SG196_HUMAN - dbPTM
SG196_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SG196_HUMAN
UniProt AC Q9H5K3
Protein Name Protein O-mannose kinase
Gene Name POMK
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif..
Protein Sequence MEKQPQNSRRGLAPREVPPAVGLLLIMALMNTLLYLCLDHFFIAPRQSTVDPTHCPYGHFRIGQMKNCSPWLSCEELRTEVRQLKRVGEGAVKRVFLSEWKEHKVALSQLTSLEMKDDFLHGLQMLKSLQGTHVVTLLGYCEDDNTMLTEYHPLGSLSNLEETLNLSKYQNVNTWQHRLELAMDYVSIINYLHHSPVGTRVMCDSNDLPKTLSQYLLTSNFSILANDLDALPLVNHSSGMLVKCGHRELHGDFVAPEQLWPYGEDVPFHDDLMPSYDEKIDIWKIPDISSFLLGHIEGSDMVRFHLFDIHKACKSQTPSERPTAQDVLETYQKVLDTLRDAMMSQAREML
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
1Acetylation-------MEKQPQNS
-------CCCCCCCC
15.2122814378
3Ubiquitination-----MEKQPQNSRR
-----CCCCCCCCCC
67.0133845483
93UbiquitinationRVGEGAVKRVFLSEW
HHCCHHHHHHHHHHH
42.1629967540
101UbiquitinationRVFLSEWKEHKVALS
HHHHHHHHHHHHHHH
45.9829967540
104UbiquitinationLSEWKEHKVALSQLT
HHHHHHHHHHHHHHC
30.2329967540
108PhosphorylationKEHKVALSQLTSLEM
HHHHHHHHHHCCHHC
17.2628450419
116UbiquitinationQLTSLEMKDDFLHGL
HHCCHHCHHCHHHHH
44.78-
165N-linked_GlycosylationSNLEETLNLSKYQNV
CCHHHHHCCHHCCCC
50.08UniProtKB CARBOHYD
220N-linked_GlycosylationSQYLLTSNFSILAND
HHHHHHCCCHHHCCC
29.46UniProtKB CARBOHYD
235N-linked_GlycosylationLDALPLVNHSSGMLV
CCCCCCCCCCCCCEE
36.69UniProtKB CARBOHYD
311UbiquitinationFHLFDIHKACKSQTP
EEEEEHHHHHHCCCC
56.67-
314UbiquitinationFDIHKACKSQTPSER
EEHHHHHHCCCCCCC
50.9229967540

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 SG196_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SG196_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 SG196_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CERS2_HUMANCERS2physical
26186194
MBOA7_HUMANMBOAT7physical
26186194
GOGA5_HUMANGOLGA5physical
26186194
CALX_HUMANCANXphysical
26186194
LRP5_HUMANLRP5physical
26186194
LRP6_HUMANLRP6physical
26186194
GOLI4_HUMANGOLIM4physical
26186194
GHITM_HUMANGHITMphysical
26186194
FANCJ_HUMANBRIP1physical
26186194
XYLT2_HUMANXYLT2physical
26186194
TM246_HUMANTMEM246physical
26186194
PMGT1_HUMANPOMGNT1physical
26186194
POMT1_HUMANPOMT1physical
26186194
TYW1B_HUMANTYW1Bphysical
26186194
MOCS3_HUMANMOCS3physical
26186194
RDH11_HUMANRDH11physical
26186194
FITM2_HUMANFITM2physical
26186194
PKDCC_HUMANPKDCCphysical
26186194
UBP30_HUMANUSP30physical
26186194
ALG5_HUMANALG5physical
26186194
KDSR_HUMANKDSRphysical
26186194
LTMD1_HUMANLETMD1physical
26186194
AT5G1_HUMANATP5G1physical
26186194
BI1_HUMANTMBIM6physical
26186194
PIGM_HUMANPIGMphysical
26186194
S19A2_HUMANSLC19A2physical
26186194
MTX1_HUMANMTX1physical
26186194
B4GT3_HUMANB4GALT3physical
26186194
TMPPE_HUMANTMPPEphysical
26186194
FA69A_HUMANFAM69Aphysical
26186194
GBB2_HUMANGNB2physical
26186194
S35F2_HUMANSLC35F2physical
26186194
YIF1A_HUMANYIF1Aphysical
26186194
HBD_HUMANHBDphysical
26186194
MBOA5_HUMANLPCAT3physical
26186194
CERS6_HUMANCERS6physical
26186194
ZDHC6_HUMANZDHHC6physical
26186194
AG10A_HUMANALG10physical
26186194
TM39B_HUMANTMEM39Bphysical
26186194
B4GT1_HUMANB4GALT1physical
26186194
RER1_HUMANRER1physical
26186194
ARV1_HUMANARV1physical
26186194
RETR3_HUMANFAM134Cphysical
26186194
NAT14_HUMANNAT14physical
26186194
DGAT1_HUMANDGAT1physical
26186194
T120A_HUMANTMEM120Aphysical
26186194
NEUFC_HUMANCYB5D2physical
26186194
T120B_HUMANTMEM120Bphysical
26186194
TNFL9_HUMANTNFSF9physical
26186194
S1PR2_HUMANS1PR2physical
26186194
PIGB_HUMANPIGBphysical
26186194
REEP4_HUMANREEP4physical
26186194
TMM56_HUMANTMEM56physical
26186194
S47A1_HUMANSLC47A1physical
26186194
PKDCC_HUMANPKDCCphysical
28514442
FANCJ_HUMANBRIP1physical
28514442
LRP5_HUMANLRP5physical
28514442
LTMD1_HUMANLETMD1physical
28514442
T120A_HUMANTMEM120Aphysical
28514442
S35F2_HUMANSLC35F2physical
28514442
ZDHC6_HUMANZDHHC6physical
28514442
GOGA5_HUMANGOLGA5physical
28514442
LRP6_HUMANLRP6physical
28514442
UBP30_HUMANUSP30physical
28514442
PIGB_HUMANPIGBphysical
28514442
AT5G1_HUMANATP5G1physical
28514442
DGAT1_HUMANDGAT1physical
28514442
XYLT2_HUMANXYLT2physical
28514442
NU4M_HUMANND4physical
28514442
RETR3_HUMANFAM134Cphysical
28514442
S19A2_HUMANSLC19A2physical
28514442
REEP4_HUMANREEP4physical
28514442
TMM56_HUMANTMEM56physical
28514442
MBOA5_HUMANLPCAT3physical
28514442
CERS6_HUMANCERS6physical
28514442
CERS2_HUMANCERS2physical
28514442
S47A1_HUMANSLC47A1physical
28514442
T120B_HUMANTMEM120Bphysical
28514442
BI1_HUMANTMBIM6physical
28514442
CALX_HUMANCANXphysical
28514442
PIGM_HUMANPIGMphysical
28514442
B4GT3_HUMANB4GALT3physical
28514442
MOCS3_HUMANMOCS3physical
28514442
GOLI4_HUMANGOLIM4physical
28514442
TYW1B_HUMANTYW1Bphysical
28514442
S22AI_HUMANSLC22A18physical
28514442
ARV1_HUMANARV1physical
28514442
NEUFC_HUMANCYB5D2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SG196_HUMAN

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Related Literatures of Post-Translational Modification

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