POMT1_HUMAN - dbPTM
POMT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationLKRPVVVTADINLSL
CCCCEEEEECCCHHH
13.65-
18PhosphorylationVTADINLSLVALTGM
EEECCCHHHHHHHHH
19.13-
103PhosphorylationSSNVPVWSLRLLPAL
CCCCCHHHHHHHHHH
12.1224719451
120PhosphorylationALSVPMAYQIVLELH
HCCCCHHHHHHHHHH
7.7924043423
129PhosphorylationIVLELHFSHCAAMGA
HHHHHHHHHHHHHHH
13.6024043423
148PhosphorylationLIENALITQSRLMLL
HHHHHHHHHHHHHHH
22.7224043423
150PhosphorylationENALITQSRLMLLES
HHHHHHHHHHHHHHH
20.8024043423
157PhosphorylationSRLMLLESVLIFFNL
HHHHHHHHHHHHHHH
23.3829978859
169PhosphorylationFNLLAVLSYLKFFNC
HHHHHHHHHHHHCCC
23.0929978859
170PhosphorylationNLLAVLSYLKFFNCQ
HHHHHHHHHHHCCCC
15.1129978859
303 (in isoform 3)Ubiquitination-29.7421906983
335UbiquitinationTLRNVFGKPVPCWLH
EEECCCCCEECEEEE
31.23-
357 (in isoform 2)Ubiquitination-34.5921906983
370UbiquitinationQVTCYPFKDVNNWWI
EEEEEECCCCCCEEE
57.15-
379UbiquitinationVNNWWIVKDPRRHQL
CCCEEEEECCCCCCE
53.532190698
379 (in isoform 1)Ubiquitination-53.5321906983
389PhosphorylationRRHQLVVSSPPRPVR
CCCCEEECCCCCCCC
29.6422210691
435N-linked_GlycosylationVSCYIDYNISMPAQN
EEEEEEECCCCCCCC
18.99UniProtKB CARBOHYD
459UbiquitinationGSDTDVWKTILSEVR
CCCHHHHHHHHHHCE
26.07-
471N-linked_GlycosylationEVRFVHVNTSAVLKL
HCEEEEECHHHHHHH
17.2819159218
479PhosphorylationTSAVLKLSGAHLPDW
HHHHHHHCCCCCCCC
32.14-
488PhosphorylationAHLPDWGYRQLEIVG
CCCCCCCCCCEEECC
7.31-
497UbiquitinationQLEIVGEKLSRGYHG
CEEECCEECCCCCCC
45.92-
539N-linked_GlycosylationAQVDVSRNLSFMARF
HHCCCHHCHHHHHHH
32.31UniProtKB CARBOHYD
547PhosphorylationLSFMARFSELQWRML
HHHHHHHHHHHHHHH
31.6624670416
581PhosphorylationTLDTNIAYWLHPRTS
ECCCCCCHHCCCCCH
12.5222817900
720PhosphorylationSNTLRPLTYGDKSLS
CCCCCCCCCCCCCCC
28.3025002506
721PhosphorylationNTLRPLTYGDKSLSP
CCCCCCCCCCCCCCH
30.8925002506
727PhosphorylationTYGDKSLSPHELKAL
CCCCCCCCHHHHHHH
31.1628674419
732UbiquitinationSLSPHELKALRWKDS
CCCHHHHHHHHCHHH
42.25-

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 POMT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POMT1_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 POMT1_HUMAN !!

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

Oops, there are no PPI records of POMT1_HUMAN !!

Drug and Disease Associations
Kegg Disease
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
613155Muscular dystrophy-dystroglycanopathy congenital with mental retardation B1 (MDDGB1)
236670Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A1 (MDDGA1)
609308Muscular 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.
Regulatory Network of POMT1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

TOP