HEXA_HUMAN - dbPTM
HEXA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEXA_HUMAN
UniProt AC P06865
Protein Name Beta-hexosaminidase subunit alpha
Gene Name HEXA
Organism Homo sapiens (Human).
Sequence Length 529
Subcellular Localization Lysosome.
Protein Description Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. The form B is active against certain oligosaccharides. The form S has no measurable activity..
Protein Sequence MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
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
4Phosphorylation----MTSSRLWFSLL
----CCCHHHHHHHH		23.4030631047
21PhosphorylationAAFAGRATALWPWPQ
HHHCCCCCCCCCCCC		22.4120068231
32UbiquitinationPWPQNFQTSDQRYVL
CCCCCCCCCCCEEEE		30.08-
32PhosphorylationPWPQNFQTSDQRYVL
CCCCCCCCCCCEEEE		30.0820068231
33PhosphorylationWPQNFQTSDQRYVLY
CCCCCCCCCCEEEEC		22.4420068231
77PhosphorylationDLLFGSGSWPRPYLT
HHHHCCCCCCCCCCC		35.2924719451
115N-linked_GlycosylationPTLESVENYTLTIND
CCCCCEEEEEEEECC		32.691533633
157N-linked_GlycosylationAEGTFFINKTEIEDF
CCCEEEEECCCCCCC		39.791533633
189PhosphorylationPLSSILDTLDVMAYN
CHHHHHHHHHHHHHC		22.78-
224UbiquitinationTFPELMRKGSYNPVT
CHHHHHHCCCCCCCC		37.94-
295N-linked_GlycosylationGPVNPSLNNTYEFMS
CCCCCCCCCHHHHHH		43.041533633
331PhosphorylationVDFTCWKSNPEIQDF
CEEEEECCCHHHHHH		32.87-
342UbiquitinationIQDFMRKKGFGEDFK
HHHHHHHCCCCHHHH		49.46-
353PhosphorylationEDFKQLESFYIQTLL
HHHHHHHHHHHHHHH		31.7624043423
355PhosphorylationFKQLESFYIQTLLDI
HHHHHHHHHHHHHHH		11.0324043423
358PhosphorylationLESFYIQTLLDIVSS
HHHHHHHHHHHHHHH		21.5224043423
364PhosphorylationQTLLDIVSSYGKGYV
HHHHHHHHHHCCCEE		20.4124043423
365PhosphorylationTLLDIVSSYGKGYVV
HHHHHHHHHCCCEEE		27.3224043423
366PhosphorylationLLDIVSSYGKGYVVW
HHHHHHHHCCCEEEE		18.4924043423
417PhosphorylationAGFRALLSAPWYLNR
HCHHHHHCCCCHHHC		32.8924719451
421PhosphorylationALLSAPWYLNRISYG
HHHCCCCHHHCCCCC		7.9524719451
490PhosphorylationRLWSNKLTSDLTFAY
HHHHCCCCCCCHHHH		23.0825404012
491PhosphorylationLWSNKLTSDLTFAYE
HHHCCCCCCCHHHHH		40.8525404012
522GlutathionylationQPLNVGFCEQEFEQT
CCCCCCCCHHHCCCC		4.3122555962
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 HEXA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEXA_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 HEXA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIC_HUMANACAT2physical
22863883
SAHH_HUMANAHCYphysical
22863883
TLS1_HUMANC9orf78physical
22863883
CAPZB_HUMANCAPZBphysical
22863883
EZRI_HUMANEZRphysical
22863883
TF3C4_HUMANGTF3C4physical
22863883
H2AV_HUMANH2AFVphysical
22863883
HERC4_HUMANHERC4physical
22863883
HXK1_HUMANHK1physical
22863883
KTN1_HUMANKTN1physical
22863883
NUBP2_HUMANNUBP2physical
22863883
PCNA_HUMANPCNAphysical
22863883
PDC10_HUMANPDCD10physical
22863883
RD23A_HUMANRAD23Aphysical
22863883
UBR7_HUMANUBR7physical
22863883
WDR61_HUMANWDR61physical
22863883
XPP1_HUMANXPNPEP1physical
22863883
STIM2_HUMANSTIM2physical
26344197
DHRS4_HUMANDHRS4physical
28514442
TERF2_HUMANTERF2physical
28514442
HEXB_HUMANHEXBphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
272800GM2-gangliosidosis 1 (GM2G1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HEXA_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-157 AND ASN-295, AND MASSSPECTROMETRY.
"Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, beta-hexosaminidase A, by site-directed mutagenesis.";
Weitz G., Proia R.L.;
J. Biol. Chem. 267:10039-10044(1992).
Cited for: GLYCOSYLATION AT ASN-115; ASN-157 AND ASN-295, AND MUTAGENESIS OFASN-115; ASN-157 AND ASN-295.

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