SAP_HUMAN - dbPTM
SAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAP_HUMAN
UniProt AC P07602
Protein Name Prosaposin
Gene Name PSAP
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Lysosome .
Prosaposin: Secreted . Secreted as a fully glycosylated 70 kDa protein composed of complex glycans.
Protein Description 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.; 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..
Protein Sequence MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationYALFLLASLLGAALA
HHHHHHHHHHHHHHH		24.89-
27MethylationLGLKECTRGSAVWCQ
CCCCCCCCCCEEEEC		49.04115489243
55UbiquitinationCLQTVWNKPTVKSLP
HHHHHHCCCCCCCCC		26.76-
71PhosphorylationDICKDVVTAAGDMLK
CHHHHHHHHHHHHHH		15.6126437602
80N-linked_GlycosylationAGDMLKDNATEEEIL
HHHHHHCCCCHHHHH		47.372842863
80N-linked_GlycosylationAGDMLKDNATEEEIL
HHHHHHCCCCHHHHH		47.372842863
82O-linked_GlycosylationDMLKDNATEEEILVY
HHHHCCCCHHHHHHH		50.6230059200
82PhosphorylationDMLKDNATEEEILVY
HHHHCCCCHHHHHHH		50.62-
89PhosphorylationTEEEILVYLEKTCDW
CHHHHHHHHHHHCCC		13.00-
93O-linked_GlycosylationILVYLEKTCDWLPKP
HHHHHHHHCCCCCCC		13.3030059200
101N-linked_GlycosylationCDWLPKPNMSASCKE
CCCCCCCCCCHHHHH		43.072842863
103O-linked_GlycosylationWLPKPNMSASCKEIV
CCCCCCCCHHHHHHH		24.5430059200
112PhosphorylationSCKEIVDSYLPVILD
HHHHHHHHHHHHHHH		20.06-
113PhosphorylationCKEIVDSYLPVILDI
HHHHHHHHHHHHHHH		15.57-
143UbiquitinationNLCESLQKHLAELNH
HHHHHHHHHHHHHHH		45.97-
152UbiquitinationLAELNHQKQLESNKI
HHHHHHHHHHHHCCC		49.66-
1522-HydroxyisobutyrylationLAELNHQKQLESNKI
HHHHHHHHHHHHCCC		49.66-
165PhosphorylationKIPELDMTEVVAPFM
CCCCCCCHHHHHHHH		25.87-
165O-linked_GlycosylationKIPELDMTEVVAPFM
CCCCCCCHHHHHHHH		25.87OGP
180PhosphorylationANIPLLLYPQDGPRS
HCCCEEECCCCCCCC		9.98-
187PhosphorylationYPQDGPRSKPQPKDN
CCCCCCCCCCCCCCC		52.39-
214O-linked_GlycosylationDIQTAVRTNSTFVQA
HHHHHHHCCCHHHHH		27.24OGP
215N-linked_GlycosylationIQTAVRTNSTFVQAL
HHHHHHCCCHHHHHH		28.6119167329
216O-linked_GlycosylationQTAVRTNSTFVQALV
HHHHHCCCHHHHHHH		23.7030059200
237SulfoxidationCDRLGPGMADICKNY
HHHHCCCHHHHHHHH		3.2228465586
281PhosphorylationVKEMPMQTLVPAKVA
HHHCCCHHCCCHHHC		24.3820068231
290UbiquitinationVPAKVASKNVIPALE
CCHHHCCCCCCCHHH		45.56-
3032-HydroxyisobutyrylationLELVEPIKKHEVPAK
HHHHCCHHHCCCCCC		59.81-
303 (in isoform 1)Ubiquitination-59.8121906983
303UbiquitinationLELVEPIKKHEVPAK
HHHHCCHHHCCCCCC		59.8121906983
305 (in isoform 2)Ubiquitination-35.9621906983
306 (in isoform 3)Ubiquitination-60.1021906983
323UbiquitinationEVCEFLVKEVTKLID
HHHHHHHHHHHHHHH		48.92-
332N-linked_GlycosylationVTKLIDNNKTEKEIL
HHHHHHCCCCHHHHH		49.2119167329
334O-linked_GlycosylationKLIDNNKTEKEILDA
HHHHCCCCHHHHHHH		55.1830059200
336UbiquitinationIDNNKTEKEILDAFD
HHCCCCHHHHHHHHH		56.11-
344UbiquitinationEILDAFDKMCSKLPK
HHHHHHHHHHHCCCH		35.04-
344AcetylationEILDAFDKMCSKLPK
HHHHHHHHHHHCCCH		35.0427452117
391O-linked_GlycosylationMLHLCSGTRLPALTV
HHHHCCCCCCCEEEE		16.85OGP
397O-linked_GlycosylationGTRLPALTVHVTQPK
CCCCCEEEEEEECCC		15.6355824899
401O-linked_GlycosylationPALTVHVTQPKDGGF
CEEEEEEECCCCCCH		25.0355824903
413AcetylationGGFCEVCKKLVGYLD
CCHHHHHHHHHHHHH		55.0825953088
414UbiquitinationGFCEVCKKLVGYLDR
CHHHHHHHHHHHHHH		43.19-
414MalonylationGFCEVCKKLVGYLDR
CHHHHHHHHHHHHHH		43.1926320211
418PhosphorylationVCKKLVGYLDRNLEK
HHHHHHHHHHHHCCC		9.65-
421MethylationKLVGYLDRNLEKNST
HHHHHHHHHCCCCCC		47.22115489251
426N-linked_GlycosylationLDRNLEKNSTKQEIL
HHHHCCCCCCHHHHH		45.6019167329
427O-linked_GlycosylationDRNLEKNSTKQEILA
HHHCCCCCCHHHHHH		48.3130059200
429UbiquitinationNLEKNSTKQEILAAL
HCCCCCCHHHHHHHH		45.84-
4382-HydroxyisobutyrylationEILAALEKGCSFLPD
HHHHHHHHHHCCCCC		67.10-
449UbiquitinationFLPDPYQKQCDQFVA
CCCCHHHHHHHHHHH		47.23-
473PhosphorylationLVEVMDPSFVCLKIG
HHHHCCCCCEEEEEC		26.5027362937
487UbiquitinationGACPSAHKPLLGTEK
CCCCCCCCCCCCCCC		36.76-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAP_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN6_HUMANCOPS6physical
16169070
CATD_HUMANCTSDphysical
12083803
SAP_HUMANPSAPphysical
12518053
ZBED1_HUMANZBED1physical
16713569
TCRG1_HUMANTCERG1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
UPAR_HUMANPLAURphysical
22939629
SNP23_HUMANSNAP23physical
22939629
SURF4_HUMANSURF4physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SUMO2_HUMANSUMO2physical
22939629
SYUA_HUMANSNCAphysical
22939629
SRSF5_HUMANSRSF5physical
22939629
SSRA_HUMANSSR1physical
22939629
TR150_HUMANTHRAP3physical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611721Combined saposin deficiency (CSAPD)
249900Leukodystrophy metachromatic due to saposin-B deficiency (MLD-SAPB)
610539Gaucher disease, atypical, due to saposin C deficiency (AGD)
611722Krabbe disease, atypical, due to saposin A deficiency (AKRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAP_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80; ASN-101; ASN-332 ANDASN-426, AND MASS SPECTROMETRY.
"Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) bysame genetic locus.";
O'Brien J.S., Kretz K.A., Dewji N., Wenger D.A., Esch F.,Fluharty A.L.;
Science 241:1098-1101(1988).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-524.

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