Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10619 (PPGB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal protective protein

EC=3.4.16.5
Alternative name(s):
Carboxypeptidase C
Carboxypeptidase L
Cathepsin A
Protective protein cathepsin A
Short name=PPCA
Protective protein for beta-galactosidase
Gene names
Name:CTSA
Synonyms:PPGB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. Ref.7

Catalytic activity

Release of a C-terminal amino acid with broad specificity.

Subunit structure

Heterodimer of a 32 kDa chain and a 20 kDa chain; disulfide-linked.

Subcellular location

Lysosome.

Involvement in disease

Galactosialidosis (GSL) [MIM:256540]: A lysosomal storage disease associated with a combined deficiency of beta-galactosidase and neuraminidase, secondary to a defect in cathepsin A. All patients have clinical manifestations typical of a lysosomal disorder, such as coarse facies, cherry red spots, vertebral changes, foam cells in the bone marrow, and vacuolated lymphocytes. Three phenotypic subtypes are recognized. The early infantile form is associated with fetal hydrops, edema, ascites, visceromegaly, skeletal dysplasia, and early death. The late infantile type is characterized by hepatosplenomegaly, growth retardation, cardiac involvement, and a normal or mildly affected mental state. The juvenile/adult form is characterized by myoclonus, ataxia, angiokeratoma, mental retardation, neurologic deterioration, absence of visceromegaly, and long survival.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the peptidase S10 family.

Sequence caution

The sequence CAI20248.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycosphingolipid metabolic process

Traceable author statement. Source: Reactome

intracellular protein transport

Traceable author statement PubMed 1387645. Source: ProtInc

positive regulation of catalytic activity

Traceable author statement PubMed 3107551. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Traceable author statement PubMed 1387645. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functioncarboxypeptidase activity

Traceable author statement PubMed 2244901. Source: ProtInc

enzyme activator activity

Traceable author statement PubMed 3107551. Source: ProtInc

serine-type carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10619-1)

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.
Isoform 2 (identifier: P10619-2)

The sequence of this isoform differs from the canonical sequence as follows:
     102-118: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.5 Ref.6
Chain29 – 480452Lysosomal protective protein
PRO_0000004274
Chain29 – 326298Lysosomal protective protein 32 kDa chain
PRO_0000004275
Chain327 – 480154Lysosomal protective protein 20 kDa chain
PRO_0000004276

Sites

Active site1781
Active site4001 By similarity
Active site4571

Amino acid modifications

Glycosylation1451N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation3331N-linked (GlcNAc...) Ref.9
Disulfide bond88 ↔ 362
Disulfide bond240 ↔ 256
Disulfide bond241 ↔ 246
Disulfide bond281 ↔ 331

Natural variations

Alternative sequence102 – 11817Missing in isoform 2.
VSP_054832
Natural variant491Q → R in GSL. Ref.13
VAR_001385
Natural variant511S → Y in GSL. Ref.14
VAR_063018
Natural variant651W → R in GSL. Ref.13
Corresponds to variant rs28934603 [ dbSNP | Ensembl ].
VAR_001386
Natural variant901S → L in GSL. Ref.13
VAR_001387
Natural variant1321V → M in GSL. Ref.14
VAR_063019
Natural variant2361L → P in GSL. Ref.14
VAR_063020
Natural variant2491Y → N in GSL; small amount of activity. Ref.13 Ref.14
VAR_001388
Natural variant3951Y → C in GSL; loss of activity. Ref.13
VAR_001389
Natural variant4061M → T in GSL. Ref.14
VAR_063021
Natural variant4391G → S in GSL. Ref.14
VAR_063022
Natural variant4401F → V in GSL. Ref.12 Ref.14
VAR_001390
Natural variant4531K → E in GSL. Ref.15
VAR_063023

Experimental info

Mutagenesis1781S → A: Inactivates the enzyme.
Mutagenesis4571H → Q: Inactivates the enzyme.
Sequence conflict191Missing in AAH00597. Ref.4
Sequence conflict561G → S in AAA36476. Ref.1

Secondary structure

................................................................................ 480
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: 46B737DEE775C508

FASTA48054,466
        10         20         30         40         50         60 
MIRAAPPPLF LLLLLLLLLV SWASRGEAAP DQDEIQRLPG LAKQPSFRQY SGYLKGSGSK 

        70         80         90        100        110        120 
HLHYWFVESQ KDPENSPVVL WLNGGPGCSS LDGLLTEHGP FLVQPDGVTL EYNPYSWNLI 

       130        140        150        160        170        180 
ANVLYLESPA GVGFSYSDDK FYATNDTEVA QSNFEALQDF FRLFPEYKNN KLFLTGESYA 

       190        200        210        220        230        240 
GIYIPTLAVL VMQDPSMNLQ GLAVGNGLSS YEQNDNSLVY FAYYHGLLGN RLWSSLQTHC 

       250        260        270        280        290        300 
CSQNKCNFYD NKDLECVTNL QEVARIVGNS GLNIYNLYAP CAGGVPSHFR YEKDTVVVQD 

       310        320        330        340        350        360 
LGNIFTRLPL KRMWHQALLR SGDKVRMDPP CTNTTAASTY LNNPYVRKAL NIPEQLPQWD 

       370        380        390        400        410        420 
MCNFLVNLQY RRLYRSMNSQ YLKLLSSQKY QILLYNGDVD MACNFMGDEW FVDSLNQKME 

       430        440        450        460        470        480 
VQRRPWLVKY GDSGEQIAGF VKEFSHIAFL TIKGAGHMVP TDKPLAAFTM FSRFLNKQPY 

« Hide

Isoform 2 [UniParc].

Checksum: 7342A76945E40684
Show »

FASTA46352,489

References

« Hide 'large scale' references
[1]"Expression of cDNA encoding the human 'protective protein' associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases."
Galjart N.J., Gillemans N., Harris A., van de Horst G.T.J., Verheijen F.W., Galjaard H., D'Azzo A.
Cell 54:755-764(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Placenta and Skin.
[5]"A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal 'protective protein'."
Jackman H.L., Tan F., Tamei H., Beurling-Harbury C., Li X.-Y., Skidgel R.A., Erdoes E.G.
J. Biol. Chem. 265:11265-11272(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-53 AND 327-351.
Tissue: Platelet.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-37.
Tissue: Platelet.
[7]"Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function."
Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J., D'Azzo A.
J. Biol. Chem. 266:14754-14762(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS.
[8]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145.
Tissue: Platelet.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-333.
Tissue: Liver.
[10]"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].
[11]"Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism."
Rudenko G., Bonten E., D'Azzo A., Hol W.G.J.
Structure 3:1249-1259(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[12]"A mutation in a mild form of galactosialidosis impairs dimerization of the protective protein and renders it unstable."
Zhou X.Y., Galjart N.J., Willemsen R., Gillemans N., Galjaard H., D'Azzo A.
EMBO J. 10:4041-4048(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSL VAL-440.
[13]"Protective protein gene mutations in galactosialidosis."
Shimmoto M., Fukuhara Y., Itoh K., Oshima A., Sakuraba H., Suzuki Y.
J. Clin. Invest. 91:2393-2398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSL ARG-49; ARG-65; LEU-90; ASN-249 AND CYS-395.
[14]"Molecular and biochemical analysis of protective protein/cathepsin A mutations: correlation with clinical severity in galactosialidosis."
Zhou X.Y., van der Spoel A., Rottier R., Hale G., Willemsen R., Berry G.T., Strisciuglio P., Morrone A., Zammarchi E., Andria G., d'Azzo A.
Hum. Mol. Genet. 5:1977-1987(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSL TYR-51; MET-132; PRO-236; ASN-249; THR-406; SER-439 AND VAL-440.
[15]"Structural and functional study of K453E mutant protective protein/cathepsin A causing the late infantile form of galactosialidosis."
Takiguchi K., Itoh K., Shimmoto M., Ozand P.T., Doi H., Sakuraba H.
J. Hum. Genet. 45:200-206(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSL GLU-453.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22960 mRNA. Translation: AAA36476.1.
AK312898 mRNA. Translation: BAG35745.1.
AL008726 Genomic DNA. Translation: CAA15501.1.
AL008726 Genomic DNA. Translation: CAI20248.1. Different initiation.
BC000597 mRNA. Translation: AAH00597.1.
BC093009 mRNA. Translation: AAH93009.1.
CCDSCCDS46609.1.
PIRA31589.
RefSeqNP_000299.2. NM_000308.2.
NP_001121167.1. NM_001127695.1. [P10619-1]
NP_001161066.1. NM_001167594.1.
UniGeneHs.609336.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVYX-ray2.20A/B29-480[»]
3BP4X-ray1.85C2-10[»]
3BP7X-ray1.80C2-10[»]
3BXNX-ray1.86C2-10[»]
4AZ0X-ray2.17A29-326[»]
B327-480[»]
4AZ3X-ray2.04A29-326[»]
B327-480[»]
4CI9X-ray1.58A29-480[»]
4CIAX-ray1.98A29-480[»]
4CIBX-ray1.89A29-480[»]
4MWSX-ray2.80A/B29-480[»]
4MWTX-ray3.85A/B29-480[»]
ProteinModelPortalP10619.
SMRP10619. Positions 29-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111472. 19 interactions.
IntActP10619. 8 interactions.
MINTMINT-3007366.
STRING9606.ENSP00000361562.

Chemistry

BindingDBP10619.
ChEMBLCHEMBL6115.

Protein family/group databases

MEROPSS10.002.

PTM databases

PhosphoSiteP10619.

Polymorphism databases

DMDM20178316.

2D gel databases

OGPP10619.

Proteomic databases

MaxQBP10619.
PaxDbP10619.
PRIDEP10619.

Protocols and materials databases

DNASU5476.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000191018; ENSP00000191018; ENSG00000064601.
ENST00000372459; ENSP00000361537; ENSG00000064601.
GeneID5476.
KEGGhsa:5476.
UCSCuc002xqh.3. human. [P10619-1]

Organism-specific databases

CTD5476.
GeneCardsGC20P044519.
HGNCHGNC:9251. CTSA.
HPACAB024930.
HPA031068.
MIM256540. phenotype.
613111. gene.
neXtProtNX_P10619.
Orphanet351. Galactosialidosis.
PharmGKBPA33572.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2939.
HOVERGENHBG053652.
InParanoidP10619.
KOK13289.
OrthoDBEOG7KQ21H.
PhylomeDBP10619.
TreeFamTF323769.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.
SignaLinkP10619.

Gene expression databases

ArrayExpressP10619.
BgeeP10619.
CleanExHS_CTSA.
GenevestigatorP10619.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSA. human.
EvolutionaryTraceP10619.
GeneWikiCathepsin_A.
GenomeRNAi5476.
NextBio21202.
PROP10619.
SOURCESearch...

Entry information

Entry namePPGB_HUMAN
AccessionPrimary (citable) accession number: P10619
Secondary accession number(s): B2R798 expand/collapse secondary AC list , Q561W6, Q5JZH1, Q96KJ2, Q9BR08, Q9BW68
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 178 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 20

Human chromosome 20: entries, gene names and cross-references to MIM