dbPTM

XIAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XIAP_HUMAN
UniProt AC	P98170
Protein Name	E3 ubiquitin-protein ligase XIAP
Gene Name	XIAP
Organism	Homo sapiens (Human).
Sequence Length	497
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	MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTFNSFEGS ------CCCCCCCCC	31.37	28348404
5	Phosphorylation	---MTFNSFEGSKTC ---CCCCCCCCCCEE	22.08	25849741
9	Phosphorylation	TFNSFEGSKTCVPAD CCCCCCCCCEEEECC	20.00	30001349
10	Ubiquitination	FNSFEGSKTCVPADI CCCCCCCCEEEECCC	57.72	21906983
12	S-nitrosocysteine	SFEGSKTCVPADINK CCCCCCEEEECCCCC	3.87	-
12	S-nitrosylation	SFEGSKTCVPADINK CCCCCCEEEECCCCC	3.87	22178444
19	Ubiquitination	CVPADINKEEEFVEE EEECCCCCHHHHHHH	67.83	-
31	Ubiquitination	VEEFNRLKTFANFPS HHHHHHHHCCCCCCC	38.06	21906983
32	Phosphorylation	EEFNRLKTFANFPSG HHHHHHHCCCCCCCC	32.35	20068231
38	Phosphorylation	KTFANFPSGSPVSAS HCCCCCCCCCCCCHH	48.00	20068231
40	Phosphorylation	FANFPSGSPVSASTL CCCCCCCCCCCHHHH	26.85	25159151
43	Phosphorylation	FPSGSPVSASTLARA CCCCCCCCHHHHHHC	21.64	20068231
45	Phosphorylation	SGSPVSASTLARAGF CCCCCCHHHHHHCCE	19.22	20068231
46	Phosphorylation	GSPVSASTLARAGFL CCCCCHHHHHHCCEE	24.93	20068231
87	Phosphorylation	VGRHRKVSPNCRFIN CCCCCCCCCCCCEEC	17.27	17698078
90	S-nitrosylation	HRKVSPNCRFINGFY CCCCCCCCCEECCEE	4.22	22178444
90	S-nitrosocysteine	HRKVSPNCRFINGFY CCCCCCCCCEECCEE	4.22	-
116	Ubiquitination	GIQNGQYKVENYLGS CCCCCCEEEEECCCC	34.87	21890473
120	Phosphorylation	GQYKVENYLGSRDHF CCEEEEECCCCCCCC	10.03	27642862
123	Phosphorylation	KVENYLGSRDHFALD EEEECCCCCCCCCCC	31.75	22322096
131	Methylation	RDHFALDRPSETHAD CCCCCCCCCCHHHHH	37.18	115920113
133	Phosphorylation	HFALDRPSETHADYL CCCCCCCCHHHHHHH	56.89	28555341
139	Phosphorylation	PSETHADYLLRTGQV CCHHHHHHHCCCCCE	14.39	17053785
168	Ubiquitination	YSEEARLKSFQNWPD CCHHHHHHHHCCCCC	43.61	21890473
176	Phosphorylation	SFQNWPDYAHLTPRE HHCCCCCHHCCCHHH	7.58	27642862
180	Phosphorylation	WPDYAHLTPRELASA CCCHHCCCHHHHHHC	15.50	25159151
206	Ubiquitination	QCFCCGGKLKNWEPC EEEECCCCCCCCCCC	41.39	-
206	Acetylation	QCFCCGGKLKNWEPC EEEECCCCCCCCCCC	41.39	25953088
208	Ubiquitination	FCCGGKLKNWEPCDR EECCCCCCCCCCCHH	64.60	-
213	S-nitrosocysteine	KLKNWEPCDRAWSEH CCCCCCCCHHHHHHH	3.61	-
213	S-nitrosylation	KLKNWEPCDRAWSEH CCCCCCCCHHHHHHH	3.61	22178444
218	Phosphorylation	EPCDRAWSEHRRHFP CCCHHHHHHHHHHCC	23.65	24719451
248	Methylation	SDAVSSDRNFPNSTN HHCCCCCCCCCCCCC	48.95	115920117
261	Phosphorylation	TNLPRNPSMADYEAR CCCCCCCCHHHHHHE	30.10	28857561
297	Ubiquitination	YALGEGDKVKCFHCG EEECCCCEEEEEECC	55.22	-
299	Ubiquitination	LGEGDKVKCFHCGGG ECCCCEEEEEECCCC	36.60	-
300	S-nitrosylation	GEGDKVKCFHCGGGL CCCCEEEEEECCCCC	2.93	22178444
300	S-nitrosocysteine	GEGDKVKCFHCGGGL CCCCEEEEEECCCCC	2.93	-
303	S-nitrosocysteine	DKVKCFHCGGGLTDW CEEEEEECCCCCCCC	2.44	-
303	S-nitrosylation	DKVKCFHCGGGLTDW CEEEEEECCCCCCCC	2.44	22178444
311	Ubiquitination	GGGLTDWKPSEDPWE CCCCCCCCCCCCHHH	41.28	-
322	Ubiquitination	DPWEQHAKWYPGCKY CHHHHHHHHCCHHHH	45.17	12747801
327	S-nitrosocysteine	HAKWYPGCKYLLEQK HHHHCCHHHHHHHHH	1.95	-
327	S-nitrosylation	HAKWYPGCKYLLEQK HHHHCCHHHHHHHHH	1.95	22178444
328	Ubiquitination	AKWYPGCKYLLEQKG HHHCCHHHHHHHHHC	44.86	21890473
334	Ubiquitination	CKYLLEQKGQEYINN HHHHHHHHCHHHHHH	53.86	-
347	Phosphorylation	NNIHLTHSLEECLVR HHHEECCCHHHHHHC	32.04	27251275
351	S-nitrosocysteine	LTHSLEECLVRTTEK ECCCHHHHHHCCCCC	2.88	-
351	S-nitrosylation	LTHSLEECLVRTTEK ECCCHHHHHHCCCCC	2.88	22178444
355	Phosphorylation	LEECLVRTTEKTPSL HHHHHHCCCCCCCCC	31.65	20068231
356	Phosphorylation	EECLVRTTEKTPSLT HHHHHCCCCCCCCCH	25.56	20068231
358	Ubiquitination	CLVRTTEKTPSLTRR HHHCCCCCCCCCHHC	64.74	21906983
359	Phosphorylation	LVRTTEKTPSLTRRI HHCCCCCCCCCHHCC	16.33	20068231
361	Phosphorylation	RTTEKTPSLTRRIDD CCCCCCCCCHHCCCC	47.83	20068231
363	Phosphorylation	TEKTPSLTRRIDDTI CCCCCCCHHCCCCCH	23.41	24719451
385	Phosphorylation	EAIRMGFSFKDIKKI HHHHCCCCHHHHHHH	26.17	24719451
387	Ubiquitination	IRMGFSFKDIKKIME HHCCCCHHHHHHHHH	58.30	-
396	Ubiquitination	IKKIMEEKIQISGSN HHHHHHHHCCCCCCC	26.97	-
400	Phosphorylation	MEEKIQISGSNYKSL HHHHCCCCCCCCCCH	21.57	-
402	Phosphorylation	EKIQISGSNYKSLEV HHCCCCCCCCCCHHH	30.14	25159151
404	Phosphorylation	IQISGSNYKSLEVLV CCCCCCCCCCHHHHH	12.03	27251275
405	Ubiquitination	QISGSNYKSLEVLVA CCCCCCCCCHHHHHH	53.46	-
405	Sumoylation	QISGSNYKSLEVLVA CCCCCCCCCHHHHHH	53.46	-
405	Sumoylation	QISGSNYKSLEVLVA CCCCCCCCCHHHHHH	53.46	-
406	Phosphorylation	ISGSNYKSLEVLVAD CCCCCCCCHHHHHHH	21.28	26657352
406	O-linked_Glycosylation	ISGSNYKSLEVLVAD CCCCCCCCHHHHHHH	21.28	32994395
419	Ubiquitination	ADLVNAQKDSMQDES HHHHHHCHHHCCCHH	49.73	-
421	Phosphorylation	LVNAQKDSMQDESSQ HHHHCHHHCCCHHHH	25.94	27732954
422	Sulfoxidation	VNAQKDSMQDESSQT HHHCHHHCCCHHHHH	9.26	21406390
426	Phosphorylation	KDSMQDESSQTSLQK HHHCCCHHHHHHHHH	35.72	27732954
427	Phosphorylation	DSMQDESSQTSLQKE HHCCCHHHHHHHHHH	35.12	25849741
429	Phosphorylation	MQDESSQTSLQKEIS CCCHHHHHHHHHHCC	33.09	27732954
430	Phosphorylation	QDESSQTSLQKEIST CCHHHHHHHHHHCCH	22.59	22072751
433	Ubiquitination	SSQTSLQKEISTEEQ HHHHHHHHHCCHHHH	63.41	2190698
436	Phosphorylation	TSLQKEISTEEQLRR HHHHHHCCHHHHHHH	30.75	20068231
437	Phosphorylation	SLQKEISTEEQLRRL HHHHHCCHHHHHHHH	49.56	20068231
448	Ubiquitination	LRRLQEEKLCKICMD HHHHHHHHHHHHHCC	59.43	-
450	S-nitrosocysteine	RLQEEKLCKICMDRN HHHHHHHHHHHCCCC	4.07	-
450	S-nitrosylation	RLQEEKLCKICMDRN HHHHHHHHHHHCCCC	4.07	20670888
470	Phosphorylation	VPCGHLVTCKQCAEA ECCCCEECHHHHHHH	21.98	18452278
480	Ubiquitination	QCAEAVDKCPMCYTV HHHHHHHHCCCEEEE	33.37	-

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
40	S	Phosphorylation	Kinase	CDK1	P06493	PSP
87	S	Phosphorylation	Kinase	AKT1	P31749	PSP
87	S	Phosphorylation	Kinase	AKT2	P31751	PSP
87	S	Phosphorylation	Kinase	PKCE	Q02156	PSP
87	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
87	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
180	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
430	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM32	Q13049	PMID:21628460
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:14523016
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:21185211

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of XIAP_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 XIAP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NTAQ1_HUMAN	WDYHV1	physical	16189514
DYL2_HUMAN	DYNLL2	physical	16189514
XIAP_HUMAN	XIAP	physical	16189514
CASP9_HUMAN	CASP9	physical	16189514
DBLOH_HUMAN	DIABLO	physical	12511567
DBLOH_HUMAN	DIABLO	physical	15280366
CASP9_HUMAN	CASP9	physical	9545235
TAB1_HUMAN	TAB1	physical	9878061
DBLOH_HUMAN	DIABLO	physical	10929712
CASP3_HUMAN	CASP3	physical	11447297
CASP3_HUMAN	CASP3	physical	11927604
CASP4_HUMAN	CASP4	physical	11927604
TAB1_HUMAN	TAB1	physical	12048196
TAB2_HUMAN	TAB2	physical	12048196
STRAB_HUMAN	STRADB	physical	12048196
CASP3_HUMAN	CASP3	physical	11257232
CASP7_HUMAN	CASP7	physical	11257232
CASP3_HUMAN	CASP3	physical	9384571
CASP7_HUMAN	CASP7	physical	9384571
CASP3_HUMAN	CASP3	physical	9230442
CASP7_HUMAN	CASP7	physical	9230442
MAGD1_HUMAN	MAGED1	physical	11546791
XAF1_HUMAN	XAF1	physical	11175744
CASP3_HUMAN	CASP3	physical	11359776
CASP7_HUMAN	CASP7	physical	11359776
HTRA2_HUMAN	HTRA2	physical	11604410
DBLOH_HUMAN	DIABLO	physical	11604410
SRTD1_HUMAN	SERTAD1	physical	19176394
CHIP_HUMAN	STUB1	physical	19011619
M3K2_HUMAN	MAP3K2	physical	18761086
AIFM1_HUMAN	AIFM1	physical	17967870
XAF1_HUMAN	XAF1	physical	17613533
BIRC5_HUMAN	BIRC5	physical	17613533
BCL10_HUMAN	BCL10	physical	16775419
DBLOH_HUMAN	DIABLO	physical	16282325
CASP9_HUMAN	CASP9	physical	15749826
BIRC5_HUMAN	BIRC5	physical	15218035
DBLOH_HUMAN	DIABLO	physical	15178455
AKT1_HUMAN	AKT1	physical	14645242
DBLOH_HUMAN	DIABLO	physical	14523016
CASP9_HUMAN	CASP9	physical	14523016
UB2L3_HUMAN	UBE2L3	physical	12525502
UB2D1_HUMAN	UBE2D1	physical	12525502
UB2D3_HUMAN	UBE2D3	physical	12525502
DBLOH_HUMAN	DIABLO	physical	12525502
CASP9_HUMAN	CASP9	physical	15300255
HTRA2_HUMAN	HTRA2	physical	15300255
DBLOH_HUMAN	DIABLO	physical	15300255
HAX1_HUMAN	HAX1	physical	20171186
UB2E1_HUMAN	UBE2E1	physical	21113135
UB2D1_HUMAN	UBE2D1	physical	21113135
UB2D2_HUMAN	UBE2D2	physical	21113135
UB2D3_HUMAN	UBE2D3	physical	21113135
UBC9_HUMAN	UBE2I	physical	21113135
UBE2W_HUMAN	UBE2W	physical	21113135
XIAP_HUMAN	XIAP	physical	21113135
CCS_HUMAN	CCS	physical	20154138
SEPT4_HUMAN	SEPT4	physical	21185211
SIAH1_HUMAN	SIAH1	physical	21185211
RIPK1_HUMAN	RIPK1	physical	21931591
RIPK2_HUMAN	RIPK2	physical	21931591
RIPK3_HUMAN	RIPK3	physical	21931591
HTRA2_HUMAN	HTRA2	physical	15781261
DBLOH_HUMAN	DIABLO	physical	15781261
RB6I2_HUMAN	ERC1	physical	20932476
PTEN_HUMAN	PTEN	physical	19473982
DBLOH_HUMAN	DIABLO	physical	19506082
UBP19_HUMAN	USP19	physical	21849505
CASP9_HUMAN	CASP9	physical	18022362
AIFM1_HUMAN	AIFM1	physical	22103349
SEPT4_HUMAN	SEPT4	physical	22185822
TRI32_HUMAN	TRIM32	physical	21628460
GDIR1_HUMAN	ARHGDIA	physical	21402697
DBLOH_HUMAN	DIABLO	physical	15200957
CASP3_HUMAN	CASP3	physical	15200957
CASP7_HUMAN	CASP7	physical	15200957
UBC_HUMAN	UBC	physical	22194841
SIVA_HUMAN	SIVA1	physical	19584092
CASP3_HUMAN	CASP3	physical	22072751
IRF3_HUMAN	IRF3	physical	22072751
UBC_HUMAN	UBC	physical	18931663
DBLOH_HUMAN	DIABLO	physical	20957035
XIAP_HUMAN	XIAP	physical	22825849
XAF1_HUMAN	XAF1	physical	22811387
RAC1_HUMAN	RAC1	physical	22117219
DBLOH_HUMAN	DIABLO	physical	11801603
HTRA2_HUMAN	HTRA2	physical	11801603
CASP9_HUMAN	CASP9	physical	11801603
DBLOH_HUMAN	DIABLO	physical	15507451
CASP3_HUMAN	CASP3	physical	15507451
CASP9_HUMAN	CASP9	physical	15507451
CASP3_HUMAN	CASP3	physical	12624662
CASP7_HUMAN	CASP7	physical	15580265
M3K7_HUMAN	MAP3K7	physical	11865055
HTRA2_HUMAN	HTRA2	physical	11803371
CASP3_HUMAN	CASP3	physical	18521960
CASP7_HUMAN	CASP7	physical	18521960
DBLOH_HUMAN	DIABLO	physical	15650747
CASP3_HUMAN	CASP3	physical	15650747
CASP3_HUMAN	CASP3	physical	16543147
BIRC3_HUMAN	BIRC3	physical	17069460
BIRC2_HUMAN	BIRC2	physical	17069460
CASP3_HUMAN	CASP3	physical	17069460
CASP9_HUMAN	CASP9	physical	16701639
HTRA2_HUMAN	HTRA2	physical	11602612
XIAP_HUMAN	XIAP	physical	11602612
DBLOH_HUMAN	DIABLO	physical	11602612
DBLOH_HUMAN	DIABLO	physical	19153467
CASP9_HUMAN	CASP9	physical	19153467
CASP7_HUMAN	CASP7	physical	11257231
DBLOH_HUMAN	DIABLO	physical	11257231
CASP7_HUMAN	CASP7	physical	11257230
CASP3_HUMAN	CASP3	physical	11257230
DBLOH_HUMAN	DIABLO	physical	11257230
CASP9_HUMAN	CASP9	physical	12620238
DBLOH_HUMAN	DIABLO	physical	11140637
RAF1_HUMAN	RAF1	physical	16964381
HTRA2_HUMAN	HTRA2	physical	11583623
DBLOH_HUMAN	DIABLO	physical	17724022
TCF25_HUMAN	TCF25	physical	18068114
CASP9_HUMAN	CASP9	physical	17179183
DBLOH_HUMAN	DIABLO	physical	17179183
CASP3_HUMAN	CASP3	physical	17291493
CASP9_HUMAN	CASP9	physical	17291493
DBLOH_MOUSE	Diablo	physical	11606597
DBLOH_HUMAN	DIABLO	physical	11606597
HSP74_HUMAN	HSPA4	physical	11606597
CHK1_HUMAN	CHEK1	physical	14759516
RIPK2_HUMAN	RIPK2	physical	19667203
DBLOH_HUMAN	DIABLO	physical	19667203
NOD1_HUMAN	NOD1	physical	19667203
NOD2_HUMAN	NOD2	physical	19667203
CASP7_HUMAN	CASP7	physical	14512414
DBLOH_HUMAN	DIABLO	physical	14512414
CASP9_HUMAN	CASP9	physical	14512414
ROA1_HUMAN	HNRNPA1	physical	17287399
LA_HUMAN	SSB	physical	17287399
HNRPC_HUMAN	HNRNPC	physical	17287399
CASP3_HUMAN	CASP3	physical	19698783
CASP7_HUMAN	CASP7	physical	19698783
CASP9_HUMAN	CASP9	physical	19698783
APAF_HUMAN	APAF1	physical	19698783
ELAV1_HUMAN	ELAVL1	physical	21102524
SEPT4_HUMAN	SEPT4	physical	21869827
UB2D1_HUMAN	UBE2D1	physical	15749826
UB2D3_HUMAN	UBE2D3	physical	15200957
UB2D1_HUMAN	UBE2D1	physical	22825849
UB2D3_HUMAN	UBE2D3	physical	22185822
PGAM5_HUMAN	PGAM5	physical	23201124
XIAP_HUMAN	XIAP	physical	23259674
UB2D2_HUMAN	UBE2D2	physical	23259674
UBC_HUMAN	UBC	physical	23259674
NOTC1_MOUSE	Notch1	physical	17318174
NOTC1_HUMAN	NOTCH1	physical	17318174
UB2D1_HUMAN	UBE2D1	physical	17318174
BIRC7_HUMAN	BIRC7	physical	22711539
BIRC2_HUMAN	BIRC2	physical	22711539
SHIP1_HUMAN	INPP5D	physical	22815893
CASP3_HUMAN	CASP3	physical	22815893
SCAR3_HUMAN	SCARA3	physical	22683311
RIPK2_HUMAN	RIPK2	physical	23818254
DBLOH_HUMAN	DIABLO	physical	23818254
UB2D3_HUMAN	UBE2D3	physical	23818254
TRAF6_HUMAN	TRAF6	physical	22493164
TRIM8_HUMAN	TRIM8	physical	22493164
DTX3_HUMAN	DTX3	physical	22493164
SEPT4_HUMAN	SEPT4	physical	15029247
SIVA_HUMAN	SIVA1	physical	22343716
XIAP_HUMAN	XIAP	physical	16338389
MDM2_HUMAN	MDM2	physical	23749209
BIRC3_HUMAN	BIRC3	physical	24552816
FAIM1_HUMAN	FAIM	physical	24305822
CRYAB_HUMAN	CRYAB	physical	23074197
IMUP_HUMAN	C19orf33	physical	22886722
AKT1_HUMAN	AKT1	physical	23640046
M3K2_HUMAN	MAP3K2	physical	24975362
M3K3_HUMAN	MAP3K3	physical	24975362
XIAP_HUMAN	XIAP	physical	24975362
UB2D1_HUMAN	UBE2D1	physical	24975362
CASP7_HUMAN	CASP7	physical	23979166
CASP3_HUMAN	CASP3	physical	23979166
DBLOH_HUMAN	DIABLO	physical	25246529
XIAP_HUMAN	XIAP	physical	19549727
UBE2N_HUMAN	UBE2N	physical	19549727
UB2D1_HUMAN	UBE2D1	physical	19549727
UB2D2_HUMAN	UBE2D2	physical	19549727
UB2E1_HUMAN	UBE2E1	physical	19549727
UB2D3_HUMAN	UBE2D3	physical	19549727
RAC1_HUMAN	RAC1	physical	25301945
CASP9_HUMAN	CASP9	physical	25416956
CASPA_HUMAN	CASP10	physical	25416956
CKS1_HUMAN	CKS1B	physical	25416956
ERCC3_HUMAN	ERCC3	physical	25416956
RFC5_HUMAN	RFC5	physical	25416956
RIPK2_HUMAN	RIPK2	physical	25416956
NEK6_HUMAN	NEK6	physical	25416956
VP37C_HUMAN	VPS37C	physical	25416956
LONF1_HUMAN	LONRF1	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
XIAP_HUMAN	XIAP	physical	11724934
UB2D2_HUMAN	UBE2D2	physical	11724934
CASP8_HUMAN	CASP8	physical	15069192
CASP9_HUMAN	CASP9	physical	15069192
CASPA_HUMAN	CASP10	physical	15069192
UB2D2_HUMAN	UBE2D2	physical	12525502
UB2L6_HUMAN	UBE2L6	physical	12525502
COMD1_HUMAN	COMMD1	physical	14685266
UB2D1_HUMAN	UBE2D1	physical	15300255
XIAP_HUMAN	XIAP	physical	18570872
DBLOH_HUMAN	DIABLO	physical	22465666
XIAP_HUMAN	XIAP	physical	25619915
BIRC5_HUMAN	BIRC5	physical	21536684
DBLOH_HUMAN	DIABLO	physical	23251006
HTRA2_HUMAN	HTRA2	physical	24698088
E2F1_HUMAN	E2F1	physical	25216527
ACV1B_HUMAN	ACVR1B	physical	25241761
RAF1_HUMAN	RAF1	physical	25241761
TRAF6_HUMAN	TRAF6	physical	25241761
CASP9_HUMAN	CASP9	physical	25241761
CASP3_HUMAN	CASP3	physical	25241761
XIAP_HUMAN	XIAP	physical	25801170
DBLOH_HUMAN	DIABLO	physical	25801170
UB2D2_HUMAN	UBE2D2	physical	25801170
CDCA4_HUMAN	CDCA4	physical	25691055
SRTD1_HUMAN	SERTAD1	physical	25691055
TLE3_HUMAN	TLE3	physical	22304967
UB2D1_HUMAN	UBE2D1	physical	22304967
XAF1_HUMAN	XAF1	physical	23323858
UBP11_HUMAN	USP11	physical	28040451
XIAP_HUMAN	XIAP	physical	27865841
XIAP_HUMAN	XIAP	physical	29053960
UB2D2_HUMAN	UBE2D2	physical	27569044
FAF1_HUMAN	FAF1	physical	28414080
TAB1_HUMAN	TAB1	physical	28414080

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300635	Lymphoproliferative syndrome, X-linked, 2 (XLP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of XIAP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Crystal structure of the BIR1 domain of XIAP in two crystal forms."; Lin S.-C., Huang Y., Lo Y.-C., Lu M., Wu H.; J. Mol. Biol. 372:847-854(2007). Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99, PHOSPHORYLATION ATSER-87, MUTAGENESIS OF SER-87, AND SUBUNIT.	17698078 [Abstract]
"Akt phosphorylation and stabilization of X-linked inhibitor ofapoptosis protein (XIAP)."; Dan H.C., Sun M., Kaneko S., Feldman R.I., Nicosia S.V., Wang H.-G.,Tsang B.K., Cheng J.Q.; J. Biol. Chem. 279:5405-5412(2004). Cited for: FUNCTION, PHOSPHORYLATION AT SER-87, UBIQUITINATION, AND PROTEASOMALDEGRADATION.	14645242 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND MASSSPECTROMETRY.	17053785 [Abstract]
S-nitrosylation
Reference	PubMed
"Transnitrosylation of XIAP regulates caspase-dependent neuronal celldeath."; Nakamura T., Wang L., Wong C.C., Scott F.L., Eckelman B.P., Han X.,Tzitzilonis C., Meng F., Gu Z., Holland E.A., Clemente A.T.,Okamoto S., Salvesen G.S., Riek R., Yates J.R. III, Lipton S.A.; Mol. Cell 39:184-195(2010). Cited for: S-NITROSYLATION AT CYS-450.	20670888 [Abstract]
Ubiquitylation
Reference	PubMed
"Identification of ubiquitination sites on the X-linked inhibitor ofapoptosis protein."; Shin H., Okada K., Wilkinson J.C., Solomon K.M., Duckett C.S.,Reed J.C., Salvesen G.S.; Biochem. J. 373:965-971(2003). Cited for: AUTOUBIQUITINATION AT LYS-322 AND LYS-328.	12747801 [Abstract]