UniProt ID | GALM_HUMAN | |
---|---|---|
UniProt AC | Q96C23 | |
Protein Name | Aldose 1-epimerase | |
Gene Name | GALM | |
Organism | Homo sapiens (Human). | |
Sequence Length | 342 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).. | |
Protein Sequence | MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFAELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTPRVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFNLAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLNGFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPKHSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MASVTRAVF ------CCCHHHHHH | 16.83 | 19413330 | |
14 | Phosphorylation | AVFGELPSGGGTVEK HHHCCCCCCCCCEEE | 63.80 | 28857561 | |
18 | Phosphorylation | ELPSGGGTVEKFQLQ CCCCCCCCEEEEEEC | 28.85 | 28857561 | |
21 | Ubiquitination | SGGGTVEKFQLQSDL CCCCCEEEEEECCCC | 33.79 | - | |
68 | Ubiquitination | ELEGYLQKQPYFGAV HHHHHHHHCCCHHHH | 51.12 | - | |
85 | Ubiquitination | RVANRIAKGTFKVDG HHHHHHHCEEEEECC | 56.99 | - | |
93 | Ubiquitination | GTFKVDGKEYHLAIN EEEEECCEEEEEEEC | 51.11 | - | |
101 | Acetylation | EYHLAINKEPNSLHG EEEEEECCCCCCCCC | 69.32 | 7430741 | |
101 | Ubiquitination | EYHLAINKEPNSLHG EEEEEECCCCCCCCC | 69.32 | - | |
115 | Ubiquitination | GGVRGFDKVLWTPRV CCCCCCCCEEECCEE | 36.65 | - | |
119 | Phosphorylation | GFDKVLWTPRVLSNG CCCCEEECCEEECCC | 9.32 | - | |
124 | Phosphorylation | LWTPRVLSNGVQFSR EECCEEECCCEEEEE | 28.78 | 28857561 | |
161 | Phosphorylation | GGELIVNYRAQASQA CCEEEEEEEEECCCC | 9.09 | - | |
226 | Ubiquitination | GTAFDLRKPVELGKH CCEEECCCCHHHHHH | 61.79 | - | |
291 | Ubiquitination | NFLDGTLKGKNGAVY CCCCCCEECCCCCEE | 68.62 | - |
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 GALM_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GALM_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 GALM_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ATOX1_HUMAN | ATOX1 | physical | 26344197 | |
GALK2_HUMAN | GALK2 | physical | 26344197 |
Kegg Disease | ||||||
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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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Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. |