XIAP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XIAP_MOUSE
• UniProt AC: Q60989
• Protein Name: E3 ubiquitin-protein ligase XIAP
• Gene Name: Xiap
• Organism: Mus musculus (Mouse).
• 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..
• Protein Sequence: MTFNSFEGTRTFVLADTNKDEEFVEEFNRLKTFANFPSSSPVSASTLARAGFLYTGEGDTVQCFSCHAAIDRWQYGDSAVGRHRRISPNCRFINGFYFENGAAQSTNPGIQNGQYKSENCVGNRNPFAPDRPPETHADYLLRTGQVVDISDTIYPRNPAMCSEEARLKSFQNWPDYAHLTPRELASAGLYYTGADDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNVNVRSESGVSSDRNFPNSTNSPRNPAMAEYEARIVTFGTWTSSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLDEKGQEYINNIHLTHSLEESLGRTAEKTPSLTKKIDDTIFQNPMVQEAIRMGFSFKDIKKTMEEKIQTSGSSYLSLEVLIADLVSAQKDNTEDESSQTSLQKDISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS

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
5	Phosphorylation	---MTFNSFEGTRTF ---CCCCCCCCEEEE	22.08	29514104
19	Ubiquitination	FVLADTNKDEEFVEE EEEECCCCCHHHHHH	69.48	22790023
31	Ubiquitination	VEEFNRLKTFANFPS HHHHHHHHHHHCCCC	38.06	22790023
78	Phosphorylation	DRWQYGDSAVGRHRR HHHHCCCCHHCCCCC	22.08	28285833
83	Ubiquitination	GDSAVGRHRRISPNC CCCHHCCCCCCCCCC	19.90	27667366
87	Phosphorylation	VGRHRRISPNCRFIN HCCCCCCCCCCCEEC	14.30	-
168	Ubiquitination	CSEEARLKSFQNWPD CCHHHHHHHHHCCCC	43.61	22790023
169	Phosphorylation	SEEARLKSFQNWPDY CHHHHHHHHHCCCCH	36.33	-
176	Phosphorylation	SFQNWPDYAHLTPRE HHHCCCCHHCCCHHH	7.58	28059163
218	Phosphorylation	EPCDRAWSEHRRHFP CCCHHHHHHHHHHCC	23.65	-
357	Ubiquitination	SLGRTAEKTPSLTKK HCCCCCCCCCCHHHH	64.37	27667366
409	Ubiquitination	SYLSLEVLIADLVSA CCCHHHHHHHHHHHH	1.63	27667366
449	S-nitrosocysteine	RLQEEKLCKICMDRN HHHHHHHHHHHCCCC	4.07	-
449	S-nitrosylation	RLQEEKLCKICMDRN 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
87	S	Phosphorylation	Kinase	PKB	P31750	Uniprot

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTEN_MOUSE	Pten	physical	19473982
SEPT4_MOUSE	Sept4	physical	21695558

Drug and Disease Associations

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