HEXB_HUMAN - dbPTM
HEXB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEXB_HUMAN
UniProt AC P07686
Protein Name Beta-hexosaminidase subunit beta
Gene Name HEXB
Organism Homo sapiens (Human).
Sequence Length 556
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..
Protein Sequence MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLSVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM
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
51UbiquitinationRAPSVSAKPGPALWP
CCCCCCCCCCCCCCC		42.8921890473
84N-linked_GlycosylationFYISHSPNSTAGPSC
EEECCCCCCCCCCCC		55.8211447134
84N-linked_GlycosylationFYISHSPNSTAGPSC
EEECCCCCCCCCCCC		55.8211447134
142N-linked_GlycosylationSECDAFPNISSDESY
CCCCCCCCCCCCCCE		40.0811447134
161AcetylationKEPVAVLKANRVWGA
ECCEEHHHHHHHHHH		36.7027452117
161UbiquitinationKEPVAVLKANRVWGA
ECCEEHHHHHHHHHH		36.7021890473
190N-linked_GlycosylationSYGTFTINESTIIDS
CCCEEEECCCCCCCC		33.8211447134
190N-linked_GlycosylationSYGTFTINESTIIDS
CCCEEEECCCCCCCC		33.8211447134
201PhosphorylationIIDSPRFSHRGILID
CCCCCCCCCCCEEEE		17.35-
209PhosphorylationHRGILIDTSRHYLPV
CCCEEEECCCCCCCH		22.22-
210PhosphorylationRGILIDTSRHYLPVK
CCEEEECCCCCCCHH		17.20-
2172-HydroxyisobutyrylationSRHYLPVKIILKTLD
CCCCCCHHHHHHHHH		23.30-
250O-linked_GlycosylationSFPYQSITFPELSNK
CCCCCEEECHHHCCC		38.08OGP
267PhosphorylationYSLSHVYTPNDVRMV
EECEEEECCCHHHHH		17.96-
297PhosphorylationDTPGHTLSWGKGQKD
CCCCCCCCCCCCCCC		34.6324719451
3002-HydroxyisobutyrylationGHTLSWGKGQKDLLT
CCCCCCCCCCCCCCH		52.49-
300UbiquitinationGHTLSWGKGQKDLLT
CCCCCCCCCCCCCCH		52.49-
303UbiquitinationLSWGKGQKDLLTPCY
CCCCCCCCCCCHHCC		60.04-
323N-linked_GlycosylationLDSFGPINPTLNTTY
CCCCCCCCCCCCHHH		27.0019159218
327N-linked_GlycosylationGPINPTLNTTYSFLT
CCCCCCCCHHHHHHH		32.6211447134
327N-linked_GlycosylationGPINPTLNTTYSFLT
CCCCCCCCHHHHHHH		32.6211447134
374UbiquitinationIQDFMRQKGFGTDFK
HHHHHHHCCCCCCHH		45.93-
3822-HydroxyisobutyrylationGFGTDFKKLESFYIQ
CCCCCHHHHHHHHHH		58.44-
385PhosphorylationTDFKKLESFYIQKVL
CCHHHHHHHHHHHHH		33.5121406692
387PhosphorylationFKKLESFYIQKVLDI
HHHHHHHHHHHHHHH		16.2421406692
412UbiquitinationWQEVFDDKAKLAPGT
EEECCCCCCCCCCCC		49.63-
427PhosphorylationIVEVWKDSAYPEELS
EEEEECCCCCHHHHH		26.4420068231
429PhosphorylationEVWKDSAYPEELSRV
EEECCCCCHHHHHHH		18.3520068231
434PhosphorylationSAYPEELSRVTASGF
CCCHHHHHHHHCCCC		28.1620068231
465UbiquitinationQDWRKYYKVEPLDFG
CCHHHHEEECCCCCC		36.7121890473
474PhosphorylationEPLDFGGTQKQKQLF
CCCCCCCCCCEEEEE		32.73-
476UbiquitinationLDFGGTQKQKQLFIG
CCCCCCCCEEEEEEC		60.34-
499PhosphorylationYVDATNLTPRLWPRA
EECCCCCCCCCCCCH		14.3924719451
512MethylationRASAVGERLWSSKDV
CHHHHHHHHHCCCCC		35.21115478457
556SulfoxidationGYCNHENM-------
CCCCCCCC-------		5.4630846556
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 HEXB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEXB_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 HEXB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HEXB_HUMANHEXBphysical
12706724
BNIP2_HUMANBNIP2physical
22863883
EZRI_HUMANEZRphysical
22863883
FUMH_HUMANFHphysical
22863883
TF3C4_HUMANGTF3C4physical
22863883
HXK1_HUMANHK1physical
22863883
HXK2_HUMANHK2physical
22863883
IPO5_HUMANIPO5physical
22863883
IPO9_HUMANIPO9physical
22863883
PDC10_HUMANPDCD10physical
22863883
PLPHP_HUMANPROSCphysical
22863883
RL22_HUMANRPL22physical
22863883
EFTU_HUMANTUFMphysical
22863883
STIM1_HUMANSTIM1physical
26344197
STIM2_HUMANSTIM2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
268800GM2-gangliosidosis 2 (GM2G2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HEXB_HUMAN

loading...

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-84; ASN-323 AND ASN-327,AND MASS SPECTROMETRY.
"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-327.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory