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Reviewed, UniProtKB/Swiss-Prot Q2M2I8 (AAK1_HUMAN)

Last modified July 7, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Phosphorylates the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2). May play a role in regulating aspects of clathrin-mediated endocytosis By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Stimulated by clathrin By similarity.

Subunit structure

Interacts with alpha-adaptin and AP-2 By similarity.

Subcellular location

Membrane; Peripheral membrane protein By similarity. 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 By similarity.

Post-translational modification

Autophosphorylated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

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Ontologies

Keywords
   Cellular componentCell membrane
Coated pit
Membrane
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid phosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcoated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 863863AP2-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 residue181Phosphoserine Ref.8
Modified residue211Phosphoserine By similarity
Modified residue2211Phosphothreonine Ref.9
Modified residue2221Phosphothreonine Ref.9
Modified residue2341Phosphotyrosine Ref.9
Modified residue2351Phosphoserine Ref.9
Modified residue3271Phosphoserine Ref.8
Modified residue3541Phosphothreonine By similarity
Modified residue3891Phosphothreonine Ref.8 Ref.9 Ref.6 Ref.7
Modified residue4411Phosphothreonine Ref.8
Modified residue6061Phosphothreonine Ref.8 Ref.9 Ref.6 Ref.4
Modified residue6181Phosphoserine Ref.9
Modified residue6201Phosphothreonine Ref.9 Ref.5
Modified residue6231Phosphoserine Ref.9
Modified residue6241Phosphoserine Ref.9
Modified residue6371Phosphoserine Ref.8 Ref.9
Modified residue6401Phosphothreonine By similarity
Modified residue6521Phosphoserine By similarity
Modified residue6701Phosphoserine Ref.8 Ref.4
Modified residue6761Phosphoserine Ref.8 Ref.4
Modified residue7311Phosphoserine Ref.8

Natural variations

Natural variant591I → V: dbSNP rs34535244.
VAR_040348
Natural variant5091K → Q: dbSNP rs6715776. Ref.1 Ref.3
VAR_031129
Natural variant5331Q → H Ref.11
VAR_040349
Natural variant6031V → A Ref.11
VAR_040350
Natural variant6941T → M Ref.11
VAR_040351
Natural variant7251P → T Ref.11
VAR_040352
Natural variant7711P → R: dbSNP rs34422616.
VAR_040353
Natural variant8351D → G Ref.11
VAR_040354

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Sequences

Sequence LengthMass (Da)Tools
Q2M2I8-1 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 012198AEE90CC0E7

FASTA86393,578
        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

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References

[1]"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], VARIANT GLN-509.
Tissue: Brain.
[2]"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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT GLN-509.
Tissue: Cerebellum.
[4]"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: Epithelium.
[5]"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.
[6]"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: Epithelium.
[7]"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.
[8]"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.
[9]"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.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-59; HIS-533; ALA-603; MET-694; THR-725; ARG-771 AND GLY-835.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB028971 mRNA. Translation: BAA83000.2. Different initiation.
AC092431 Genomic DNA. Translation: AAX88861.1.
AC079121 Genomic DNA. Translation: AAY14931.1.
BC104842 mRNA. Translation: AAI04843.1.
BC111965 mRNA. Translation: AAI11966.1.
IPIIPI00479760.
RefSeqNP_055726.3.
UniGeneHs.468878

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ2M2I8.

Proteomic databases

PRIDEQ2M2I8.

Genome annotation databases

EnsemblENSG00000115977. Homo sapiens. [Contig view]
GeneID22848.
KEGGhsa:22848.
UCSCuc002sfp.2. human.

Organism-specific databases

GeneCardsGC02M069561.
HGNCHGNC:19679. AAK1.
HPAHPA017931.
PharmGKBPA134990616.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ2M2I8.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.

Gene expression databases

ArrayExpressQ2M2I8.
BgeeQ2M2I8.
CleanExHS_AAK1.
GermOnlineENSG00000115977. Homo sapiens.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43313.

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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: March 20, 2007
Last modified: July 7, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents