UniProt ID | POMT1_HUMAN | |
---|---|---|
UniProt AC | Q9Y6A1 | |
Protein Name | Protein O-mannosyl-transferase 1 | |
Gene Name | POMT1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 747 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient.. | |
Protein Sequence | MWGFLKRPVVVTADINLSLVALTGMGLLSRLWRLTYPRAVVFDEVYYGQYISFYMKQIFFLDDSGPPFGHMVLALGGYLGGFDGNFLWNRIGAEYSSNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVGADVQCCMRPACMGQMQMSQGVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVFRSGPHDQIMSSAFQASLEGGLARITQGQPLEVAFGSQVTLRNVFGKPVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGYHGSTVWNVEEHRYGASQEQRERERELHSPAQVDVSRNLSFMARFSELQWRMLALRSDDSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRRRNVHDLPQDAWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCRSQLQRSIFSALVVAWYSSACHVSNTLRPLTYGDKSLSPHELKALRWKDSWDILIRKH | |
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 |
---|---|---|---|---|---|
12 | Phosphorylation | LKRPVVVTADINLSL CCCCEEEEECCCHHH | 13.65 | - | |
18 | Phosphorylation | VTADINLSLVALTGM EEECCCHHHHHHHHH | 19.13 | - | |
103 | Phosphorylation | SSNVPVWSLRLLPAL CCCCCHHHHHHHHHH | 12.12 | 24719451 | |
120 | Phosphorylation | ALSVPMAYQIVLELH HCCCCHHHHHHHHHH | 7.79 | 24043423 | |
129 | Phosphorylation | IVLELHFSHCAAMGA HHHHHHHHHHHHHHH | 13.60 | 24043423 | |
148 | Phosphorylation | LIENALITQSRLMLL HHHHHHHHHHHHHHH | 22.72 | 24043423 | |
150 | Phosphorylation | ENALITQSRLMLLES HHHHHHHHHHHHHHH | 20.80 | 24043423 | |
157 | Phosphorylation | SRLMLLESVLIFFNL HHHHHHHHHHHHHHH | 23.38 | 29978859 | |
169 | Phosphorylation | FNLLAVLSYLKFFNC HHHHHHHHHHHHCCC | 23.09 | 29978859 | |
170 | Phosphorylation | NLLAVLSYLKFFNCQ HHHHHHHHHHHCCCC | 15.11 | 29978859 | |
303 (in isoform 3) | Ubiquitination | - | 29.74 | 21906983 | |
335 | Ubiquitination | TLRNVFGKPVPCWLH EEECCCCCEECEEEE | 31.23 | - | |
357 (in isoform 2) | Ubiquitination | - | 34.59 | 21906983 | |
370 | Ubiquitination | QVTCYPFKDVNNWWI EEEEEECCCCCCEEE | 57.15 | - | |
379 | Ubiquitination | VNNWWIVKDPRRHQL CCCEEEEECCCCCCE | 53.53 | 2190698 | |
379 (in isoform 1) | Ubiquitination | - | 53.53 | 21906983 | |
389 | Phosphorylation | RRHQLVVSSPPRPVR CCCCEEECCCCCCCC | 29.64 | 22210691 | |
435 | N-linked_Glycosylation | VSCYIDYNISMPAQN EEEEEEECCCCCCCC | 18.99 | UniProtKB CARBOHYD | |
459 | Ubiquitination | GSDTDVWKTILSEVR CCCHHHHHHHHHHCE | 26.07 | - | |
471 | N-linked_Glycosylation | EVRFVHVNTSAVLKL HCEEEEECHHHHHHH | 17.28 | 19159218 | |
479 | Phosphorylation | TSAVLKLSGAHLPDW HHHHHHHCCCCCCCC | 32.14 | - | |
488 | Phosphorylation | AHLPDWGYRQLEIVG CCCCCCCCCCEEECC | 7.31 | - | |
497 | Ubiquitination | QLEIVGEKLSRGYHG CEEECCEECCCCCCC | 45.92 | - | |
539 | N-linked_Glycosylation | AQVDVSRNLSFMARF HHCCCHHCHHHHHHH | 32.31 | UniProtKB CARBOHYD | |
547 | Phosphorylation | LSFMARFSELQWRML HHHHHHHHHHHHHHH | 31.66 | 24670416 | |
581 | Phosphorylation | TLDTNIAYWLHPRTS ECCCCCCHHCCCCCH | 12.52 | 22817900 | |
720 | Phosphorylation | SNTLRPLTYGDKSLS CCCCCCCCCCCCCCC | 28.30 | 25002506 | |
721 | Phosphorylation | NTLRPLTYGDKSLSP CCCCCCCCCCCCCCH | 30.89 | 25002506 | |
727 | Phosphorylation | TYGDKSLSPHELKAL CCCCCCCCHHHHHHH | 31.16 | 28674419 | |
732 | Ubiquitination | SLSPHELKALRWKDS CCCHHHHHHHHCHHH | 42.25 | - |
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 POMT1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of POMT1_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 POMT1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of POMT1_HUMAN !! |
Kegg Disease | ||||||
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H00120 | Dystroglycanopathy; Walker-Warburg syndrome (WWS); Muscle-eye-brain disease (MEB); Fukuyama congenit | |||||
H00590 | Congenital muscular dystrophies (CMD/MDC), including: Merosin-deficient CMD (MDC1A); Ullrich CMD (UC | |||||
H00593 | Limb-girdle muscular dystrophy (LGMD) | |||||
OMIM Disease | ||||||
613155 | Muscular dystrophy-dystroglycanopathy congenital with mental retardation B1 (MDDGB1) | |||||
236670 | Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A1 (MDDGA1) | |||||
609308 | Muscular dystrophy-dystroglycanopathy limb-girdle C1 (MDDGC1) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-471, AND MASSSPECTROMETRY. |