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P48147

- PPCE_HUMAN

UniProt

P48147 - PPCE_HUMAN

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Protein

Prolyl endopeptidase

Gene

PREP

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

Functioni

Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.

Catalytic activityi

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei554 – 5541Charge relay systemPROSITE-ProRule annotation
Active sitei641 – 6411Charge relay systemPROSITE-ProRule annotation
Active sitei680 – 6801Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: ProtInc
  2. serine-type exopeptidase activity Source: InterPro
  3. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS09.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl endopeptidase (EC:3.4.21.26)
Short name:
PE
Alternative name(s):
Post-proline cleaving enzyme
Gene namesi
Name:PREP
Synonyms:PEP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9358. PREP.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. membrane Source: UniProtKB
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 710710Prolyl endopeptidasePRO_0000122401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei157 – 1571N6-acetyllysine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP48147.
PaxDbiP48147.
PRIDEiP48147.

PTM databases

PhosphoSiteiP48147.

Miscellaneous databases

PMAP-CutDBQ8N6D4.

Expressioni

Gene expression databases

BgeeiP48147.
CleanExiHS_PREP.
GenevestigatoriP48147.

Organism-specific databases

HPAiCAB025414.
HPA031388.
HPA031389.
HPA031390.

Interactioni

Subunit structurei

Monomer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GAPDHP044065EBI-1049962,EBI-354056

Protein-protein interaction databases

BioGridi111541. 7 interactions.
IntActiP48147. 1 interaction.
MINTiMINT-5004282.
STRINGi9606.ENSP00000358106.

Structurei

Secondary structure

1
710
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 194Combined sources
Beta strandi22 – 254Combined sources
Helixi29 – 324Combined sources
Helixi37 – 5519Combined sources
Helixi59 – 7012Combined sources
Beta strandi80 – 823Combined sources
Beta strandi85 – 917Combined sources
Beta strandi99 – 1057Combined sources
Beta strandi111 – 1144Combined sources
Helixi116 – 1194Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi136 – 14510Combined sources
Beta strandi151 – 1577Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 17110Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi182 – 1898Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi209 – 2146Combined sources
Helixi219 – 2213Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi246 – 25712Combined sources
Beta strandi260 – 2656Combined sources
Helixi266 – 2683Combined sources
Beta strandi270 – 2734Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi290 – 2967Combined sources
Beta strandi299 – 3046Combined sources
Beta strandi312 – 3176Combined sources
Helixi323 – 3253Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi337 – 3448Combined sources
Turni345 – 3473Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi358 – 3658Combined sources
Turni366 – 3683Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi379 – 3868Combined sources
Beta strandi392 – 3998Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi406 – 4116Combined sources
Beta strandi414 – 4163Combined sources
Beta strandi420 – 4234Combined sources
Helixi432 – 4343Combined sources
Beta strandi435 – 4439Combined sources
Beta strandi449 – 4579Combined sources
Beta strandi468 – 4714Combined sources
Helixi486 – 49510Combined sources
Beta strandi498 – 5025Combined sources
Helixi511 – 5166Combined sources
Helixi520 – 5234Combined sources
Helixi524 – 53916Combined sources
Helixi545 – 5473Combined sources
Beta strandi548 – 5536Combined sources
Helixi555 – 56612Combined sources
Helixi568 – 5703Combined sources
Beta strandi572 – 5787Combined sources
Turni583 – 5853Combined sources
Helixi586 – 5883Combined sources
Helixi592 – 5954Combined sources
Helixi596 – 5994Combined sources
Helixi605 – 61410Combined sources
Helixi616 – 6183Combined sources
Beta strandi632 – 6387Combined sources
Helixi647 – 65913Combined sources
Turni660 – 6623Combined sources
Beta strandi670 – 6778Combined sources
Helixi686 – 70419Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DDUX-ray1.56A2-710[»]
ProteinModelPortaliP48147.
SMRiP48147. Positions 2-710.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48147.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9A family.Curated

Phylogenomic databases

eggNOGiCOG1505.
GeneTreeiENSGT00530000063426.
HOGENOMiHOG000238967.
HOVERGENiHBG007251.
InParanoidiP48147.
KOiK01322.
OMAiDYQTIQI.
OrthoDBiEOG78PV88.
PhylomeDBiP48147.
TreeFamiTF300655.

Family and domain databases

Gene3Di2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERiPTHR11757. PTHR11757. 1 hit.
PfamiPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSiPR00862. PROLIGOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48147-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSLQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT
60 70 80 90 100
VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL
110 120 130 140 150
YVQDSLEGEA RVFLDPNILS DDGTVALRGY AFSEDGEYFA YGLSASGSDW
160 170 180 190 200
VTIKFMKVDG AKELPDVLER VKFSCMAWTH DGKGMFYNSY PQQDGKSDGT
210 220 230 240 250
ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS
260 270 280 290 300
IREGCDPVNR LWYCDLQQES SGIAGILKWV KLIDNFEGEY DYVTNEGTVF
310 320 330 340 350
TFKTNRQSPN YRVINIDFRD PEESKWKVLV PEHEKDVLEW IACVRSNFLV
360 370 380 390 400
LCYLHDVKNI LQLHDLTTGA LLKTFPLDVG SIVGYSGQKK DTEIFYQFTS
410 420 430 440 450
FLSPGIIYHC DLTKEELEPR VFREVTVKGI DASDYQTVQI FYPSKDGTKI
460 470 480 490 500
PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGILA
510 520 530 540 550
VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI
560 570 580 590 600
NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG
610 620 630 640 650
CSDSKQHFEW LVKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL
660 670 680 690 700
KFIATLQYIV GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI
710
ARCLNVDWIP
Length:710
Mass (Da):80,700
Last modified:November 25, 2008 - v2
Checksum:i139072B990820B90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → F in CAA52605. (PubMed:7959018)Curated
Sequence conflicti4 – 41L → F in BAA04661. (PubMed:8089089)Curated
Sequence conflicti16 – 161V → I in BAA04661. (PubMed:8089089)Curated
Sequence conflicti245 – 2451R → C in BAA04661. (PubMed:8089089)Curated
Sequence conflicti298 – 2981T → A in BAA04661. (PubMed:8089089)Curated
Sequence conflicti319 – 3191R → W in CAA52605. (PubMed:7959018)Curated
Sequence conflicti440 – 4401I → L in BAA04661. (PubMed:8089089)Curated
Sequence conflicti459 – 4591G → S in BAA04661. (PubMed:8089089)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti351 – 3511L → V.
Corresponds to variant rs12192054 [ dbSNP | Ensembl ].
VAR_047790
Natural varianti706 – 7061V → I.1 Publication
Corresponds to variant rs1051484 [ dbSNP | Ensembl ].
VAR_047791

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74496 mRNA. Translation: CAA52605.1.
D21102 mRNA. Translation: BAA04661.1.
AY660966 mRNA. Translation: AAV70495.1.
AL590871, AL133406, AL139191 Genomic DNA. Translation: CAH72545.1.
AL139191, AL133406, AL590871 Genomic DNA. Translation: CAI21416.1.
AL133406, AL139191, AL590871 Genomic DNA. Translation: CAI42689.1.
CH471051 Genomic DNA. Translation: EAW48426.1.
BC030636 mRNA. Translation: AAH30636.1.
CCDSiCCDS5053.1.
PIRiI38134.
JC2257.
RefSeqiNP_002717.3. NM_002726.4.
UniGeneiHs.436564.

Genome annotation databases

EnsembliENST00000369110; ENSP00000358106; ENSG00000085377.
GeneIDi5550.
KEGGihsa:5550.
UCSCiuc003prc.3. human.

Polymorphism databases

DMDMi215273868.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74496 mRNA. Translation: CAA52605.1 .
D21102 mRNA. Translation: BAA04661.1 .
AY660966 mRNA. Translation: AAV70495.1 .
AL590871 , AL133406 , AL139191 Genomic DNA. Translation: CAH72545.1 .
AL139191 , AL133406 , AL590871 Genomic DNA. Translation: CAI21416.1 .
AL133406 , AL139191 , AL590871 Genomic DNA. Translation: CAI42689.1 .
CH471051 Genomic DNA. Translation: EAW48426.1 .
BC030636 mRNA. Translation: AAH30636.1 .
CCDSi CCDS5053.1.
PIRi I38134.
JC2257.
RefSeqi NP_002717.3. NM_002726.4.
UniGenei Hs.436564.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DDU X-ray 1.56 A 2-710 [» ]
ProteinModelPortali P48147.
SMRi P48147. Positions 2-710.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111541. 7 interactions.
IntActi P48147. 1 interaction.
MINTi MINT-5004282.
STRINGi 9606.ENSP00000358106.

Chemistry

BindingDBi P48147.
ChEMBLi CHEMBL3202.
DrugBanki DB00107. Oxytocin.
GuidetoPHARMACOLOGYi 2395.

Protein family/group databases

MEROPSi S09.001.

PTM databases

PhosphoSitei P48147.

Polymorphism databases

DMDMi 215273868.

Proteomic databases

MaxQBi P48147.
PaxDbi P48147.
PRIDEi P48147.

Protocols and materials databases

DNASUi 5550.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369110 ; ENSP00000358106 ; ENSG00000085377 .
GeneIDi 5550.
KEGGi hsa:5550.
UCSCi uc003prc.3. human.

Organism-specific databases

CTDi 5550.
GeneCardsi GC06M105725.
HGNCi HGNC:9358. PREP.
HPAi CAB025414.
HPA031388.
HPA031389.
HPA031390.
MIMi 600400. gene.
neXtProti NX_P48147.
PharmGKBi PA33730.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1505.
GeneTreei ENSGT00530000063426.
HOGENOMi HOG000238967.
HOVERGENi HBG007251.
InParanoidi P48147.
KOi K01322.
OMAi DYQTIQI.
OrthoDBi EOG78PV88.
PhylomeDBi P48147.
TreeFami TF300655.

Miscellaneous databases

EvolutionaryTracei P48147.
GeneWikii Prolyl_endopeptidase.
GenomeRNAii 5550.
NextBioi 21508.
PMAP-CutDB Q8N6D4.
PROi P48147.
SOURCEi Search...

Gene expression databases

Bgeei P48147.
CleanExi HS_PREP.
Genevestigatori P48147.

Family and domain databases

Gene3Di 2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view ]
PANTHERi PTHR11757. PTHR11757. 1 hit.
Pfami PF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view ]
PRINTSi PR00862. PROLIGOPTASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase."
    Vanhoof G., Goossens F., Hendriks L., De Meester I., Hendriks D., Vriend G., van Broeckhoven C., Scharpe S.
    Gene 149:363-366(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  2. "Molecular cloning and characterization of prolyl endopeptidase from human T cells."
    Shirasawa Y., Osawa T., Hirashima A.
    J. Biochem. 115:724-729(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-706.
  3. "cDNA cloning and recombinant expression of human brain prolyl oligopeptidase."
    Tarrago T., Giralt E.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Skin.
  7. "The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family."
    Goossens F., De Meester I., Vanhoof G., Hendriks D., Vriend G., Scharpe S.
    Eur. J. Biochem. 233:432-441(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 136-149, SUBUNIT, CHARACTERIZATION.
    Tissue: Lymphocyte.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP)."
    Haffner C.D., Diaz C.J., Miller A.B., Reid R.A., Madauss K.P., Hassell A., Hanlon M.H., Porter D.J., Becherer J.D., Carter L.H.
    Bioorg. Med. Chem. Lett. 18:4360-4363(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 2-710 IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiPPCE_HUMAN
AccessioniPrimary (citable) accession number: P48147
Secondary accession number(s): Q8N6D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 137 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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