AAK1_HUMAN - dbPTM
AAK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAK1_HUMAN
UniProt AC Q2M2I8
Protein Name AP2-associated protein kinase 1
Gene Name AAK1
Organism Homo sapiens (Human).
Sequence Length 961
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..
Protein Sequence MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
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		10.8522814378
7Phosphorylation-MKKFFDSRREQGGS
-CCCCCCCCHHCCCC		28.2528857561
14PhosphorylationSRREQGGSGLGSGSS
CCHHCCCCCCCCCCC		37.3523401153
18PhosphorylationQGGSGLGSGSSGGGG
CCCCCCCCCCCCCCC		40.3123401153
20PhosphorylationGSGLGSGSSGGGGST
CCCCCCCCCCCCCCC		27.7523401153
21PhosphorylationSGLGSGSSGGGGSTS
CCCCCCCCCCCCCCC		45.0123927012
26PhosphorylationGSSGGGGSTSGLGSG
CCCCCCCCCCCCCCC		23.7530266825
27PhosphorylationSSGGGGSTSGLGSGY
CCCCCCCCCCCCCCC		30.0423927012
28PhosphorylationSGGGGSTSGLGSGYI
CCCCCCCCCCCCCCC		33.4523927012
32PhosphorylationGSTSGLGSGYIGRVF
CCCCCCCCCCCCCCC		33.2023927012
34PhosphorylationTSGLGSGYIGRVFGI
CCCCCCCCCCCCCCC		11.2523927012
88UbiquitinationEHDLQVCKREIQIMR
HHHHHHHHHHHHHHH		54.9629967540
88AcetylationEHDLQVCKREIQIMR
HHHHHHHHHHHHHHH		54.9625953088
169UbiquitinationVARLHQCKTPIIHRD
HHHHHCCCCCEECCC		51.2529967540
178UbiquitinationPIIHRDLKVENILLH
CEECCCCCEEEEEEC		52.36-
201UbiquitinationDFGSATNKFQNPQTE
CCCCCCCCCCCCCCC		43.9329967540
219UbiquitinationAVEDEIKKYTTLSYR
CHHHHHHHHCCCCCC		54.1929967540
221PhosphorylationEDEIKKYTTLSYRAP
HHHHHHHCCCCCCCC		30.0918669648
222PhosphorylationDEIKKYTTLSYRAPE
HHHHHHCCCCCCCCH		15.6018669648
230SulfoxidationLSYRAPEMVNLYSGK
CCCCCCHHHCCCCCC		2.0530846556
234PhosphorylationAPEMVNLYSGKIITT
CCHHHCCCCCCEECC		15.3518669648
235PhosphorylationPEMVNLYSGKIITTK
CHHHCCCCCCEECCH		36.4518669648
253PhosphorylationWALGCLLYKLCYFTL
HHHHHHHHHHHHHHC		6.7520068231
292PhosphorylationDMHCLIRYMLEPDPD
CHHHHHHHHCCCCCC		10.0819664994
311PhosphorylationIYQVSYFSFKLLKKE
CEEEEEEEHHHHCCC		17.1524719451
317TrimethylationFSFKLLKKECPIPNV
EEHHHHCCCCCCCCC		65.60-
317MethylationFSFKLLKKECPIPNV
EEHHHHCCCCCCCCC		65.60-
327PhosphorylationPIPNVQNSPIPAKLP
CCCCCCCCCCCCCCC		13.7117192257
347PhosphorylationSEAAAKKTQPKARLT
HHHHHHHHCCCCCCC		49.777899663
354PhosphorylationTQPKARLTDPIPTTE
HCCCCCCCCCCCCCC		33.8919060867
354O-linked_GlycosylationTQPKARLTDPIPTTE
HCCCCCCCCCCCCCC		33.8922564745
359PhosphorylationRLTDPIPTTETSIAP
CCCCCCCCCCCCCCC		37.6725477569
359O-linked_GlycosylationRLTDPIPTTETSIAP
CCCCCCCCCCCCCCC		37.6722564745
360O-linked_GlycosylationLTDPIPTTETSIAPR
CCCCCCCCCCCCCCC		31.7322564745
360PhosphorylationLTDPIPTTETSIAPR
CCCCCCCCCCCCCCC		31.7320071362
362PhosphorylationDPIPTTETSIAPRQR
CCCCCCCCCCCCCCC		24.2820071362
363PhosphorylationPIPTTETSIAPRQRP
CCCCCCCCCCCCCCC		15.5524719451
375PhosphorylationQRPKAGQTQPNPGIL
CCCCCCCCCCCCCCC		45.1129255136
389PhosphorylationLPIQPALTPRKRATV
CCCCCCCCCCCCCCC		24.1329255136
391MethylationIQPALTPRKRATVQP
CCCCCCCCCCCCCCC		35.54-
441PhosphorylationKQPQAPPTPQQTPST
CCCCCCCCCCCCCCH		32.4417192257
441O-linked_GlycosylationKQPQAPPTPQQTPST
CCCCCCCCCCCCCCH		32.4422564745
445PhosphorylationAPPTPQQTPSTQAQG
CCCCCCCCCCHHHCC		17.6027251275
447O-linked_GlycosylationPTPQQTPSTQAQGLP
CCCCCCCCHHHCCCC		36.2222564745
447PhosphorylationPTPQQTPSTQAQGLP
CCCCCCCCHHHCCCC		36.2227251275
448PhosphorylationTPQQTPSTQAQGLPA
CCCCCCCHHHCCCCC		29.1827251275
448O-linked_GlycosylationTPQQTPSTQAQGLPA
CCCCCCCHHHCCCCC		29.1822564745
460PhosphorylationLPAQAQATPQHQQQL
CCCHHCCCHHHHHHH		16.0528555341
507O-linked_GlycosylationFQAVHPATQKPAIAQ
HHHCCCCCCCCCCCC		41.3922564745
519O-linked_GlycosylationIAQFPVVSQGGSQQQ
CCCCCEECCCCCHHH		24.2822564745
605PhosphorylationRQQPKVQTTPPPAVQ
CCCCCCCCCCCCCCC		44.2330266825
606PhosphorylationQQPKVQTTPPPAVQG
CCCCCCCCCCCCCCC		19.3919664994
618PhosphorylationVQGQKVGSLTPPSSP
CCCCCCCCCCCCCCC		31.8629255136
620PhosphorylationGQKVGSLTPPSSPKT
CCCCCCCCCCCCCCC		34.5529255136
623PhosphorylationVGSLTPPSSPKTQRA
CCCCCCCCCCCCCCC		61.5529255136
624PhosphorylationGSLTPPSSPKTQRAG
CCCCCCCCCCCCCCC		35.8729255136
627PhosphorylationTPPSSPKTQRAGHRR
CCCCCCCCCCCCCCH		27.0323927012
637PhosphorylationAGHRRILSDVTHSAV
CCCCHHHHCCCHHHH		27.8829255136
640PhosphorylationRRILSDVTHSAVFGV
CHHHHCCCHHHHHCC		18.3322167270
642PhosphorylationILSDVTHSAVFGVPA
HHHCCCHHHHHCCCC		19.4330266825
650PhosphorylationAVFGVPASKSTQLLQ
HHHCCCCCHHHHHHH		22.5226846344
652PhosphorylationFGVPASKSTQLLQAA
HCCCCCHHHHHHHHH		20.91180503
653PhosphorylationGVPASKSTQLLQAAA
CCCCCHHHHHHHHHH		27.2930266825
664PhosphorylationQAAAAEASLNKSKSA
HHHHHHHHHCCCCCC		24.7923403867
668PhosphorylationAEASLNKSKSATTTP
HHHHHCCCCCCCCCC		30.6728176443
670PhosphorylationASLNKSKSATTTPSG
HHHCCCCCCCCCCCC		37.6329255136
672PhosphorylationLNKSKSATTTPSGSP
HCCCCCCCCCCCCCC		37.9929255136
673PhosphorylationNKSKSATTTPSGSPR
CCCCCCCCCCCCCCC		36.1029255136
674PhosphorylationKSKSATTTPSGSPRT
CCCCCCCCCCCCCCC		15.8829255136
676PhosphorylationKSATTTPSGSPRTSQ
CCCCCCCCCCCCCCC		50.2226846344
678PhosphorylationATTTPSGSPRTSQQN
CCCCCCCCCCCCCCC		18.6226846344
681PhosphorylationTPSGSPRTSQQNVYN
CCCCCCCCCCCCEEC		33.9821082442
682PhosphorylationPSGSPRTSQQNVYNP
CCCCCCCCCCCEECC		30.9221082442
687PhosphorylationRTSQQNVYNPSEGST
CCCCCCEECCCCCCC		28.9821082442
690PhosphorylationQQNVYNPSEGSTWNP
CCCEECCCCCCCCCC		51.4521082442
693PhosphorylationVYNPSEGSTWNPFDD
EECCCCCCCCCCCCC		26.6329978859
694PhosphorylationYNPSEGSTWNPFDDD
ECCCCCCCCCCCCCC		39.8723090842
704PhosphorylationPFDDDNFSKLTAEEL
CCCCCCHHHCCHHHH		32.7723090842
705AcetylationFDDDNFSKLTAEELL
CCCCCHHHCCHHHHH		45.8030586633
731PhosphorylationHPEKLGGSAESLIPG
CHHHHCCCHHHHCCC		27.3720058876
734PhosphorylationKLGGSAESLIPGFQS
HHCCCHHHHCCCCCC		31.1722199227
741PhosphorylationSLIPGFQSTQGDAFA
HHCCCCCCCCCCCEE		22.0422199227
742PhosphorylationLIPGFQSTQGDAFAT
HCCCCCCCCCCCEEE		26.2826074081
749PhosphorylationTQGDAFATTSFSAGT
CCCCCEEECCCCCCC		19.2727251275
750PhosphorylationQGDAFATTSFSAGTA
CCCCEEECCCCCCCC		25.0927251275
797PhosphorylationKLIEGLKSPDTSLLL
HHHHCCCCCCHHCCC		32.8131437539
800PhosphorylationEGLKSPDTSLLLPDL
HCCCCCCHHCCCCCC		25.3429523821
801PhosphorylationGLKSPDTSLLLPDLL
CCCCCCHHCCCCCCC		25.1329523821
811PhosphorylationLPDLLPMTDPFGSTS
CCCCCCCCCCCCCCC		38.2820071362
846PhosphorylationPVPQRLPSQTESVTS
CCCCCCCCCCCCCCC		55.0929255136
848PhosphorylationPQRLPSQTESVTSNR
CCCCCCCCCCCCCCC		34.2729255136
850PhosphorylationRLPSQTESVTSNRTD
CCCCCCCCCCCCCCC		33.8028450419
852PhosphorylationPSQTESVTSNRTDSL
CCCCCCCCCCCCCCC		29.5746156163
853PhosphorylationSQTESVTSNRTDSLT
CCCCCCCCCCCCCCC		23.3526699800
926PhosphorylationDPIPVLITKNPQGGH
CCCCEEEECCCCCCC		22.1726657352
937PhosphorylationQGGHSRNSSGSSESS
CCCCCCCCCCCCCCC		34.6627732954
938PhosphorylationGGHSRNSSGSSESSL
CCCCCCCCCCCCCCH		46.3627732954
940PhosphorylationHSRNSSGSSESSLPN
CCCCCCCCCCCCHHH		32.6427732954
941PhosphorylationSRNSSGSSESSLPNL
CCCCCCCCCCCHHHH		45.0527732954
943PhosphorylationNSSGSSESSLPNLAR
CCCCCCCCCHHHHHH		38.8427732954
944PhosphorylationSSGSSESSLPNLARS
CCCCCCCCHHHHHHH		43.7427732954
951PhosphorylationSLPNLARSLLLVDQL
CHHHHHHHHHHHHHH		20.1255817227
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
389TPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAK1_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 AAK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AP2A1_HUMANAP2A1physical
25852190
AP2B1_HUMANAP2B1physical
25852190
AP2M1_HUMANAP2M1physical
25852190
PLEC_HUMANPLECphysical
27173435
VIP2_HUMANPPIP5K2physical
27173435
SC24B_HUMANSEC24Bphysical
27173435
UB2D2_HUMANUBE2D2physical
27173435
LUZP1_HUMANLUZP1physical
27173435
URGCP_HUMANURGCPphysical
27173435
DVL3_HUMANDVL3physical
27173435
QSER1_HUMANQSER1physical
27173435
WNK1_HUMANWNK1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AAK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-606; SER-637AND THR-653, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-18; SER-20;SER-21; THR-354; THR-389; THR-441; THR-448; THR-606; SER-618; THR-620;SER-623; SER-624; SER-637; THR-640; SER-642; SER-650; SER-652;SER-668; SER-670; THR-672; THR-674; SER-676; SER-678; THR-681;SER-682; TYR-687; SER-690 AND SER-731, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; THR-620; SER-623AND SER-624, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221; THR-222; TYR-234;SER-235; THR-389; THR-606; SER-618; THR-620; SER-623; SER-624 ANDSER-637, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-327; THR-389;THR-441; THR-606; SER-637; SER-670; SER-676 AND SER-731, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; SER-670 ANDSER-676, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND THR-606, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620, AND MASSSPECTROMETRY.

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