GALT3_HUMAN - dbPTM
GALT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GALT3_HUMAN
UniProt AC Q14435
Protein Name Polypeptide N-acetylgalactosaminyltransferase 3
Gene Name GALNT3
Organism Homo sapiens (Human).
Sequence Length 633
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein . Resides preferentially in the trans and medial parts of the Golgi stack.
Protein Description Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis..
Protein Sequence MAHLKRLVKLHIKRHYHKKFWKLGAVIFFFIIVLVLMQREVSVQYSKEESRMERNMKNKNKMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNAPGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYVKQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTPTFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRLQCKNFTWYLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHGLGGNQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQIWEIQKDQLLYNPFLKMCLSANGEHPSLVSCNPSDPLQKWILSQND
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
42PhosphorylationVLMQREVSVQYSKEE
HHHHHHHHHCCCHHH
9.9622210691
130O-linked_GlycosylationASGKAFKTTNLSVEE
CCCCCEECCCCCHHH
17.9255824007
130PhosphorylationASGKAFKTTNLSVEE
CCCCCEECCCCCHHH
17.9228102081
131O-linked_GlycosylationSGKAFKTTNLSVEEQ
CCCCEECCCCCHHHH
34.4555824011
131PhosphorylationSGKAFKTTNLSVEEQ
CCCCEECCCCCHHHH
34.4528102081
132N-linked_GlycosylationGKAFKTTNLSVEEQK
CCCEECCCCCHHHHH
35.23UniProtKB CARBOHYD
134PhosphorylationAFKTTNLSVEEQKEK
CEECCCCCHHHHHHH
29.5626657352
297N-linked_GlycosylationLLARIAENYTAVVSP
HHHHHHHHCEEEECC
30.36UniProtKB CARBOHYD
395PhosphorylationGGENIEMSFRVWQCG
CCCCEEEEEEEEEEC
9.3424719451
421PhosphorylationGHVFRSKSPHSFPKG
EEEECCCCCCCCCCC
29.1428674419
447PhosphorylationAEVWMDEYKEIFYRR
HHHHHHHHHHHHHHC
15.06-
460AcetylationRRNTDAAKIVKQKAF
HCCCCHHHHHHHHHH
50.1511789869
472AcetylationKAFGDLSKRFEIKHR
HHHCCHHHHHHEEHH
69.2911789879
484N-linked_GlycosylationKHRLQCKNFTWYLNN
EHHHCCCCEEEHHCC
47.40UniProtKB CARBOHYD
598PhosphorylationIQKDQLLYNPFLKMC
EECCHHHCCHHHHHH
29.40-
626AcetylationNPSDPLQKWILSQND
CCCCHHHHHHHCCCC
43.8319815523

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 GALT3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GALT3_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 GALT3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APBP2_HUMANAPPBP2physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GALT3_HUMAN

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Related Literatures of Post-Translational Modification

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