TNR5_HUMAN - dbPTM
TNR5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNR5_HUMAN
UniProt AC P25942
Protein Name Tumor necrosis factor receptor superfamily member 5
Gene Name CD40
Organism Homo sapiens (Human).
Sequence Length 277
Subcellular Localization Isoform I: Cell membrane
Single-pass type I membrane protein.
Isoform II: Secreted.
Protein Description Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion..
Protein Sequence MVRLPLQCVLWGCLLTAVHPEPPTACREKQYLINSQCCSLCQPGQKLVSDCTEFTETECLPCGESEFLDTWNRETHCHQHKYCDPNLGLRVQQKGTSETDTICTCEEGWHCTSEACESCVLHRSCSPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWTSCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFGILFAILLVLVFIKKVAKKPTNKAPHPKQEPQEINFPDDLPGSNTAAPVQETLHGCQPVTQEDGKESRISVQERQ
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
153N-linked_GlycosylationCPVGFFSNVSSAFEK
CCCCCCCCCHHHHHH
32.31UniProtKB CARBOHYD
156PhosphorylationGFFSNVSSAFEKCHP
CCCCCCHHHHHHHCC
32.4724719451
180N-linked_GlycosylationVVQQAGTNKTDVVCG
EEEECCCCCCCCEEC
44.2917660510
223PhosphorylationKKVAKKPTNKAPHPK
HHHHCCCCCCCCCCC
59.22-
254PhosphorylationTAAPVQETLHGCQPV
CCCCHHHHHCCCEEE
13.6322817900
269PhosphorylationTQEDGKESRISVQER
CCCCCCCCCCCCCCC
38.1028060719
272PhosphorylationDGKESRISVQERQ--
CCCCCCCCCCCCC--
19.3528355574

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 TNR5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNR5_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 TNR5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UGGG1_HUMANUGGT1physical
17353931
CALR_HUMANCALRphysical
17353931
SGK1_HUMANSGK1physical
17353931
UBP15_HUMANUSP15physical
17353931
RFC5_HUMANRFC5physical
17353931
ERP44_HUMANERP44physical
17353931
RPAB3_HUMANPOLR2Hphysical
17353931
ZNT7_HUMANSLC30A7physical
17353931
THIO_HUMANTXNphysical
17353931
DDX3X_HUMANDDX3Xphysical
17353931
RN219_HUMANRNF219physical
17353931
S39A7_HUMANSLC39A7physical
17353931
FBRL_HUMANFBLphysical
17353931
RIPK2_HUMANRIPK2physical
9642260
TRAF3_HUMANTRAF3physical
9990007
TRAF5_HUMANTRAF5physical
9990007
TRAF6_HUMANTRAF6physical
9990007
TRAF2_HUMANTRAF2physical
9990007
TYDP2_HUMANTDP2physical
10764746
CD20_HUMANMS4A1physical
9933087
TRAF3_HUMANTRAF3physical
7527023
TRAF3_HUMANTRAF3physical
10984535
XRCC6_HUMANXRCC6physical
10514012
XRCC5_HUMANXRCC5physical
10514012
TRAF5_HUMANTRAF5physical
8790348
TRAF3_HUMANTRAF3physical
9384571
TRAF6_HUMANTRAF6physical
9384571
TRAF2_HUMANTRAF2physical
9020361
TRAF2_HUMANTRAF2physical
21282461
HSP74_HUMANHSPA4physical
12356871
TRAF3_HUMANTRAF3physical
7859281
TRAF2_HUMANTRAF2physical
16260598
TRAF3_HUMANTRAF3physical
16260598
TRAF6_HUMANTRAF6physical
16260598
TRAF1_HUMANTRAF1physical
9718306
TRAF2_HUMANTRAF2physical
9718306
TRAF3_HUMANTRAF3physical
9718306
TRAF6_HUMANTRAF6physical
9718306
BIRC2_HUMANBIRC2physical
11562359
TRAF2_HUMANTRAF2physical
11562359
TRAF3_HUMANTRAF3physical
11562359
TRAF4_HUMANTRAF4physical
11562359
TRAF5_HUMANTRAF5physical
11562359
TRAF5_HUMANTRAF5physical
21041727
TRAF2_HUMANTRAF2physical
21041727
TRAF3_HUMANTRAF3physical
21041727
TRAF6_HUMANTRAF6physical
21041727
BIRC2_HUMANBIRC2physical
21041727
TRAF3_HUMANTRAF3physical
14517219
TRAF5_HUMANTRAF5physical
9511754
TRAF3_HUMANTRAF3physical
9168896
TRAF2_HUMANTRAF2physical
9168896
TRAF2_HUMANTRAF2physical
19667091
TRAF3_HUMANTRAF3physical
19667091
TRAF3_HUMANTRAF3physical
7530216
PK3CA_HUMANPIK3CAphysical
12637493
CBL_HUMANCBLphysical
12637493
TRAF2_HUMANTRAF2physical
12637493
TRAF3_HUMANTRAF3physical
12637493
TRAF6_HUMANTRAF6physical
12637493
TRAF2_HUMANTRAF2physical
21071692
TRAF2_HUMANTRAF2physical
10352240
TRAF3_HUMANTRAF3physical
10352240
TRAF2_HUMANTRAF2physical
20449947
TRAF6_HUMANTRAF6physical
20449947
M3K8_HUMANMAP3K8physical
15670770
TRAF2_HUMANTRAF2physical
20676093
TRAF5_HUMANTRAF5physical
20676093
TRAF6_HUMANTRAF6physical
20676093
TRAF3_MOUSETraf3physical
23334419
OTU7B_MOUSEOtud7bphysical
23334419
TRAF2_MOUSETraf2physical
23334419
BIRC3_MOUSEBirc3physical
23334419
P85A_HUMANPIK3R1physical
21200133
TRAF3_HUMANTRAF3physical
24260396
TRAF2_HUMANTRAF2physical
25416956
FAF1_HUMANFAF1physical
24810049
TRAF3_HUMANTRAF3physical
24810049
TRAF1_HUMANTRAF1physical
20614026
IKKA_HUMANCHUKphysical
20614026
TRAF6_HUMANTRAF6physical
20614026
DBLOH_HUMANDIABLOphysical
20614026
TNR5_HUMANCD40physical
20614026
IKKB_HUMANIKBKBphysical
20614026
TRAF3_HUMANTRAF3physical
20614026
TRAF5_HUMANTRAF5physical
20614026
BIRC2_HUMANBIRC2physical
20614026
RNF31_HUMANRNF31physical
20614026
HTRA2_HUMANHTRA2physical
20614026
TRAF2_HUMANTRAF2physical
20614026
TRAF6_HUMANTRAF6physical
24812060
TRAF2_HUMANTRAF2physical
27716849
TRAF3_HUMANTRAF3physical
27716849
STING_HUMANTMEM173physical
27716849

Drug and Disease Associations
Kegg Disease
H00086 Hyper IgM syndromes, autosomal recessive type, including the following three diseases: Activation-in
H00093 Combined immunodeficiencies (CIDs), including the following nine diseases: X-linked hyper IgM syndro
OMIM Disease
606843Immunodeficiency with hyper-IgM 3 (HIGM3)
Kegg Drug
D06071 Teneliximab (USAN/INN)
D08896 Dacetuzumab (USAN)
D08942 Lucatumumab (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNR5_HUMAN

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Related Literatures of Post-Translational Modification

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