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P36776 (LONM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lon protease homolog, mitochondrial

EC=3.4.21.-
Alternative name(s):
LONHs
Lon protease-like protein
Short name=LONP
Mitochondrial ATP-dependent protease Lon
Serine protease 15
Gene names
Name:LONP1
Synonyms:PRSS15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length959 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein. Ref.1 Ref.9 Ref.11 Ref.12

Subunit structure

Homohexamer or homoheptamer. Organized in a ring with a central cavity. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with PEO1 and mitochondrial DNA polymerase subunit POLG. Ref.10 Ref.15

Subcellular location

Mitochondrion matrix Ref.7.

Tissue specificity

Duodenum, heart, lung and liver, but not thymus.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Sequence caution

The sequence CAA52291.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

cellular response to oxidative stress

Inferred from direct assay Ref.12. Source: UniProtKB

chaperone-mediated protein complex assembly

Inferred from electronic annotation. Source: UniProtKB-HAMAP

misfolded or incompletely synthesized protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial DNA metabolic process

Non-traceable author statement Ref.10. Source: UniProtKB

mitochondrial genome maintenance

Non-traceable author statement Ref.12. Source: UniProtKB

mitochondrion organization

Inferred from mutant phenotype PubMed 15683722. Source: UniProtKB

oxidation-dependent protein catabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.10. Source: UniProtKB

proteolysis involved in cellular protein catabolic process

Inferred from direct assay Ref.12Ref.1. Source: UniProtKB

regulation of mitochondrial DNA replication

Inferred from electronic annotation. Source: UniProtKB-HAMAP

response to aluminum ion

Inferred from electronic annotation. Source: Ensembl

response to hormone

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from expression pattern PubMed 17418790. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

mitochondrial matrix

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

mitochondrion

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionADP binding

Inferred from direct assay Ref.10. Source: UniProtKB

ATP binding

Inferred from direct assay Ref.10. Source: UniProtKB

ATP-dependent peptidase activity

Inferred from direct assay Ref.12Ref.1. Source: UniProtKB

DNA polymerase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

G-quadruplex DNA binding

Inferred from direct assay PubMed 18174225. Source: UniProtKB

mitochondrial heavy strand promoter anti-sense binding

Inferred from direct assay Ref.8. Source: UniProtKB

mitochondrial light strand promoter anti-sense binding

Inferred from direct assay Ref.8. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

serine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded RNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6767Mitochondrion By similarity
Chain68 – 959892Lon protease homolog, mitochondrial HAMAP-Rule MF_03120
PRO_0000026734

Regions

Domain124 – 368245Lon
Nucleotide binding523 – 5308ATP By similarity

Sites

Active site8551 By similarity
Active site8981 By similarity

Natural variations

Natural variant871E → D.
Corresponds to variant rs34413649 [ dbSNP | Ensembl ].
VAR_051564
Natural variant2411R → Q.
Corresponds to variant rs11085147 [ dbSNP | Ensembl ].
VAR_051565
Natural variant8291A → T.
Corresponds to variant rs35804229 [ dbSNP | Ensembl ].
VAR_067708
Natural variant9111V → I. Ref.2 Ref.6
Corresponds to variant rs1062373 [ dbSNP | Ensembl ].
VAR_067709

Experimental info

Mutagenesis8551S → A: Lacks both ATPase and protease activity, but retains DNA binding activity. Ref.10
Sequence conflict1 – 5555MAAST…PWALW → MAGLWRRALATCDCGERRGA GCCGGRCWPRRGAGSHCSRS VVAPRPADLRRLSSLGTV in AAA61616. Ref.1
Sequence conflict65 – 662WR → CG in AAA61616. Ref.1
Sequence conflict257 – 2582EL → DV in AAA61616. Ref.1
Sequence conflict4561N → D in AAA61616. Ref.1
Sequence conflict5561A → T in AAA61616. Ref.1
Sequence conflict8421L → P in AAA61616. Ref.1
Sequence conflict8591T → A in AAA61616. Ref.1

Secondary structure

.............................. 959
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36776 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: B5E03D9C27C220FF

FASTA959106,489
        10         20         30         40         50         60 
MAASTGYVRL WGAARCWVLR RPMLAAAGGR VPTAAGAWLL RGQRTCDASP PWALWGRGPA 

        70         80         90        100        110        120 
IGGQWRGFWE ASSRGGGAFS GGEDASEGGA EEGAGGAGGS AGAGEGPVIT ALTPMTIPDV 

       130        140        150        160        170        180 
FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV ELLRRKVRLA QPYVGVFLKR DDSNESDVVE 

       190        200        210        220        230        240 
SLDEIYHTGT FAQIHEMQDL GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK 

       250        260        270        280        290        300 
RGKKEAEDEL SARHPAELAM EPTPELPAEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI 

       310        320        330        340        350        360 
RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNIPKRLY 

       370        380        390        400        410        420 
KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK 

       430        440        450        460        470        480 
FRERLKELVV PKHVMDVVDE ELSKLGLLDN HSSEFNVTRN YLDWLTSIPW GKYSNENLDL 

       490        500        510        520        530        540 
ARAQAVLEED HYGMEDVKKR ILEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL 

       550        560        570        580        590        600 
NREYFRFSVG GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLILID EVDKIGRGYQ 

       610        620        630        640        650        660 
GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG 

       670        680        690        700        710        720 
YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI KQYCRESGVR NLQKQVEKVL 

       730        740        750        760        770        780 
RKSAYKIVSG EAESVEVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV 

       790        800        810        820        830        840 
ETSLRRPQDK DAKGDKDGSL EVTGQLGEVM KESARIAYTF ARAFLMQHAP ANDYLVTSHI 

       850        860        870        880        890        900 
HLHVPEGATP KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKIL PVGGIKEKTI 

       910        920        930        940        950 
AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE QAEALAVER 

« Hide

References

« Hide 'large scale' references
[1]"A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease."
Wang N., Gottesman S., Willingham M.C., Gottesman M.M., Maurizi M.R.
Proc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Brain.
[2]"Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-911.
[3]"Chromosomal mapping and genomic organization of the ATP-dependent human LON protease gene."
Huang N.N., Maurizi M.R., Torres R.R., Polymeropoulos M.H., Lennon G.G., Gottesman M.M.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Eye.
[6]"Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases."
Amerik A.Y., Petukhova G.V., Grigorenko V.G., Lykov I.P., Yarovoi S.V., Lipkin V.M., Gorbalenya A.E.
FEBS Lett. 340:25-28(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-959, VARIANT ILE-911.
Tissue: Brain.
[7]"Synthesis, processing, and localization of human Lon protease."
Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.
J. Biol. Chem. 269:29308-29313(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner."
Fu G.K., Markovitz D.M.
Biochemistry 37:1905-1909(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[9]"Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism."
Bota D.A., Davies K.J.
Nat. Cell Biol. 4:674-680(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate."
Liu T., Lu B., Lee I., Ondrovicova G., Kutejova E., Suzuki C.K.
J. Biol. Chem. 279:13902-13910(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, MUTAGENESIS OF SER-855, SUBUNIT, INTERACTION WITH PEO1 AND POLG.
[11]"Cleavage site selection within a folded substrate by the ATP-dependent lon protease."
Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D., Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.
J. Biol. Chem. 280:25103-25110(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance."
Lu B., Yadav S., Shah P.G., Liu T., Tian B., Pukszta S., Villaluna N., Kutejova E., Newlon C.S., Santos J.H., Suzuki C.K.
J. Biol. Chem. 282:17363-17374(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING.
[13]"Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors."
Granot Z., Kobiler O., Melamed-Book N., Eimerl S., Bahat A., Lu B., Braun S., Maurizi M.R., Suzuki C.K., Oppenheim A.B., Orly J.
Mol. Endocrinol. 21:2164-2177(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity."
Garcia-Nafria J., Ondrovicova G., Blagova E., Levdikov V.M., Bauer J.A., Suzuki C.K., Kutejova E., Wilkinson A.J., Wilson K.S.
Protein Sci. 19:987-999(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 753-959, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02389 mRNA. Translation: AAA61616.1.
HQ204946 Genomic DNA. Translation: ADP90374.1.
HQ204947 Genomic DNA. Translation: ADP90375.1.
HQ204948 Genomic DNA. Translation: ADP90376.1.
HQ204949 Genomic DNA. Translation: ADP90377.1.
HQ204950 Genomic DNA. Translation: ADP90378.1.
HQ204951 Genomic DNA. Translation: ADP90379.1.
HQ204952 Genomic DNA. Translation: ADP90380.1.
HQ204953 Genomic DNA. Translation: ADP90381.1.
HQ204954 Genomic DNA. Translation: ADP90382.1.
HQ204955 Genomic DNA. Translation: ADP90383.1.
HQ204956 Genomic DNA. Translation: ADP90384.1.
HQ204957 Genomic DNA. Translation: ADP90385.1.
HQ204958 Genomic DNA. Translation: ADP90386.1.
HQ204959 Genomic DNA. Translation: ADP90387.1.
HQ204960 Genomic DNA. Translation: ADP90388.1.
HQ204961 Genomic DNA. Translation: ADP90389.1.
HQ204962 Genomic DNA. Translation: ADP90390.1.
HQ204963 Genomic DNA. Translation: ADP90391.1.
HQ204964 Genomic DNA. Translation: ADP90392.1.
HQ204965 Genomic DNA. Translation: ADP90393.1.
HQ204966 Genomic DNA. Translation: ADP90394.1.
HQ204968 Genomic DNA. Translation: ADP90396.1.
HQ204969 Genomic DNA. Translation: ADP90397.1.
HQ204970 Genomic DNA. Translation: ADP90398.1.
HQ204971 Genomic DNA. Translation: ADP90399.1.
HQ204972 Genomic DNA. Translation: ADP90400.1.
HQ204973 Genomic DNA. Translation: ADP90401.1.
HQ204974 Genomic DNA. Translation: ADP90402.1.
HQ204975 Genomic DNA. Translation: ADP90403.1.
HQ204976 Genomic DNA. Translation: ADP90404.1.
HQ204977 Genomic DNA. Translation: ADP90405.1.
HQ204978 Genomic DNA. Translation: ADP90406.1.
HQ204979 Genomic DNA. Translation: ADP90407.1.
HQ204980 Genomic DNA. Translation: ADP90408.1.
HQ204981 Genomic DNA. Translation: ADP90409.1.
HQ204982 Genomic DNA. Translation: ADP90410.1.
HQ204983 Genomic DNA. Translation: ADP90411.1.
HQ204984 Genomic DNA. Translation: ADP90412.1.
HQ204985 Genomic DNA. Translation: ADP90413.1.
AF059309 expand/collapse EMBL AC list , AF059296, AF059297, AF059298, AF059299, AF059300, AF059301, AF059302, AF059303, AF059304, AF059305, AF059306, AF059307, AF059308 Genomic DNA. Translation: AAD24414.1.
CH471139 Genomic DNA. Translation: EAW69151.1.
CH471139 Genomic DNA. Translation: EAW69154.1.
BC000235 mRNA. Translation: AAH00235.1.
X74215 mRNA. Translation: CAA52291.1. Different initiation.
X76040 mRNA. Translation: CAA53625.1.
PIRS42366.
S57342.
RefSeqNP_001263408.1. NM_001276479.1.
NP_001263409.1. NM_001276480.1.
NP_004784.2. NM_004793.3.
UniGeneHs.350265.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X36X-ray2.00A/B/C/D/E/F753-959[»]
ProteinModelPortalP36776.
SMRP36776. Positions 288-408, 419-953.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114762. 29 interactions.
IntActP36776. 20 interactions.
MINTMINT-3014242.
STRING9606.ENSP00000353826.

Protein family/group databases

MEROPSS16.002.

PTM databases

PhosphoSiteP36776.

Polymorphism databases

DMDM12644239.

Proteomic databases

PaxDbP36776.
PRIDEP36776.

Protocols and materials databases

DNASU9361.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360614; ENSP00000353826; ENSG00000196365.
GeneID9361.
KEGGhsa:9361.
UCSCuc002mcx.4. human.

Organism-specific databases

CTD9361.
GeneCardsGC19M005691.
HGNCHGNC:9479. LONP1.
HPAHPA002034.
HPA002192.
MIM605490. gene.
neXtProtNX_P36776.
PharmGKBPA162394145.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0466.
HOGENOMHOG000261409.
HOVERGENHBG000798.
InParanoidP36776.
KOK08675.
OMARSAENFG.
OrthoDBEOG7HQN7C.
PhylomeDBP36776.
TreeFamTF105001.

Enzyme and pathway databases

BRENDA3.4.21.53. 2681.

Gene expression databases

ArrayExpressP36776.
BgeeP36776.
CleanExHS_LONP1.
GenevestigatorP36776.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_03120. lonm_euk.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027503. Lonm_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERPTHR10046. PTHR10046. 1 hit.
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFPIRSF001174. Lon_proteas. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00763. lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLONP1. human.
EvolutionaryTraceP36776.
GeneWikiLONP1.
GenomeRNAi9361.
NextBio35055.
PROP36776.
SOURCESearch...

Entry information

Entry nameLONM_HUMAN
AccessionPrimary (citable) accession number: P36776
Secondary accession number(s): D6W635 expand/collapse secondary AC list , E5KMH8, P36777, Q9UQ95
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM