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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: E3 ubiquitin-protein ligase XIAP

UniprotKB/SwissProt ID: Q60989 (Q60989)

Gene Name: Xiap

Organism: Mus musculus (Mouse)

Function: 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 (By similarity). Acts as a direct caspase inhibitor (By similarity). Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry (By similarity). Inhibits apoptosis in intestinal crypt cells, its activity is mitigated via its interaction with SEPTIN4 isoform ARTS (PubMed:30389919). Inactivates CASP9 by keeping it in a monomeric, inactive state (By similarity). 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, RIPK2, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS, PTEN and BIRC5/survivin (PubMed:18761086, PubMed:19473982). Acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (PubMed:29452636). 'Lys-63'-linked polyubiquitination of RIPK2 also promotes recruitment of the LUBAC complex to RIPK2 (By similarity). Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation (By similarity). Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation (By similarity). Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation (By similarity). Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation (By similarity). Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation (By similarity). Ubiquitinates and therefore mediates the proteasomal degradation of BCL2 in response to apoptosis (By similarity). 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 (By similarity). Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8 (By similarity). Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES (By similarity). 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). Positive regulator of dermal wound repair, potentially via its interaction with SEPTIN4 (PubMed:23788729)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001370 BIR_rpt
IPR048875 BIRC2-3-like_UBA
IPR050784 IAP
IPR042579 XIAP/BIRC8_UBA
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The S-nitrosylation sites of Q60989

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 213 CGGKLKNWEP C DRAWSEHRRH  CCCCCCCCEE E EEEECCCCCH  3.61%
2 299 YALGEGDKVK C FHCGGGLTDW  CCCCCCCCEE E EEEECCCCCH  2.93%
3 302 GEGDKVKCFH C GGGLTDWKPS  CCCCCCCCEE E EEEECCCCCH  2.44%
4 449 QLRRLQEEKL C KICMDRNIAI  CCCCCCCCEE E EEEECCCCCH  4.07%