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. |
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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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
13 | Ubiquitination | RMLLCFAFLWVLGIA HHHHHHHHHHHHHHH | 2.50 | - | |
21 | Ubiquitination | LWVLGIAYYMYSGGG HHHHHHHHHHHCCCC | 6.19 | - | |
25 | O-linked_Glycosylation | GIAYYMYSGGGSALA HHHHHHHCCCCCCCC | 17.90 | OGP | |
29 | O-linked_Glycosylation | YMYSGGGSALAGGAG HHHCCCCCCCCCCCC | 24.31 | OGP | |
42 | Ubiquitination | AGGGAGRKEDWNEID CCCCCCCCCCCCCCC | 60.14 | - | |
42 | Sumoylation | AGGGAGRKEDWNEID CCCCCCCCCCCCCCC | 60.14 | - | |
52 | Ubiquitination | WNEIDPIKKKDLHHS CCCCCCCCHHHCCCC | 60.19 | - | |
52 | 2-Hydroxyisobutyrylation | WNEIDPIKKKDLHHS CCCCCCCCHHHCCCC | 60.19 | - | |
53 | Ubiquitination | NEIDPIKKKDLHHSN CCCCCCCHHHCCCCC | 52.84 | - | |
67 | O-linked_Glycosylation | NGEEKAQSMETLPPG CHHHHHHHHCCCCCC | 24.36 | 55829319 | |
67 | Phosphorylation | NGEEKAQSMETLPPG CHHHHHHHHCCCCCC | 24.36 | 22210691 | |
70 | O-linked_Glycosylation | EKAQSMETLPPGKVR HHHHHHCCCCCCCCC | 35.60 | 55829323 | |
70 | Phosphorylation | EKAQSMETLPPGKVR HHHHHHCCCCCCCCC | 35.60 | 22210691 | |
72 | Ubiquitination | AQSMETLPPGKVRWP HHHHCCCCCCCCCCC | 42.91 | - | |
86 | Phosphorylation | PDFNQEAYVGGTMVR CCCCCEEEECCEEEE | 10.00 | 28102081 | |
90 | Phosphorylation | QEAYVGGTMVRSGQD CEEEECCEEEECCCC | 13.43 | 28102081 | |
94 | O-linked_Glycosylation | VGGTMVRSGQDPYAR ECCEEEECCCCHHHH | 29.42 | OGP | |
94 | Phosphorylation | VGGTMVRSGQDPYAR ECCEEEECCCCHHHH | 29.42 | 27486199 | |
99 | Ubiquitination | VRSGQDPYARNKFNQ EECCCCHHHHHCCCH | 26.87 | - | |
99 | Phosphorylation | VRSGQDPYARNKFNQ EECCCCHHHHHCCCH | 26.87 | 28102081 | |
103 | Sumoylation | QDPYARNKFNQVESD CCHHHHHCCCHHHHH | 39.89 | - | |
103 | Ubiquitination | QDPYARNKFNQVESD CCHHHHHCCCHHHHH | 39.89 | - | |
103 | Sumoylation | QDPYARNKFNQVESD CCHHHHHCCCHHHHH | 39.89 | - | |
103 | Acetylation | QDPYARNKFNQVESD CCHHHHHCCCHHHHH | 39.89 | 26051181 | |
109 | Phosphorylation | NKFNQVESDKLRMDR HCCCHHHHHHHCCCC | 40.98 | 20886841 | |
109 | Acetylation | NKFNQVESDKLRMDR HCCCHHHHHHHCCCC | 40.98 | 45474409 | |
111 | 2-Hydroxyisobutyrylation | FNQVESDKLRMDRAI CCHHHHHHHCCCCCC | 47.47 | - | |
111 | Acetylation | FNQVESDKLRMDRAI CCHHHHHHHCCCCCC | 47.47 | 26051181 | |
111 | Ubiquitination | FNQVESDKLRMDRAI CCHHHHHHHCCCCCC | 47.47 | - | |
128 | Ubiquitination | TRHDQCQRKQWRVDL CCHHHHHCCCEECCC | 40.53 | - | |
162 | Ubiquitination | TVVSVLKKSPPHLIK HHHHHHHHCCCHHEE | 65.12 | - | |
169 | Ubiquitination | KSPPHLIKEIILVDD HCCCHHEEEEEEECC | 49.58 | - | |
189 | Ubiquitination | EDGALLGKIEKVRVL HCCCCCCEEEEEEEE | 47.89 | 21906983 | |
218 | Ubiquitination | GADAAQAKVLTFLDS CCHHHHHHHHHHHHH | 26.20 | - | |
250 | Phosphorylation | EDRTRVVSPIIDVIN CCCCCCCCCEEEEEE | 13.92 | - | |
292 | Phosphorylation | MTPEQRRSRQGNPVA CCHHHHHHCCCCCCC | 31.01 | 21406692 | |
302 | Ubiquitination | GNPVAPIKTPMIAGG CCCCCCCCCCEECCC | 45.58 | - | |
302 | Acetylation | GNPVAPIKTPMIAGG CCCCCCCCCCEECCC | 45.58 | 30588867 | |
303 | Phosphorylation | NPVAPIKTPMIAGGL CCCCCCCCCEECCCE | 20.86 | 24043423 | |
317 | Phosphorylation | LFVMDKFYFEELGKY EEEEEEHHHHHHCCC | 18.80 | - | |
363 | Acetylation | RVGHVFRKQHPYTFP CCCEEEECCCCCCCC | 41.30 | 21651894 | |
363 | Ubiquitination | RVGHVFRKQHPYTFP CCCEEEECCCCCCCC | 41.30 | - | |
367 | Phosphorylation | VFRKQHPYTFPGGSG EEECCCCCCCCCCCC | 20.91 | 24114839 | |
368 | O-linked_Glycosylation | FRKQHPYTFPGGSGT EECCCCCCCCCCCCC | 28.01 | 55833067 | |
368 | Phosphorylation | FRKQHPYTFPGGSGT EECCCCCCCCCCCCC | 28.01 | 20068231 | |
373 | Phosphorylation | PYTFPGGSGTVFARN CCCCCCCCCCEEECC | 36.89 | 24114839 | |
373 | Acetylation | PYTFPGGSGTVFARN CCCCCCCCCCEEECC | 36.89 | 50672827 | |
375 | Phosphorylation | TFPGGSGTVFARNTR CCCCCCCCEEECCCH | 17.72 | 20068231 | |
392 | Phosphorylation | AEVWMDEYKNFYYAA HHHHHHHHCCEEEEE | 13.63 | - | |
393 | Ubiquitination | EVWMDEYKNFYYAAV HHHHHHHCCEEEEEC | 38.23 | - | |
402 | Phosphorylation | FYYAAVPSARNVPYG EEEEECCCCCCCCCC | 33.01 | - | |
402 | O-linked_Glycosylation | FYYAAVPSARNVPYG EEEEECCCCCCCCCC | 33.01 | 31492838 | |
408 | Phosphorylation | PSARNVPYGNIQSRL CCCCCCCCCCHHHHH | 20.65 | 20068231 | |
413 | Phosphorylation | VPYGNIQSRLELRKK CCCCCHHHHHHHHHH | 34.73 | 20068231 | |
420 | Methylation | SRLELRKKLSCKPFK HHHHHHHHHCCCCCH | 38.92 | - | |
434 | Phosphorylation | KWYLENVYPELRVPD HHHHHHCCHHHCCCC | 11.54 | - | |
506 | Phosphorylation | VVDRAPGSLIKLQGC EHHCCCCCEEEEECC | 26.34 | 24719451 | |
509 | Ubiquitination | RAPGSLIKLQGCREN CCCCCEEEEECCCCC | 39.80 | - | |
509 | Acetylation | RAPGSLIKLQGCREN CCCCCEEEEECCCCC | 39.80 | 25953088 | |
521 | Acetylation | RENDSRQKWEQIEGN CCCCCHHHHHHHHCC | 52.14 | 26051181 | |
521 | Ubiquitination | RENDSRQKWEQIEGN CCCCCHHHHHHHHCC | 52.14 | - | |
529 | Acetylation | WEQIEGNSKLRHVGS HHHHHCCCCEEEECC | 43.88 | 50672829 | |
529 | Phosphorylation | WEQIEGNSKLRHVGS HHHHHCCCCEEEECC | 43.88 | - | |
530 | Ubiquitination | EQIEGNSKLRHVGSN HHHHCCCCEEEECCC | 54.24 | - | |
530 | Sumoylation | EQIEGNSKLRHVGSN HHHHCCCCEEEECCC | 54.24 | - | |
530 | Sumoylation | EQIEGNSKLRHVGSN HHHHCCCCEEEECCC | 54.24 | - | |
536 | Phosphorylation | SKLRHVGSNLCLDSR CCEEEECCCCEECCC | 26.07 | 30108239 | |
546 | Ubiquitination | CLDSRTAKSGGLSVE EECCCCCCCCCEEEE | 49.36 | - | |
551 | Phosphorylation | TAKSGGLSVEVCGPA CCCCCCEEEEEECHH | 21.36 | 30243723 | |
560 | Phosphorylation | EVCGPALSQQWKFTL EEECHHHHHEEEEEE | 23.56 | 30243723 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of GALT2_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 GALT2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RS15A_HUMAN | RPS15A | physical | 22939629 | |
RT05_HUMAN | MRPS5 | physical | 22939629 | |
PR40A_HUMAN | PRPF40A | physical | 22939629 | |
KASH5_HUMAN | CCDC155 | physical | 25416956 |
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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