AKAP1_HUMAN
ID AKAP1_HUMAN Reviewed; 903 AA.
AC Q92667; A8K8Q1; D3DTZ0; Q13320; Q9BW14;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=A-kinase anchor protein 1, mitochondrial;
DE AltName: Full=A-kinase anchor protein 149 kDa;
DE Short=AKAP 149 {ECO:0000303|PubMed:8769136};
DE AltName: Full=Dual specificity A-kinase-anchoring protein 1;
DE Short=D-AKAP-1;
DE AltName: Full=Protein kinase A-anchoring protein 1;
DE Short=PRKA1;
DE AltName: Full=Spermatid A-kinase anchor protein 84;
DE Short=S-AKAP84 {ECO:0000303|PubMed:7499250};
DE Flags: Precursor;
GN Name=AKAP1 {ECO:0000312|HGNC:HGNC:367}; Synonyms=AKAP149, PRKA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Colon;
RX PubMed=8769136; DOI=10.1006/bbrc.1996.1172;
RA Trendelenburg G., Hummel M., Riecken E.-O., Hanski C.;
RT "Molecular characterization of AKAP149, a novel A kinase anchor protein
RT with a KH domain.";
RL Biochem. Biophys. Res. Commun. 225:313-319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=7499250; DOI=10.1074/jbc.270.46.27804;
RA Lin R.-Y., Moss S.B., Rubin C.S.;
RT "Characterization of S-AKAP84, a novel developmentally regulated A kinase
RT anchor protein of male germ cells.";
RL J. Biol. Chem. 270:27804-27811(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP INTERACTION WITH CFAP91.
RC TISSUE=Testis;
RX PubMed=12223483; DOI=10.1074/jbc.m206201200;
RA Yukitake H., Furusawa M., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT "AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary
RT complex between AMY-1, A-kinase anchor protein 84 and a regulatory subunit
RT of cAMP-dependent protein kinase and is phosphorylated by its kinase.";
RL J. Biol. Chem. 277:45480-45492(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND THR-533, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND THR-533, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-107; SER-151;
RP SER-169; SER-445; THR-533 AND SER-592, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-151; SER-429;
RP THR-533; SER-573; THR-590 AND SER-592, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP INTERACTION WITH CLPB, AND FUNCTION.
RX PubMed=31522117; DOI=10.1016/j.isci.2019.08.056;
RA Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O.,
RA Tamada T., Koshiba T.;
RT "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes:
RT Insight into a Role of the Coiled-Coil Region.";
RL IScience 19:1065-1078(2019).
CC -!- FUNCTION: Binds to type I and II regulatory subunits of protein kinase
CC A and anchors them to the cytoplasmic face of the mitochondrial outer
CC membrane (By similarity). Involved in mitochondrial-mediated antiviral
CC innate immunity (PubMed:31522117). Promotes translocation of NDUFS1
CC into mitochondria to regulate mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) activity (By similarity).
CC {ECO:0000250|UniProtKB:O08715, ECO:0000269|PubMed:31522117}.
CC -!- SUBUNIT: Interacts with SLC8A3 (By similarity). Interacts with CFAP91
CC (PubMed:12223483). Interacts with CLPB (PubMed:31522117). Interacts
CC with NDUFS1 (By similarity). {ECO:0000250|UniProtKB:O08715,
CC ECO:0000269|PubMed:12223483, ECO:0000269|PubMed:31522117}.
CC -!- INTERACTION:
CC Q92667; P13861: PRKAR2A; NbExp=5; IntAct=EBI-2119593, EBI-2556122;
CC Q92667-2; Q7Z4T9-3: CFAP91; NbExp=3; IntAct=EBI-2120060, EBI-17172567;
CC Q92667-2; Q99417: MYCBP; NbExp=2; IntAct=EBI-2120060, EBI-716185;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O08715}. Mitochondrion
CC {ECO:0000250|UniProtKB:O08715}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AKAP149;
CC IsoId=Q92667-1; Sequence=Displayed;
CC Name=2; Synonyms=S-AKAP84;
CC IsoId=Q92667-2; Sequence=VSP_002845, VSP_002846;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in thymus, prostate, testis,
CC ovary, colon and small intestine (PubMed:8769136). Isoform 2 is highly
CC expressed in testis and detected at much lower levels in kidney,
CC pancreas, liver, lung and brain (PubMed:7499250).
CC {ECO:0000269|PubMed:7499250, ECO:0000269|PubMed:8769136}.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; X97335; CAA66000.1; -; mRNA.
DR EMBL; U34074; AAC50279.1; -; mRNA.
DR EMBL; AK292416; BAF85105.1; -; mRNA.
DR EMBL; CH471109; EAW94515.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94516.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94518.1; -; Genomic_DNA.
DR EMBL; BC000729; AAH00729.1; -; mRNA.
DR CCDS; CCDS11594.1; -. [Q92667-1]
DR PIR; I39173; I39173.
DR RefSeq; NP_001229831.1; NM_001242902.1. [Q92667-1]
DR RefSeq; NP_001229832.1; NM_001242903.1. [Q92667-1]
DR RefSeq; NP_003479.1; NM_003488.3. [Q92667-1]
DR RefSeq; XP_005257764.1; XM_005257707.2.
DR RefSeq; XP_005257766.1; XM_005257709.2.
DR RefSeq; XP_016880678.1; XM_017025189.1.
DR RefSeq; XP_016880679.1; XM_017025190.1. [Q92667-1]
DR RefSeq; XP_016880680.1; XM_017025191.1.
DR AlphaFoldDB; Q92667; -.
DR SMR; Q92667; -.
DR BioGRID; 113818; 480.
DR CORUM; Q92667; -.
DR ELM; Q92667; -.
DR IntAct; Q92667; 54.
DR MINT; Q92667; -.
DR STRING; 9606.ENSP00000478212; -.
DR GlyGen; Q92667; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92667; -.
DR MetOSite; Q92667; -.
DR PhosphoSitePlus; Q92667; -.
DR SwissPalm; Q92667; -.
DR BioMuta; AKAP1; -.
DR DMDM; 8134304; -.
DR EPD; Q92667; -.
DR jPOST; Q92667; -.
DR MassIVE; Q92667; -.
DR MaxQB; Q92667; -.
DR PaxDb; Q92667; -.
DR PeptideAtlas; Q92667; -.
DR PRIDE; Q92667; -.
DR ProteomicsDB; 75399; -. [Q92667-1]
DR ProteomicsDB; 75400; -. [Q92667-2]
DR Antibodypedia; 2388; 186 antibodies from 33 providers.
DR DNASU; 8165; -.
DR Ensembl; ENST00000314126.4; ENSP00000314075.3; ENSG00000121057.13. [Q92667-2]
DR Ensembl; ENST00000337714.8; ENSP00000337736.3; ENSG00000121057.13. [Q92667-1]
DR Ensembl; ENST00000481416.5; ENSP00000433212.1; ENSG00000121057.13. [Q92667-2]
DR Ensembl; ENST00000539273.5; ENSP00000443139.1; ENSG00000121057.13. [Q92667-1]
DR Ensembl; ENST00000571629.5; ENSP00000459968.1; ENSG00000121057.13. [Q92667-1]
DR Ensembl; ENST00000572557.5; ENSP00000459895.1; ENSG00000121057.13. [Q92667-1]
DR Ensembl; ENST00000621116.4; ENSP00000478212.1; ENSG00000121057.13. [Q92667-1]
DR GeneID; 8165; -.
DR KEGG; hsa:8165; -.
DR MANE-Select; ENST00000337714.8; ENSP00000337736.3; NM_003488.4; NP_003479.1.
DR UCSC; uc002iux.4; human. [Q92667-1]
DR CTD; 8165; -.
DR DisGeNET; 8165; -.
DR GeneCards; AKAP1; -.
DR HGNC; HGNC:367; AKAP1.
DR HPA; ENSG00000121057; Tissue enhanced (skeletal).
DR MIM; 602449; gene.
DR neXtProt; NX_Q92667; -.
DR OpenTargets; ENSG00000121057; -.
DR PharmGKB; PA24661; -.
DR VEuPathDB; HostDB:ENSG00000121057; -.
DR eggNOG; KOG2279; Eukaryota.
DR GeneTree; ENSGT00390000001360; -.
DR HOGENOM; CLU_016731_0_0_1; -.
DR InParanoid; Q92667; -.
DR OMA; VMEDSGC; -.
DR PhylomeDB; Q92667; -.
DR TreeFam; TF105401; -.
DR PathwayCommons; Q92667; -.
DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q92667; -.
DR BioGRID-ORCS; 8165; 26 hits in 1082 CRISPR screens.
DR ChiTaRS; AKAP1; human.
DR GeneWiki; AKAP1; -.
DR GenomeRNAi; 8165; -.
DR Pharos; Q92667; Tbio.
DR PRO; PR:Q92667; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92667; protein.
DR Bgee; ENSG00000121057; Expressed in secondary oocyte and 214 other tissues.
DR ExpressionAtlas; Q92667; baseline and differential.
DR Genevisible; Q92667; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW RNA-binding; Transit peptide; Transmembrane.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..903
FT /note="A-kinase anchor protein 1, mitochondrial"
FT /id="PRO_0000016659"
FT DOMAIN 607..671
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 758..817
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 96..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..357
FT /note="PKA-RII subunit binding domain"
FT REGION 513..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08715"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 533
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 572..593
FT /note="GSDRNSMDSVDSCCSLKKTESF -> VAAPPPGKRGTLITRCPGFFEC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:7499250"
FT /id="VSP_002845"
FT VAR_SEQ 594..903
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7499250"
FT /id="VSP_002846"
FT VARIANT 18
FT /note="A -> V (in dbSNP:rs17761023)"
FT /id="VAR_049676"
FT VARIANT 60
FT /note="V -> M (in dbSNP:rs2230770)"
FT /id="VAR_024512"
FT VARIANT 102
FT /note="C -> Y (in dbSNP:rs2230771)"
FT /id="VAR_049677"
FT VARIANT 124
FT /note="R -> C (in dbSNP:rs17833723)"
FT /id="VAR_049678"
FT CONFLICT 795
FT /note="D -> H (in Ref. 5; AAH00729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 903 AA; 97342 MW; 0C906FAFFB0DBAF7 CRC64;
MAIQFRSLFP LALPGMLALL GWWWFFSRKK GHVSSHDEQQ VEAGAVQLRA DPAIKEPLPV
EDVCPKVVST PPSVTEPPEK ELSTVSKLPA EPPALLQTHP PCRRSESSGI LPNTTDMRLR
PGTRRDDSTK LELALTGGEA KSIPLECPLS SPKGVLFSSK SAEVCKQDSP FSRVPRKVQP
GYPVVPAEKR SSGERARETG GAEGTGDAVL GEKVLEEALL SREHVLELEN SKGPSLASLE
GEEDKGKSSS SQVVGPVQEE EYVAEKLPSR FIESAHTELA KDDAAPAPPV ADAKAQDRGV
EGELGNEESL DRNEEGLDRN EEGLDRNEES LDRNEEGLDR NEEIKRAAFQ IISQVISEAT
EQVLATTVGK VAGRVCQASQ LQGQKEESCV PVHQKTVLGP DTAEPATAEA AVAPPDAGLP
LPGLPAEGSP PPKTYVSCLK SLLSSPTKDS KPNISAHHIS LASCLALTTP SEELPDRAGI
LVEDATCVTC MSDSSQSVPL VASPGHCSDS FSTSGLEDSC TETSSSPRDK AITPPLPEST
VPFSNGVLKG ELSDLGAEDG WTMDAEADHS GGSDRNSMDS VDSCCSLKKT ESFQNAQAGS
NPKKVDLIIW EIEVPKHLVG RLIGKQGRYV SFLKQTSGAK IYISTLPYTQ SVQICHIEGS
QHHVDKALNL IGKKFKELNL TNIYAPPLPS LALPSLPMTS WLMLPDGITV EVIVVNQVNA
GHLFVQQHTH PTFHALRSLD QQMYLCYSQP GIPTLPTPVE ITVICAAPGA DGAWWRAQVV
ASYEETNEVE IRYVDYGGYK RVKVDVLRQI RSDFVTLPFQ GAEVLLDSVM PLSDDDQFSP
EADAAMSEMT GNTALLAQVT SYSPTGLPLI QLWSVVGDEV VLINRSLVER GLAQWVDSYY
TSL
