UniProt ID | B4GT5_HUMAN | |
---|---|---|
UniProt AC | O43286 | |
Protein Name | Beta-1,4-galactosyltransferase 5 | |
Gene Name | B4GALT5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 388 | |
Subcellular Localization |
Golgi apparatus, Golgi stack membrane Single-pass type II membrane protein. Trans cisternae of Golgi stack. |
|
Protein Description | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.. | |
Protein Sequence | MRARRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNVRTIGAQVYEQVLRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDYIHELFSKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLLPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPHHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVNEY | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
59 | Phosphorylation | LIRDNVRTIGAQVYE EEECCHHHHHHHHHH | 21.34 | - | |
59 | O-linked_Glycosylation | LIRDNVRTIGAQVYE EEECCHHHHHHHHHH | 21.34 | 46171049 | |
71 | Phosphorylation | VYEQVLRSAYAKRNS HHHHHHHHHHHHHCC | 22.82 | - | |
73 | Phosphorylation | EQVLRSAYAKRNSSV HHHHHHHHHHHCCCC | 17.57 | - | |
75 | Ubiquitination | VLRSAYAKRNSSVND HHHHHHHHHCCCCCC | 39.16 | 27667366 | |
77 | N-linked_Glycosylation | RSAYAKRNSSVNDSD HHHHHHHCCCCCCCC | 37.62 | UniProtKB CARBOHYD | |
81 | N-linked_Glycosylation | AKRNSSVNDSDYPLD HHHCCCCCCCCCCCC | 45.04 | UniProtKB CARBOHYD | |
90 | N-linked_Glycosylation | SDYPLDLNHSETFLQ CCCCCCCCCCHHHHH | 35.98 | UniProtKB CARBOHYD | |
98 | O-linked_Glycosylation | HSETFLQTTTFLPED CCHHHHHCCCCCCCH | 29.92 | OGP | |
111 | N-linked_Glycosylation | EDFTYFANHTCPERL CHHCHHCCCCCCCCC | 22.54 | UniProtKB CARBOHYD | |
128 | N-linked_Glycosylation | MKGPIDINMSEIGMD CCCCCCCCHHHHCHH | 24.95 | UniProtKB CARBOHYD | |
142 | Phosphorylation | DYIHELFSKDPTIKL HHHHHHHCCCCCEEE | 49.09 | 24719451 | |
156 | Phosphorylation | LGGHWKPSDCMPRWK ECCEECHHHCCCCCE | 39.45 | 26074081 | |
258 | Ubiquitination | MPRHFATKLDKYMYL CCHHHHHHHHHHHHH | 51.78 | 27667366 | |
285 | Ubiquitination | LTVEQFRKINGFPNA CCHHHHHHHCCCCCC | 41.64 | - | |
321 | Phosphorylation | VSRPEGDTGKYKSIP CCCCCCCCCCCCCCC | 46.56 | 30576142 | |
323 | Ubiquitination | RPEGDTGKYKSIPHH CCCCCCCCCCCCCCC | 52.15 | 21906983 | |
325 | Ubiquitination | EGDTGKYKSIPHHHR CCCCCCCCCCCCCCC | 45.45 | 22817900 | |
364 | N-linked_Glycosylation | NNLNYFANITYDALY CCCHHHHCCCHHHHH | 19.75 | UniProtKB CARBOHYD | |
373 | N-linked_Glycosylation | TYDALYKNITVNLTP CHHHHHCCEEEECCH | 22.93 | UniProtKB CARBOHYD | |
375 | Phosphorylation | DALYKNITVNLTPEL HHHHCCEEEECCHHH | 16.85 | - | |
388 | Phosphorylation | ELAQVNEY------- HHHHHCCC------- | 20.74 | - |
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 B4GT5_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of B4GT5_HUMAN !! |
* 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 B4GT5_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of B4GT5_HUMAN !! |
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. |
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