_030639552P → T.1 PublicationCorresponds to variant rs17855815dbSNPEnsembl.1
Natural variantiVAR_030640564T → A.1 PublicationCorresponds to variant rs17855816dbSNPEnsembl.1
Natural variantiVAR_022450626Q → R.3 PublicationsCorresponds to variant rs4233367dbSNPEnsembl.1
Natural variantiVAR_030641836R → K.Corresponds to variant rs11807350dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_057293697 – 837YGYNN…WAGRK → CGTAWGSQLALQRGHCSLRD TVRPWATGPAFDTASPSGWQ PPGHTPPIQLLRAPADPFNA TPHSPGLAAPKSTDSGDPSA APLGGQEITSLSRLPFLGTG ASDLAGRKRELLLLPHAKTQ WGGAVGVRPAPPLCPNAQAG PALVSCPGRQ in isoform 2. 1 PublicationAdd BLAST141

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148213 mRNA. Translation: AAD41494.1.
DQ364570 mRNA. Translation: ABC88384.1. Frameshift.
AY044847 Genomic DNA. Translation: AAL02262.1.
AB014588 mRNA. Translation: BAA31663.2. Different initiation.
AY358886 mRNA. Translation: AAQ89245.1.
AL590714 Genomic DNA. Translation: CAH72146.1.
BC063293 mRNA. Translation: AAH63293.1.
CCDSiCCDS1223.1. [O75173-1]
PIRiT00355.
RefSeqiNP_001307265.1. NM_001320336.1. [O75173-2]
NP_005090.3. NM_005099.5. [O75173-1]
UniGeneiHs.211604.

Genome annotation databases

EnsembliENST00000367996; ENSP00000356975; ENSG00000158859. [O75173-1]
GeneIDi9507.
KEGGihsa:9507.
UCSCiuc001fyt.5. human. [O75173-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148213 mRNA. Translation: AAD41494.1.
DQ364570 mRNA. Translation: ABC88384.1. Frameshift.
AY044847 Genomic DNA. Translation: AAL02262.1.
AB014588 mRNA. Translation: BAA31663.2. Different initiation.
AY358886 mRNA. Translation: AAQ89245.1.
AL590714 Genomic DNA. Translation: CAH72146.1.
BC063293 mRNA. Translation: AAH63293.1.
CCDSiCCDS1223.1. [O75173-1]
PIRiT00355.
RefSeqiNP_001307265.1. NM_001320336.1. [O75173-2]
NP_005090.3. NM_005099.5. [O75173-1]
UniGeneiHs.211604.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RJPX-ray2.80A/B/C/D213-520[»]
3B2ZX-ray2.80A/B/C/D/E/F/G/H213-520[»]
4WK7X-ray1.24A213-439[»]
4WKEX-ray1.62A213-439[»]
4WKIX-ray1.60A213-439[»]
ProteinModelPortaliO75173.
SMRiO75173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114885. 26 interactors.
IntActiO75173. 2 interactors.
STRINGi9606.ENSP00000356975.

Chemistry databases

BindingDBiO75173.
ChEMBLiCHEMBL2318.
DrugBankiDB06822. Tinzaparin.
GuidetoPHARMACOLOGYi1677.

Protein family/group databases

MEROPSiM12.221.

PTM databases

iPTMnetiO75173.
PhosphoSitePlusiO75173.

Polymorphism and mutation databases

BioMutaiADAMTS4.

Proteomic databases

PaxDbiO75173.
PeptideAtlasiO75173.
PRIDEiO75173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367996; ENSP00000356975; ENSG00000158859. [O75173-1]
GeneIDi9507.
KEGGihsa:9507.
UCSCiuc001fyt.5. human. [O75173-1]

Organism-specific databases

CTDi9507.
DisGeNETi9507.
GeneCardsiADAMTS4.
H-InvDBHIX0001237.
HGNCiHGNC:220. ADAMTS4.
HPAiCAB025876.
MIMi603876. gene.
neXtProtiNX_O75173.
OpenTargetsiENSG00000158859.
PharmGKBiPA24548.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiO75173.
KOiK07764.
OMAiKFRYGYN.
OrthoDBiEOG091G00AX.
PhylomeDBiO75173.
TreeFamiTF331949.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000158859-MONOMER.
ZFISH:ENSG00000158859-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

ChiTaRSiADAMTS4. human.
EvolutionaryTraceiO75173.
GeneWikiiADAMTS4.
GenomeRNAii9507.
PMAP-CutDBO75173.
PROiO75173.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158859.
CleanExiHS_ADAMTS4.
ExpressionAtlasiO75173. baseline and differential.
GenevisibleiO75173. HS.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS4_HUMAN
AccessioniPrimary (citable) accession number: O75173
Secondary accession number(s): Q2HYD0
, Q5VTW2, Q6P4Q8, Q6UWA8, Q9UN83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 175 of the entry and version 3 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

Caution

Has sometimes been referred to as ADAMTS2.Curated

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.