GENTAUR Molecular Products.

 AAK1_PIG                Reviewed;         968 AA.
 F1SPM8;
 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
 19-OCT-2011, sequence version 2.
 28-FEB-2018, entry version 40.
 RecName: Full=AP2-associated protein kinase 1 {ECO:0000303|PubMed:11877457};
          EC=2.7.11.1 {ECO:0000250|UniProtKB:P0C1X8};
 AltName: Full=Adaptor-associated kinase 1 {ECO:0000303|PubMed:11877457};
 Name=AAK1;
 Sus scrofa (Pig).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
 Sus.
 NCBI_TaxID=9823;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Porcine genome sequencing project;
 Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-54.
 Uenishi H., Morozumi T., Toki D., Eguchi-Ogawa T., Tanaka-Matsuda M.;
 "Porcine ESTs using full-length-enriched cDNA libraries.";
 Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
 [3] {ECO:0000305}
 FUNCTION.
 PubMed=11877457; DOI=10.1083/jcb.200111068;
 Ricotta D., Conner S.D., Schmid S.L., von Figura K., Honing S.;
 "Phosphorylation of the AP2 mu subunit by AAK1 mediates high affinity
 binding to membrane protein sorting signals.";
 J. Cell Biol. 156:791-795(2002).
 -!- 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.
     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. {ECO:0000269|PubMed:11877457}.
 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
     {ECO:0000250|UniProtKB:P0C1X8}.
 -!- ENZYME REGULATION: Stimulated by clathrin.
     {ECO:0000250|UniProtKB:P0C1X8}.
 -!- SUBUNIT: Interacts with alpha-adaptin, AP-2, clathrin, NUMB and
     EPS15. 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 (By similarity). {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:F1MH24,
     ECO:0000250|UniProtKB:P0C1X8}; Peripheral membrane protein
     {ECO:0000250|UniProtKB:F1MH24, ECO:0000250|UniProtKB:P0C1X8}.
     Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:F1MH24,
     ECO:0000250|UniProtKB:P0C1X8}. 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).
     {ECO:0000250|UniProtKB:F1MH24, ECO:0000250|UniProtKB:P0C1X8}.
 -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P0C1X8}.
 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
     protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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 EMBL; CU467585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; FS674854; -; NOT_ANNOTATED_CDS; mRNA.
 SMR; F1SPM8; -.
 STRING; 9823.ENSSSCP00000008900; -.
 PaxDb; F1SPM8; -.
 PeptideAtlas; F1SPM8; -.
 PRIDE; F1SPM8; -.
 Ensembl; ENSSSCT00000009130; ENSSSCP00000008900; ENSSSCG00000008337.
 eggNOG; KOG1989; Eukaryota.
 eggNOG; ENOG410Y515; LUCA.
 GeneTree; ENSGT00880000137958; -.
 InParanoid; F1SPM8; -.
 Reactome; R-SSC-8856825; Cargo recognition for clathrin-mediated endocytosis.
 Reactome; R-SSC-8856828; Clathrin-mediated endocytosis.
 Proteomes; UP000008227; Chromosome 3.
 GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
 GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
 GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
 GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
 GO; GO:0043195; C:terminal bouton; ISS:UniProtKB.
 GO; GO:0035612; F:AP-2 adaptor complex binding; ISS:UniProtKB.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0005112; F:Notch binding; ISS:UniProtKB.
 GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
 GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
 GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
 GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
 GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
 GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IDA:UniProtKB.
 GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
 InterPro; IPR011009; Kinase-like_dom_sf.
 InterPro; IPR000719; Prot_kinase_dom.
 InterPro; IPR008271; Ser/Thr_kinase_AS.
 Pfam; PF00069; Pkinase; 1.
 SMART; SM00220; S_TKc; 1.
 SUPFAM; SSF56112; SSF56112; 1.
 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
 PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
 2: Evidence at transcript level;
 Acetylation; ATP-binding; Cell membrane; Coated pit;
 Complete proteome; Endocytosis; Kinase; Membrane; Methylation;
 Nucleotide-binding; Phosphoprotein; Reference proteome;
 Serine/threonine-protein kinase; Transferase.
 CHAIN         1    968       AP2-associated protein kinase 1.
                              /FTId=PRO_0000413362.
 DOMAIN       46    315       Protein kinase. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 NP_BIND      52     60       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 COMPBIAS    397    621       Gln-rich.
 COMPBIAS    665    670       Poly-Ala.
 ACT_SITE    176    176       Proton acceptor. {ECO:0000255|PROSITE-
                              ProRule:PRU00159, ECO:0000255|PROSITE-
                              ProRule:PRU10027}.
 BINDING      74     74       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 MOD_RES       1      1       N-acetylmethionine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES      14     14       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     234    234       Phosphotyrosine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     235    235       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     354    354       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     389    389       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     391    391       Omega-N-methylarginine.
                              {ECO:0000250|UniProtKB:Q3UHJ0}.
 MOD_RES     613    613       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     625    625       Phosphoserine.
                              {ECO:0000250|UniProtKB:P0C1X8}.
 MOD_RES     627    627       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     630    630       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     631    631       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     644    644       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     657    657       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     660    660       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     694    694       Phosphotyrosine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     738    738       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q2M2I8}.
 MOD_RES     853    853       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q3UHJ0}.
 MOD_RES     944    944       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q3UHJ0}.
 MOD_RES     945    945       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q3UHJ0}.
 SEQUENCE   968 AA;  104310 MW;  4F07200E056E047D CRC64;
 MKKFFDSRRE QGGSGLGSGS SGGGGSTSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFAIV
 FLVRTSNGMK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW
 EVLILMDFCR GGQVVNLMNQ RLQTGFTESE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE
 NILLHDRGHY VLCDFGSATN KFQNPQTEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT
 TKADIWALGC LLYKLCYFTL PFGESQVAIC DGNFTIPDNS RYSQDMHCLI RYMLEPDPDK
 RPDIYQVSFF SFKLLKKECP VPNVQNSPIP AKLPEPVKAS EAAAKKTQPK ARLTDPIPTT
 ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRAMVQPPP QVAGSSNQPG LLASVPQPKT
 QAPPSQPLPQ SQAKQPQAPP APQQPPSAPA QGLPAQAQAT PQHQQQLFLK QQPQPPQPQP
 QAQAPPVKSL KFYPFYPMCK GRQTVSSQFQ AVHPAAQQPA IAQFPAVSQG SSQQQLIQNF
 YQQQQQQQQQ QQLATTLHQQ QLLTQQAALQ QKTTVAAIQP PQAQPATASQ PPPAQEPAQI
 QAPVRQQPKV QTTPPPAIQG QKLGSLTPPS SPKAQRAGHR RILSDVTHSA VFGVPASKST
 QLLQAAAAEA SLNKSKSATT TPSGSPRASQ QNVYNPSEGS TWNPFDDDNF SKLTAEELLN
 KDFAKLGEGK HPEKLGGSAE SLIPGFQPTQ GDAFAASSFA AGTAEKRKGG QAVDSSLPLL
 SVSDPFIPLQ VPDAPEKLIE GLKSPDTSLL LPDLLPMTDP FGSTSDAVIE KADVAVESLI
 PGLEPPVPQR LPSQTESVAS NRTDSLTGED ALIDCSLLSN PTTDLLEEFA PIAISAPAHK
 AAEDSNLISG FDVPEGSDKV AEDEFDPIPV LITKNPQGGH SRNSSGSSES SLPNLARSLL
 LVDQLIDL

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