TR13B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TR13B_HUMAN
• UniProt AC: O14836
• Protein Name: Tumor necrosis factor receptor superfamily member 13B
• Gene Name: TNFRSF13B
• Organism: Homo sapiens (Human).
• Sequence Length: 293
• Subcellular Localization: Membrane; Single-pass type III membrane protein.
• Protein Description: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity..
• Protein Sequence: MSGLGRSRRGGRSRVDQEERFPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCRSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLRSPVNLPPELRRQRSGEVENNSDNSGRYQGLEHRGSEASPALPGLKLSADQVALVYSTLGLCLCAVLCCFLVAVACFLKKRGDPCSCQPRSRPRQSPAKSSQDHAMEAGSPVSTSPEPVETCSFCFPECRAPTQESAVTPGTPDPTCAGRWGCHTRTTVLQPCPHIPDSGLGIVCVPAQEGGPGA

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
110	Phosphorylation	FCENKLRSPVNLPPE HCCCCCCCCCCCCHH	43.57	-
128	N-linked_Glycosylation	QRSGEVENNSDNSGR HHCCCCCCCCCCCCC	59.49	UniProtKB CARBOHYD
207	Ubiquitination	RPRQSPAKSSQDHAM CCCCCCCCCHHHCHH	54.76	-
209	Phosphorylation	RQSPAKSSQDHAMEA CCCCCCCHHHCHHHC	38.63	30108239
218	Phosphorylation	DHAMEAGSPVSTSPE HCHHHCCCCCCCCCC	29.22	30108239
221	Phosphorylation	MEAGSPVSTSPEPVE HHCCCCCCCCCCCCC	26.93	30108239
222	Phosphorylation	EAGSPVSTSPEPVET HCCCCCCCCCCCCCC	48.84	30108239
223	Phosphorylation	AGSPVSTSPEPVETC CCCCCCCCCCCCCCC	21.54	30108239
229	Phosphorylation	TSPEPVETCSFCFPE CCCCCCCCCCCCCCC	17.43	30108239
231	Phosphorylation	PEPVETCSFCFPECR CCCCCCCCCCCCCCC	32.25	30108239
247	Phosphorylation	PTQESAVTPGTPDPT CCCCCCCCCCCCCCC	18.73	30108239
250	Phosphorylation	ESAVTPGTPDPTCAG CCCCCCCCCCCCCCC	26.23	28674151
254	Phosphorylation	TPGTPDPTCAGRWGC CCCCCCCCCCCCCCC	23.51	30108239

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TR13B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TR13B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TR13B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAMLG_HUMAN	CAMLG	physical	9311921
TN13B_HUMAN	TNFSF13B	physical	10956646
TNF13_HUMAN	TNFSF13	physical	10956646
TN13B_HUMAN	TNFSF13B	physical	10880535
TN13B_MOUSE	Tnfsf13b	physical	10880535
TRAF2_HUMAN	TRAF2	physical	10880535
TRAF5_HUMAN	TRAF5	physical	10880535
TRAF6_HUMAN	TRAF6	physical	10880535
TRAF3_HUMAN	TRAF3	physical	12471121
MYD88_HUMAN	MYD88	physical	20676093
TRAF2_HUMAN	TRAF2	physical	20676093
TRAF5_HUMAN	TRAF5	physical	20676093
TRAF6_HUMAN	TRAF6	physical	20676093
CAMLG_HUMAN	CAMLG	physical	20676093
IRAK4_HUMAN	IRAK4	physical	20676093
IRAK1_HUMAN	IRAK1	physical	20676093
FIZ1_HUMAN	FIZ1	physical	28514442
ZN579_HUMAN	ZNF579	physical	28514442
ZN646_HUMAN	ZNF646	physical	28514442
CD70_HUMAN	CD70	physical	28514442
RBM26_HUMAN	RBM26	physical	28514442
RBM27_HUMAN	RBM27	physical	28514442
ZFP91_HUMAN	ZFP91	physical	28514442
RRP1_HUMAN	RRP1	physical	28514442
ZN638_HUMAN	ZNF638	physical	28514442
RBM23_HUMAN	RBM23	physical	28514442
RN166_HUMAN	RNF166	physical	28514442
TEX10_HUMAN	TEX10	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
CHTOP_HUMAN	CHTOP	physical	28514442
TR10B_HUMAN	TNFRSF10B	physical	28514442
EHD4_HUMAN	EHD4	physical	28514442
RM44_HUMAN	MRPL44	physical	28514442
TYK2_HUMAN	TYK2	physical	28514442
SENP3_HUMAN	SENP3	physical	28514442
DDX50_HUMAN	DDX50	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.