TNR11_HUMAN - dbPTM
TNR11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNR11_HUMAN
UniProt AC Q9Y6Q6
Protein Name Tumor necrosis factor receptor superfamily member 11A
Gene Name TNFRSF11A
Organism Homo sapiens (Human).
Sequence Length 616
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein .
Isoform RANK-e5a: Cell membrane
Single-pass type I membrane protein .
Protein Description Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells..
Protein Sequence MAPRARRRRPLFALLLLCALLARLQVALQIAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLPGLIILLLFASVALVAAIIFGVCYRKKGKALTANLWHWINEACGRLSGDKESSGDSCVSTHTANFGQQGACEGVLLLTLEEKTFPEDMCYPDQGGVCQGTCVGGGPYAQGEDARMLSLVSKTEIEEDSFRQMPTEDEYMDRPSQPTDQLLFLTEPGSKSTPPFSEPLEVGENDSLSQCFTGTQSTVGSESCNCTEPLCRTDWTPMSSENYLQKEVDSGHCPHWAASPSPNWADVCTGCRNPPGEDCEPLVGSPKRGPLPQCAYGMGLPPEEEASRTEARDQPEDGADGRLPSSARAGAGSGSSPGGQSPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA
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
57PhosphorylationCEPGKYMSSKCTTTS
CCCCCCCCCCCCCCC		24.4522210691
105N-linked_GlycosylationLVAVVAGNSTTPRRC
EEEEEECCCCCCCCC		26.84UniProtKB CARBOHYD
174N-linked_GlycosylationDKCRPWTNCTFLGKR
CCCCCCCCCCCCCCE		20.97UniProtKB CARBOHYD
197PhosphorylationSDAVCSSSLPARKPP
CCCCCCCCCCCCCCC		23.2924719451
370PhosphorylationLTEPGSKSTPPFSEP
EECCCCCCCCCCCCC		48.0927080861
371PhosphorylationTEPGSKSTPPFSEPL
ECCCCCCCCCCCCCC		38.4227080861
375PhosphorylationSKSTPPFSEPLEVGE
CCCCCCCCCCCCCCC		44.0427080861
385PhosphorylationLEVGENDSLSQCFTG
CCCCCCCCHHHHCCC		41.3127080861
387PhosphorylationVGENDSLSQCFTGTQ
CCCCCCHHHHCCCCC		28.9327080861
391PhosphorylationDSLSQCFTGTQSTVG
CCHHHHCCCCCCCCC		47.1227080861
393PhosphorylationLSQCFTGTQSTVGSE
HHHHCCCCCCCCCCC		19.1127080861
395PhosphorylationQCFTGTQSTVGSESC
HHCCCCCCCCCCCCC		25.5427080861
396PhosphorylationCFTGTQSTVGSESCN
HCCCCCCCCCCCCCC		21.0427080861
399PhosphorylationGTQSTVGSESCNCTE
CCCCCCCCCCCCCCC		23.2327080861
437PhosphorylationHCPHWAASPSPNWAD
CCCCCCCCCCCCHHH		20.4027080861
439PhosphorylationPHWAASPSPNWADVC
CCCCCCCCCCHHHHC		28.5027080861
463PhosphorylationDCEPLVGSPKRGPLP
CCCCCCCCCCCCCCC		21.5526657352
503PhosphorylationGADGRLPSSARAGAG
CCCCCCCCCCCCCCC		41.0229116813
504PhosphorylationADGRLPSSARAGAGS
CCCCCCCCCCCCCCC		21.6029083192
511PhosphorylationSARAGAGSGSSPGGQ
CCCCCCCCCCCCCCC		34.6627080861
513PhosphorylationRAGAGSGSSPGGQSP
CCCCCCCCCCCCCCC		34.7527080861
514PhosphorylationAGAGSGSSPGGQSPA
CCCCCCCCCCCCCCC		30.9627080861
519PhosphorylationGSSPGGQSPASGNVT
CCCCCCCCCCCCCCC		26.2127080861
522PhosphorylationPGGQSPASGNVTGNS
CCCCCCCCCCCCCCC		33.9927080861
526PhosphorylationSPASGNVTGNSNSTF
CCCCCCCCCCCCCEE		34.3527080861
529PhosphorylationSGNVTGNSNSTFISS
CCCCCCCCCCEEECC		33.2427080861
531PhosphorylationNVTGNSNSTFISSGQ
CCCCCCCCEEECCCC		25.2327080861
532PhosphorylationVTGNSNSTFISSGQV
CCCCCCCEEECCCCE		29.2827080861
580PhosphorylationETLARRDSFAGNGPR
HHHHHCCCCCCCCCC		18.3825159151
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 TNR11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNR11_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 TNR11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAB2_HUMANTAB2physical
11809792
TRAF6_HUMANTRAF6physical
11809792
M3K7_HUMANMAP3K7physical
11809792
TRAF5_HUMANTRAF5physical
9685412
TRAF6_HUMANTRAF6physical
9685412
TRAF2_HUMANTRAF2physical
9685412
TRAF6_HUMANTRAF6physical
10075662
TRAF5_HUMANTRAF5physical
10075662
TRAF2_HUMANTRAF2physical
10075662
TRAF1_HUMANTRAF1physical
9852070
TRAF3_HUMANTRAF3physical
9852070
TRAF5_HUMANTRAF5physical
9852070
TRAF6_HUMANTRAF6physical
9852070
TRAF2_HUMANTRAF2physical
9852070
TRAF1_HUMANTRAF1physical
10025951
TRAF3_HUMANTRAF3physical
10025951
TRAF6_HUMANTRAF6physical
10025951
TRAF2_HUMANTRAF2physical
10025951
TRAF5_MOUSETraf5physical
10025951
TRAF1_HUMANTRAF1physical
9774460
TRAF2_HUMANTRAF2physical
9774460
TRAF3_HUMANTRAF3physical
9774460
TRAF5_HUMANTRAF5physical
9774460
TRAF6_HUMANTRAF6physical
9774460
TRAF6_HUMANTRAF6physical
26038599
RACK1_HUMANGNB2L1physical
26038599
VAV3_HUMANVAV3physical
27507811
TRAF6_HUMANTRAF6physical
27507811
Drug and Disease Associations
Kegg Disease
H00436 Osteopetrosis, including: Osteopetrosis, severe neonatal or infantile forms; Osteopetrosis, intermed
H00437 Paget's disease of bone and related disorders, including: ; Paget's disease of bone (PDB); Familial
OMIM Disease
174810Familial expansile osteolysis (FEO)
602080Paget disease of bone 2 (PDB2)
612301Osteopetrosis, autosomal recessive 7 (OPTB7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNR11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-463, AND MASSSPECTROMETRY.

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