HYAL2_HUMAN - dbPTM
HYAL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HYAL2_HUMAN
UniProt AC Q12891
Protein Name Hyaluronidase-2
Gene Name HYAL2
Organism Homo sapiens (Human).
Sequence Length 473
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor .
Protein Description Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R..
Protein Sequence MRAGPGPTVTLALVLAVSWAMELKPTAPPIFTGRPFVVAWDVPTQDCGPRLKVPLDLNAFDVQASPNEGFVNQNITIFYRDRLGLYPRFDSAGRSVHGGVPQNVSLWAHRKMLQKRVEHYIRTQESAGLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASRHPDWPPDRIVKQAQYEFEFAAQQFMLETLRYVKAVRPRHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSRHGRNFVSFRVQEALRVARTHHANHALPVYVFTRPTYSRRLTGLSEMDLISTIGESAALGAAGVILWGDAGYTTSTETCQYLKDYLTRLLVPYVVNVSWATQYCSRAQCHGHGRCVRRNPSASTFLHLSTNSFRLVPGHAPGEPQLRPVGELSWADIDHLQTHFRCQCYLGWSGEQCQWDHRQAAGGASEAWAGSHLTSLLALAALAFTWTL
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
32O-linked_GlycosylationPTAPPIFTGRPFVVA
CCCCCCCCCCCEEEE
32.76OGP
74N-linked_GlycosylationNEGFVNQNITIFYRD
CCCCCCCCEEEEEEC
28.32UniProtKB CARBOHYD
103N-linked_GlycosylationVHGGVPQNVSLWAHR
CCCCCCCCCHHHHHH
21.19UniProtKB CARBOHYD
148UbiquitinationWVRNWQDKDVYRRLS
EEECCCCHHHHHHHH
33.71-
190PhosphorylationAQQFMLETLRYVKAV
HHHHHHHHHHHHHHH
16.75-
216PhosphorylationPDCYNHDYVQNWESY
CCCCCCHHHCCHHHH
9.07-
291PhosphorylationANHALPVYVFTRPTY
CCCCCEEEEEECCCC
6.47-
297PhosphorylationVYVFTRPTYSRRLTG
EEEEECCCCHHHCCC
30.73-
298PhosphorylationYVFTRPTYSRRLTGL
EEEECCCCHHHCCCC
11.67-
303PhosphorylationPTYSRRLTGLSEMDL
CCCHHHCCCCCHHHH
33.9826307563
306PhosphorylationSRRLTGLSEMDLIST
HHHCCCCCHHHHHHH
32.0226307563
312PhosphorylationLSEMDLISTIGESAA
CCHHHHHHHHHHHHH
22.6726307563
313PhosphorylationSEMDLISTIGESAAL
CHHHHHHHHHHHHHH
26.4726307563
317PhosphorylationLISTIGESAALGAAG
HHHHHHHHHHHCCCE
17.3926307563
333PhosphorylationILWGDAGYTTSTETC
EEECCCCCCCCHHHH
14.4726307563
334PhosphorylationLWGDAGYTTSTETCQ
EECCCCCCCCHHHHH
17.2226307563
335PhosphorylationWGDAGYTTSTETCQY
ECCCCCCCCHHHHHH
25.7626307563
336PhosphorylationGDAGYTTSTETCQYL
CCCCCCCCHHHHHHH
19.2226307563
337PhosphorylationDAGYTTSTETCQYLK
CCCCCCCHHHHHHHH
32.9726307563
339PhosphorylationGYTTSTETCQYLKDY
CCCCCHHHHHHHHHH
12.6626307563
342PhosphorylationTSTETCQYLKDYLTR
CCHHHHHHHHHHHHH
20.1926307563
357N-linked_GlycosylationLLVPYVVNVSWATQY
HHHHEECCHHHHHHH
16.44UniProtKB CARBOHYD
385PhosphorylationRRNPSASTFLHLSTN
CCCCCCCCEEEECCC
29.9024719451
391PhosphorylationSTFLHLSTNSFRLVP
CCEEEECCCCEECCC
41.0424719451
448GPI-anchorDHRQAAGGASEAWAG
CHHHHCCCCCHHHHH
22.62-

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 HYAL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HYAL2_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 HYAL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRA32_HUMANKRTAP3-2physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
PON2_HUMANPON2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HYAL2_HUMAN

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Related Literatures of Post-Translational Modification

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