UN93B_HUMAN - dbPTM
UN93B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UN93B_HUMAN
UniProt AC Q9H1C4
Protein Name Protein unc-93 homolog B1
Gene Name UNC93B1
Organism Homo sapiens (Human).
Sequence Length 597
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Endosome. Lysosome. Cytoplasmic vesicle, phagosome. Relocalizes from endoplasmic reticulum to endosome and lysosome upon cell-stimulation with CpG dinucleotides (By similarity). Colocalizes
Protein Description Plays an important role in innate and adaptive immunity by regulating nucleotide-sensing Toll-like receptor (TLR) signaling. Required for the transport of a subset of TLRs (including TLR3, TLR7 and TLR9) from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. May play a role in autoreactive B-cells removal..
Protein Sequence MEAEPPLYPMAGAAGPQGDEDLLGVPDGPEAPLDELVGAYPNYNEEEEERRYYRRKRLGVLKNVLAASAGGMLTYGVYLGLLQMQLILHYDETYREVKYGNMGLPDIDSKMLMGINVTPIAALLYTPVLIRFFGTKWMMFLAVGIYALFVSTNYWERYYTLVPSAVALGMAIVPLWASMGNYITRMAQKYHEYSHYKEQDGQGMKQRPPRGSHAPYLLVFQAIFYSFFHLSFACAQLPMIYFLNHYLYDLNHTLYNVQSCGTNSHGILSGFNKTVLRTLPRSGNLIVVESVLMAVAFLAMLLVLGLCGAAYRPTEEIDLRSVGWGNIFQLPFKHVRDYRLRHLVPFFIYSGFEVLFACTGIALGYGVCSVGLERLAYLLVAYSLGASAASLLGLLGLWLPRPVPLVAGAGVHLLLTFILFFWAPVPRVLQHSWILYVAAALWGVGSALNKTGLSTLLGILYEDKERQDFIFTIYHWWQAVAIFTVYLGSSLHMKAKLAVLLVTLVAAAVSYLRMEQKLRRGVAPRQPRIPRPQHKVRGYRYLEEDNSDESDAEGEHGDGAEEEAPPAGPRPGPEPAGLGRRPCPYEQAQGGDGPEEQ
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
12UbiquitinationPPLYPMAGAAGPQGD
CCCCCCCCCCCCCCC		15.0922817900
60UbiquitinationYRRKRLGVLKNVLAA
HHHHHHHHHHHHHHH		9.0022817900
68PhosphorylationLKNVLAASAGGMLTY
HHHHHHHHHCCHHHH		23.1024043423
74PhosphorylationASAGGMLTYGVYLGL
HHHCCHHHHHHHHHH		14.8824043423
75PhosphorylationSAGGMLTYGVYLGLL
HHCCHHHHHHHHHHH		10.7124043423
78PhosphorylationGMLTYGVYLGLLQMQ
CHHHHHHHHHHHHHH		7.2424043423
90PhosphorylationQMQLILHYDETYREV
HHHHHHHCCCHHCHH		16.4222210691
93PhosphorylationLILHYDETYREVKYG
HHHHCCCHHCHHCCC		25.6124043423
94PhosphorylationILHYDETYREVKYGN
HHHCCCHHCHHCCCC		11.6124043423
148UbiquitinationLAVGIYALFVSTNYW
HHHHHHHHHHCCCHH		2.1521890473
193PhosphorylationMAQKYHEYSHYKEQD
HHHHHHHHHCCCCCC		6.34-
196UbiquitinationKYHEYSHYKEQDGQG
HHHHHHCCCCCCCCC		15.4121890473
197UbiquitinationYHEYSHYKEQDGQGM
HHHHHCCCCCCCCCC		43.4021906983
251N-linked_GlycosylationNHYLYDLNHTLYNVQ
HHHHHHHCCCCEEEC		24.17UniProtKB CARBOHYD
272N-linked_GlycosylationHGILSGFNKTVLRTL
CCHHCCCCHHHHHHC		42.48UniProtKB CARBOHYD
274PhosphorylationILSGFNKTVLRTLPR
HHCCCCHHHHHHCCC		26.3624719451
333UbiquitinationNIFQLPFKHVRDYRL
CCCCCCCCCHHHHHH		38.9721906983
350UbiquitinationLVPFFIYSGFEVLFA
HHHHHHHCHHHHHHH		31.9921987572
398UbiquitinationLLGLLGLWLPRPVPL
HHHHHHHHCCCCCCC		11.5221987572
449N-linked_GlycosylationWGVGSALNKTGLSTL
HCHHHHHHHHCHHHH		39.29UniProtKB CARBOHYD
464UbiquitinationLGILYEDKERQDFIF
HHHHHCCCCCCCEEH		42.74-
510PhosphorylationTLVAAAVSYLRMEQK
HHHHHHHHHHHHHHH		17.45-
535UbiquitinationRIPRPQHKVRGYRYL
CCCCCCCCCCCEEEE		28.5121987572
539PhosphorylationPQHKVRGYRYLEEDN
CCCCCCCEEEECCCC		5.8728796482
541PhosphorylationHKVRGYRYLEEDNSD
CCCCCEEEECCCCCC		15.2430266825
547PhosphorylationRYLEEDNSDESDAEG
EEECCCCCCCCCCCC		55.8923927012
550PhosphorylationEEDNSDESDAEGEHG
CCCCCCCCCCCCCCC		47.3023927012
585PhosphorylationLGRRPCPYEQAQGGD
CCCCCCCHHHHCCCC		27.6521945579
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 UN93B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UN93B_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 UN93B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MRP1_HUMANABCC1physical
21903422
ANKH1_HUMANANKHD1physical
21903422
CCD47_HUMANCCDC47physical
21903422
CDIPT_HUMANCDIPTphysical
21903422
CLPT1_HUMANCLPTM1physical
21903422
CLP1L_HUMANCLPTM1Lphysical
21903422
OST48_HUMANDDOSTphysical
21903422
SYFA_HUMANFARSAphysical
21903422
FAKD5_HUMANFASTKD5physical
21903422
GOT1B_HUMANGOLT1Bphysical
21903422
HM13_HUMANHM13physical
21903422
IRAK1_HUMANIRAK1physical
21903422
LGAT1_HUMANLPGAT1physical
21903422
MBOA7_HUMANMBOAT7physical
21903422
NPC1_HUMANNPC1physical
21903422
PIGN_HUMANPIGNphysical
21903422
SCAM3_HUMANSCAMP3physical
21903422
SE1L1_HUMANSEL1Lphysical
21903422
SPNS1_HUMANSPNS1physical
21903422
STT3A_HUMANSTT3Aphysical
21903422
STT3B_HUMANSTT3Bphysical
21903422
SURF4_HUMANSURF4physical
21903422
TM9S2_HUMANTM9SF2physical
21903422
TM9S3_HUMANTM9SF3physical
21903422
TMCO1_HUMANTMCO1physical
21903422
YIPF3_HUMANYIPF3physical
21903422
YIPF5_HUMANYIPF5physical
21903422
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610551Herpes simplex encephalitis 1 (HSE1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UN93B_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-541; SER-547 ANDSER-550, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-550, ANDMASS SPECTROMETRY.

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