GALT2_HUMAN - dbPTM
GALT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GALT2_HUMAN
UniProt AC Q10471
Protein Name Polypeptide N-acetylgalactosaminyltransferase 2
Gene Name GALNT2
Organism Homo sapiens (Human).
Sequence Length 571
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein . Secreted . Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.
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 a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region..
Protein Sequence MRRRSRMLLCFAFLWVLGIAYYMYSGGGSALAGGAGGGAGRKEDWNEIDPIKKKDLHHSNGEEKAQSMETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLRMDRAIPDTRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKKSPPHLIKEIILVDDYSNDPEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNEHWLEPLLERVAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAPIKTPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHVFRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKNFYYAAVPSARNVPYGNIQSRLELRKKLSCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNLQQ
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
13UbiquitinationRMLLCFAFLWVLGIA
HHHHHHHHHHHHHHH
2.50-
21UbiquitinationLWVLGIAYYMYSGGG
HHHHHHHHHHHCCCC
6.19-
25O-linked_GlycosylationGIAYYMYSGGGSALA
HHHHHHHCCCCCCCC
17.90OGP
29O-linked_GlycosylationYMYSGGGSALAGGAG
HHHCCCCCCCCCCCC
24.31OGP
42UbiquitinationAGGGAGRKEDWNEID
CCCCCCCCCCCCCCC
60.14-
42SumoylationAGGGAGRKEDWNEID
CCCCCCCCCCCCCCC
60.14-
52UbiquitinationWNEIDPIKKKDLHHS
CCCCCCCCHHHCCCC
60.19-
522-HydroxyisobutyrylationWNEIDPIKKKDLHHS
CCCCCCCCHHHCCCC
60.19-
53UbiquitinationNEIDPIKKKDLHHSN
CCCCCCCHHHCCCCC
52.84-
67O-linked_GlycosylationNGEEKAQSMETLPPG
CHHHHHHHHCCCCCC
24.3655829319
67PhosphorylationNGEEKAQSMETLPPG
CHHHHHHHHCCCCCC
24.3622210691
70O-linked_GlycosylationEKAQSMETLPPGKVR
HHHHHHCCCCCCCCC
35.6055829323
70PhosphorylationEKAQSMETLPPGKVR
HHHHHHCCCCCCCCC
35.6022210691
72UbiquitinationAQSMETLPPGKVRWP
HHHHCCCCCCCCCCC
42.91-
86PhosphorylationPDFNQEAYVGGTMVR
CCCCCEEEECCEEEE
10.0028102081
90PhosphorylationQEAYVGGTMVRSGQD
CEEEECCEEEECCCC
13.4328102081
94O-linked_GlycosylationVGGTMVRSGQDPYAR
ECCEEEECCCCHHHH
29.42OGP
94PhosphorylationVGGTMVRSGQDPYAR
ECCEEEECCCCHHHH
29.4227486199
99UbiquitinationVRSGQDPYARNKFNQ
EECCCCHHHHHCCCH
26.87-
99PhosphorylationVRSGQDPYARNKFNQ
EECCCCHHHHHCCCH
26.8728102081
103SumoylationQDPYARNKFNQVESD
CCHHHHHCCCHHHHH
39.89-
103UbiquitinationQDPYARNKFNQVESD
CCHHHHHCCCHHHHH
39.89-
103SumoylationQDPYARNKFNQVESD
CCHHHHHCCCHHHHH
39.89-
103AcetylationQDPYARNKFNQVESD
CCHHHHHCCCHHHHH
39.8926051181
109PhosphorylationNKFNQVESDKLRMDR
HCCCHHHHHHHCCCC
40.9820886841
109AcetylationNKFNQVESDKLRMDR
HCCCHHHHHHHCCCC
40.9845474409
1112-HydroxyisobutyrylationFNQVESDKLRMDRAI
CCHHHHHHHCCCCCC
47.47-
111AcetylationFNQVESDKLRMDRAI
CCHHHHHHHCCCCCC
47.4726051181
111UbiquitinationFNQVESDKLRMDRAI
CCHHHHHHHCCCCCC
47.47-
128UbiquitinationTRHDQCQRKQWRVDL
CCHHHHHCCCEECCC
40.53-
162UbiquitinationTVVSVLKKSPPHLIK
HHHHHHHHCCCHHEE
65.12-
169UbiquitinationKSPPHLIKEIILVDD
HCCCHHEEEEEEECC
49.58-
189UbiquitinationEDGALLGKIEKVRVL
HCCCCCCEEEEEEEE
47.8921906983
218UbiquitinationGADAAQAKVLTFLDS
CCHHHHHHHHHHHHH
26.20-
250PhosphorylationEDRTRVVSPIIDVIN
CCCCCCCCCEEEEEE
13.92-
292PhosphorylationMTPEQRRSRQGNPVA
CCHHHHHHCCCCCCC
31.0121406692
302UbiquitinationGNPVAPIKTPMIAGG
CCCCCCCCCCEECCC
45.58-
302AcetylationGNPVAPIKTPMIAGG
CCCCCCCCCCEECCC
45.5830588867
303PhosphorylationNPVAPIKTPMIAGGL
CCCCCCCCCEECCCE
20.8624043423
317PhosphorylationLFVMDKFYFEELGKY
EEEEEEHHHHHHCCC
18.80-
363AcetylationRVGHVFRKQHPYTFP
CCCEEEECCCCCCCC
41.3021651894
363UbiquitinationRVGHVFRKQHPYTFP
CCCEEEECCCCCCCC
41.30-
367PhosphorylationVFRKQHPYTFPGGSG
EEECCCCCCCCCCCC
20.9124114839
368O-linked_GlycosylationFRKQHPYTFPGGSGT
EECCCCCCCCCCCCC
28.0155833067
368PhosphorylationFRKQHPYTFPGGSGT
EECCCCCCCCCCCCC
28.0120068231
373PhosphorylationPYTFPGGSGTVFARN
CCCCCCCCCCEEECC
36.8924114839
373AcetylationPYTFPGGSGTVFARN
CCCCCCCCCCEEECC
36.8950672827
375PhosphorylationTFPGGSGTVFARNTR
CCCCCCCCEEECCCH
17.7220068231
392PhosphorylationAEVWMDEYKNFYYAA
HHHHHHHHCCEEEEE
13.63-
393UbiquitinationEVWMDEYKNFYYAAV
HHHHHHHCCEEEEEC
38.23-
402PhosphorylationFYYAAVPSARNVPYG
EEEEECCCCCCCCCC
33.01-
402O-linked_GlycosylationFYYAAVPSARNVPYG
EEEEECCCCCCCCCC
33.0131492838
408PhosphorylationPSARNVPYGNIQSRL
CCCCCCCCCCHHHHH
20.6520068231
413PhosphorylationVPYGNIQSRLELRKK
CCCCCHHHHHHHHHH
34.7320068231
420MethylationSRLELRKKLSCKPFK
HHHHHHHHHCCCCCH
38.92-
434PhosphorylationKWYLENVYPELRVPD
HHHHHHCCHHHCCCC
11.54-
506PhosphorylationVVDRAPGSLIKLQGC
EHHCCCCCEEEEECC
26.3424719451
509UbiquitinationRAPGSLIKLQGCREN
CCCCCEEEEECCCCC
39.80-
509AcetylationRAPGSLIKLQGCREN
CCCCCEEEEECCCCC
39.8025953088
521AcetylationRENDSRQKWEQIEGN
CCCCCHHHHHHHHCC
52.1426051181
521UbiquitinationRENDSRQKWEQIEGN
CCCCCHHHHHHHHCC
52.14-
529AcetylationWEQIEGNSKLRHVGS
HHHHHCCCCEEEECC
43.8850672829
529PhosphorylationWEQIEGNSKLRHVGS
HHHHHCCCCEEEECC
43.88-
530UbiquitinationEQIEGNSKLRHVGSN
HHHHCCCCEEEECCC
54.24-
530SumoylationEQIEGNSKLRHVGSN
HHHHCCCCEEEECCC
54.24-
530SumoylationEQIEGNSKLRHVGSN
HHHHCCCCEEEECCC
54.24-
536PhosphorylationSKLRHVGSNLCLDSR
CCEEEECCCCEECCC
26.0730108239
546UbiquitinationCLDSRTAKSGGLSVE
EECCCCCCCCCEEEE
49.36-
551PhosphorylationTAKSGGLSVEVCGPA
CCCCCCEEEEEECHH
21.3630243723
560PhosphorylationEVCGPALSQQWKFTL
EEECHHHHHEEEEEE
23.5630243723

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 GALT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GALT2_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 GALT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS15A_HUMANRPS15Aphysical
22939629
RT05_HUMANMRPS5physical
22939629
PR40A_HUMANPRPF40Aphysical
22939629
KASH5_HUMANCCDC155physical
25416956

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 GALT2_HUMAN

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Related Literatures of Post-Translational Modification

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