AKP13_RAT
ID AKP13_RAT Reviewed; 2760 AA.
AC F1M3G7; Q8VHU6;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=A-kinase anchor protein 13;
DE Short=AKAP-13;
DE AltName: Full=AKAP-Lbc {ECO:0000303|PubMed:17537920};
GN Name=Akap13 {ECO:0000312|RGD:727893};
GN Synonyms=Rt13 {ECO:0000303|PubMed:11696353};
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 {ECO:0000312|Proteomes:UP000002494};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAL40924.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1151-1748, AND INTERACTION WITH RHOA AND
RP PRKAR2A.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAL40924.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAL40924.1};
RX PubMed=11696353; DOI=10.1016/s0014-5793(01)02995-7;
RA Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E.,
RA Hundsrucker C., Maric K., Rosenthal W.;
RT "Ht31: the first protein kinase A anchoring protein to integrate protein
RT kinase A and Rho signaling.";
RL FEBS Lett. 507:264-268(2001).
RN [4]
RP FUNCTION, AND INDUCTION BY PHENYLEPHRINE.
RX PubMed=17537920; DOI=10.1073/pnas.0701099104;
RA Appert-Collin A., Cotecchia S., Nenniger-Tosato M., Pedrazzini T.,
RA Diviani D.;
RT "The A-kinase anchoring protein (AKAP)-Lbc-signaling complex mediates
RT alpha1 adrenergic receptor-induced cardiomyocyte hypertrophy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10140-10145(2007).
RN [5]
RP FUNCTION.
RX PubMed=20139090; DOI=10.1074/jbc.m110.106856;
RA Mayers C.M., Wadell J., McLean K., Venere M., Malik M., Shibata T.,
RA Driggers P.H., Kino T., Guo X.C., Koide H., Gorivodsky M., Grinberg A.,
RA Mukhopadhyay M., Abu-Asab M., Westphal H., Segars J.H.;
RT "The Rho guanine nucleotide exchange factor AKAP13 (BRX) is essential for
RT cardiac development in mice.";
RL J. Biol. Chem. 285:12344-12354(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1585; SER-1628; SER-1630;
RP SER-1891; SER-1894; SER-1907; SER-2292; SER-2511 AND SER-2676, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [7]
RP FUNCTION, AND INTERACTION WITH IKBKB.
RX PubMed=23090968; DOI=10.1128/mcb.00887-12;
RA del Vescovo C.D., Cotecchia S., Diviani D.;
RT "A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support
RT interleukin-6-mediated cardiomyocyte hypertrophy.";
RL Mol. Cell. Biol. 33:14-27(2013).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH PKN1; MAPK14; ZAK AND
RP MAP2K3.
RX PubMed=23716597; DOI=10.1128/mcb.00031-13;
RA Perez Lopez I., Cariolato L., Maric D., Gillet L., Abriel H., Diviani D.;
RT "A-kinase anchoring protein Lbc coordinates a p38 activating signaling
RT complex controlling compensatory cardiac hypertrophy.";
RL Mol. Cell. Biol. 33:2903-2917(2013).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=25892096; DOI=10.1002/jbmr.2534;
RA Koide H., Holmbeck K., Lui J.C., Guo X.C., Driggers P., Chu T., Tatsuno I.,
RA Quaglieri C., Kino T., Baron J., Young M.F., Robey P.G., Segars J.H.;
RT "Mice deficient in AKAP13 (BRX) are osteoporotic and have impaired
RT osteogenesis.";
RL J. Bone Miner. Res. 30:1887-1895(2015).
CC -!- FUNCTION: Scaffold protein that plays an important role in assembling
CC signaling complexes downstream of several types of G protein-coupled
CC receptors. Activates RHOA in response to signaling via G protein-
CC coupled receptors via its function as Rho guanine nucleotide exchange
CC factor (PubMed:17537920). May also activate other Rho family members.
CC Part of a kinase signaling complex that links ADRA1A and ADRA1B
CC adrenergic receptor signaling to the activation of downstream p38 MAP
CC kinases, such as MAPK11 and MAPK14 (PubMed:17537920, PubMed:23716597).
CC Part of a signaling complex that links ADRA1B signaling to the
CC activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B
CC transcriptional activity (PubMed:23090968). Part of a RHOA-dependent
CC signaling cascade that mediates responses to lysophosphatidic acid
CC (LPA), a signaling molecule that activates G-protein coupled receptors
CC and potentiates transcriptional activation of the glucocorticoid
CC receptor NR3C1 (By similarity). Part of a signaling cascade that
CC stimulates MEF2C-dependent gene expression in response to
CC lysophosphatidic acid (LPA) (PubMed:20139090). Part of a signaling
CC pathway that activates MAPK11 and/or MAPK14 and leads to increased
CC transcription activation of the estrogen receptors ESR1 and ESR2 (By
CC similarity). Part of a signaling cascade that links cAMP and EGFR
CC signaling to BRAF signaling and to PKA-mediated phosphorylation of
CC KSR1, leading to the activation of downstream MAP kinases, such as
CC MAPK1 or MAPK3 (By similarity). Functions as scaffold protein that
CC anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes
CC activation of PRKD1, leading to increased phosphorylation of HDAC5 and
CC ultimately cardiomyocyte hypertrophy (By similarity). Has no guanine
CC nucleotide exchange activity on CDC42, Ras or Rac (By similarity).
CC Required for normal embryonic heart development, and in particular for
CC normal sarcomere formation in the developing cardiomyocytes (By
CC similarity). Plays a role in cardiomyocyte growth and cardiac
CC hypertrophy in response to activation of the beta-adrenergic receptor
CC by phenylephrine or isoproterenol (PubMed:17537920). Required for
CC normal adaptive cardiac hypertrophy in response to pressure overload
CC (By similarity). Plays a role in osteogenesis (By similarity).
CC {ECO:0000250|UniProtKB:E9Q394, ECO:0000250|UniProtKB:Q12802,
CC ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:20139090,
CC ECO:0000269|PubMed:23090968}.
CC -!- SUBUNIT: Interacts with the cAMP-dependent protein kinase (PKA)
CC holoenzyme and with the regulatory subunit PRKAR2A (PubMed:11696353).
CC Interacts with RHOA (PubMed:11696353). Interacts also with RHOB and
CC RHOC. Identified in a ternary complex with RHOA and PRKAR2A. Identified
CC in a complex with NR3C1 and RHOA. Interacts with BRAF and KSR1.
CC Identified in a complex with BRAF and KSR1 (By similarity). Component
CC of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK
CC and MAP2K3 (PubMed:23716597). Within this complex, AKAP13 interacts
CC directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By
CC similarity). Interacts (phosphorylated form) with YWHAB and YWHAZ.
CC Interaction with YWHAB inhibits activation of RHOA, interferes with
CC PKN1 binding and activation of MAP kinases. Interacts with GNA12.
CC Interacts with IKBKB (PubMed:23090968). Interacts with ESR1, THRA,
CC PPARA and NME2 (By similarity). Interacts (via the C-terminal domain
CC after the PH domain) with MEF2C and RXRB. Interacts (via the C-terminal
CC domain after the PH domain) with PRKD1 (By similarity).
CC {ECO:0000250|UniProtKB:E9Q394, ECO:0000250|UniProtKB:Q12802,
CC ECO:0000269|PubMed:11696353, ECO:0000269|PubMed:23090968,
CC ECO:0000269|PubMed:23716597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q12802}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q12802}. Nucleus {ECO:0000250|UniProtKB:Q12802}.
CC Membrane {ECO:0000250|UniProtKB:Q12802}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q12802}. Note=Colocalizes with the actin
CC cytoskeleton at the cell cortex. {ECO:0000250|UniProtKB:Q12802}.
CC -!- TISSUE SPECIFICITY: Detected in bone osteoblasts (at protein level).
CC {ECO:0000269|PubMed:25892096}.
CC -!- INDUCTION: Up-regulated in cardiomyocytes in response to phenylephrine
CC (in vitro). {ECO:0000269|PubMed:17537920}.
CC -!- DOMAIN: The DH domain is sufficient for interaction with RHOA, and for
CC guanine nucleotide exchange (GEF) activity with RHOA. Forms that lack
CC C-terminal regulatory domains have transforming activity and function
CC as oncogenes. {ECO:0000250|UniProtKB:Q12802}.
CC -!- DOMAIN: The PH domain does not play a role in lipid-binding. Instead,
CC it inhibits the guanine nucleotide exchange (GEF) activity of the
CC isolated DH domain (in vitro). {ECO:0000250|UniProtKB:Q12802}.
CC -!- DOMAIN: The C-terminal domain after the PH domain is involved in
CC protein-protein interactions that are required for normal, compensatory
CC cardiac hypertrophy in response to pressure overload.
CC {ECO:0000250|UniProtKB:E9Q394}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL40924.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AABR07004317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07004318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07004319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473980; EDM08537.1; -; Genomic_DNA.
DR EMBL; AF387102; AAL40924.1; ALT_INIT; mRNA.
DR RefSeq; NP_001099741.2; NM_001106271.2.
DR SMR; F1M3G7; -.
DR STRING; 10116.ENSRNOP00000014802; -.
DR iPTMnet; F1M3G7; -.
DR PhosphoSitePlus; F1M3G7; -.
DR jPOST; F1M3G7; -.
DR PaxDb; F1M3G7; -.
DR PeptideAtlas; F1M3G7; -.
DR PRIDE; F1M3G7; -.
DR GeneID; 293024; -.
DR KEGG; rno:293024; -.
DR UCSC; RGD:727893; rat.
DR CTD; 11214; -.
DR RGD; 727893; Akap13.
DR VEuPathDB; HostDB:ENSRNOG00000010964; -.
DR eggNOG; KOG3520; Eukaryota.
DR HOGENOM; CLU_000597_0_0_1; -.
DR InParanoid; F1M3G7; -.
DR OMA; XDQKSTV; -.
DR OrthoDB; 69816at2759; -.
DR TreeFam; TF325887; -.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:F1M3G7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000010964; Expressed in lung and 19 other tissues.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0086023; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISS:UniProtKB.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0051168; P:nuclear export; IMP:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:1900169; P:regulation of glucocorticoid mediated signaling pathway; ISO:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0060297; P:regulation of sarcomere organization; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR028852; AKAP13.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944:SF18; PTHR13944:SF18; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..2760
FT /note="A-kinase anchor protein 13"
FT /id="PRO_0000436320"
FT DOMAIN 1956..2153
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 2176..2280
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1753..1800
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 356..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..504
FT /note="Important for interaction with PRKAR2A"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT REGION 530..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1228
FT /note="Important for interaction with PRKAR2A"
FT /evidence="ECO:0000269|PubMed:11696353"
FT REGION 1392..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1695
FT /note="Important for interaction with MAP2K3"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT REGION 1592..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1881..2760
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT REGION 2422..2450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2568..2588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2660..2760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2292..2329
FT /evidence="ECO:0000255"
FT COILED 2516..2632
FT /evidence="ECO:0000255"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2426..2449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2660..2681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2690..2722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 801
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 932
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9Q394"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1654
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1892
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 1894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 2415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12802"
FT MOD_RES 2511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q394"
FT MOD_RES 2676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 1348
FT /note="V -> A (in Ref. 3; AAL40924)"
FT /evidence="ECO:0000305"
FT CONFLICT 1542..1559
FT /note="Missing (in Ref. 3; AAL40924)"
FT /evidence="ECO:0000305"
FT CONFLICT 1745..1747
FT /note="EKD -> KKK (in Ref. 3; AAL40924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2760 AA; 301403 MW; DC1C4A92AF76188C CRC64;
MKLSPQQAPL YGDCVVTVLL AEEDKVEDDA IFYLIFSGST LYHCTSTRKV SSDTLETIAP
GHDCCETVKV LLCASKEGLP VFVVAEEDFH FVQDEAYDAA QFLATSAGNQ QALNFTRFLD
RSGPPSGDVN SLDEKVALAF RHLKLPAEWN VLGTDHTLHD GGPRETLMHF AVRLGLLRLT
WFLLQKPGGR GALSIHNKEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG
DYSVRHHREL DIYTLTSESE SHCEPHGDSC TGHISKLMNI QQQLMKTNLK QMDNLMPLMV
TTQDSSCVPC VPEPSDHQQL PFEETKSTVC CQGSPGRKDA SPCDLSSVVE EENLICSHKK
NKDTGRPGEG VEPASAVDSR SASHQDSCLQ SIPDCGVKGR EGLPSCGNRN EVTGTQYSGV
ATCQQPLSSE SSVPQDVLVT EPDARQHSSG RELPDSSSTD AGAPEKAGEL EHSLLTPDAT
TQNSKPQVGE SAKERLENSD ISSAEATAVQ ALREPKQKAD VTNHVFAARA AGADAPAEAS
PAWSPEEIPT GKPGMETQER GCEGGITSDQ SSQVLPAAAA ATENKVLDGL ELETLPACPC
ETASSLDLTV SGPRPDGMPK QNSESSAQHA QSLNSQAPLC SIAGAGTPSA ESACPQSTET
SSGGSVIEHG SGEASLPEST AAQPEPQGLC TAPCPEDPQA DTVTSDTAAH NQKSVGSCHL
CALDAKNQEK DLRQDTPSVN TLEDVPHLPS VVPQSEEKLE PDQVSPRGSS FSLASSPESE
SVTKDDVLSL VSSQKEKGTA TPQLHRAPAC SDGPDGRDLN DTDKVGDGAA SPPTPSAVEL
QTSMGNTSPV GVGEQEGSSL TATLEVLSDS LLQSVDKAAL VSDSLLPEEG GSIVVPESST
ALGQGGKDKA TKCPSVKEDV HSSEMSREDQ RTPPPGQEIS RLCEKPMSAL CAGEKALQHS
NSPDTPSACL QTETKHNKEV APQSSPLMKG GAVQNLVPPK TSLSADSEQK TSSTEQSGSS
LLPGGASEAL RCSQPSLSVS VESIQFQGKT SACKVSRNAM EDVTVADAFL ATAEPTKEDA
LHHVKDISDL LNQEKKTTPG LPEALLDKGV TDLQEVITPE IEPLDCKREK LEGTDLSCPT
SKSKETPNNE ETTQPPARDL PTETGLSAIN DNGPQADMKH VTQASVPGEE SNVTTVLGMV
STQAADGPPG ADSIEETATR IVEAVIKQIK ASNTLRTQVE IQNPPLSSSE IKEIENTGSE
SARVFLPGEP LQMENTQKET TGHCSVETEA PEKIILAVHR PEPAPEMPDT KTGGEVDLLS
KRSAASEEEA IGNGAATPKM KQAPGTQVIN RESWCAIEPC PEAASLLASK QSSECRSFID
VGLGTECATK EGVLQRESGS DSDLFHSPSD EMDSIIFSKP EEEQLLCDTT GSSSSTDDTA
SLDRHSSHGS DVSLPQTSKL NRSRNHQSSN GFFSHGVDPE SREGESEPAG SGEMEEEEMD
SITEVPANRS FLRNSMRSLS PFRRHSWGPG KNAASDAEMN QRSSMQVLGH VVRRPPIHRR
SMSWCPSGVQ YSAALNADFN IRSFSLEGLT GGGGVGNKPS SSLEISSANS SELRNPFSGE
EQRSSLMSLS EEHLEPDQRQ HHRMFDQQTC YRSKQQGFNY CTSAISSPLT KSISLMTISH
PGLDNSRPFH SASANLTESI TEENCNFLPP SPSKKSFEEK SGTKVSRTFS YIRNKMSSSK
KSKKEKDKKT LNGHTFSPIP IVGPINCSQC MKPFTNKDAY TCASCGAFVH KGCRENLASC
AKVKMKQPKG SLQAHDTSSL PTVIMRNKSS QPKERPRSAV LLAEEAIAAP MFTNRRSQQS
VSLSKSVSIQ NITGVGNDEN MSNTWKFLSH STDSLNKICK VNESTESLTD EGVGTDMNEG
QLMGDFESDS KQLEAESWSR TVDSKFLKQQ KKDVVKRQEV IYELMQTELH HIRTLKIMSD
VYSRGMMTDL LFEQQMVEKL FPCLDELISI HSQFFQRILE RKKESLVDKS EKNFLIKRIG
DVLVSQFSGE NAERLKKTYG KFCGQHNQSV NYFKDLYTKD KRFQAFVKKK MSSSVVRRLG
IPECILLVTQ RITKYPVLFQ RILQCTKDNE VEQEDLTQSL SLVKDVIGAV DSKVASYEKK
VRLGEIYTKT DSKSIMRMKS GQMFAKEDLR RKKLVRDGSV FLKSATGRLK EKDQKYVFAS
LDHKSTVISL KKLIVREVAH EEKGLFLISM GVKDPEMVEV HASSREERNS WIQIIQDTIN
SLNRDEDEGI PSENEEEKRL LDTKARELKE QLQQKDQQIL LLLEEKEMIF RDMTECSTPL
PEDCSPTHSP RMLFRSNTEE ALKGGPLMKS AISEVEILQG LVSGSLGGTL GQPISSPVEQ
EVMAGPISLP RRAETFGGFD CHQLNASKGG EKEEGDDGQD LRRTESDSGL KKGGNANLVF
MLKRNSEQVV QSIVHLHELL TMLQGVVLQQ DSYIEDQKLV LTEKVLTRSA SRPSSLIEQE
KQRSLEKQRQ DLANLQKQQA QHLEEKRRRE REWEARELEL RDREAKLAER EETVRRRQQD
LERDREELQQ KKGTYQCDLE RLRAAQKQLE REQEQLKRDA EQLSQRQMEQ DLCQVSNKHG
RLMRVPSFLP NSDEFSLLST PSITKSGSLD SELSVSPKRN SISRTQKDKG PFHILSSASQ
TKVPEGQSQA PSSTSTSTRL FGLSKPKEKK EKKKKSKGSR TQPGDGPAPE VPAEGEEIFC
