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Protein

Prosaposin

Gene

PSAP

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

Functioni

Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.
Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.
Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).
Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.By similarity1 Publication
Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei215Not glycosylated; in variant MLD-SAPB Ile-2171

GO - Molecular functioni

  • enzyme activator activity Source: ProtInc
  • G-protein coupled receptor binding Source: GO_Central
  • lipid binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

TCDBi1.C.35.2.1. the amoebapore (amoebapore) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Prosaposin
Alternative name(s):
Proactivator polypeptide
Cleaved into the following 5 chains:
Alternative name(s):
Protein A
Alternative name(s):
Cerebroside sulfate activator
Short name:
CSAct
Dispersin
Sphingolipid activator protein 1
Short name:
SAP-1
Sulfatide/GM1 activator
Alternative name(s):
A1 activator
Co-beta-glucosidase
Glucosylceramidase activator
Sphingolipid activator protein 2
Short name:
SAP-2
Alternative name(s):
Component C
Protein C
Gene namesi
Name:PSAP
Synonyms:GLBA, SAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9498. PSAP.

Subcellular locationi

Prosaposin :
  • Secreted By similarity

  • Note: Secreted as a fully glycosylated 70 kDa protein composed of complex glycans.By similarity

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: ProtInc
  • lysosomal lumen Source: Reactome
  • lysosomal membrane Source: Reactome
  • lysosome Source: UniProtKB
  • mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Involvement in diseasei

Combined saposin deficiency (CSAPD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDue to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.
See also OMIM:611721
Leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn atypical form of metachromatic leukodystrophy. It is characterized by tissue accumulation of cerebroside-3-sulfate, demyelination, periventricular white matter abnormalities, peripheral neuropathy. Additional neurological features include dysarthria, ataxic gait, psychomotor regression, seizures, cognitive decline and spastic quadriparesis.
See also OMIM:249900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031823215N → H in MLD-SAPB; reduces the intracellular activity of the protein significantly. 1 PublicationCorresponds to variant rs121918107dbSNPEnsembl.1
Natural variantiVAR_031899215N → K in MLD-SAPB. 1 PublicationCorresponds to variant rs770171865dbSNPEnsembl.1
Natural variantiVAR_006943217T → I in MLD-SAPB; juvenile; affects glycosylation at N-215. 2 PublicationsCorresponds to variant rs121918103dbSNPEnsembl.1
Natural variantiVAR_006944241C → S in MLD-SAPB; severe. 1 PublicationCorresponds to variant rs1130793dbSNPEnsembl.1
Gaucher disease, atypical, due to saposin C deficiency (AGD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by marked glucosylceramide accumulation in the spleen without having a deficiency of glucosylceramide-beta glucosidase characteristic of classic Gaucher disease. Gaucher disease is a lysosomal storage disorder characterized by skeletal deterioration, hepatosplenomegaly, and organ dysfunction. There are several subtypes based on the presence and severity of neurological involvement.
See also OMIM:610539
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042441349L → P in AGD. 1 PublicationCorresponds to variant rs121918110dbSNPEnsembl.1
Natural variantiVAR_006945388C → F in AGD. 1 Publication1
Krabbe disease, atypical, due to saposin A deficiency (AKRD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of galactosylceramide metabolism. Clinical features include neurologic regression around age 3 months, loss of spontaneous movements, hyporeflexia, generalized brain atrophy, and diffuse white matter dysmyelination.
See also OMIM:611722
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04244070Missing in AKRD. 1 Publication1

Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi240I → C: Strongly decreases stimulation of cerebroside sulfate hydrolysis. 1 Publication1

Keywords - Diseasei

Disease mutation, Gangliosidosis, Gaucher disease, Leukodystrophy, Metachromatic leukodystrophy

Organism-specific databases

DisGeNETi5660.
MalaCardsiPSAP.
MIMi249900. phenotype.
610539. phenotype.
611721. phenotype.
611722. phenotype.
OpenTargetsiENSG00000197746.
Orphaneti309252. Atypical Gaucher disease due to saposin C deficiency.
139406. Encephalopathy due to prosaposin deficiency.
206436. Infantile Krabbe disease.
309271. Metachromatic leukodystrophy, adult form.
309263. Metachromatic leukodystrophy, juvenile form.
309256. Metachromatic leukodystrophy, late infantile form.
PharmGKBiPA33845.

Chemistry databases

ChEMBLiCHEMBL3580523.

Polymorphism and mutation databases

BioMutaiPSAP.
DMDMi134218.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Combined sources2 PublicationsAdd BLAST16
ChainiPRO_000042477417 – 524Prosaposin1 PublicationAdd BLAST508
PropeptideiPRO_000003161617 – 59CuratedAdd BLAST43
ChainiPRO_000003161760 – 142Saposin-A1 PublicationAdd BLAST83
PropeptideiPRO_0000031618143 – 194CuratedAdd BLAST52
ChainiPRO_0000031619195 – 274Saposin-B-Val2 PublicationsAdd BLAST80
ChainiPRO_0000031620195 – 273Saposin-B1 PublicationAdd BLAST79
PropeptideiPRO_0000031621275 – 310CuratedAdd BLAST36
ChainiPRO_0000031622311 – 390Saposin-C1 PublicationAdd BLAST80
PropeptideiPRO_0000031623393 – 404CuratedAdd BLAST12
ChainiPRO_0000031624405 – 486Saposin-D1 PublicationAdd BLAST82
PropeptideiPRO_0000031625487 – 524CuratedAdd BLAST38

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi63 ↔ 1381 Publication
Disulfide bondi66 ↔ 1321 Publication
Glycosylationi80N-linked (GlcNAc...)PROSITE-ProRule annotation3 Publications1
Disulfide bondi94 ↔ 1061 Publication
Glycosylationi101N-linked (GlcNAc...)PROSITE-ProRule annotation3 Publications1
Disulfide bondi198 ↔ 2711 Publication
Disulfide bondi201 ↔ 2651 Publication
GlycosylationiCAR_000176215N-linked (GlcNAc...) (complex)PROSITE-ProRule annotation1 Publication1
Disulfide bondi230 ↔ 241PROSITE-ProRule annotation1 Publication
Disulfide bondi315 ↔ 388PROSITE-ProRule annotation1 Publication
Disulfide bondi318 ↔ 382PROSITE-ProRule annotation1 Publication
Glycosylationi332N-linked (GlcNAc...)PROSITE-ProRule annotation2 Publications1
Disulfide bondi346 ↔ 357PROSITE-ProRule annotation1 Publication
Disulfide bondi409 ↔ 4821 Publication
Disulfide bondi412 ↔ 4761 Publication
Glycosylationi426N-linked (GlcNAc...)PROSITE-ProRule annotation2 Publications1
Disulfide bondi440 ↔ 4511 Publication

Post-translational modificationi

The lysosomal precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins.
N-linked glycans show a high degree of microheterogeneity.2 Publications
The one residue extended Saposin-B-Val is only found in 5% of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP07602.
PaxDbiP07602.
PeptideAtlasiP07602.
PRIDEiP07602.
TopDownProteomicsiP07602-1. [P07602-1]

PTM databases

iPTMnetiP07602.
PhosphoSitePlusiP07602.
UniCarbKBiP07602.

Expressioni

Gene expression databases

BgeeiENSG00000197746.
CleanExiHS_PSAP.
ExpressionAtlasiP07602. baseline and differential.
GenevisibleiP07602. HS.

Organism-specific databases

HPAiCAB004647.
HPA004426.

Interactioni

Subunit structurei

Saposin-B is a homodimer. Prosaposin exists as a roughly half-half mixture of monomers and disulfide-linked dimers (PubMed:10406958, PubMed:12510003, PubMed:7730378, PubMed:21835174). Monomeric prosaposin interacts (via C-terminus) with sortilin/SORT1, the interaction is required for targeting to lysosomes (PubMed:14657016, PubMed:22431521).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP14P319443EBI-716699,EBI-2510738
ZBED1O960063EBI-716699,EBI-740037

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111639. 42 interactors.
DIPiDIP-29803N.
IntActiP07602. 19 interactors.
MINTiMINT-1193270.
STRINGi9606.ENSP00000378394.

Structurei

Secondary structure

1524
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi61 – 78Combined sources18
Helixi83 – 96Combined sources14
Beta strandi97 – 99Combined sources3
Helixi100 – 122Combined sources23
Helixi128 – 134Combined sources7
Helixi196 – 214Combined sources19
Helixi218 – 229Combined sources12
Helixi230 – 233Combined sources4
Helixi237 – 257Combined sources21
Helixi261 – 267Combined sources7
Helixi314 – 330Combined sources17
Helixi335 – 345Combined sources11
Helixi346 – 348Combined sources3
Helixi351 – 373Combined sources23
Helixi378 – 384Combined sources7
Turni386 – 388Combined sources3
Helixi409 – 422Combined sources14
Helixi429 – 439Combined sources11
Helixi440 – 442Combined sources3
Helixi445 – 447Combined sources3
Helixi448 – 466Combined sources19
Helixi472 – 478Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M12NMR-A311-390[»]
1N69X-ray2.20A/B/C195-273[»]
1SN6NMR-A311-390[»]
2DOBX-ray2.00A60-140[»]
2GTGX-ray2.40A311-391[»]
2QYPX-ray2.45A/B311-392[»]
2R0RX-ray2.50A/B407-484[»]
2R1QX-ray2.50A407-484[»]
2RB3X-ray2.10A/B/C/D407-484[»]
2Z9AX-ray2.50A/B311-389[»]
3BQPX-ray1.30A/B405-484[»]
3BQQX-ray2.00A/B/C/D405-484[»]
4DDJX-ray1.90A60-140[»]
4UEXX-ray1.80A/B60-142[»]
4V2OX-ray2.13A/B/C195-273[»]
DisProtiDP00733.
ProteinModelPortaliP07602.
SMRiP07602.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 58Saposin A-type 1PROSITE-ProRule annotationAdd BLAST41
Domaini59 – 142Saposin B-type 1PROSITE-ProRule annotationAdd BLAST84
Domaini194 – 275Saposin B-type 2PROSITE-ProRule annotationAdd BLAST82
Domaini311 – 392Saposin B-type 3PROSITE-ProRule annotationAdd BLAST82
Domaini405 – 486Saposin B-type 4PROSITE-ProRule annotationAdd BLAST82
Domaini488 – 524Saposin A-type 2PROSITE-ProRule annotationAdd BLAST37

Sequence similaritiesi

Contains 2 saposin A-type domains.PROSITE-ProRule annotation
Contains 4 saposin B-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1340. Eukaryota.
ENOG410XSI5. LUCA.
GeneTreeiENSGT00530000063434.
HOVERGENiHBG002617.
InParanoidiP07602.
KOiK12382.
PhylomeDBiP07602.
TreeFamiTF316942.

Family and domain databases

Gene3Di1.10.225.10. 4 hits.
InterProiIPR003119. SAP_A.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
IPR011001. Saposin-like.
IPR021165. Saposin_chordata.
IPR008139. SaposinB_dom.
[Graphical view]
PfamiPF02199. SapA. 2 hits.
PF05184. SapB_1. 4 hits.
PF03489. SapB_2. 4 hits.
[Graphical view]
PIRSFiPIRSF002431. Saposin. 1 hit.
PRINTSiPR01797. SAPOSIN.
SMARTiSM00162. SAPA. 2 hits.
SM00741. SapB. 4 hits.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 4 hits.
PROSITEiPS51110. SAP_A. 2 hits.
PS50015. SAP_B. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform Sap-mu-0 (identifier: P07602-1) [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
MYALFLLASL LGAALAGPVL GLKECTRGSA VWCQNVKTAS DCGAVKHCLQ
60 70 80 90 100
TVWNKPTVKS LPCDICKDVV TAAGDMLKDN ATEEEILVYL EKTCDWLPKP
110 120 130 140 150
NMSASCKEIV DSYLPVILDI IKGEMSRPGE VCSALNLCES LQKHLAELNH
160 170 180 190 200
QKQLESNKIP ELDMTEVVAP FMANIPLLLY PQDGPRSKPQ PKDNGDVCQD
210 220 230 240 250
CIQMVTDIQT AVRTNSTFVQ ALVEHVKEEC DRLGPGMADI CKNYISQYSE
260 270 280 290 300
IAIQMMMHMQ PKEICALVGF CDEVKEMPMQ TLVPAKVASK NVIPALELVE
310 320 330 340 350
PIKKHEVPAK SDVYCEVCEF LVKEVTKLID NNKTEKEILD AFDKMCSKLP
360 370 380 390 400
KSLSEECQEV VDTYGSSILS ILLEEVSPEL VCSMLHLCSG TRLPALTVHV
410 420 430 440 450
TQPKDGGFCE VCKKLVGYLD RNLEKNSTKQ EILAALEKGC SFLPDPYQKQ
460 470 480 490 500
CDQFVAEYEP VLIEILVEVM DPSFVCLKIG ACPSAHKPLL GTEKCIWGPS
510 520
YWCQNTETAA QCNAVEHCKR HVWN
Length:524
Mass (Da):58,113
Last modified:August 1, 1990 - v2
Checksum:i71977F7A8C9E1533
GO
Isoform Sap-mu-6 (identifier: P07602-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-259: M → MDQ

Show »
Length:526
Mass (Da):58,356
Checksum:i2A6E54624BA9D814
GO
Isoform Sap-mu-9 (identifier: P07602-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     260-260: Q → QDQQ

Show »
Length:527
Mass (Da):58,484
Checksum:i293FBB7472D82BD0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti369L → P in CAG33027 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04244070Missing in AKRD. 1 Publication1
Natural variantiVAR_031823215N → H in MLD-SAPB; reduces the intracellular activity of the protein significantly. 1 PublicationCorresponds to variant rs121918107dbSNPEnsembl.1
Natural variantiVAR_031899215N → K in MLD-SAPB. 1 PublicationCorresponds to variant rs770171865dbSNPEnsembl.1
Natural variantiVAR_006943217T → I in MLD-SAPB; juvenile; affects glycosylation at N-215. 2 PublicationsCorresponds to variant rs121918103dbSNPEnsembl.1
Natural variantiVAR_006944241C → S in MLD-SAPB; severe. 1 PublicationCorresponds to variant rs1130793dbSNPEnsembl.1
Natural variantiVAR_042441349L → P in AGD. 1 PublicationCorresponds to variant rs121918110dbSNPEnsembl.1
Natural variantiVAR_006945388C → F in AGD. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_006014259M → MDQ in isoform Sap-mu-6. Curated1
Alternative sequenceiVSP_006015260Q → QDQQ in isoform Sap-mu-9. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03077 mRNA. Translation: AAA52560.1.
D00422 mRNA. Translation: BAA00321.1.
BT006849 mRNA. Translation: AAP35495.1.
CR456746 mRNA. Translation: CAG33027.1.
AL731541, AC073370 Genomic DNA. Translation: CAI40837.1.
CH471083 Genomic DNA. Translation: EAW54437.1.
BC001503 mRNA. Translation: AAH01503.1.
BC004275 mRNA. Translation: AAH04275.1.
BC007612 mRNA. Translation: AAH07612.1.
M86181 Genomic DNA. No translation available.
X57107 Genomic DNA. Translation: CAA40391.1.
X57108 Genomic DNA. Translation: CAA40392.1.
M12710 mRNA. No translation available.
J03015 mRNA. Translation: AAB59494.1.
M32221 mRNA. Translation: AAA60303.1.
M60257 mRNA. Translation: AAA36595.1.
M60258 mRNA. Translation: AAA36596.1.
M60255 mRNA. Translation: AAA36594.1.
CCDSiCCDS7311.1. [P07602-1]
PIRiJX0061. SAHUP.
RefSeqiNP_001035930.1. NM_001042465.2. [P07602-3]
NP_001035931.1. NM_001042466.2. [P07602-2]
NP_002769.1. NM_002778.3. [P07602-1]
UniGeneiHs.523004.

Genome annotation databases

EnsembliENST00000394936; ENSP00000378394; ENSG00000197746. [P07602-1]
GeneIDi5660.
KEGGihsa:5660.
UCSCiuc001jsm.4. human. [P07602-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03077 mRNA. Translation: AAA52560.1.
D00422 mRNA. Translation: BAA00321.1.
BT006849 mRNA. Translation: AAP35495.1.
CR456746 mRNA. Translation: CAG33027.1.
AL731541, AC073370 Genomic DNA. Translation: CAI40837.1.
CH471083 Genomic DNA. Translation: EAW54437.1.
BC001503 mRNA. Translation: AAH01503.1.
BC004275 mRNA. Translation: AAH04275.1.
BC007612 mRNA. Translation: AAH07612.1.
M86181 Genomic DNA. No translation available.
X57107 Genomic DNA. Translation: CAA40391.1.
X57108 Genomic DNA. Translation: CAA40392.1.
M12710 mRNA. No translation available.
J03015 mRNA. Translation: AAB59494.1.
M32221 mRNA. Translation: AAA60303.1.
M60257 mRNA. Translation: AAA36595.1.
M60258 mRNA. Translation: AAA36596.1.
M60255 mRNA. Translation: AAA36594.1.
CCDSiCCDS7311.1. [P07602-1]
PIRiJX0061. SAHUP.
RefSeqiNP_001035930.1. NM_001042465.2. [P07602-3]
NP_001035931.1. NM_001042466.2. [P07602-2]
NP_002769.1. NM_002778.3. [P07602-1]
UniGeneiHs.523004.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M12NMR-A311-390[»]
1N69X-ray2.20A/B/C195-273[»]
1SN6NMR-A311-390[»]
2DOBX-ray2.00A60-140[»]
2GTGX-ray2.40A311-391[»]
2QYPX-ray2.45A/B311-392[»]
2R0RX-ray2.50A/B407-484[»]
2R1QX-ray2.50A407-484[»]
2RB3X-ray2.10A/B/C/D407-484[»]
2Z9AX-ray2.50A/B311-389[»]
3BQPX-ray1.30A/B405-484[»]
3BQQX-ray2.00A/B/C/D405-484[»]
4DDJX-ray1.90A60-140[»]
4UEXX-ray1.80A/B60-142[»]
4V2OX-ray2.13A/B/C195-273[»]
DisProtiDP00733.
ProteinModelPortaliP07602.
SMRiP07602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111639. 42 interactors.
DIPiDIP-29803N.
IntActiP07602. 19 interactors.
MINTiMINT-1193270.
STRINGi9606.ENSP00000378394.

Chemistry databases

ChEMBLiCHEMBL3580523.

Protein family/group databases

TCDBi1.C.35.2.1. the amoebapore (amoebapore) family.

PTM databases

iPTMnetiP07602.
PhosphoSitePlusiP07602.
UniCarbKBiP07602.

Polymorphism and mutation databases

BioMutaiPSAP.
DMDMi134218.

Proteomic databases

EPDiP07602.
PaxDbiP07602.
PeptideAtlasiP07602.
PRIDEiP07602.
TopDownProteomicsiP07602-1. [P07602-1]

Protocols and materials databases

DNASUi5660.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394936; ENSP00000378394; ENSG00000197746. [P07602-1]
GeneIDi5660.
KEGGihsa:5660.
UCSCiuc001jsm.4. human. [P07602-1]

Organism-specific databases

CTDi5660.
DisGeNETi5660.
GeneCardsiPSAP.
HGNCiHGNC:9498. PSAP.
HPAiCAB004647.
HPA004426.
MalaCardsiPSAP.
MIMi176801. gene.
249900. phenotype.
610539. phenotype.
611721. phenotype.
611722. phenotype.
neXtProtiNX_P07602.
OpenTargetsiENSG00000197746.
Orphaneti309252. Atypical Gaucher disease due to saposin C deficiency.
139406. Encephalopathy due to prosaposin deficiency.
206436. Infantile Krabbe disease.
309271. Metachromatic leukodystrophy, adult form.
309263. Metachromatic leukodystrophy, juvenile form.
309256. Metachromatic leukodystrophy, late infantile form.
PharmGKBiPA33845.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1340. Eukaryota.
ENOG410XSI5. LUCA.
GeneTreeiENSGT00530000063434.
HOVERGENiHBG002617.
InParanoidiP07602.
KOiK12382.
PhylomeDBiP07602.
TreeFamiTF316942.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiPSAP. human.
EvolutionaryTraceiP07602.
GeneWikiiProsaposin.
GenomeRNAii5660.
PROiP07602.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197746.
CleanExiHS_PSAP.
ExpressionAtlasiP07602. baseline and differential.
GenevisibleiP07602. HS.

Family and domain databases

Gene3Di1.10.225.10. 4 hits.
InterProiIPR003119. SAP_A.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
IPR011001. Saposin-like.
IPR021165. Saposin_chordata.
IPR008139. SaposinB_dom.
[Graphical view]
PfamiPF02199. SapA. 2 hits.
PF05184. SapB_1. 4 hits.
PF03489. SapB_2. 4 hits.
[Graphical view]
PIRSFiPIRSF002431. Saposin. 1 hit.
PRINTSiPR01797. SAPOSIN.
SMARTiSM00162. SAPA. 2 hits.
SM00741. SapB. 4 hits.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 4 hits.
PROSITEiPS51110. SAP_A. 2 hits.
PS50015. SAP_B. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAP_HUMAN
AccessioniPrimary (citable) accession number: P07602
Secondary accession number(s): P07292
, P15793, P78538, P78541, P78546, P78547, P78558, Q53Y86, Q6IBQ6, Q92739, Q92740, Q92741, Q92742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1990
Last modified: November 30, 2016
This is version 211 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

Miscellaneous

Saposin-B co-purifies with 1 molecule of phosphatidylethanolamine.

Keywords - Technical termi

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

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. 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.