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Protein Page:
XIAP (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
XIAP an apoptotic suppressor protein. Inhibist apoptosis through binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2. Inhibits apoptosis induced by menadione, a potent inducer of free radicals, and ICE. Inhibits cell-death proteases, caspase-3, caspase-7, and perhaps caspase-9. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; EC 6.3.2.-; Ligase; Ubiquitin ligase; Apoptosis
Chromosomal Location of Human Ortholog: Xq25
Cellular Component: cytoplasm; cytosol; nucleoplasm; nucleus; spindle microtubule
Molecular Function: caspase inhibitor activity; ligase activity; protein binding; ubiquitin-protein ligase activity; zinc ion binding
Biological Process: apoptosis; copper ion homeostasis; negative regulation of apoptosis; negative regulation of caspase activity; positive regulation of protein ubiquitination; programmed cell death; protein ubiquitination; regulation of BMP signaling pathway; regulation of cell proliferation; regulation of inflammatory response; regulation of innate immune response; response to DNA damage stimulus; Wnt receptor signaling pathway
Disease: Lymphoproliferative Syndrome, X-linked, 1; Lymphoproliferative Syndrome, X-linked, 2
Reference #:  P98170 (UniProtKB)
Alt. Names/Synonyms: API3; apoptosis inhibitor 3; baculoviral IAP repeat-containing 4; Baculoviral IAP repeat-containing protein 4; BIRC4; E3 ubiquitin-protein ligase XIAP; hIAP-3; hIAP3; hILP; IAP-3; IAP-like protein; IAP3; ILP; ILP1; Inhibitor of apoptosis protein 3; MIHA; X-linked IAP; X-linked inhibitor of apoptosis; X-linked inhibitor of apoptosis protein; XIAP; XLP2
Gene Symbols: XIAP
Molecular weight: 56,685 Da
Basal Isoelectric point: 6.22  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  ErbB/HER Signaling  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

XIAP

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S87‑p
apoptosis, inhibited: S87‑p
protein degradation: S430‑p
protein stabilization: S87‑p
ubiquitination: S430‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S5‑p ___MTFNsFEGSkTC
0 1 K10‑ub FNsFEGSkTCVPADI
0 1 K19 CVPADINKEEEFVEE
0 5 K31‑ub VEEFNRLktFANFPS
0 2 T32‑p EEFNRLktFANFPSG
0 1 S40‑p FANFPSGsPVSAstL
0 2 S45‑p SGsPVSAstLARAGF
0 2 T46‑p GsPVSAstLARAGFL
5 0 S87‑p VGRHRKVsPNCRFIN
0 2 K116‑ub GIQNGQYkVENyLGs
0 1 Y120‑p GQYkVENyLGsRDHF
0 1 S123‑p kVENyLGsRDHFALD
1 1 Y139‑p PSETHADyLLRTGQV
0 5 K168‑ub YSEEARLkSFQNWPD
0 1 S169 SEEARLkSFQNWPDY
0 2 T180‑p WPDYAHLtPRELASA
0 1 K208‑ub FCCGGKLkNWEPCDR
1 0 K322‑ub DPWEQHAkWYPGCkY
1 1 K328‑ub AkWYPGCkYLLEQKG
0 3 K358‑ub CLVRTTEkTPsLTRR
0 1 S361‑p RTTEkTPsLTRRIDD
0 1 S400‑p MEEKIQIsGsNykSL
0 1 S402‑p EKIQIsGsNykSLEV
0 2 Y404‑p IQIsGsNykSLEVLV
0 3 K405‑ub QIsGsNykSLEVLVA
0 1 T429‑p MQDESSQtsLQkEIS
1 1 S430‑p QDESSQtsLQkEIST
0 1 K433‑ub SSQtsLQkEISTEEQ
  mouse

 
S5 ___MTFNSFEGTRTF
R10 FNSFEGTRTFVLADT
K19‑ub FVLADTNkDEEFVEE
K31‑ub VEEFNRLkTFANFPS
T32 EEFNRLkTFANFPSS
S40 FANFPSSSPVSASTL
S45 SSSPVSASTLARAGF
T46 SSPVSASTLARAGFL
S87‑p VGRHRRIsPNCRFIN
K116 GIQNGQYKSENCVGN
C120 GQYKSENCVGNRNPF
N123 KSENCVGNRNPFAPD
Y139 PPETHADYLLRTGQV
K168‑ub CSEEARLksFQNWPD
S169‑p SEEARLksFQNWPDY
T180 WPDYAHLTPRELASA
K208 FCCGGKLKNWEPCDR
K321 DPWEQHAKWYPGCKY
K327 AKWYPGCKYLLDEKG
K357 SLGRTAEKTPSLTKK
S360 RTAEKTPSLTKKIDD
S399 MEEKIQTSGSSYLSL
S401 EKIQTSGSSYLSLEV
Y403 IQTSGSSYLSLEVLI
L404 QTSGSSYLSLEVLIA
T428 TEDESSQTSLQKDIS
S429 EDESSQTSLQKDIST
K432 SSQTSLQKDISTEEQ
  rat

 
S5 ___MTFNSFEGSRTV
R10 FNSFEGSRTVVPADT
K19 VVPADTNKDEEFVEE
K31 VEEFNRLKTFANFPS
T32 EEFNRLKTFANFPSS
S40 FANFPSSSPVSASTL
S45 SSSPVSASTLARAGF
T46 SSPVSASTLARAGFL
S87 VGRHRRISPNCRFIN
K116 GIQNGQYKSENCVGN
C120 GQYKSENCVGNRNHF
N123 KSENCVGNRNHFALD
Y139‑p PSETHADyLLRTGQV
K168 CSEEARLKTFQNWPD
T169 SEEARLKTFQNWPDY
S180 WPDYAHLSPRELASA
K208 FCCGGKLKNWEPCDR
K321 DPWEQHAKWYPGCKY
K327 AKWYPGCKYLLDEKG
K357 SVVRTAEKTPSVTKK
S360 RTAEKTPSVTKKIDD
S399 MEEKLQTSGSNYLSL
S401 EKLQTSGSNYLSLEV
Y403 LQTSGSNYLSLEVLI
L404 QTSGSNYLSLEVLIA
T428 SQDESSQTSLQKDIS
S429 QDESSQTSLQKDIST
K432 SSQTSLQKDISTEEQ
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