Q2M2I8 (AAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AP2-associated protein kinase 1
EC=2.7.11.1

Alternative name(s):
Adaptor-associated kinase 1

Gene names

Name:	AAK1
Synonyms:	KIAA1048

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	961 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.5 Ref.13 Ref.18
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Stimulated by clathrin By similarity.
Subunit structure	Interacts with alpha-adaptin, AP-2, clathrin, NUMB and EPS15 isoform 2. Interacts with membrane-bound activated NOTCH1 but not with the inactive full-length form of NOTCH1. Preferentially interacts with monoubiquitinated activated NOTCH1 compared to the non-ubiquitinated form. Ref.1 Ref.13 Ref.18
Subcellular location	Cell membrane; Peripheral membrane protein By similarity. Membrane › clathrin-coated pit By similarity. Note: 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 migrating cells By similarity.
Tissue specificity	Detected in brain, heart and liver. Isoform 1 is the predominant isoform in brain. Ref.1
Post-translational modification	Autophosphorylated By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Sequence caution	The sequence BAA83000.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Coated pit Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of Notch signaling pathway Inferred from direct assay Ref.18. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein stabilization Inferred from direct assay Ref.18. Source: UniProtKB regulation of clathrin-mediated endocytosis Inferred from direct assay Ref.13. Source: UniProtKB regulation of protein localization Inferred from direct assay Ref.13. Source: UniProtKB
Cellular component	cell leading edge Inferred from sequence or structural similarity. Source: UniProtKB clathrin-coated vesicle Inferred from sequence or structural similarity. Source: UniProtKB coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB terminal button Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	AP-2 adaptor complex binding Inferred from direct assay Ref.1. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW Notch binding Inferred from direct assay Ref.18. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q2M2I8-1)

Also known as: AAK1L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q2M2I8-2)

Also known as: AAK1S;

The sequence of this isoform differs from the canonical sequence as follows:
     823-961: EKADVAVESL...LLLVDQLIDL → GKVIISVSSV...SPATPEAKAI

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 961	961	AP2-associated protein kinase 1		PRO_0000250578
Regions
	Domain	46 – 315	270	Protein kinase
	Nucleotide binding	52 – 60	9	ATP By similarity
	Compositional bias	12 – 42	31	Gly-rich
	Compositional bias	397 – 614	218	Gln-rich
	Compositional bias	658 – 663	6	Poly-Ala
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	74	1	ATP By similarity
Amino acid modifications
	Modified residue	14	1	Phosphoserine Ref.15
	Modified residue	18	1	Phosphoserine Ref.11 Ref.15
	Modified residue	20	1	Phosphoserine Ref.15
	Modified residue	21	1	Phosphoserine Ref.15
	Modified residue	221	1	Phosphothreonine Ref.12
	Modified residue	222	1	Phosphothreonine Ref.12
	Modified residue	234	1	Phosphotyrosine Ref.12
	Modified residue	235	1	Phosphoserine Ref.12
	Modified residue	327	1	Phosphoserine Ref.11
	Modified residue	354	1	Phosphothreonine Ref.15
	Modified residue	389	1	Phosphothreonine Ref.8 Ref.9 Ref.11 Ref.12 Ref.15 Ref.16
	Modified residue	441	1	Phosphothreonine Ref.11 Ref.15
	Modified residue	448	1	Phosphothreonine Ref.15
	Modified residue	606	1	Phosphothreonine Ref.6 Ref.8 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16
	Modified residue	618	1	Phosphoserine Ref.12 Ref.15
	Modified residue	620	1	Phosphothreonine Ref.7 Ref.12 Ref.14 Ref.15
	Modified residue	623	1	Phosphoserine Ref.12 Ref.14 Ref.15
	Modified residue	624	1	Phosphoserine Ref.12 Ref.14 Ref.15
	Modified residue	637	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.15 Ref.16
	Modified residue	640	1	Phosphothreonine Ref.15
	Modified residue	642	1	Phosphoserine Ref.15
	Modified residue	650	1	Phosphoserine Ref.15
	Modified residue	652	1	Phosphoserine Ref.15
	Modified residue	653	1	Phosphothreonine Ref.16
	Modified residue	668	1	Phosphoserine Ref.15
	Modified residue	670	1	Phosphoserine Ref.6 Ref.11 Ref.15
	Modified residue	672	1	Phosphothreonine Ref.15
	Modified residue	674	1	Phosphothreonine Ref.15
	Modified residue	676	1	Phosphoserine Ref.6 Ref.11 Ref.15
	Modified residue	678	1	Phosphoserine Ref.15
	Modified residue	681	1	Phosphothreonine Ref.15
	Modified residue	682	1	Phosphoserine Ref.15
	Modified residue	687	1	Phosphotyrosine Ref.15
	Modified residue	690	1	Phosphoserine Ref.15
	Modified residue	731	1	Phosphoserine Ref.11 Ref.15
Natural variations
	Alternative sequence	823 – 961	139	EKADV…QLIDL → GKVIISVSSVMHDMCACFKN DKYLVNQSLGNSPATPEAKA I in isoform 2.		VSP_039459
	Natural variant	59	1	I → V. Ref.19 Corresponds to variant rs34535244 [ dbSNP | Ensembl ].		VAR_040348
	Natural variant	509	1	K → Q. Ref.2 Ref.4 Corresponds to variant rs6715776 [ dbSNP | Ensembl ].		VAR_031129
	Natural variant	533	1	Q → H. Ref.19		VAR_040349
	Natural variant	603	1	V → A. Ref.19 Corresponds to variant rs56038532 [ dbSNP | Ensembl ].		VAR_040350
	Natural variant	694	1	T → M. Ref.19 Corresponds to variant rs55889248 [ dbSNP | Ensembl ].		VAR_040351
	Natural variant	725	1	P → T. Ref.19 Corresponds to variant rs35285785 [ dbSNP | Ensembl ].		VAR_040352
	Natural variant	771	1	P → R. Ref.19 Corresponds to variant rs34422616 [ dbSNP | Ensembl ].		VAR_040353
	Natural variant	835	1	G → D. Ref.19		VAR_040354
Experimental info
	Mutagenesis	74	1	K → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Does not interact with monoubiquitinated NOTCH1. Ref.5 Ref.13 Ref.18
	Mutagenesis	176	1	D → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Ref.5 Ref.13
	Mutagenesis	777 – 779	3	DPF → AAA: Does not affect interaction with NOTCH1 but abolishes interaction with ESP15. Ref.18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AAK1L) [UniParc]. Last modified July 13, 2010. Version 3. Checksum: 1FB44D0FDEF6CAD0	FASTA	961	103,885
	10 20 30 40 50 60 MKKFFDSRRE QGGSGLGSGS SGGGGSTSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFAIV 70 80 90 100 110 120 FLVRTSNGMK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW 130 140 150 160 170 180 EVLILMDFCR GGQVVNLMNQ RLQTGFTENE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE 190 200 210 220 230 240 NILLHDRGHY VLCDFGSATN KFQNPQTEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT 250 260 270 280 290 300 TKADIWALGC LLYKLCYFTL PFGESQVAIC DGNFTIPDNS RYSQDMHCLI RYMLEPDPDK 310 320 330 340 350 360 RPDIYQVSYF SFKLLKKECP IPNVQNSPIP AKLPEPVKAS EAAAKKTQPK ARLTDPIPTT 370 380 390 400 410 420 ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPPP QAAGSSNQPG LLASVPQPKP 430 440 450 460 470 480 QAPPSQPLPQ TQAKQPQAPP TPQQTPSTQA QGLPAQAQAT PQHQQQLFLK QQQQQQQPPP 490 500 510 520 530 540 AQQQPAGTFY QQQQAQTQQF QAVHPATQKP AIAQFPVVSQ GGSQQQLMQN FYQQQQQQQQ 550 560 570 580 590 600 QQQQQQLATA LHQQQLMTQQ AALQQKPTMA AGQQPQPQPA AAPQPAPAQE PAIQAPVRQQ 610 620 630 640 650 660 PKVQTTPPPA VQGQKVGSLT PPSSPKTQRA GHRRILSDVT HSAVFGVPAS KSTQLLQAAA 670 680 690 700 710 720 AEASLNKSKS ATTTPSGSPR TSQQNVYNPS EGSTWNPFDD DNFSKLTAEE LLNKDFAKLG 730 740 750 760 770 780 EGKHPEKLGG SAESLIPGFQ STQGDAFATT SFSAGTAEKR KGGQTVDSGL PLLSVSDPFI 790 800 810 820 830 840 PLQVPDAPEK LIEGLKSPDT SLLLPDLLPM TDPFGSTSDA VIEKADVAVE SLIPGLEPPV 850 860 870 880 890 900 PQRLPSQTES VTSNRTDSLT GEDSLLDCSL LSNPTTDLLE EFAPTAISAP VHKAAEDSNL 910 920 930 940 950 960 ISGFDVPEGS DKVAEDEFDP IPVLITKNPQ GGHSRNSSGS SESSLPNLAR SLLLVDQLID L
	Isoform 2 (AAK1S) [UniParc]. Checksum: 012198AEE90CC0E7	FASTA	863	93,578
	10 20 30 40 50 60 MKKFFDSRRE QGGSGLGSGS SGGGGSTSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFAIV 70 80 90 100 110 120 FLVRTSNGMK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW 130 140 150 160 170 180 EVLILMDFCR GGQVVNLMNQ RLQTGFTENE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE 190 200 210 220 230 240 NILLHDRGHY VLCDFGSATN KFQNPQTEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT 250 260 270 280 290 300 TKADIWALGC LLYKLCYFTL PFGESQVAIC DGNFTIPDNS RYSQDMHCLI RYMLEPDPDK 310 320 330 340 350 360 RPDIYQVSYF SFKLLKKECP IPNVQNSPIP AKLPEPVKAS EAAAKKTQPK ARLTDPIPTT 370 380 390 400 410 420 ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPPP QAAGSSNQPG LLASVPQPKP 430 440 450 460 470 480 QAPPSQPLPQ TQAKQPQAPP TPQQTPSTQA QGLPAQAQAT PQHQQQLFLK QQQQQQQPPP 490 500 510 520 530 540 AQQQPAGTFY QQQQAQTQQF QAVHPATQKP AIAQFPVVSQ GGSQQQLMQN FYQQQQQQQQ 550 560 570 580 590 600 QQQQQQLATA LHQQQLMTQQ AALQQKPTMA AGQQPQPQPA AAPQPAPAQE PAIQAPVRQQ 610 620 630 640 650 660 PKVQTTPPPA VQGQKVGSLT PPSSPKTQRA GHRRILSDVT HSAVFGVPAS KSTQLLQAAA 670 680 690 700 710 720 AEASLNKSKS ATTTPSGSPR TSQQNVYNPS EGSTWNPFDD DNFSKLTAEE LLNKDFAKLG 730 740 750 760 770 780 EGKHPEKLGG SAESLIPGFQ STQGDAFATT SFSAGTAEKR KGGQTVDSGL PLLSVSDPFI 790 800 810 820 830 840 PLQVPDAPEK LIEGLKSPDT SLLLPDLLPM TDPFGSTSDA VIGKVIISVS SVMHDMCACF 850 860 KNDKYLVNQS LGNSPATPEA KAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel AAK1 splice variant functions at multiple steps of the endocytic pathway." Henderson D.M., Conner S.D. Mol. Biol. Cell 18:2698-2706(2007) [PubMed: 17494869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CLATHRIN, TISSUE SPECIFICITY. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-509. Tissue: Brain.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-509. Tissue: Cerebellum.
[5]	"Differential requirements for AP-2 in clathrin-mediated endocytosis." Conner S.D., Schmid S.L. J. Cell Biol. 162:773-779(2003) [PubMed: 12952931] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-74 AND ASP-176.
[6]	"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) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; SER-670 AND SER-676, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND THR-606, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, MASS SPECTROMETRY. Tissue: T-cell.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed: 18691976] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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) [PubMed: 18669648] [Abstract] 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 AND SER-637, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"AAK1 regulates Numb function at an early step in clathrin-mediated endocytosis." Sorensen E.B., Conner S.D. Traffic 9:1791-1800(2008) [PubMed: 18657069] [Abstract] Cited for: FUNCTION, INTERACTION WITH NUMB, MUTAGENESIS OF LYS-74 AND ASP-176.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; THR-620; SER-623 AND SER-624, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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) [PubMed: 19369195] [Abstract] 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, MASS SPECTROMETRY.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-606; SER-637 AND THR-653, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"The adaptor-associated kinase 1, AAK1, is a positive regulator of the Notch pathway." Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J., Olivo-Marin J.C., Israel A. J. Biol. Chem. 286:18720-18730(2011) [PubMed: 21464124] [Abstract] Cited for: FUNCTION, INTERACTION WITH EPS15 AND NOTCH1, MUTAGENESIS OF LYS-74 AND 777-ASP--PHE-779.
[19]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-59; HIS-533; ALA-603; MET-694; THR-725; ARG-771 AND ASP-835.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB028971 mRNA. Translation: BAA83000.2. Different initiation. AC092431 Genomic DNA. Translation: AAX88861.1. AC079121 Genomic DNA. Translation: AAY14931.1. AC136007 Genomic DNA. No translation available. BC104842 mRNA. Translation: AAI04843.1. BC111965 mRNA. Translation: AAI11966.1.
IPI	IPI00479760. IPI00916402.
RefSeq	NP_055726.3. NM_014911.3.
UniGene	Hs.468878.
3D structure databases
ProteinModelPortal	Q2M2I8.
SMR	Q2M2I8. Positions 34-315.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q2M2I8. 2 interactions.
STRING	Q2M2I8.
PTM databases
PhosphoSite	Q2M2I8.
Polymorphism databases
DMDM	300669613.
Proteomic databases
PRIDE	Q2M2I8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000406297; ENSP00000385181; ENSG00000115977.
GeneID	22848.
KEGG	hsa:22848.
UCSC	uc002sfp.2. human.
Organism-specific databases
CTD	22848.
GeneCards	GC02M069685.
H-InvDB	HIX0002128.
HGNC	HGNC:19679. AAK1.
HPA	HPA017931. HPA020289.
neXtProt	NX_Q2M2I8.
PharmGKB	PA134990616.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07275.
HOVERGEN	HBG080803.
OMA	EGKHPEK.
PhylomeDB	Q2M2I8.
Gene expression databases
ArrayExpress	Q2M2I8.
Bgee	Q2M2I8.
CleanEx	HS_AAK1.
Genevestigator	Q2M2I8.
GermOnline	ENSG00000115977. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
KO	K08853.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	43313.

Entry information

Entry name

AAK1_HUMAN

Accession

Primary (citable) accession number: Q2M2I8
Secondary accession number(s): Q4ZFZ3, Q53RX6, Q9UPV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	July 13, 2010
Last modified:	January 25, 2012
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.