GLCM_HUMAN - dbPTM
GLCM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLCM_HUMAN
UniProt AC P04062
Protein Name Glucosylceramidase
Gene Name GBA
Organism Homo sapiens (Human).
Sequence Length 536
Subcellular Localization Lysosome membrane
Peripheral membrane protein
Lumenal side . Interaction with saposin-C promotes membrane association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2.
Protein Description
Protein Sequence MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
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
24PhosphorylationRVSIMAGSLTGLLLL
HHHHHHHHHHHHHHH		17.1424043423
26PhosphorylationSIMAGSLTGLLLLQA
HHHHHHHHHHHHHHH		27.7224043423
31UbiquitinationSLTGLLLLQAVSWAS
HHHHHHHHHHHHHHC		2.87-
35PhosphorylationLLLLQAVSWASGARP
HHHHHHHHHHCCCCC		21.6824043423
38PhosphorylationLQAVSWASGARPCIP
HHHHHHHCCCCCCCC		27.0824043423
58N-linked_GlycosylationSSVVCVCNATYCDSF
CEEEEEECCEECCCC		18.2112792654
98N-linked_GlycosylationSMGPIQANHTGTGLL
EECCEECCCCCCEEE		19.51UniProtKB CARBOHYD
118UbiquitinationEQKFQKVKGFGGAMT
HHHHHCCCCCCCHHC		56.40-
136PhosphorylationALNILALSPPAQNLL
HHHHHHHCCHHHHHH		24.19-
185N-linked_GlycosylationPDDFQLHNFSLPEED
CCCCCCCCCCCCHHH		36.4712754519
194UbiquitinationSLPEEDTKLKIPLIH
CCCHHHCCCHHHHHH		61.17-
1962-HydroxyisobutyrylationPEEDTKLKIPLIHRA
CHHHCCCHHHHHHHH		43.78-
225UbiquitinationWTSPTWLKTNGAVNG
CCCCCCHHCCCCCCC		31.35-
233UbiquitinationTNGAVNGKGSLKGQP
CCCCCCCCCCCCCCC		39.87-
237UbiquitinationVNGKGSLKGQPGDIY
CCCCCCCCCCCCCHH		58.14-
244PhosphorylationKGQPGDIYHQTWARY
CCCCCCHHHHHHHHH		7.82-
259PhosphorylationFVKFLDAYAEHKLQF
HHHHHHHHHHHEEEE		16.5220068231
309N-linked_GlycosylationDLGPTLANSTHHNVR
HHCHHHHCCCCCCEE		51.0212754519
310O-linked_GlycosylationLGPTLANSTHHNVRL
HCHHHHCCCCCCEEE		24.4230059200
319SulfoxidationHHNVRLLMLDDQRLL
CCCEEEEEECCCCEE		4.5821406390
332UbiquitinationLLLPHWAKVVLTDPE
EECCCEEEEEECCHH		27.90-
336PhosphorylationHWAKVVLTDPEAAKY
CEEEEEECCHHHHHH		37.59-
405PhosphorylationRGMQYSHSIITNLLY
CCCCCHHHHHHHHHH		15.11-
412PhosphorylationSIITNLLYHVVGWTD
HHHHHHHHHHHCCCC		8.85-
447UbiquitinationPIIVDITKDTFYKQP
CEEEECCCCCCCCCC		55.92-
451PhosphorylationDITKDTFYKQPMFYH
ECCCCCCCCCCCEEE		15.7122817900
501N-linked_GlycosylationSAVVVVLNRSSKDVP
CEEEEEEECCCCCCC		30.13UniProtKB CARBOHYD
512UbiquitinationKDVPLTIKDPAVGFL
CCCCCEEECCCCCEE		53.04-
523PhosphorylationVGFLETISPGYSIHT
CCEEEECCCCCEEEE		21.49-
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 GLCM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLCM_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 GLCM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
22160715
HSP74_HUMANHSPA4physical
22160715
TCPA_HUMANTCP1physical
22160715
PRKN_HUMANPARK2physical
20643691
TCPA_HUMANTCP1physical
21098288
CBL_HUMANCBLphysical
21098288
ITCH_HUMANITCHphysical
23255161
SYUA_HUMANSNCAphysical
23266198
PCBP2_HUMANPCBP2physical
26344197
ATP5J_HUMANATP5Jphysical
26496610
CALX_HUMANCANXphysical
26496610
DHC24_HUMANDHCR24physical
26496610
FMR1_HUMANFMR1physical
26496610
CH60_HUMANHSPD1physical
26496610
KS6A3_HUMANRPS6KA3physical
26496610
ENPL_HUMANHSP90B1physical
26496610
TCPG_HUMANCCT3physical
26496610
TOP3B_HUMANTOP3Bphysical
26496610
SCAM3_HUMANSCAMP3physical
26496610
INADL_HUMANINADLphysical
26496610
HYOU1_HUMANHYOU1physical
26496610
TCPQ_HUMANCCT8physical
26496610
ZMY11_HUMANZMYND11physical
26496610
B4GT7_HUMANB4GALT7physical
26496610
SK2L2_HUMANSKIV2L2physical
26496610
IMP3_HUMANIMP3physical
26496610
BMP2K_HUMANBMP2Kphysical
26496610
ZCHC8_HUMANZCCHC8physical
26496610
FGD6_HUMANFGD6physical
26496610
BRE1A_HUMANRNF20physical
26496610
JPH1_HUMANJPH1physical
26496610
ZFP91_HUMANZFP91physical
26496610
CCHL_HUMANHCCSphysical
27173435
COMT_HUMANCOMTphysical
27173435
SG196_HUMANPOMKphysical
27173435
ARL8B_HUMANARL8Bphysical
27173435
RDH11_HUMANRDH11physical
27173435
ESYT1_HUMANESYT1physical
27173435
Drug and Disease Associations
Kegg Disease
H00066 Lewy body dementia (LBD); Dementia with Lewy bodies (DLB)
H00126 Gaucher disease
H00810 Progressive myoclonic epilepsy (PME), including: Lafora disease (LBD); Unverricht-Lundborg disease (
OMIM Disease
230800Gaucher disease (GD)
230800Gaucher disease 1 (GD1)
230900Gaucher disease 2 (GD2)
231000Gaucher disease 3 (GD3)
231005Gaucher disease 3C (GD3C)
608013Gaucher disease perinatal lethal (GDPL)
Note=Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
168600
Kegg Drug
D02810 Alglucerase (JAN/USAN/INN); Ceredase (TN)
D03020 Imiglucerase (genetical recombination) (JAN); Imiglucerase (USAN/INN); Cerezyme (TN)
D09029 Velaglucerase alfa (USAN); Vpriv (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLCM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease.";
Brumshtein B., Wormald M.R., Silman I., Futerman A.H., Sussman J.L.;
Acta Crystallogr. D 62:1458-1465(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 40-536, AND GLYCOSYLATION ATASN-58; ASN-98 AND ASN-185.
"X-ray structure of human acid-beta-glucosidase, the defective enzymein Gaucher disease.";
Dvir H., Harel M., McCarthy A.A., Toker L., Silman I., Futerman A.H.,Sussman J.L.;
EMBO Rep. 4:704-709(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-536, GLYCOSYLATION ATASN-58, AND DISULFIDE BONDS.
"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-98 AND ASN-309, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-98; ASN-185 AND ASN-309.

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