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Q2M2I8

- AAK1_HUMAN

UniProt

Q2M2I8 - AAK1_HUMAN

Protein

AP2-associated protein kinase 1

Gene

AAK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Stimulated by clathrin.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741ATPPROSITE-ProRule annotation
    Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi52 – 609ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. AP-2 adaptor complex binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. Notch binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. positive regulation of Notch signaling pathway Source: UniProtKB
    3. protein autophosphorylation Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB
    5. protein stabilization Source: UniProtKB
    6. regulation of clathrin-mediated endocytosis Source: UniProtKB
    7. regulation of protein localization Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ2M2I8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP2-associated protein kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    Adaptor-associated kinase 1
    Gene namesi
    Name:AAK1
    Synonyms:KIAA1048
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:19679. AAK1.

    Subcellular locationi

    Cell membrane By similarity; 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.By similarity

    GO - Cellular componenti

    1. cell leading edge Source: UniProtKB
    2. clathrin-coated vesicle Source: UniProtKB
    3. coated pit Source: UniProtKB-SubCell
    4. extrinsic component of plasma membrane Source: UniProtKB
    5. terminal bouton Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741K → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Does not interact with monoubiquitinated NOTCH1. 3 Publications
    Mutagenesisi176 – 1761D → A: Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. 2 Publications
    Mutagenesisi777 – 7793DPF → AAA: Does not affect interaction with NOTCH1 but abolishes interaction with ESP15.

    Organism-specific databases

    PharmGKBiPA134990616.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 961961AP2-associated protein kinase 1PRO_0000250578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei234 – 2341Phosphotyrosine1 Publication
    Modified residuei235 – 2351Phosphoserine1 Publication
    Modified residuei354 – 3541Phosphothreonine1 Publication
    Modified residuei389 – 3891Phosphothreonine6 Publications
    Modified residuei441 – 4411Phosphothreonine1 Publication
    Modified residuei606 – 6061Phosphothreonine4 Publications
    Modified residuei620 – 6201Phosphothreonine3 Publications
    Modified residuei623 – 6231Phosphoserine2 Publications
    Modified residuei624 – 6241Phosphoserine3 Publications
    Modified residuei637 – 6371Phosphoserine7 Publications
    Modified residuei650 – 6501Phosphoserine1 Publication
    Modified residuei653 – 6531Phosphothreonine1 Publication
    Modified residuei687 – 6871Phosphotyrosine1 Publication
    Modified residuei731 – 7311Phosphoserine2 Publications

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ2M2I8.
    PaxDbiQ2M2I8.
    PRIDEiQ2M2I8.

    PTM databases

    PhosphoSiteiQ2M2I8.

    Expressioni

    Tissue specificityi

    Detected in brain, heart and liver. Isoform 1 is the predominant isoform in brain.1 Publication

    Gene expression databases

    ArrayExpressiQ2M2I8.
    BgeeiQ2M2I8.
    CleanExiHS_AAK1.
    GenevestigatoriQ2M2I8.

    Organism-specific databases

    HPAiHPA017931.
    HPA020289.

    Interactioni

    Subunit structurei

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATP13A2Q9NQ112EBI-1383433,EBI-6308763

    Protein-protein interaction databases

    BioGridi116520. 3 interactions.
    IntActiQ2M2I8. 3 interactions.
    STRINGi9606.ENSP00000386456.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2M2I8.
    SMRiQ2M2I8. Positions 32-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 315270Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 4231Gly-richAdd
    BLAST
    Compositional biasi397 – 614218Gln-richAdd
    BLAST
    Compositional biasi658 – 6636Poly-Ala

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000232173.
    HOVERGENiHBG080803.
    KOiK08853.
    OMAiQLIQNFY.
    PhylomeDBiQ2M2I8.
    TreeFamiTF317300.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q2M2I8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKKFFDSRRE QGGSGLGSGS SGGGGSTSGL GSGYIGRVFG IGRQQVTVDE    50
    VLAEGGFAIV FLVRTSNGMK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH 100
    KNIVGYIDSS INNVSSGDVW EVLILMDFCR GGQVVNLMNQ RLQTGFTENE 150
    VLQIFCDTCE AVARLHQCKT PIIHRDLKVE NILLHDRGHY VLCDFGSATN 200
    KFQNPQTEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT TKADIWALGC 250
    LLYKLCYFTL PFGESQVAIC DGNFTIPDNS RYSQDMHCLI RYMLEPDPDK 300
    RPDIYQVSYF SFKLLKKECP IPNVQNSPIP AKLPEPVKAS EAAAKKTQPK 350
    ARLTDPIPTT ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPPP 400
    QAAGSSNQPG LLASVPQPKP QAPPSQPLPQ TQAKQPQAPP TPQQTPSTQA 450
    QGLPAQAQAT PQHQQQLFLK QQQQQQQPPP AQQQPAGTFY QQQQAQTQQF 500
    QAVHPATQKP AIAQFPVVSQ GGSQQQLMQN FYQQQQQQQQ QQQQQQLATA 550
    LHQQQLMTQQ AALQQKPTMA AGQQPQPQPA AAPQPAPAQE PAIQAPVRQQ 600
    PKVQTTPPPA VQGQKVGSLT PPSSPKTQRA GHRRILSDVT HSAVFGVPAS 650
    KSTQLLQAAA AEASLNKSKS ATTTPSGSPR TSQQNVYNPS EGSTWNPFDD 700
    DNFSKLTAEE LLNKDFAKLG EGKHPEKLGG SAESLIPGFQ STQGDAFATT 750
    SFSAGTAEKR KGGQTVDSGL PLLSVSDPFI PLQVPDAPEK LIEGLKSPDT 800
    SLLLPDLLPM TDPFGSTSDA VIEKADVAVE SLIPGLEPPV PQRLPSQTES 850
    VTSNRTDSLT GEDSLLDCSL LSNPTTDLLE EFAPTAISAP VHKAAEDSNL 900
    ISGFDVPEGS DKVAEDEFDP IPVLITKNPQ GGHSRNSSGS SESSLPNLAR 950
    SLLLVDQLID L 961
    Length:961
    Mass (Da):103,885
    Last modified:July 13, 2010 - v3
    Checksum:i1FB44D0FDEF6CAD0
    GO
    Isoform 2 (identifier: Q2M2I8-2) [UniParc]FASTAAdd to Basket

    Also known as: AAK1S

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

    Show »
    Length:863
    Mass (Da):93,578
    Checksum:i012198AEE90CC0E7
    GO

    Sequence cautioni

    The sequence BAA83000.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591I → V.1 Publication
    Corresponds to variant rs34535244 [ dbSNP | Ensembl ].
    VAR_040348
    Natural varianti509 – 5091K → Q.2 Publications
    Corresponds to variant rs6715776 [ dbSNP | Ensembl ].
    VAR_031129
    Natural varianti533 – 5331Q → H.1 Publication
    VAR_040349
    Natural varianti603 – 6031V → A.1 Publication
    Corresponds to variant rs56038532 [ dbSNP | Ensembl ].
    VAR_040350
    Natural varianti694 – 6941T → M.1 Publication
    Corresponds to variant rs55889248 [ dbSNP | Ensembl ].
    VAR_040351
    Natural varianti725 – 7251P → T.1 Publication
    Corresponds to variant rs35285785 [ dbSNP | Ensembl ].
    VAR_040352
    Natural varianti771 – 7711P → R.1 Publication
    Corresponds to variant rs34422616 [ dbSNP | Ensembl ].
    VAR_040353
    Natural varianti835 – 8351G → D.1 Publication
    VAR_040354

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei823 – 961139EKADV…QLIDL → GKVIISVSSVMHDMCACFKN DKYLVNQSLGNSPATPEAKA I in isoform 2. 2 PublicationsVSP_039459Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1893.2. [Q2M2I8-1]
    RefSeqiNP_055726.3. NM_014911.3.
    UniGeneiHs.468878.

    Genome annotation databases

    EnsembliENST00000406297; ENSP00000385181; ENSG00000115977. [Q2M2I8-2]
    ENST00000409085; ENSP00000386456; ENSG00000115977. [Q2M2I8-1]
    GeneIDi22848.
    KEGGihsa:22848.
    UCSCiuc002sfp.2. human. [Q2M2I8-1]
    uc010fdk.2. human. [Q2M2I8-2]

    Polymorphism databases

    DMDMi300669613.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1893.2. [Q2M2I8-1 ]
    RefSeqi NP_055726.3. NM_014911.3.
    UniGenei Hs.468878.

    3D structure databases

    ProteinModelPortali Q2M2I8.
    SMRi Q2M2I8. Positions 32-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116520. 3 interactions.
    IntActi Q2M2I8. 3 interactions.
    STRINGi 9606.ENSP00000386456.

    Chemistry

    BindingDBi Q2M2I8.
    ChEMBLi CHEMBL3830.
    GuidetoPHARMACOLOGYi 1921.

    PTM databases

    PhosphoSitei Q2M2I8.

    Polymorphism databases

    DMDMi 300669613.

    Proteomic databases

    MaxQBi Q2M2I8.
    PaxDbi Q2M2I8.
    PRIDEi Q2M2I8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000406297 ; ENSP00000385181 ; ENSG00000115977 . [Q2M2I8-2 ]
    ENST00000409085 ; ENSP00000386456 ; ENSG00000115977 . [Q2M2I8-1 ]
    GeneIDi 22848.
    KEGGi hsa:22848.
    UCSCi uc002sfp.2. human. [Q2M2I8-1 ]
    uc010fdk.2. human. [Q2M2I8-2 ]

    Organism-specific databases

    CTDi 22848.
    GeneCardsi GC02M069685.
    H-InvDB HIX0161871.
    HGNCi HGNC:19679. AAK1.
    HPAi HPA017931.
    HPA020289.
    neXtProti NX_Q2M2I8.
    PharmGKBi PA134990616.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000232173.
    HOVERGENi HBG080803.
    KOi K08853.
    OMAi QLIQNFY.
    PhylomeDBi Q2M2I8.
    TreeFami TF317300.

    Enzyme and pathway databases

    SignaLinki Q2M2I8.

    Miscellaneous databases

    ChiTaRSi AAK1. human.
    GeneWikii AAK1.
    GenomeRNAii 22848.
    NextBioi 43313.
    PROi Q2M2I8.

    Gene expression databases

    ArrayExpressi Q2M2I8.
    Bgeei Q2M2I8.
    CleanExi HS_AAK1.
    Genevestigatori Q2M2I8.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiAAK1_HUMAN
    AccessioniPrimary (citable) accession number: Q2M2I8
    Secondary accession number(s): Q4ZFZ3, Q53RX6, Q9UPV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 92 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3