B3GN2_HUMAN - dbPTM
B3GN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B3GN2_HUMAN
UniProt AC Q9NY97
Protein Name N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
Gene Name B3GNT2
Organism Homo sapiens (Human).
Sequence Length 397
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein .
Protein Description Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors. [PubMed: 9892646 Probably constitutes the main polylactosamine synthase.]
Protein Sequence MSVGRRRIKLLGILMMANVFIYFIMEVSKSSSQEKNGKGEVIIPKEKFWKISTPPEAYWNREQEKLNRQYNPILSMLTNQTGEAGRLSNISHLNYCEPDLRVTSVVTGFNNLPDRFKDFLLYLRCRNYSLLIDQPDKCAKKPFLLLAIKSLTPHFARRQAIRESWGQESNAGNQTVVRVFLLGQTPPEDNHPDLSDMLKFESEKHQDILMWNYRDTFFNLSLKEVLFLRWVSTSCPDTEFVFKGDDDVFVNTHHILNYLNSLSKTKAKDLFIGDVIHNAGPHRDKKLKYYIPEVVYSGLYPPYAGGGGFLYSGHLALRLYHITDQVHLYPIDDVYTGMCLQKLGLVPEKHKGFRTFDIEEKNKNNICSYVDLMLVHSRKPQEMIDIWSQLQSAHLKC
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
22PhosphorylationMMANVFIYFIMEVSK
HHHHHHHHHHHHHHH		3.9022817900
28PhosphorylationIYFIMEVSKSSSQEK
HHHHHHHHHCCCCCC		17.32-
45UbiquitinationKGEVIIPKEKFWKIS
CCEEEEEHHHHCCCC		64.2322817900
46 (in isoform 2)Ubiquitination-48.4021890473
47UbiquitinationEVIIPKEKFWKISTP
EEEEEHHHHCCCCCC		63.7522817900
50UbiquitinationIPKEKFWKISTPPEA
EEHHHHCCCCCCHHH		29.8821890473
50 (in isoform 1)Ubiquitination-29.8821890473
50UbiquitinationIPKEKFWKISTPPEA
EEHHHHCCCCCCHHH		29.8821890473
79N-linked_GlycosylationPILSMLTNQTGEAGR
HHHHHHHCCCCCCCC		33.1916335952
89N-linked_GlycosylationGEAGRLSNISHLNYC
CCCCCCCCCCCCCCC		44.36UniProtKB CARBOHYD
122PhosphorylationRFKDFLLYLRCRNYS
HHHHHHHHHHCCCCE		8.3423025827
127N-linked_GlycosylationLLYLRCRNYSLLIDQ
HHHHHCCCCEEEECC		34.08UniProtKB CARBOHYD
137UbiquitinationLLIDQPDKCAKKPFL
EEECCCHHHCCCCHH		42.65-
173N-linked_GlycosylationGQESNAGNQTVVRVF
CCCCCCCCCEEEEEE		31.75UniProtKB CARBOHYD
175PhosphorylationESNAGNQTVVRVFLL
CCCCCCCEEEEEEEE		25.6024719451
195 (in isoform 2)Ubiquitination-28.4921890473
199UbiquitinationPDLSDMLKFESEKHQ
CCHHHHHHHCCHHHC		40.2121906983
199 (in isoform 1)Ubiquitination-40.2121890473
219N-linked_GlycosylationNYRDTFFNLSLKEVL
CCHHHCCCCCHHHHH		25.24UniProtKB CARBOHYD
221PhosphorylationRDTFFNLSLKEVLFL
HHHCCCCCHHHHHHH		38.2024719451
264 (in isoform 2)Ubiquitination-60.3821890473
264UbiquitinationNYLNSLSKTKAKDLF
HHHHHCCCCCCHHHC		60.38-
268UbiquitinationSLSKTKAKDLFIGDV
HCCCCCCHHHCCCHH		57.4221906983
268 (in isoform 1)Ubiquitination-57.4221890473
349UbiquitinationKLGLVPEKHKGFRTF
HHCCCCCCCCCCCCC		44.5427667366
357 (in isoform 2)Ubiquitination-46.9421890473
361 (in isoform 1)Ubiquitination-61.5021890473
361UbiquitinationRTFDIEEKNKNNICS
CCCCCHHHCCCCCCH		61.502190698
368PhosphorylationKNKNNICSYVDLMLV
HCCCCCCHHHEEEHH		25.1322210691
377PhosphorylationVDLMLVHSRKPQEMI
HEEEHHHCCCHHHHH		34.2222210691
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 B3GN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of B3GN2_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 B3GN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM246_HUMANTMEM246physical
21988832
TBB8_HUMANTUBB8physical
26186194
C1GLC_HUMANC1GALT1C1physical
26186194
TOR3A_HUMANTOR3Aphysical
26186194
TMTC3_HUMANTMTC3physical
26186194
LDLR_HUMANLDLRphysical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
AMD_HUMANPAMphysical
26186194
ADA10_HUMANADAM10physical
26186194
NDUAA_HUMANNDUFA10physical
26186194
PON2_HUMANPON2physical
26186194
FAM3A_HUMANFAM3Aphysical
26186194
CAN2_HUMANCAPN2physical
26186194
ITA7_HUMANITGA7physical
26186194
FAM3C_HUMANFAM3Cphysical
26186194
CDK3_HUMANCDK3physical
26186194
MOXD1_HUMANMOXD1physical
26186194
GALT7_HUMANGALNT7physical
26186194
ATS2_HUMANADAMTS2physical
26186194
PCD20_HUMANPCDH20physical
26186194
CDK3_HUMANCDK3physical
28514442
C1GLC_HUMANC1GALT1C1physical
28514442
FAM3C_HUMANFAM3Cphysical
28514442
ARMC6_HUMANARMC6physical
28514442
TOIP2_HUMANTOR1AIP2physical
28514442
IFG15_HUMANTOR1AIP2physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
CAN2_HUMANCAPN2physical
28514442
LDLR_HUMANLDLRphysical
28514442
PON2_HUMANPON2physical
28514442
ITA7_HUMANITGA7physical
28514442
NDUAA_HUMANNDUFA10physical
28514442
ITAV_HUMANITGAVphysical
28514442
AMD_HUMANPAMphysical
28514442
FKRP_HUMANFKRPphysical
28514442
MOXD1_HUMANMOXD1physical
28514442
GALT7_HUMANGALNT7physical
28514442
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 B3GN2_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory