UST_HUMAN - dbPTM
UST_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UST_HUMAN
UniProt AC Q9Y2C2
Protein Name Uronyl 2-sulfotransferase
Gene Name UST
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin..
Protein Sequence MKKKQQHPGGGADPWPHGAPMGGAPPGLGSWKRRVPLLPFLRFSLRDYGFCMATLLVFCLGSLLYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVNRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVKKTVPSPEAVQILYQRMRYEYEFYHYVKEQFHLLKRKFGLKSHVSKPPLRPHFFIPTPLETEEPIDDEEQDDEKWLEDIYKR
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
32UbiquitinationPPGLGSWKRRVPLLP
CCCCCCHHHHCCCHH
31.8322817900
44PhosphorylationLLPFLRFSLRDYGFC
CHHHHHHHHHHHCHH
18.9627966365
84N-linked_GlycosylationDLRQYLGNSTYLDDH
HHHHHHCCCCCCCCC
28.69UniProtKB CARBOHYD
115PhosphorylationNRVGKCGSRTVVLLL
CCCCCCCHHHHHHHH
33.96-
117PhosphorylationVGKCGSRTVVLLLRI
CCCCCHHHHHHHHHH
19.36-
126PhosphorylationVLLLRILSEKHGFNL
HHHHHHHHHHHCCCE
42.0824719451
140N-linked_GlycosylationLVTSDIHNKTRLTKN
EECCCCCCCCCCCHH
47.96UniProtKB CARBOHYD
155N-linked_GlycosylationEQMELIKNISTAEQP
HHHHHHHHCCCCCCC
26.84UniProtKB CARBOHYD
157PhosphorylationMELIKNISTAEQPYL
HHHHHHCCCCCCCEE
30.84-
158PhosphorylationELIKNISTAEQPYLF
HHHHHCCCCCCCEEE
30.34-
173N-linked_GlycosylationTRHVHFLNFSRFGGD
ECCEEECCHHHCCCC
31.72UniProtKB CARBOHYD
319N-linked_GlycosylationPEHRKLGNMTVTVKK
HHHCCCCCEEEEEEE
33.13UniProtKB CARBOHYD
359UbiquitinationKEQFHLLKRKFGLKS
HHHHHHHHHHHCCCC
60.96-

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 UST_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UST_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 UST_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S27A6_HUMANSLC27A6physical
28514442
INHBE_HUMANINHBEphysical
28514442
PPT2_HUMANPPT2physical
28514442
CALX_HUMANCANXphysical
28514442
DCAKD_HUMANDCAKDphysical
28514442
PON2_HUMANPON2physical
28514442
GSLG1_HUMANGLG1physical
28514442
GOLI4_HUMANGOLIM4physical
28514442
XYLT2_HUMANXYLT2physical
28514442
MA1A1_HUMANMAN1A1physical
28514442
JAG2_HUMANJAG2physical
28514442
OCAD1_HUMANOCIAD1physical
28514442
LDLR_HUMANLDLRphysical
28514442
IMPA3_HUMANIMPAD1physical
28514442
ERO1B_HUMANERO1LBphysical
28514442
OMA1_HUMANOMA1physical
28514442

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

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Related Literatures of Post-Translational Modification

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