XIAP_RAT - dbPTM
XIAP_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XIAP_RAT
UniProt AC Q9R0I6
Protein Name E3 ubiquitin-protein ligase XIAP
Gene Name Xiap
Organism Rattus norvegicus (Rat).
Sequence Length 496
Subcellular Localization Cytoplasm. Nucleus. TLE3 promotes its nuclear localization..
Protein Description Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program (By similarity)..
Protein Sequence MTFNSFEGSRTVVPADTNKDEEFVEEFNRLKTFANFPSSSPVSASTLARAGFLYTGEGDTVQCFSCHAAVDRWQYGDSAVGRHRRISPNCRFINGFYFENGATQSTSPGIQNGQYKSENCVGNRNHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMCSEEARLKTFQNWPDYAHLSPRELASAGLYYTGIDDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNVNVRSESGVSSDRNFPNSTNSPRNPAMAEYDARIVTFGTWLYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLDEKGQEYINNIHLTHSLGESVVRTAEKTPSVTKKIDDTIFQNPMVQEAIRMGFNFKDIKKTMEEKLQTSGSNYLSLEVLIADLVSAQKDNSQDESSQTSLQKDISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCCTVITFKQKIFMS
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
5Phosphorylation---MTFNSFEGSRTV
---CCCCCCCCCEEE
22.0823984901
87PhosphorylationVGRHRRISPNCRFIN
HCCCCCCCCCCCEEC
14.30-
139PhosphorylationPSETHADYLLRTGQV
CCHHCHHHHCCCCCE
14.3916602692
252PhosphorylationSDRNFPNSTNSPRNP
CCCCCCCCCCCCCCH
29.2427097102
253PhosphorylationDRNFPNSTNSPRNPA
CCCCCCCCCCCCCHH
46.4827097102
255PhosphorylationNFPNSTNSPRNPAMA
CCCCCCCCCCCHHHH
25.8927097102
449S-nitrosocysteineRLQEEKLCKICMDRN
HHHHHHHHHHHCCCC
4.07-
449S-nitrosylationRLQEEKLCKICMDRN
HHHHHHHHHHHCCCC
4.07-

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
87SPhosphorylationKinasePKBP47196
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 XIAP_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XIAP_RAT

loading...

Related Literatures of Post-Translational Modification

TOP