XAF1_HUMAN - dbPTM
XAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XAF1_HUMAN
UniProt AC Q6GPH4
Protein Name XIAP-associated factor 1
Gene Name XAF1
Organism Homo sapiens (Human).
Sequence Length 301
Subcellular Localization Cytoplasm. Nucleus. Mitochondrion. Found in the cytoplasm and nucleus of placental syncytiotrophoblasts. Translocates to mitochondria upon TNF-alpha treatment.
Isoform 1: Nucleus.
Isoform 5: Nucleus.
Protein Description Seems to function as a negative regulator of members of the IAP (inhibitor of apoptosis protein) family. Inhibits anti-caspase activity of BIRC4. Induces cleavage and inactivation of BIRC4 independent of caspase activation. Mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells. May inhibit BIRC4 indirectly by activating the mitochondrial apoptosis pathway. After translocation to mitochondria, promotes translocation of BAX to mitochondria and cytochrome c release from mitochondria. Seems to promote the redistribution of BIRC4 from the cytoplasm to the nucleus, probably independent of BIRC4 inactivation which seems to occur in the cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of BIRC5/survivin; the process requires the E3 ligase activity of BIRC4. Seems to be involved in cellular sensitivity to the proapoptotic actions of TRAIL. May be a tumor suppressor by mediating apoptosis resistance of cancer cells..
Protein Sequence MEGDFSVCRNCKRHVVSANFTLHEAYCLRFLVLCPECEEPVPKETMEEHCKLEHQQVGCTMCQQSMQKSSLEFHKANECQERPVECKFCKLDMQLSKLELHESYCGSRTELCQGCGQFIMHRMLAQHRDVCRSEQAQLGKGERISAPEREIYCHYCNQMIPENKYFHHMGKCCPDSEFKKHFPVGNPEILPSSLPSQAAENQTSTMEKDVRPKTRSINRFPLHSESSSKKAPRSKNKTLDPLLMSEPKPRTSSPRGDKAAYDILRRCSQCGILLPLPILNQHQEKCRWLASSKGKQVRNFS
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
2 (in isoform 6)Phosphorylation-68.4230631047
13 (in isoform 6)Phosphorylation-29.9930631047
14 (in isoform 6)Phosphorylation-15.1530631047
69PhosphorylationCQQSMQKSSLEFHKA
HHHHHHHHHHHHHCC		24.2224719451
70PhosphorylationQQSMQKSSLEFHKAN
HHHHHHHHHHHHCCH		38.6726657352
75UbiquitinationKSSLEFHKANECQER
HHHHHHHCCHHHHCC		59.2229967540
103PhosphorylationSKLELHESYCGSRTE
HHHHHCHHHHCCHHH		18.2527251275
104PhosphorylationKLELHESYCGSRTEL
HHHHCHHHHCCHHHH		9.61-
140AcetylationSEQAQLGKGERISAP
HHHHHCCCCCCCCCC		67.2125953088
140UbiquitinationSEQAQLGKGERISAP
HHHHHCCCCCCCCCC		67.21-
152UbiquitinationSAPEREIYCHYCNQM
CCCCCCEEHHHHCCC		2.8929967540
152PhosphorylationSAPEREIYCHYCNQM
CCCCCCEEHHHHCCC		2.89-
155PhosphorylationEREIYCHYCNQMIPE
CCCEEHHHHCCCCCC		6.91-
161UbiquitinationHYCNQMIPENKYFHH
HHHCCCCCCCCCCCC		33.4929967540
171UbiquitinationKYFHHMGKCCPDSEF
CCCCCCCCCCCCHHH		25.7029967540
180UbiquitinationCPDSEFKKHFPVGNP
CCCHHHHHHCCCCCH		56.6629967540
192PhosphorylationGNPEILPSSLPSQAA
CCHHHCCCCCCHHHH		40.8527251275
193PhosphorylationNPEILPSSLPSQAAE
CHHHCCCCCCHHHHC		42.2227251275
196PhosphorylationILPSSLPSQAAENQT
HCCCCCCHHHHCCCC		37.4327251275
214PhosphorylationEKDVRPKTRSINRFP
CHHCCCCCCCCCCCC		32.1226074081
216PhosphorylationDVRPKTRSINRFPLH
HCCCCCCCCCCCCCC		29.4626074081
224PhosphorylationINRFPLHSESSSKKA
CCCCCCCCCCCCCCC		47.0225690035
226PhosphorylationRFPLHSESSSKKAPR
CCCCCCCCCCCCCCC		42.8228348404
227PhosphorylationFPLHSESSSKKAPRS
CCCCCCCCCCCCCCC		41.9725690035
228PhosphorylationPLHSESSSKKAPRSK
CCCCCCCCCCCCCCC		47.6724850871
237UbiquitinationKAPRSKNKTLDPLLM
CCCCCCCCCCCHHHH		54.95-
239UbiquitinationPRSKNKTLDPLLMSE
CCCCCCCCCHHHHCC		7.3429967540
252PhosphorylationSEPKPRTSSPRGDKA
CCCCCCCCCCCCCHH		39.3626074081
253PhosphorylationEPKPRTSSPRGDKAA
CCCCCCCCCCCCHHH		20.2926074081
258UbiquitinationTSSPRGDKAAYDILR
CCCCCCCHHHHHHHH		37.4329967540
261PhosphorylationPRGDKAAYDILRRCS
CCCCHHHHHHHHHHH		14.3621552520
268PhosphorylationYDILRRCSQCGILLP
HHHHHHHHCCCCEEE		27.0530576142
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
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:22811387
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XAF1_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 XAF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RN114_HUMANRNF114physical
23645206
P53_HUMANTP53physical
25313037
SIAH2_HUMANSIAH2physical
25313037
HIPK2_HUMANHIPK2genetic
25313037
XIAP_HUMANXIAPphysical
23323858
TRAF2_HUMANTRAF2physical
27768232
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XAF1_HUMAN

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Related Literatures of Post-Translational Modification

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