AAK1_MOUSE
ID AAK1_MOUSE Reviewed; 959 AA.
AC Q3UHJ0; B2RUJ0; Q3TY53; Q6ZPZ6; Q80XP6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
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; Synonyms=Kiaa1048;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 473-959 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 417-959 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-604; THR-618 AND SER-622, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-604; THR-618;
RP SER-635; SER-844; SER-935 AND SER-936, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH NOTCH1.
RX PubMed=21464124; DOI=10.1074/jbc.m110.190769;
RA Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J.,
RA Olivo-Marin J.C., Israel A.;
RT "The adaptor-associated kinase 1, AAK1, is a positive regulator of the
RT Notch pathway.";
RL J. Biol. Chem. 286:18720-18730(2011).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-391, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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. Preferentially, may phosphorylate
CC substrates on threonine residues. Regulates phosphorylation of other
CC AP-2 subunits as well as AP-2 localization and AP-2-mediated
CC internalization of ligand complexes. Phosphorylates NUMB and regulates
CC its cellular localization, promoting NUMB localization to endosomes.
CC Binds to and stabilizes the activated form of NOTCH1, increases its
CC localization in endosomes and regulates its transcriptional activity.
CC {ECO:0000250|UniProtKB:Q2M2I8}.
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 (By similarity). Interacts
CC with EPS15 isoform 2 (By similarity). Interacts with membrane-bound
CC activated NOTCH1 but not with the inactive full-length form of NOTCH1
CC (PubMed:21464124). Preferentially interacts with monoubiquitinated
CC activated NOTCH1 compared to the non-ubiquitinated form
CC (PubMed:21464124). {ECO:0000250|UniProtKB:P0C1X8,
CC ECO:0000250|UniProtKB:Q2M2I8, ECO:0000269|PubMed:21464124}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:F1MH24};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane,
CC clathrin-coated pit {ECO:0000250|UniProtKB:P0C1X8}. Presynapse
CC {ECO:0000250|UniProtKB:P0C1X8}. 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:0000250|UniProtKB:P0C1X8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UHJ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHJ0-2; Sequence=VSP_020670;
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; AK147363; BAE27867.1; -; mRNA.
DR EMBL; AK158879; BAE34710.1; -; mRNA.
DR EMBL; BC043125; AAH43125.1; -; mRNA.
DR EMBL; BC141176; AAI41177.1; -; mRNA.
DR EMBL; AK129272; BAC98082.1; -; mRNA.
DR CCDS; CCDS20317.1; -. [Q3UHJ0-2]
DR CCDS; CCDS39544.1; -. [Q3UHJ0-1]
DR RefSeq; NP_001035195.1; NM_001040106.2. [Q3UHJ0-1]
DR RefSeq; NP_808430.2; NM_177762.6. [Q3UHJ0-2]
DR PDB; 7LVH; X-ray; 2.65 A; A/B=26-330.
DR PDB; 7LVI; X-ray; 2.20 A; A/B=26-330.
DR PDB; 7RJ6; X-ray; 2.13 A; A/B=26-330.
DR PDB; 7RJ7; X-ray; 2.12 A; A/B=26-330.
DR PDB; 7RJ8; X-ray; 2.59 A; A/B=26-330.
DR PDBsum; 7LVH; -.
DR PDBsum; 7LVI; -.
DR PDBsum; 7RJ6; -.
DR PDBsum; 7RJ7; -.
DR PDBsum; 7RJ8; -.
DR AlphaFoldDB; Q3UHJ0; -.
DR SMR; Q3UHJ0; -.
DR BioGRID; 234710; 12.
DR IntAct; Q3UHJ0; 4.
DR MINT; Q3UHJ0; -.
DR STRING; 10090.ENSMUSP00000086948; -.
DR iPTMnet; Q3UHJ0; -.
DR PhosphoSitePlus; Q3UHJ0; -.
DR SwissPalm; Q3UHJ0; -.
DR EPD; Q3UHJ0; -.
DR jPOST; Q3UHJ0; -.
DR MaxQB; Q3UHJ0; -.
DR PaxDb; Q3UHJ0; -.
DR PeptideAtlas; Q3UHJ0; -.
DR PRIDE; Q3UHJ0; -.
DR ProteomicsDB; 286010; -. [Q3UHJ0-1]
DR ProteomicsDB; 286011; -. [Q3UHJ0-2]
DR Antibodypedia; 7943; 369 antibodies from 39 providers.
DR DNASU; 269774; -.
DR Ensembl; ENSMUST00000003710; ENSMUSP00000003710; ENSMUSG00000057230. [Q3UHJ0-2]
DR Ensembl; ENSMUST00000089519; ENSMUSP00000086948; ENSMUSG00000057230. [Q3UHJ0-1]
DR GeneID; 269774; -.
DR KEGG; mmu:269774; -.
DR UCSC; uc009css.1; mouse. [Q3UHJ0-1]
DR UCSC; uc009cst.1; mouse. [Q3UHJ0-2]
DR CTD; 22848; -.
DR MGI; MGI:1098687; Aak1.
DR VEuPathDB; HostDB:ENSMUSG00000057230; -.
DR eggNOG; KOG1989; Eukaryota.
DR GeneTree; ENSGT00940000155968; -.
DR HOGENOM; CLU_000288_109_5_1; -.
DR InParanoid; Q3UHJ0; -.
DR OMA; ASLNKSX; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; Q3UHJ0; -.
DR TreeFam; TF317300; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 269774; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Aak1; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UHJ0; protein.
DR Bgee; ENSMUSG00000057230; Expressed in vestibular membrane of cochlear duct and 255 other tissues.
DR ExpressionAtlas; Q3UHJ0; baseline and differential.
DR Genevisible; Q3UHJ0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISS:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISS: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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell membrane; Cell projection; Coated pit; Endocytosis; Kinase; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..959
FT /note="AP2-associated protein kinase 1"
FT /id="PRO_0000250579"
FT DOMAIN 46..315
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 340..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..958
FT /note="Clathrin-binding domain (CBD)"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT REGION 836..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..943
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 353..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..943
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 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C1X8"
FT MOD_RES 618
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT MOD_RES 651
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M2I8"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 509..589
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020670"
FT CONFLICT 79
FT /note="N -> K (in Ref. 1; BAE27867)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="N -> S (in Ref. 3; BAC98082)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="L -> V (in Ref. 2; AAI41177)"
FT /evidence="ECO:0000305"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 81..96
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:7LVH"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:7LVI"
FT TURN 140..144
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 148..166
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7LVI"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:7LVI"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:7LVI"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:7LVI"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:7LVI"
SQ SEQUENCE 959 AA; 103346 MW; B7D666EFD56D097A 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 RYMLEPDPDK
RPDIYQVSYF SFKLLKKECP VPNVQNSPIP AKLPEPVKAS EAAVKKTQPK ARLTDPIPTT
ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPLP QAAGPSNQPG LLPSVSQPKA
QATPSQPLQS SQPKQPQAPP TPQQTPATQT QGLPTQAQAT PQHQQQHLLK QQQQQQQQPQ
QPTAPPQPAG TFYQQQQQQQ QQQAQTQQFQ AVHPAAQQPV TAQFPVGSQG GAQQQLMQNF
YHQQQQQQQQ QQQLMAQQAA LQQKTAVVVP QSQAQPATAP QAAAAQEPGQ IQAPVRQQPK
VQTTPPPTIQ GQKVGSLTPP SSPKTQRAGH RRILSDVTHS AVFGVPASKS TQLLQAAAAE
ASLNKSKSAT TTPSGSPRTS QQNVSNASEG STWNPFDDDN FSKLTAEELL NKDFAKLGEG
KLPEKLGGSA ESLIPGFQPT QGDAFTTPSF SAGTAEKRKG GQAVDSGIPL LSVSDPFIPL
QVPDAPEKLI EGLKSPDTSL LLPDLLPMTD PFGSTSDAVI DKADVAVESL IPGLEPPVAQ
RLPSQTESVT SNRTDSLTGE DSLLDCSLLS NPTAGLLEEF APIALSAPTH KAAEDSNLIS
GFGVAEGSEK VAEDEFDPIP VLITKNTQGG HSRNSSGSSE SSLPNLARSL LLVDQLIDL
