HYAL4_HUMAN - dbPTM
HYAL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HYAL4_HUMAN
UniProt AC Q2M3T9
Protein Name Hyaluronidase-4
Gene Name HYAL4
Organism Homo sapiens (Human).
Sequence Length 481
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide..
Protein Sequence MKVLSEGQLKLCVVQPVHLTSWLLIFFILKSISCLKPARLPIYQRKPFIAAWNAPTDQCLIKYNLRLNLKMFPVIGSPLAKARGQNVTIFYVNRLGYYPWYTSQGVPINGGLPQNISLQVHLEKADQDINYYIPAEDFSGLAVIDWEYWRPQWARNWNSKDVYRQKSRKLISDMGKNVSATDIEYLAKVTFEESAKAFMKETIKLGIKSRPKGLWGYYLYPDCHNYNVYAPNYSGSCPEDEVLRNNELSWLWNSSAALYPSIGVWKSLGDSENILRFSKFRVHESMRISTMTSHDYALPVFVYTRLGYRDEPLFFLSKQDLVSTIGESAALGAAGIVIWGDMNLTASKANCTKVKQFVSSDLGSYIANVTRAAEVCSLHLCRNNGRCIRKMWNAPSYLHLNPASYHIEASEDGEFTVKGKASDTDLAVMADTFSCHCYQGYEGADCREIKTADGCSGVSPSPGSLMTLCLLLLASYRSIQL
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
31PhosphorylationLIFFILKSISCLKPA
HHHHHHHHHHCCCCC
19.1126074081
33PhosphorylationFFILKSISCLKPARL
HHHHHHHHCCCCCCC
22.0826074081
43PhosphorylationKPARLPIYQRKPFIA
CCCCCCCCCCCCEEE
10.5826074081
86N-linked_GlycosylationLAKARGQNVTIFYVN
HHHHCCCCEEEEEEC
35.41UniProtKB CARBOHYD
88PhosphorylationKARGQNVTIFYVNRL
HHCCCCEEEEEECCC
16.9624719451
115N-linked_GlycosylationINGGLPQNISLQVHL
CCCCCCCCEEEEEEH
24.71UniProtKB CARBOHYD
177N-linked_GlycosylationLISDMGKNVSATDIE
HHHHCCCCCCHHHHH
27.5219139490
267PhosphorylationPSIGVWKSLGDSENI
CCCCHHHHCCCCHHH
23.1327732954
271PhosphorylationVWKSLGDSENILRFS
HHHHCCCCHHHCHHH
30.6427732954
296PhosphorylationSTMTSHDYALPVFVY
EECCCCCCCEEEEEE
12.47-
323PhosphorylationLSKQDLVSTIGESAA
EEHHHHHHHHHHHHH
22.9226434552
343N-linked_GlycosylationIVIWGDMNLTASKAN
EEEECCCCCCCCCCC
38.69UniProtKB CARBOHYD
345PhosphorylationIWGDMNLTASKANCT
EECCCCCCCCCCCCC
24.7126434552
347PhosphorylationGDMNLTASKANCTKV
CCCCCCCCCCCCCHH
27.3726434552
416PhosphorylationASEDGEFTVKGKASD
ECCCCCEEEEEEECC
19.6022468782
422PhosphorylationFTVKGKASDTDLAVM
EEEEEEECCCCEEEE
44.5222468782
424PhosphorylationVKGKASDTDLAVMAD
EEEEECCCCEEEEEE
30.3422468782

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 HYAL4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HYAL4_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 HYAL4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G3PT_HUMANGAPDHSphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HYAL4_HUMAN

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Related Literatures of Post-Translational Modification

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