GLT12_HUMAN - dbPTM
GLT12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLT12_HUMAN
UniProt AC Q8IXK2
Protein Name Polypeptide N-acetylgalactosaminyltransferase 12
Gene Name GALNT12
Organism Homo sapiens (Human).
Sequence Length 581
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
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 non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs..
Protein Sequence MWGRTARRRCPRELRRGREALLVLLALLALAGLGSVLRAQRGAGAGAAEPGPPRTPRPGRREPVMPRPPVPANALGARGEAVRLQLQGEELRLQEESVRLHQINIYLSDRISLHRRLPERWNPLCKEKKYDYDNLPRTSVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKERLANELSGLPKVRLIRANKREGLVRARLLGASAARGDVLTFLDCHCECHEGWLEPLLQRIHEEESAVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHTVPERERIRMQSPVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVYPELHVPEDRPGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML
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
112UbiquitinationIYLSDRISLHRRLPE
EEECCCCCHHHCCHH
21.0124816145
122UbiquitinationRRLPERWNPLCKEKK
HCCHHHCCHHHHCCC
26.3624816145
126UbiquitinationERWNPLCKEKKYDYD
HHCCHHHHCCCCCCC
79.03-
128UbiquitinationWNPLCKEKKYDYDNL
CCHHHHCCCCCCCCC
41.97-
129UbiquitinationNPLCKEKKYDYDNLP
CHHHHCCCCCCCCCC
44.43-
196UbiquitinationNELSGLPKVRLIRAN
HHHCCCCHHEEEECC
45.0624816145
300PhosphorylationRERIRMQSPVDVIRS
HHHHCCCCCCCCCCC
19.9729083192
307PhosphorylationSPVDVIRSPTMAGGL
CCCCCCCCCCCCCCH
17.3824719451
309PhosphorylationVDVIRSPTMAGGLFA
CCCCCCCCCCCCHHH
22.3924719451
318PhosphorylationAGGLFAVSKKYFEYL
CCCHHHCCHHHHHHH
21.7229083192
320UbiquitinationGLFAVSKKYFEYLGS
CHHHCCHHHHHHHCC
47.90-
343PhosphorylationGGENLEFSFRIWQCG
CCCCCEEEEEEEEEC
12.3024719451
375UbiquitinationQAPYSRNKALANSVR
CCCCCHHHHHHHHHH
43.6029967540
544PhosphorylationGSLFHEQSKKCVQAA
CCCCHHHHHHHHHHH
30.9725247763
555PhosphorylationVQAARKESSDSFVPL
HHHHHHHCCCCCHHH
42.3426657352
556PhosphorylationQAARKESSDSFVPLL
HHHHHHCCCCCHHHH
38.0627486199
558PhosphorylationARKESSDSFVPLLRD
HHHHCCCCCHHHHHH
30.0527486199

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 GLT12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLT12_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 GLT12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUC1_HUMANMUC1physical
12135769
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLT12_HUMAN

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Related Literatures of Post-Translational Modification

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