AAK1_MOUSE - dbPTM
AAK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAK1_MOUSE
UniProt AC Q3UHJ0
Protein Name AP2-associated protein kinase 1
Gene Name Aak1
Organism Mus musculus (Mouse).
Sequence Length 959
Subcellular Localization Cell membrane
Peripheral membrane protein. Membrane, clathrin-coated pit. Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migr
Protein Description Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity)..
Protein Sequence MKKFFDSRREQGSSGLGSGSSGGGGSSSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFALVFLVRTSNGVKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQAEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGSFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPVPNVQNSPIPAKLPEPVKASEAAVKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPLPQAAGPSNQPGLLPSVSQPKAQATPSQPLQSSQPKQPQAPPTPQQTPATQTQGLPTQAQATPQHQQQHLLKQQQQQQQQPQQPTAPPQPAGTFYQQQQQQQQQQAQTQQFQAVHPAAQQPVTAQFPVGSQGGAQQQLMQNFYHQQQQQQQQQQQLMAQQAALQQKTAVVVPQSQAQPATAPQAAAAQEPGQIQAPVRQQPKVQTTPPPTIQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVSNASEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKLPEKLGGSAESLIPGFQPTQGDAFTTPSFSAGTAEKRKGGQAVDSGIPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIDKADVAVESLIPGLEPPVAQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTAGLLEEFAPIALSAPTHKAAEDSNLISGFGVAEGSEKVAEDEFDPIPVLITKNTQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
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
1Acetylation-------MKKFFDSR
-------CCCCCCCC		10.85-
7Phosphorylation-MKKFFDSRREQGSS
-CCCCCCCCCCCCCC		28.2529899451
13PhosphorylationDSRREQGSSGLGSGS
CCCCCCCCCCCCCCC		22.4122322096
14PhosphorylationSRREQGSSGLGSGSS
CCCCCCCCCCCCCCC		44.8824925903
18PhosphorylationQGSSGLGSGSSGGGG
CCCCCCCCCCCCCCC		40.3125521595
20PhosphorylationSSGLGSGSSGGGGSS
CCCCCCCCCCCCCCC		27.7524925903
21PhosphorylationSGLGSGSSGGGGSSS
CCCCCCCCCCCCCCC		45.0125521595
26PhosphorylationGSSGGGGSSSGLGSG
CCCCCCCCCCCCCCC		25.3024925903
27PhosphorylationSSGGGGSSSGLGSGY
CCCCCCCCCCCCCCC		31.5325619855
28PhosphorylationSGGGGSSSGLGSGYI
CCCCCCCCCCCCCCC		39.4724925903
32PhosphorylationGSSSGLGSGYIGRVF
CCCCCCCCCCCCCCC		33.2025619855
34PhosphorylationSSGLGSGYIGRVFGI
CCCCCCCCCCCCCCC		11.2525619855
234PhosphorylationAPEMVNLYSGKIITT
CCHHHCCCCCCEECC		15.35-
235PhosphorylationPEMVNLYSGKIITTK
CHHHCCCCCCEECCH		36.45-
354 (in isoform 2)Phosphorylation-33.8919144319
354PhosphorylationTQPKARLTDPIPTTE
CCCCCCCCCCCCCCC		33.898009991
359 (in isoform 2)Phosphorylation-37.6719144319
359PhosphorylationRLTDPIPTTETSIAP
CCCCCCCCCCCCCCC		37.6719144319
360 (in isoform 2)Phosphorylation-31.7319144319
360O-linked_GlycosylationLTDPIPTTETSIAPR
CCCCCCCCCCCCCCC		31.7322645316
360PhosphorylationLTDPIPTTETSIAPR
CCCCCCCCCCCCCCC		31.7319144319
362 (in isoform 2)Phosphorylation-24.2819144319
362PhosphorylationDPIPTTETSIAPRQR
CCCCCCCCCCCCCCC		24.2819144319
389PhosphorylationLPIQPALTPRKRATV
CCCCCCCCCCCCCCC		24.1323527152
391MethylationIQPALTPRKRATVQP
CCCCCCCCCCCCCCC		35.5424129315
425PhosphorylationPKAQATPSQPLQSSQ
CCCCCCCCCCCCCCC		39.8229514104
441PhosphorylationKQPQAPPTPQQTPAT
CCCCCCCCCCCCCCC		32.4429899451
445PhosphorylationAPPTPQQTPATQTQG
CCCCCCCCCCCCCCC		15.0528285833
455PhosphorylationTQTQGLPTQAQATPQ
CCCCCCCCCCCCCHH		41.3951457083
460PhosphorylationLPTQAQATPQHQQQH
CCCCCCCCHHHHHHH		16.0551457091
523 (in isoform 2)Phosphorylation-33.5419144319
537 (in isoform 2)Phosphorylation-2.3819144319
541PhosphorylationQQLMQNFYHQQQQQQ
HHHHHHHHHHHHHHH		13.2822807455
554 (in isoform 2)Phosphorylation-2.3919144319
572O-linked_GlycosylationTAVVVPQSQAQPATA
CEEEECHHHCCCCCC		22.7822645316
578O-linked_GlycosylationQSQAQPATAPQAAAA
HHHCCCCCCCHHHHH		45.6255410609
593 (in isoform 2)Phosphorylation-13.2419144319
603PhosphorylationRQQPKVQTTPPPTIQ
CCCCCCCCCCCCCCC		44.2324925903
604PhosphorylationQQPKVQTTPPPTIQG
CCCCCCCCCCCCCCC		19.3924925903
608PhosphorylationVQTTPPPTIQGQKVG
CCCCCCCCCCCEEEC		31.5424925903
616PhosphorylationIQGQKVGSLTPPSSP
CCCEEECCCCCCCCC		31.8625521595
618PhosphorylationGQKVGSLTPPSSPKT
CEEECCCCCCCCCCC		34.5518388127
621PhosphorylationVGSLTPPSSPKTQRA
ECCCCCCCCCCCCCC		61.5518388127
622PhosphorylationGSLTPPSSPKTQRAG
CCCCCCCCCCCCCCC		35.8718388127
625PhosphorylationTPPSSPKTQRAGHRR
CCCCCCCCCCCCCCH		27.0325168779
635PhosphorylationAGHRRILSDVTHSAV
CCCCHHHHCCCHHHH		27.8824925903
638PhosphorylationRRILSDVTHSAVFGV
CHHHHCCCHHHHHCC		18.3325521595
640PhosphorylationILSDVTHSAVFGVPA
HHHCCCHHHHHCCCC		19.4325521595
648O-linked_GlycosylationAVFGVPASKSTQLLQ
HHHCCCCCHHHHHHH		22.529439843
648PhosphorylationAVFGVPASKSTQLLQ
HHHCCCCCHHHHHHH		22.5224925903
650PhosphorylationFGVPASKSTQLLQAA
HCCCCCHHHHHHHHH		20.9125521595
651PhosphorylationGVPASKSTQLLQAAA
CCCCCHHHHHHHHHH		27.2925521595
662PhosphorylationQAAAAEASLNKSKSA
HHHHHHHHHCCCCCC		24.7928833060
666PhosphorylationAEASLNKSKSATTTP
HHHHHCCCCCCCCCC		30.6722324799
668PhosphorylationASLNKSKSATTTPSG
HHHCCCCCCCCCCCC		37.6325521595
670PhosphorylationLNKSKSATTTPSGSP
HCCCCCCCCCCCCCC		37.9927742792
671PhosphorylationNKSKSATTTPSGSPR
CCCCCCCCCCCCCCC		36.1027087446
672PhosphorylationKSKSATTTPSGSPRT
CCCCCCCCCCCCCCC		15.8825521595
674PhosphorylationKSATTTPSGSPRTSQ
CCCCCCCCCCCCCCC		50.2227087446
676PhosphorylationATTTPSGSPRTSQQN
CCCCCCCCCCCCCCC		18.6225521595
679PhosphorylationTPSGSPRTSQQNVSN
CCCCCCCCCCCCCCC		33.9825521595
680PhosphorylationPSGSPRTSQQNVSNA
CCCCCCCCCCCCCCC		30.9225521595
685PhosphorylationRTSQQNVSNASEGST
CCCCCCCCCCCCCCC		33.9423737553
688PhosphorylationQQNVSNASEGSTWNP
CCCCCCCCCCCCCCC		46.9023737553
691PhosphorylationVSNASEGSTWNPFDD
CCCCCCCCCCCCCCC		26.6323737553
692PhosphorylationSNASEGSTWNPFDDD
CCCCCCCCCCCCCCC		39.8723737553
729PhosphorylationLPEKLGGSAESLIPG
CCHHHCCCHHHHCCC		27.3727087446
732PhosphorylationKLGGSAESLIPGFQP
HHCCCHHHHCCCCCC		31.1722324799
740PhosphorylationLIPGFQPTQGDAFTT
HCCCCCCCCCCCCCC		34.1125159016
746PhosphorylationPTQGDAFTTPSFSAG
CCCCCCCCCCCCCCC		39.2525159016
747PhosphorylationTQGDAFTTPSFSAGT
CCCCCCCCCCCCCCC		15.5225195567
749PhosphorylationGDAFTTPSFSAGTAE
CCCCCCCCCCCCCCC		29.7325168779
751PhosphorylationAFTTPSFSAGTAEKR
CCCCCCCCCCCCCCC		30.0825168779
754PhosphorylationTPSFSAGTAEKRKGG
CCCCCCCCCCCCCCC		31.2129899451
774PhosphorylationGIPLLSVSDPFIPLQ
CCCEEEECCCCCCCC		35.8729899451
795PhosphorylationKLIEGLKSPDTSLLL
HHHHCCCCCCHHCCC		32.8122817900
798PhosphorylationEGLKSPDTSLLLPDL
HCCCCCCHHCCCCCC		25.3429899451
799PhosphorylationGLKSPDTSLLLPDLL
CCCCCCHHCCCCCCC		25.1320415495
816PhosphorylationTDPFGSTSDAVIDKA
CCCCCCCCHHHHCHH		25.8520415495
844PhosphorylationPVAQRLPSQTESVTS
CHHHCCCCCCCCCCC		55.0925521595
846PhosphorylationAQRLPSQTESVTSNR
HHCCCCCCCCCCCCC		34.2728833060
848PhosphorylationRLPSQTESVTSNRTD
CCCCCCCCCCCCCCC		33.8028833060
854PhosphorylationESVTSNRTDSLTGED
CCCCCCCCCCCCCCC		33.9051457099
856PhosphorylationVTSNRTDSLTGEDSL
CCCCCCCCCCCCCCH		27.5020415495
858PhosphorylationSNRTDSLTGEDSLLD
CCCCCCCCCCCCHHH		42.3420415495
862PhosphorylationDSLTGEDSLLDCSLL
CCCCCCCCHHHHHHH		26.9129899451
867PhosphorylationEDSLLDCSLLSNPTA
CCCHHHHHHHCCCCC		31.8220415495
932PhosphorylationKNTQGGHSRNSSGSS
CCCCCCCCCCCCCCC		36.1122871156
935PhosphorylationQGGHSRNSSGSSESS
CCCCCCCCCCCCCCC		34.6625521595
936PhosphorylationGGHSRNSSGSSESSL
CCCCCCCCCCCCCCH		46.3625521595
938PhosphorylationHSRNSSGSSESSLPN
CCCCCCCCCCCCHHH		32.6422324799
939PhosphorylationSRNSSGSSESSLPNL
CCCCCCCCCCCHHHH		45.0522324799
941PhosphorylationNSSGSSESSLPNLAR
CCCCCCCCCHHHHHH		38.8422324799
942PhosphorylationSSGSSESSLPNLARS
CCCCCCCCHHHHHHH		43.7422324799
949PhosphorylationSLPNLARSLLLVDQL
CHHHHHHHHHHHHHH		20.1229899451
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
635SPhosphorylationKinaseSTK38Q91VJ4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAK1_MOUSE !!
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 AAK1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AAK1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AAK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-604; THR-618; SER-622AND SER-635, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; THR-638 ANDSER-650, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-604; THR-618;SER-621; SER-635; SER-650; SER-729; SER-935 AND SER-936, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND MASSSPECTROMETRY.

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