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Alix (human)

Overview Alix an adaptor protein that may regulate the function of receptor and cytoskeleton-associated tyrosine kinases. A class E vacuolar protein sorting (VPS) factor involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. In case of infection, the HIV-1 virus directly takes advantage of its function for viral exocytosis and budding, via its interaction with HIV-1 p6 protein. May play a role in the regulation of both apoptosis and cell proliferation. Note: This description may include information from UniProtKB. Protein type: Apoptosis; Adaptor/scaffold Cellular Component: cytoplasm; melanosome; microtubule organizing center; cytosol Molecular Function: protein binding; calcium-dependent protein binding Biological Process: protein transport; apoptosis; cell division; virus-host interaction; cell cycle Reference #:  Q8WUM4 (UniProtKB) Alt. Names/Synonyms: AIP1; ALG-2 interacting protein 1; ALG-2 interacting protein X; ALG-2-interacting protein 1; ALIX; apoptosis-linked gene 2-interacting protein X; dopamine receptor interacting protein 4; DRIP4; Hp95; KIAA1375; MGC17003; PDC6I; PDCD6-interacting protein; PDCD6IP; programmed cell death 6 interacting protein; Programmed cell death 6-interacting protein Gene Symbols: PDCD6IP Molecular weight: 96,023 Da Basal Isoelectric point: 6.13  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below Alix 2OEV - A=1-698 (human) 2OEW - A=1-359 (human) 2OEX - A/B=359-702 (human) 2OJQ - A=360-702 (human) 2R02 - A=2-698 (human) 2R03 - A=2-698 (human) 2R05 - A=2-698 (human) 2XS1 - A=1-698 (human) 2XS8 - A=1-698 (human) 2ZNE - D/C=799-814 (human) 3C3O - A=1-359 (human) 3C3Q - A=1-359 (human) 3C3R - A=1-359 (human) 3E1R - C=797-809 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2OEV 2OEW 2OEX 2OJQ 2R02 2R03 2R05 2XS1 2XS8 2ZNE 3C3O 3C3Q 3C3R 3E1R  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein

	Sites Implicated In
cell adhesion, altered: Y319‑p molecular association, regulation: Y319‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: 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.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	2		K19-u	TSEVDLAkPLVkFIQ
0	1		K23-u	DLAkPLVkFIQQTYP
0	7		Y39-p	GGEEQAQyCRAAEEL
0	1		K48-a	RAAEELSkLRRAAVG
0	2		K48-u	RAAEELSkLRRAAVG
0	1		K60	AVGRPLDKHEGALET
0	2		K101-u	TWKDAFDkGSLFGGS
0	1		T186-p	ISPDTVGtLSLIMLA
0	1		K215-a	MKDAIIAkLANQAAD
0	5		K215-u	MKDAIIAkLANQAAD
0	4		Y223-p	LANQAADyFGDAFKQ
0	1		Y258-p	IMQANAEyHQSILAK
0	1		K268-a	SILAKQQkkFGEEIA
0	1		K269-a	ILAKQQkkFGEEIAR
0	1		K285	QHAAELIKTVASRYD
0	3		Y294-p	VASRYDEyVNVKDFS
0	1		K298	YDEyVNVKDFSDKIN
2	60		Y319-p	KKDNDFIyHDRVPDL
0	2		K350-u	VNVPISQkFTDLFEk
0	1		K357-u	kFTDLFEkMVPVSVQ
0	1		S366-p	VPVSVQQsLAAyNQR
0	1		Y370-p	VQQsLAAyNQRKADL
0	4		Y485-p	RTPSNELykPLRAEG
0	2		K486-u	TPSNELykPLRAEGT
0	19		K501-u	NFRTVLDkAVQADGQ
0	1		K627	KKQEGLLKNIQVSHQ
0	12		K638-u	VSHQEFSkMkQSNNE
0	46		K640-u	HQEFSkMkQSNNEAN
0	9		K707-u	TERDELLkDLQQsIA
0	1		S712-p	LLkDLQQsIAREPsA
0	3		S718-p	QsIAREPsAPSIPtP
0	4		T724-p	PsAPSIPtPAyQSsP
0	96		Y727-p	PSIPtPAyQSsPAGG
0	3		S730-p	PtPAyQSsPAGGHAP
0	6		T738-p	PAGGHAPtPPtPAPR
0	5		T741-p	GHAPtPPtPAPRTMP
0	1		R745	tPPtPAPRTMPPTkP
0	7		K751-u	PRTMPPTkPQPPARP

	mouse
K19-u	TSEVDLAkPLVKFIQ
K23	DLAkPLVKFIQQTYP
Y39	GGEEQAQYCRAAEEL
K48	RAAEELSKLRRSALG
K48-u	RAAEELSkLRRSALG
K60-u	ALGRPLDkHEGALET
K101-u	TWKDAFDkGSLFGGS
T186	ISPDTVGTLSLIMLA
K215	MKDAIIAKLANQAAD
K215	MKDAIIAKLANQAAD
Y223	LANQAADYFGDAFKQ
Y258	IMQANAEYHQSILAK
K268-a	SILAKQQkkFGEEIA
K269-a	ILAKQQkkFGEEIAR
K285-u	QHAAELIkNVASRYD
Y294	VASRYDEYVNVkDFS
K298-u	YDEYVNVkDFSDKIN
Y319	KKDNDFIYHDRVPDL
K350-u	VNVPVSQkFTDLFEK
K357	kFTDLFEKMVPVSVQ
S366	VPVSVQQSLAVFSQR
F370	VQQSLAVFSQRKADL
Y485	RTPSNDLYKPLRAEG
K486	TPSNDLYKPLRAEGA
K501-u	KFRAVLDkAVQADGQ
K627-u	KKQEGLLkNIQVSHQ
K638-u	VSHQEFSkMkQSNNE
K640-u	HQEFSkMkQSNNEAN
K707-u	TERDELLkDLQQSIA
S712	LLkDLQQSIAREPsA
S718-p	QSIAREPsAPSIPPP
P724	PsAPSIPPPAyQSSP
Y727-p	PSIPPPAyQSSPAAG
S730	PPPAyQSSPAAGHAA
A738	PAAGHAAAPPTPAPR
T741	GHAAAPPTPAPRTMP
R745	APPTPAPRTMPPAKP
K751	PRTMPPAKPQPPARP

	rat
K19	TSEVDLAKPLVKFIQ
K23	DLAKPLVKFIQQTYP
Y39	GGEEQAQYCRAAEEL
K48	RAAEELSKLRRSALG
K48	RAAEELSKLRRSALG
K60	ALGRPLDKHEGALET
K101	TWKDAFDKGSLFGGS
T186	ISPDTVGTLSLIMLA
K215	MKDAIIAKLANQAAD
K215	MKDAIIAKLANQAAD
Y223	LANQAADYFGDAFKQ
Y263	IMQANAEYHQSILAK
K273	SILAKQQKKFGEEIA
K274	ILAKQQKKFGEEIAR
K290	QHAAELIKNVASRYD
Y299	VASRYDEYVNVKDFS
K303	YDEYVNVKDFSDKIN
Y324	KKDNDFIYHDRVPDL
K355	VNVPISQKFTDLFEK
K362	KFTDLFEKMVPVSVQ
S371	VPVSVQQSLAVFSQR
F375	VQQSLAVFSQRKADL
Y490	RTPSNDLYKPLRAEG
K491	TPSNDLYKPLRAEGA
K506	KFRAVLDKAVQADGQ
K632	KKQEGLLKNIQVSHQ
K643	VSHQEFSKMKQSNSE
K645	HQEFSKMKQSNSEAS
K712	TERDELLKDLQQSIA
S717	LLKDLQQSIAREPSA
S723	QSIAREPSAPSIPPP
P729	PSAPSIPPPAYQSSP
Y732	PSIPPPAYQSSPAGG
S735	PPPAYQSSPAGGHAT
A743	PAGGHATAPTPAPrT
T745	GGHATAPTPAPrTMP
R749-m1	TAPTPAPrTMPPAKP
K755	PrTMPPAKPQPPARP

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