GALM_HUMAN - dbPTM
GALM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MASVTRAVF
------CCCHHHHHH
16.8319413330
14PhosphorylationAVFGELPSGGGTVEK
HHHCCCCCCCCCEEE
63.8028857561
18PhosphorylationELPSGGGTVEKFQLQ
CCCCCCCCEEEEEEC
28.8528857561
21UbiquitinationSGGGTVEKFQLQSDL
CCCCCEEEEEECCCC
33.79-
68UbiquitinationELEGYLQKQPYFGAV
HHHHHHHHCCCHHHH
51.12-
85UbiquitinationRVANRIAKGTFKVDG
HHHHHHHCEEEEECC
56.99-
93UbiquitinationGTFKVDGKEYHLAIN
EEEEECCEEEEEEEC
51.11-
101AcetylationEYHLAINKEPNSLHG
EEEEEECCCCCCCCC
69.327430741
101UbiquitinationEYHLAINKEPNSLHG
EEEEEECCCCCCCCC
69.32-
115UbiquitinationGGVRGFDKVLWTPRV
CCCCCCCCEEECCEE
36.65-
119PhosphorylationGFDKVLWTPRVLSNG
CCCCEEECCEEECCC
9.32-
124PhosphorylationLWTPRVLSNGVQFSR
EECCEEECCCEEEEE
28.7828857561
161PhosphorylationGGELIVNYRAQASQA
CCEEEEEEEEECCCC
9.09-
226UbiquitinationGTAFDLRKPVELGKH
CCEEECCCCHHHHHH
61.79-
291UbiquitinationNFLDGTLKGKNGAVY
CCCCCCEECCCCCEE
68.62-

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 GALM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GALM_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 GALM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATOX1_HUMANATOX1physical
26344197
GALK2_HUMANGALK2physical
26344197

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 GALM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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