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Protein Page:
APPL (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
APPL an effector protein of the small GTPase Rab5, a key regulator of endocytosis. Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. Contains a PH domain and an N-terminal PID domain. Its interaction with RAB5A/Rab5 is essential for its recruitment to endosomal membranes as well as its role in cell proliferation. Binds DCC and the catalytic domain of the inactive form of AKT2 through its PID domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex. Phosphorylated upon DNA damage. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Adaptor/scaffold
Cellular Component: early endosome membrane; cytoplasm; endosome membrane; vesicle membrane; NuRD complex; nucleus; cytosol
Molecular Function: protein kinase B binding; protein binding; phospholipid binding
Biological Process: regulation of apoptosis; cell proliferation; apoptosis; insulin receptor signaling pathway; regulation of glucose import; signal transduction; cell cycle
Reference #:  Q9UKG1 (UniProtKB)
Alt. Names/Synonyms: Adapter protein containing PH domain, PTB domain and leucine zipper motif 1; adaptor protein containing pH domain, PTB domain and leucine zipper motif 1; adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1; AKT2 interactor; APPL; APPL1; DCC-interacting protein 13-alpha; Dip13-alpha; DIP13A; DIP13alpha; DP13A; KIAA1428; signaling adaptor protein DIP13alpha
Gene Symbols: APPL1
Molecular weight: 79,663 Da
Basal Isoelectric point: 5.28  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

APPL
Protein Structure Not Found.


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Sites Implicated In
endocytosis, inhibited: S410‑p
molecular association, regulation: S410‑p
receptor recycling, altered: S410‑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
 

Show Multiple Sequence Alignment


 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 3 K63-u AATHLTSkLLkEYEK
0 6 K66-u HLTSkLLkEYEKQRF
0 1 K70 kLLkEYEKQRFPLGG
0 1 S97-p SKVIDELssCHAVLS
0 1 S98-p KVIDELssCHAVLST
0 2 Y161-p RENDKVKyEVTEDVy
0 2 Y168-p yEVTEDVyTSRKKQH
0 1 S258-p IEDLEVAsDPLYVPD
0 1 K350-a QITSFDGkksSILQA
0 1 K350-u QITSFDGkksSILQA
0 1 K351-u ITSFDGkksSILQAE
0 1 S352-p TSFDGkksSILQAES
0 1 S374-p ICTINNIsKQIyLSE
0 5 Y378-p NNIsKQIyLSENPEE
0 5 T399-p QSALEAVtPsPsFQQ
1 13 S401-p ALEAVtPsPsFQQRH
1 3 S403-p EAVtPsPsFQQRHEs
1 0 S410-p sFQQRHEsLRPAAGQ
0 1 T422-p AGQSRPPtARTSsSG
0 1 S427-p PPtARTSsSGsLGSE
1 2 S430-p ARTSsSGsLGSESTN
0 1 S459-p PIQFDIIsPVCEDQP
0 8 T479-p FGQGGRRtNPFGESG
0 1 K490-u GESGGSTksETEDSI
0 1 S491-p ESGGSTksETEDSIL
0 1 S509-p FIVRFLGsMEVksDD
0 2 K513-u FLGsMEVksDDHPDV
0 1 S514-p LGsMEVksDDHPDVV
0 5 Y522-p DDHPDVVyEtMRQIL
0 1 T524-p HPDVVyEtMRQILAA
0 1 Y604-p SNLSSVCyIFESNNE
0 5 S636-p AELDRRAsEKQKEIE
0 2 S689-p EGQFVVLsSsQsEEs
0 2 S691-p QFVVLsSsQsEEsDL
0 2 S693-p VVLsSsQsEEsDLGE
0 2 S696-p sSsQsEEsDLGEGGK
  mouse

 
K63-u AATHLTSkLLkEYEk
K66-u HLTSkLLkEYEkQRF
K70-u kLLkEYEkQRFPLGG
S97 SKVIDELSSCHAVLS
S98 KVIDELSSCHAVLST
Y161-p RENDKVKyEVTEDVy
Y168-p yEVTEDVyTSRKKQH
S258 IEDLEVASDPLYLPD
K350 QITSFDGKKSSILQA
K350 QITSFDGKKSSILQA
K351 ITSFDGKKSSILQAE
S352 TSFDGKKSSILQAES
S374 ICTINNISKQIYLSE
Y378 NNISKQIYLSENPEE
T399-p QSALEAVtPsPsFQQ
S401-p ALEAVtPsPsFQQRH
S403-p EAVtPsPsFQQRHES
S410 sFQQRHESLRPGGQS
T421 GGQSRPPTARTSSSG
S426 PPTARTSSSGsLGSE
S429-p ARTSSSGsLGSESTN
S458 PIQFDIISPVCEDQP
T478 FGQGGRRTNPFGESG
K489 GESGGSTKSETEDSI
S490 ESGGSTKSETEDSIL
S508 FIVRFLGSMEVkSDD
K512-u FLGSMEVkSDDHPDV
S513 LGSMEVkSDDHPDVV
Y521 DDHPDVVYETMRQIL
T523 HPDVVYETMRQILAA
Y603 SNLSSVCYIFESNNE
S635 AELDRRASEKQKEIE
S687-p SEGQLVLsSSQsEEs
S689 GQLVLsSSQsEEsDL
S691-p LVLsSSQsEEsDLGE
S694-p sSSQsEEsDLGEEGK
  rat

 
K63 AATHLTSKLLKEYEK
K66 HLTSKLLKEYEKQRF
K70 KLLKEYEKQRFPLGG
S97 SKVIDELSSCHAVLS
S98 KVIDELSSCHAVLST
Y161 RENDKVKYEVTEDVY
Y168 YEVTEDVYTSRKKQH
S258 IEDLEVASDPLYLPD
K350 QITSFDGKKSSILQA
K350 QITSFDGKKSSILQA
K351 ITSFDGKKSSILQAE
S352 TSFDGKKSSILQAES
S374 ICTINNISKQIYLSE
Y378 NNISKQIYLSENPEE
T399-p QSALEAVtPsPsFQQ
S401-p ALEAVtPsPsFQQRH
S403-p EAVtPsPsFQQRHES
S410 sFQQRHESLRPGGQS
T421 GGQSRPPTARTSSSG
S426 PPTARTSSSGSLGSE
S429 ARTSSSGSLGSESTN
S458 PIQFDIISPVCEDQP
T478 FGQGGRRTNPFGESG
K489 GESGGSTKSETEDSI
S490 ESGGSTKSETEDSIL
S508 FIVRFLGSMEVKSDD
K512 FLGSMEVKSDDHPDV
S513 LGSMEVKSDDHPDVV
Y521 DDHPDVVYETMRQIL
T523 HPDVVYETMRQILAA
Y603 SNLSSVCYIFESNNE
S635 AELDRRASEKQKEIE
S687 SEGQLVLSSSQSEES
S689 GQLVLSSSQSEESDL
S691 LVLSSSQSEESDLGE
S694 SSSQSEESDLGEEGK
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