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Protein

Lysosomal protective protein

Gene

CTSA

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

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei178 – 1781
Active sitei400 – 4001By similarity
Active sitei457 – 4571

GO - Molecular functioni

  1. carboxypeptidase activity Source: ProtInc
  2. enzyme activator activity Source: ProtInc
  3. serine-type carboxypeptidase activity Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. glycosphingolipid metabolic process Source: Reactome
  4. intracellular protein transport Source: ProtInc
  5. positive regulation of catalytic activity Source: GOC
  6. post-translational protein modification Source: Reactome
  7. protein N-linked glycosylation via asparagine Source: Reactome
  8. small molecule metabolic process Source: Reactome
  9. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.16.5. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121399. MHC class II antigen presentation.
REACT_264366. Sialic acid metabolism.
SignaLinkiP10619.

Protein family/group databases

MEROPSiS10.002.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 2 chains:
Gene namesi
Name:CTSA
Synonyms:PPGB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9251. CTSA.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. extracellular vesicular exosome Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: HPA
  4. lysosomal lumen Source: Reactome
  5. lysosome Source: UniProtKB
  6. membrane Source: UniProtKB
  7. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Galactosialidosis (GSL)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:256540
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491Q → R in GSL. 1 Publication
VAR_001385
Natural varianti51 – 511S → Y in GSL. 1 Publication
VAR_063018
Natural varianti65 – 651W → R in GSL. 1 Publication
Corresponds to variant rs28934603 [ dbSNP | Ensembl ].
VAR_001386
Natural varianti90 – 901S → L in GSL. 1 Publication
VAR_001387
Natural varianti132 – 1321V → M in GSL. 1 Publication
VAR_063019
Natural varianti236 – 2361L → P in GSL. 1 Publication
VAR_063020
Natural varianti249 – 2491Y → N in GSL; small amount of activity. 2 Publications
VAR_001388
Natural varianti395 – 3951Y → C in GSL; loss of activity. 1 Publication
VAR_001389
Natural varianti406 – 4061M → T in GSL. 1 Publication
VAR_063021
Natural varianti439 – 4391G → S in GSL. 1 Publication
VAR_063022
Natural varianti440 – 4401F → V in GSL. 2 Publications
VAR_001390
Natural varianti453 – 4531K → E in GSL. 1 Publication
VAR_063023

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi178 – 1781S → A: Inactivates the enzyme. 1 Publication
Mutagenesisi457 – 4571H → Q: Inactivates the enzyme. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi256540. phenotype.
Orphaneti351. Galactosialidosis.
PharmGKBiPA33572.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28282 PublicationsAdd
BLAST
Chaini29 – 480452Lysosomal protective proteinPRO_0000004274Add
BLAST
Chaini29 – 326298Lysosomal protective protein 32 kDa chainPRO_0000004275Add
BLAST
Chaini327 – 480154Lysosomal protective protein 20 kDa chainPRO_0000004276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi88 ↔ 362
Glycosylationi145 – 1451N-linked (GlcNAc...)2 Publications
Disulfide bondi240 ↔ 256
Disulfide bondi241 ↔ 246
Disulfide bondi281 ↔ 331
Glycosylationi333 – 3331N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP10619.
PaxDbiP10619.
PRIDEiP10619.

2D gel databases

OGPiP10619.

PTM databases

PhosphoSiteiP10619.

Expressioni

Gene expression databases

BgeeiP10619.
CleanExiHS_CTSA.
ExpressionAtlasiP10619. baseline and differential.
GenevestigatoriP10619.

Organism-specific databases

HPAiCAB024930.
HPA031068.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi111472. 23 interactions.
IntActiP10619. 8 interactions.
MINTiMINT-3007366.
STRINGi9606.ENSP00000361562.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 333Combined sources
Beta strandi41 – 433Combined sources
Beta strandi49 – 557Combined sources
Beta strandi60 – 678Combined sources
Turni73 – 753Combined sources
Beta strandi78 – 825Combined sources
Turni85 – 873Combined sources
Helixi91 – 966Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi110 – 1123Combined sources
Helixi117 – 1193Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi136 – 1394Combined sources
Helixi146 – 16318Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi172 – 1776Combined sources
Helixi180 – 19213Combined sources
Beta strandi199 – 2068Combined sources
Helixi211 – 22414Combined sources
Helixi230 – 24011Combined sources
Helixi254 – 26815Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi286 – 2927Combined sources
Beta strandi295 – 2984Combined sources
Helixi315 – 3173Combined sources
Helixi318 – 3214Combined sources
Beta strandi324 – 3274Combined sources
Helixi335 – 3417Combined sources
Helixi344 – 3496Combined sources
Helixi364 – 3696Combined sources
Beta strandi375 – 3773Combined sources
Helixi378 – 3869Combined sources
Beta strandi391 – 3977Combined sources
Beta strandi401 – 4033Combined sources
Helixi405 – 41410Combined sources
Beta strandi424 – 4296Combined sources
Helixi431 – 4333Combined sources
Beta strandi435 – 44410Combined sources
Beta strandi447 – 4526Combined sources
Helixi459 – 4624Combined sources
Helixi464 – 47512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10619.
SMRiP10619. Positions 29-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10619.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
GeneTreeiENSGT00770000120552.
HOVERGENiHBG053652.
InParanoidiP10619.
KOiK13289.
OrthoDBiEOG7KQ21H.
PhylomeDBiP10619.
TreeFamiTF323769.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 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: P10619-1) [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
MIRAAPPPLF LLLLLLLLLV SWASRGEAAP DQDEIQRLPG LAKQPSFRQY
60 70 80 90 100
SGYLKGSGSK HLHYWFVESQ KDPENSPVVL WLNGGPGCSS LDGLLTEHGP
110 120 130 140 150
FLVQPDGVTL EYNPYSWNLI ANVLYLESPA GVGFSYSDDK FYATNDTEVA
160 170 180 190 200
QSNFEALQDF FRLFPEYKNN KLFLTGESYA GIYIPTLAVL VMQDPSMNLQ
210 220 230 240 250
GLAVGNGLSS YEQNDNSLVY FAYYHGLLGN RLWSSLQTHC CSQNKCNFYD
260 270 280 290 300
NKDLECVTNL QEVARIVGNS GLNIYNLYAP CAGGVPSHFR YEKDTVVVQD
310 320 330 340 350
LGNIFTRLPL KRMWHQALLR SGDKVRMDPP CTNTTAASTY LNNPYVRKAL
360 370 380 390 400
NIPEQLPQWD MCNFLVNLQY RRLYRSMNSQ YLKLLSSQKY QILLYNGDVD
410 420 430 440 450
MACNFMGDEW FVDSLNQKME VQRRPWLVKY GDSGEQIAGF VKEFSHIAFL
460 470 480
TIKGAGHMVP TDKPLAAFTM FSRFLNKQPY
Length:480
Mass (Da):54,466
Last modified:April 16, 2002 - v2
Checksum:i46B737DEE775C508
GO
Isoform 2 (identifier: P10619-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-118: Missing.

Note: Gene prediction based on EST data.

Show »
Length:463
Mass (Da):52,489
Checksum:i7342A76945E40684
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191Missing in AAH00597 (PubMed:15489334).Curated
Sequence conflicti56 – 561G → S in AAA36476 (PubMed:3136930).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491Q → R in GSL. 1 Publication
VAR_001385
Natural varianti51 – 511S → Y in GSL. 1 Publication
VAR_063018
Natural varianti65 – 651W → R in GSL. 1 Publication
Corresponds to variant rs28934603 [ dbSNP | Ensembl ].
VAR_001386
Natural varianti90 – 901S → L in GSL. 1 Publication
VAR_001387
Natural varianti132 – 1321V → M in GSL. 1 Publication
VAR_063019
Natural varianti236 – 2361L → P in GSL. 1 Publication
VAR_063020
Natural varianti249 – 2491Y → N in GSL; small amount of activity. 2 Publications
VAR_001388
Natural varianti395 – 3951Y → C in GSL; loss of activity. 1 Publication
VAR_001389
Natural varianti406 – 4061M → T in GSL. 1 Publication
VAR_063021
Natural varianti439 – 4391G → S in GSL. 1 Publication
VAR_063022
Natural varianti440 – 4401F → V in GSL. 2 Publications
VAR_001390
Natural varianti453 – 4531K → E in GSL. 1 Publication
VAR_063023

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei102 – 11817Missing in isoform 2. CuratedVSP_054832Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS46609.1. [P10619-1]
PIRiA31589.
RefSeqiNP_000299.2. NM_000308.2.
NP_001121167.1. NM_001127695.1. [P10619-1]
NP_001161066.1. NM_001167594.1.
UniGeneiHs.609336.

Genome annotation databases

EnsembliENST00000191018; ENSP00000191018; ENSG00000064601. [P10619-1]
ENST00000372459; ENSP00000361537; ENSG00000064601. [P10619-1]
GeneIDi5476.
KEGGihsa:5476.
UCSCiuc002xqh.3. human. [P10619-1]

Polymorphism databases

DMDMi20178316.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS46609.1. [P10619-1]
PIRiA31589.
RefSeqiNP_000299.2. NM_000308.2.
NP_001121167.1. NM_001127695.1. [P10619-1]
NP_001161066.1. NM_001167594.1.
UniGeneiHs.609336.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10619.
SMRiP10619. Positions 29-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111472. 23 interactions.
IntActiP10619. 8 interactions.
MINTiMINT-3007366.
STRINGi9606.ENSP00000361562.

Chemistry

BindingDBiP10619.
ChEMBLiCHEMBL6115.
GuidetoPHARMACOLOGYi1581.

Protein family/group databases

MEROPSiS10.002.

PTM databases

PhosphoSiteiP10619.

Polymorphism databases

DMDMi20178316.

2D gel databases

OGPiP10619.

Proteomic databases

MaxQBiP10619.
PaxDbiP10619.
PRIDEiP10619.

Protocols and materials databases

DNASUi5476.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000191018; ENSP00000191018; ENSG00000064601. [P10619-1]
ENST00000372459; ENSP00000361537; ENSG00000064601. [P10619-1]
GeneIDi5476.
KEGGihsa:5476.
UCSCiuc002xqh.3. human. [P10619-1]

Organism-specific databases

CTDi5476.
GeneCardsiGC20P044519.
HGNCiHGNC:9251. CTSA.
HPAiCAB024930.
HPA031068.
MIMi256540. phenotype.
613111. gene.
neXtProtiNX_P10619.
Orphaneti351. Galactosialidosis.
PharmGKBiPA33572.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2939.
GeneTreeiENSGT00770000120552.
HOVERGENiHBG053652.
InParanoidiP10619.
KOiK13289.
OrthoDBiEOG7KQ21H.
PhylomeDBiP10619.
TreeFamiTF323769.

Enzyme and pathway databases

BRENDAi3.4.16.5. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121399. MHC class II antigen presentation.
REACT_264366. Sialic acid metabolism.
SignaLinkiP10619.

Miscellaneous databases

ChiTaRSiCTSA. human.
EvolutionaryTraceiP10619.
GeneWikiiCathepsin_A.
GenomeRNAii5476.
NextBioi21202.
PROiP10619.
SOURCEiSearch...

Gene expression databases

BgeeiP10619.
CleanExiHS_CTSA.
ExpressionAtlasiP10619. baseline and differential.
GenevestigatoriP10619.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1987) [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.
    , 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(2003) [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.
    , 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(2000) [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(2003) [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(1989) [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(2002) [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(1990) [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(2005) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-333.
    Tissue: Liver.
  10. 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(1994) [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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GSL VAL-440.
  13. 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(1995) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GSL GLU-453.

Entry informationi

Entry nameiPPGB_HUMAN
AccessioniPrimary (citable) accession number: P10619
Secondary accession number(s): B2R798
, Q561W6, Q5JZH1, Q96KJ2, Q9BR08, Q9BW68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 16, 2002
Last modified: April 1, 2015
This is version 186 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 20
    Human chromosome 20: 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

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 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.