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Q2M2I8 (AAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP2-associated protein kinase 1

EC=2.7.11.1
Alternative name(s):
Adaptor-associated kinase 1
Gene names
Name:AAK1
Synonyms:KIAA1048
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length961 AA.
Sequence statusComplete.
Protein existenceEvidence 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.12 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.12 Ref.18

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Membraneclathrin-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 inbrain. Ref.1

Post-translational modification

Autophosphorylated By similarity.

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 processEndocytosis
   Cellular componentCell membrane
Coated pit
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

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 phosphorylation

Inferred from direct assay Ref.1Ref.12. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of clathrin-mediated endocytosis

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of protein localization

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentcell 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 component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

terminal bouton

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionAP-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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATP13A2Q9NQ112EBI-1383433,EBI-6308763

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 961961AP2-associated protein kinase 1
PRO_0000250578

Regions

Domain46 – 315270Protein kinase
Nucleotide binding52 – 609ATP By similarity
Compositional bias12 – 4231Gly-rich
Compositional bias397 – 614218Gln-rich
Compositional bias658 – 6636Poly-Ala

Sites

Active site1761Proton acceptor By similarity
Binding site741ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.20
Modified residue141Phosphoserine Ref.14
Modified residue2341Phosphotyrosine Ref.11
Modified residue2351Phosphoserine Ref.11
Modified residue3541Phosphothreonine Ref.14
Modified residue3891Phosphothreonine Ref.7 Ref.8 Ref.10 Ref.11 Ref.14 Ref.15
Modified residue4411Phosphothreonine Ref.10
Modified residue6061Phosphothreonine Ref.7 Ref.11 Ref.15 Ref.19
Modified residue6201Phosphothreonine Ref.11 Ref.16 Ref.19
Modified residue6231Phosphoserine Ref.11 Ref.16
Modified residue6241Phosphoserine Ref.11 Ref.16 Ref.19
Modified residue6371Phosphoserine Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.19
Modified residue6501Phosphoserine Ref.14
Modified residue6531Phosphothreonine Ref.15
Modified residue6871Phosphotyrosine Ref.14
Modified residue7311Phosphoserine Ref.10 Ref.14

Natural variations

Alternative sequence823 – 961139EKADV…QLIDL → GKVIISVSSVMHDMCACFKN DKYLVNQSLGNSPATPEAKA I in isoform 2.
VSP_039459
Natural variant591I → V. Ref.21
Corresponds to variant rs34535244 [ dbSNP | Ensembl ].
VAR_040348
Natural variant5091K → Q. Ref.2 Ref.4
Corresponds to variant rs6715776 [ dbSNP | Ensembl ].
VAR_031129
Natural variant5331Q → H. Ref.21
VAR_040349
Natural variant6031V → A. Ref.21
Corresponds to variant rs56038532 [ dbSNP | Ensembl ].
VAR_040350
Natural variant6941T → M. Ref.21
Corresponds to variant rs55889248 [ dbSNP | Ensembl ].
VAR_040351
Natural variant7251P → T. Ref.21
Corresponds to variant rs35285785 [ dbSNP | Ensembl ].
VAR_040352
Natural variant7711P → R. Ref.21
Corresponds to variant rs34422616 [ dbSNP | Ensembl ].
VAR_040353
Natural variant8351G → D. Ref.21
VAR_040354

Experimental info

Mutagenesis741K → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Does not interact with monoubiquitinated NOTCH1. Ref.5 Ref.12 Ref.18
Mutagenesis1761D → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Ref.5 Ref.12
Mutagenesis777 – 7793DPF → AAA: Does not affect interaction with NOTCH1 but abolishes interaction with ESP15. Ref.18

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AAK1L) [UniParc].

Last modified July 13, 2010. Version 3.
Checksum: 1FB44D0FDEF6CAD0

FASTA961103,885
        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 

« Hide

Isoform 2 (AAK1S) [UniParc].

Checksum: 012198AEE90CC0E7
Show »

FASTA86393,578

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-74 AND ASP-176.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND THR-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-441; SER-637 AND SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234; SER-235; THR-389; THR-606; THR-620; SER-623; SER-624 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"AAK1 regulates Numb function at an early step in clathrin-mediated endocytosis."
Sorensen E.B., Conner S.D.
Traffic 9:1791-1800(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NUMB, MUTAGENESIS OF LYS-74 AND ASP-176.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-354; THR-389; SER-637; SER-650; TYR-687 AND SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-606; SER-637 AND THR-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620; SER-623; SER-624 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPS15 AND NOTCH1, MUTAGENESIS OF LYS-74 AND 777-ASP--PHE-779.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; THR-620; SER-624 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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. expand/collapse author list , 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] [Europe PMC] [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.
RefSeqNP_055726.3. NM_014911.3.
UniGeneHs.468878.

3D structure databases

ProteinModelPortalQ2M2I8.
SMRQ2M2I8. Positions 32-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116520. 3 interactions.
IntActQ2M2I8. 3 interactions.
STRING9606.ENSP00000386456.

Chemistry

BindingDBQ2M2I8.
ChEMBLCHEMBL3830.
GuidetoPHARMACOLOGY1921.

PTM databases

PhosphoSiteQ2M2I8.

Polymorphism databases

DMDM300669613.

Proteomic databases

PaxDbQ2M2I8.
PRIDEQ2M2I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000406297; ENSP00000385181; ENSG00000115977. [Q2M2I8-2]
ENST00000409085; ENSP00000386456; ENSG00000115977. [Q2M2I8-1]
GeneID22848.
KEGGhsa:22848.
UCSCuc002sfp.2. human. [Q2M2I8-1]
uc010fdk.2. human. [Q2M2I8-2]

Organism-specific databases

CTD22848.
GeneCardsGC02M069685.
H-InvDBHIX0161871.
HGNCHGNC:19679. AAK1.
HPAHPA017931.
HPA020289.
neXtProtNX_Q2M2I8.
PharmGKBPA134990616.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000232173.
HOVERGENHBG080803.
KOK08853.
OMAQLIQNFY.
PhylomeDBQ2M2I8.
TreeFamTF317300.

Enzyme and pathway databases

SignaLinkQ2M2I8.

Gene expression databases

ArrayExpressQ2M2I8.
BgeeQ2M2I8.
CleanExHS_AAK1.
GenevestigatorQ2M2I8.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAAK1. human.
GeneWikiAAK1.
GenomeRNAi22848.
NextBio43313.
PROQ2M2I8.

Entry information

Entry nameAAK1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM