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AAK1_RAT
ID   AAK1_RAT                Reviewed;         962 AA.
AC   P0C1X8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=AP2-associated protein kinase 1;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:Q2M2I8};
DE   AltName: Full=Adaptor-associated kinase 1;
GN   Name=Aak1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   FUNCTION, INTERACTION WITH ALPHA-ADAPTIN, AND SUBCELLULAR LOCATION.
RX   PubMed=11877461; DOI=10.1083/jcb.200108123;
RA   Conner S.D., Schmid S.L.;
RT   "Identification of an adaptor-associated kinase, AAK1, as a regulator of
RT   clathrin-mediated endocytosis.";
RL   J. Cell Biol. 156:921-929(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619; THR-621; SER-625;
RP   SER-638 AND SER-939, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating
CC       the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which
CC       ensures high affinity binding of AP-2 to cargo membrane proteins during
CC       the initial stages of endocytosis (PubMed:11877461). Preferentially,
CC       may phosphorylate substrates on threonine residues (By similarity).
CC       Regulates phosphorylation of other AP-2 subunits as well as AP-2
CC       localization and AP-2-mediated internalization of ligand complexes (By
CC       similarity). Phosphorylates NUMB and regulates its cellular
CC       localization, promoting NUMB localization to endosomes (By similarity).
CC       Binds to and stabilizes the activated form of NOTCH1, increases its
CC       localization in endosomes and regulates its transcriptional activity
CC       (By similarity). {ECO:0000250|UniProtKB:Q2M2I8,
CC       ECO:0000269|PubMed:11877461}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q2M2I8};
CC   -!- ACTIVITY REGULATION: Stimulated by clathrin.
CC       {ECO:0000250|UniProtKB:Q2M2I8}.
CC   -!- SUBUNIT: Interacts (via CBD domain) with clathrin (By similarity).
CC       Interacts with AP-2 complex (By similarity). Interacts with NUMB (By
CC       similarity). Interacts with alpha-adaptin (PubMed:11877461). Interacts
CC       with EPS15 (By similarity). Interacts with membrane-bound activated
CC       NOTCH1 but not with the inactive full-length form of NOTCH1 (By
CC       similarity). Preferentially interacts with monoubiquitinated activated
CC       NOTCH1 compared to the non-ubiquitinated form (By similarity).
CC       {ECO:0000250|UniProtKB:Q2M2I8, ECO:0000269|PubMed:11877461}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:F1MH24};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane,
CC       clathrin-coated pit {ECO:0000269|PubMed:11877461}. Presynapse
CC       {ECO:0000269|PubMed:11877461}. Note=Active when found in clathrin-
CC       coated pits at the plasma membrane. In neuronal cells, enriched at
CC       presynaptic terminals. In non-neuronal cells, enriched at leading edge
CC       of migrating cells. {ECO:0000269|PubMed:11877461}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q2M2I8}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AABR03032075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03032129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0C1X8; -.
DR   SMR; P0C1X8; -.
DR   IntAct; P0C1X8; 1.
DR   MINT; P0C1X8; -.
DR   STRING; 10116.ENSRNOP00000044665; -.
DR   iPTMnet; P0C1X8; -.
DR   PhosphoSitePlus; P0C1X8; -.
DR   jPOST; P0C1X8; -.
DR   PaxDb; P0C1X8; -.
DR   PRIDE; P0C1X8; -.
DR   UCSC; RGD:1305520; rat.
DR   RGD; 1305520; Aak1.
DR   eggNOG; KOG1989; Eukaryota.
DR   InParanoid; P0C1X8; -.
DR   PhylomeDB; P0C1X8; -.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:P0C1X8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR   GO; GO:0071439; C:clathrin complex; IDA:UniProtKB.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0043195; C:terminal bouton; IDA:UniProtKB.
DR   GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005112; F:Notch binding; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IDA:UniProtKB.
DR   GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell membrane; Cell projection; Coated pit;
KW   Endocytosis; Kinase; Membrane; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Synapse; Transferase.
FT   CHAIN           1..962
FT                   /note="AP2-associated protein kinase 1"
FT                   /id="PRO_0000250580"
FT   DOMAIN          46..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..961
FT                   /note="Clathrin-binding domain (CBD)"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   REGION          839..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          925..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..446
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         52..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         234
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         353
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         388
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         390
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHJ0"
FT   MOD_RES         440
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         607
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         619
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         621
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         624
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         654
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         732
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT   MOD_RES         847
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHJ0"
FT   MOD_RES         938
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHJ0"
FT   MOD_RES         939
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   962 AA;  103761 MW;  755E6F250C7A373E CRC64;
     MKKFFDSRRE QGSSGLGSGS SGGGGSSSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFALV
     FLVRTSNGVK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW
     EVLILMDFCR GGQVVNLMNQ RLQTGFTENE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE
     NILLHDRGHY VLCDFGSATN KFQNPQAEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT
     TKADIWALGC LLYKLCYFTL PFGESQVAIC DGSFTIPDNS RYSQDMHCLI YMLEPDPDKR
     PDIYQVSYFS FKLLKKECPV PNVQNSPIPT KLPEPVKASE AAVKKTQPKA RLTDPIPTTE
     TSIAPRQRPK AGQTQPNPGI LPIQPALTPR KRATVQPLPQ ATGPSNQPSL LASVSQPKAQ
     ATPSQPLQSS QPKQPQAPPT PQQTPAPQTQ GLPTQAQATP QHQQQLLLKQ QQQQQQQQQQ
     QQPQQPTAPP QPSGTFYQQQ QPQQQQAQTQ QQFQAVHPAA QQSVTAQFPV VSQGGSQQQL
     MQNFYQQQQQ QQQQQQQLMA QQAALQQKTA VVVPQPQAQP ATAPQAAAAQ EPQIQAPARQ
     QPKVQTTPPP TIQGQKVGSL TPPSSPKTQR AGHRRILSDV THSAVFGVPA SKSTQLLHAA
     AAEASLSKSK SATTTPSGSP RTSQQNVSNA SEGSTWNPFD DDNFSKLTAE ELLNKDFAKL
     GEGKLPEKLG GSAESLIPGF QATQGDAFAT SSFSAGTAEK RKGGQAVDSG IPLLSVSDPF
     IPLQVPDAPE KLIEGLKSPD TSLLLPDLLP MTDPFGSTSD AVIEKADAAV ESLIPGLEPP
     VAQRLPSHTE SVTSNRTDSL TGEDSLLDCS LLSNPTADLL DEFAPIALSA STHKAAEDSN
     LISGFGVAEG SEKVAEDEFD PIPVLITKNT QGGHSRNSSG SSESSLPNLA RSLLLVDQLI
     DL
 
 
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