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A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)

 AKP13_HUMAN             Reviewed;        2813 AA.
Q12802; Q14572; Q59FP6; Q86W90; Q8WXQ6; Q96JP6; Q96P79; Q9Y5T0;
Q9Y5T6;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
13-FEB-2019, entry version 174.
RecName: Full=A-kinase anchor protein 13;
Short=AKAP-13;
AltName: Full=AKAP-Lbc {ECO:0000303|PubMed:11546812};
AltName: Full=Breast cancer nuclear receptor-binding auxiliary protein {ECO:0000303|PubMed:9627117};
AltName: Full=Guanine nucleotide exchange factor Lbc;
AltName: Full=Human thyroid-anchoring protein 31 {ECO:0000303|PubMed:11696353};
AltName: Full=Lymphoid blast crisis oncogene {ECO:0000303|PubMed:24993829};
Short=LBC oncogene {ECO:0000303|PubMed:24993829};
AltName: Full=Non-oncogenic Rho GTPase-specific GTP exchange factor;
AltName: Full=Protein kinase A-anchoring protein 13;
Short=PRKA13;
AltName: Full=p47;
Name=AKAP13;
Synonyms=BRX {ECO:0000303|PubMed:9627117},
HT31 {ECO:0000303|PubMed:11696353}, LBC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
VARIANTS CYS-574 AND SER-2457.
PubMed=11696353; DOI=10.1016/S0014-5793(01)02995-7;
Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V.,
Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.;
"Ht31: the first protein kinase A anchoring protein to integrate
protein kinase A and Rho signaling.";
FEBS Lett. 507:264-268(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PKA HOLOENZYME;
PRKAR2A; GNA12; RHOA; RHOB AND RHOC, IDENTIFICATION IN A COMPLEX WITH
RHOA AND PRKAR2A, MUTAGENESIS OF ALA-1251; ILE-1260 AND TYR-2153, AND
VARIANTS VAL-624; MET-897 AND SER-2457.
PubMed=11546812; DOI=10.1074/jbc.M106629200;
Diviani D., Soderling J., Scott J.D.;
"AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective
Rho-mediated stress fiber formation.";
J. Biol. Chem. 276:44247-44257(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-452; ARG-494;
CYS-574; LYS-689; ALA-845; MET-897; ALA-1062; ASN-1086 AND THR-1216.
TISSUE=Lung;
Miyamoto M., Ono Y.;
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Hippocampus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1385-2813 (ISOFORM 1), FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ESR1; THRA
AND PPARA, AND VARIANT SER-2457.
TISSUE=Testis;
PubMed=9627117; DOI=10.1038/sj.onc.1201783;
Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O.,
Pagliai K., Gray K., Gutkind S., Segars J.;
"Characterization of Brx, a novel Dbl family member that modulates
estrogen receptor action.";
Oncogene 16:2513-2526(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1827-2813 (ISOFORM 3), FUNCTION,
SUBCELLULAR LOCATION, DOMAIN, AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=9891067; DOI=10.1128/MCB.19.2.1334;
Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.-D.,
Knoll J.H.M., Urano T., Feig L.A., Toksoz D.;
"Activation of the Lbc Rho exchange factor proto-oncogene by
truncation of an extended C terminus that regulates transformation and
targeting.";
Mol. Cell. Biol. 19:1334-1345(1999).
[7]
ERRATUM.
Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.D., Knoll J.H.,
Urano T., Feig L.A., Toksoz D.;
Mol. Cell. Biol. 19:3930-3930(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1913-2335 (ISOFORM 3).
PubMed=8290273;
Toksoz D., Williams D.A.;
"Novel human oncogene lbc detected by transfection with distinct
homology regions to signal transduction products.";
Oncogene 9:621-628(1994).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 754-1768, INTERACTION WITH PKA
HOLOENZYME AND PRKAR2A, AND MUTAGENESIS OF ALA-1265.
TISSUE=Thyroid;
PubMed=1618839;
Carr D.W., Hausken Z.E., Fraser I.D.C., Stofko-Hahn R.E., Scott J.D.;
"Association of the type II cAMP-dependent protein kinase with a human
thyroid RII-anchoring protein. Cloning and characterization of the
RII-binding domain.";
J. Biol. Chem. 267:13376-13382(1992).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1486-2813 (ISOFORM 3), AND
VARIANT SER-2457.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
FUNCTION IN ACTIVATION OF ESR2.
PubMed=11579095; DOI=10.1074/jbc.M106927200;
Driggers P.H., Segars J.H., Rubino D.M.;
"The proto-oncoprotein Brx activates estrogen receptor beta by a p38
mitogen-activated protein kinase pathway.";
J. Biol. Chem. 276:46792-46797(2001).
[12]
INTERACTION WITH NME2.
PubMed=15249197; DOI=10.1016/j.bbrc.2004.06.067;
Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.;
"Lbc proto-oncogene product binds to and could be negatively regulated
by metastasis suppressor nm23-H2.";
Biochem. Biophys. Res. Commun. 320:1063-1068(2004).
[13]
FUNCTION, INTERACTION WITH YWHAB; YWHAZ AND PKA, PHOSPHORYLATION AT
SER-1565, AND MUTAGENESIS OF ALA-1251; ILE-1260 AND SER-1565.
PubMed=15229649; DOI=10.1038/sj.emboj.7600287;
Diviani D., Abuin L., Cotecchia S., Pansier L.;
"Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the
AKAP-Lbc signaling complex.";
EMBO J. 23:2811-2820(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1565, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH NR3C1 AND RHOA.
PubMed=16469733; DOI=10.1074/jbc.M509339200;
Kino T., Souvatzoglou E., Charmandari E., Ichijo T., Driggers P.,
Mayers C., Alatsatianos A., Manoli I., Westphal H., Chrousos G.P.,
Segars J.H.;
"Rho family Guanine nucleotide exchange factor Brx couples
extracellular signals to the glucocorticoid signaling system.";
J. Biol. Chem. 281:9118-9126(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2728, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
FUNCTION, AND INTERACTION WITH RHOA.
PubMed=17537920; DOI=10.1073/pnas.0701099104;
Appert-Collin A., Cotecchia S., Nenniger-Tosato M., Pedrazzini T.,
Diviani D.;
"The A-kinase anchoring protein (AKAP)-Lbc-signaling complex mediates
alpha1 adrenergic receptor-induced cardiomyocyte hypertrophy.";
Proc. Natl. Acad. Sci. U.S.A. 104:10140-10145(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1645; SER-1647;
SER-1876; SER-1929; SER-1932; SER-2398; SER-2703; SER-2709 AND
SER-2728, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1642; SER-1645;
SER-1647; SER-1876 AND SER-2728, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
FUNCTION, AND INTERACTION WITH KSR1; BRAF; PKA CATALYTIC SUBUNIT AND
PRKAR2A.
PubMed=21102438; DOI=10.1038/ncb2130;
Smith F.D., Langeberg L.K., Cellurale C., Pawson T., Morrison D.K.,
Davis R.J., Scott J.D.;
"AKAP-Lbc enhances cyclic AMP control of the ERK1/2 cascade.";
Nat. Cell Biol. 12:1242-1249(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; SER-983 AND
SER-1929, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
FUNCTION, INTERACTION WITH PKN1; YWHAB; MAPK14 AND ZAK, IDENTIFICATION
IN A COMPLEX WITH PKN1; MAPK14; MAP2K3 AND ZAK, REGION, AND
MUTAGENESIS OF SER-1565.
PubMed=21224381; DOI=10.1074/jbc.M110.185645;
Cariolato L., Cavin S., Diviani D.;
"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
complex involved in alpha1-adrenergic receptor-induced p38
activation.";
J. Biol. Chem. 286:7925-7937(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1642; SER-1645;
SER-1647; SER-1895; SER-1929; THR-1930; SER-1932; SER-2563 AND
SER-2728, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-815; SER-983; SER-1507;
SER-1876; SER-1929; SER-1932; THR-2467; SER-2709 AND SER-2728, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
FUNCTION, INTERACTION WITH IKBKB, AND MUTAGENESIS OF TRP-2324.
PubMed=23090968; DOI=10.1128/MCB.00887-12;
del Vescovo C.D., Cotecchia S., Diviani D.;
"A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support
interleukin-6-mediated cardiomyocyte hypertrophy.";
Mol. Cell. Biol. 33:14-27(2013).
[29]
FUNCTION.
PubMed=23716597; DOI=10.1128/MCB.00031-13;
Perez Lopez I., Cariolato L., Maric D., Gillet L., Abriel H.,
Diviani D.;
"A-kinase anchoring protein Lbc coordinates a p38 activating signaling
complex controlling compensatory cardiac hypertrophy.";
Mol. Cell. Biol. 33:2903-2917(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1489; SER-1540;
THR-2467; SER-2473 AND SER-2728, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1670, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[32]
STRUCTURE BY NMR OF 493-516 IN COMPLEX WITH PRKAR2A PEPTIDE, AND
INTERACTION WITH PRKAR2A.
PubMed=11285229; DOI=10.1093/emboj/20.7.1651;
Newlon M.G., Roy M., Morikis D., Carr D.W., Westphal R., Scott J.D.,
Jennings P.A.;
"A novel mechanism of PKA anchoring revealed by solution structures of
anchoring complexes.";
EMBO J. 20:1651-1662(2001).
[33]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1968-2338 IN COMPLEX WITH
RHOA, FUNCTION, INTERACTION WITH RHOA, DOMAIN, AND MUTAGENESIS OF
GLN-2148; LYS-2152 AND ASP-2189.
PubMed=25186459; DOI=10.1042/BJ20140606;
Abdul Azeez K.R., Knapp S., Fernandes J.M., Klussmann E., Elkins J.M.;
"The crystal structure of the RhoA-AKAP-Lbc DH-PH domain complex.";
Biochem. J. 464:231-239(2014).
[34]
STRUCTURE BY NMR OF 2164-2346, FUNCTION, INTERACTION WITH RHOA,
DOMAIN, AND MUTAGENESIS OF GLU-2001; ARG-2136; ARG-2289 AND PHE-2299.
PubMed=24993829; DOI=10.1074/jbc.M114.561787;
Lenoir M., Sugawara M., Kaur J., Ball L.J., Overduin M.;
"Structural insights into the activation of the RhoA GTPase by the
lymphoid blast crisis (Lbc) oncoprotein.";
J. Biol. Chem. 289:23992-24004(2014).
-!- FUNCTION: Scaffold protein that plays an important role in
assembling signaling complexes downstream of several types of G
protein-coupled receptors. Activates RHOA in response to signaling
via G protein-coupled receptors via its function as Rho guanine
nucleotide exchange factor (PubMed:11546812, PubMed:15229649,
PubMed:23090968, PubMed:25186459, PubMed:24993829). May also
activate other Rho family members (PubMed:11546812). Part of a
kinase signaling complex that links ADRA1A and ADRA1B adrenergic
receptor signaling to the activation of downstream p38 MAP
kinases, such as MAPK11 and MAPK14 (PubMed:17537920,
PubMed:23716597, PubMed:21224381). Part of a signaling complex
that links ADRA1B signaling to the activation of RHOA and
IKBKB/IKKB, leading to increased NF-kappa-B transcriptional
activity (PubMed:23090968). Part of a RHOA-dependent signaling
cascade that mediates responses to lysophosphatidic acid (LPA), a
signaling molecule that activates G-protein coupled receptors and
potentiates transcriptional activation of the glucocorticoid
receptor NR3C1 (PubMed:16469733). Part of a signaling cascade that
stimulates MEF2C-dependent gene expression in response to
lysophosphatidic acid (LPA) (By similarity). Part of a signaling
pathway that activates MAPK11 and/or MAPK14 and leads to increased
transcription activation of the estrogen receptors ESR1 and ESR2
(PubMed:9627117, PubMed:11579095). Part of a signaling cascade
that links cAMP and EGFR signaling to BRAF signaling and to PKA-
mediated phosphorylation of KSR1, leading to the activation of
downstream MAP kinases, such as MAPK1 or MAPK3 (PubMed:21102438).
Functions as scaffold protein that anchors cAMP-dependent protein
kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading
to increased phosphorylation of HDAC5 and ultimately cardiomyocyte
hypertrophy (By similarity). Has no guanine nucleotide exchange
activity on CDC42, Ras or Rac (PubMed:11546812). Required for
normal embryonic heart development, and in particular for normal
sarcomere formation in the developing cardiomyocytes (By
similarity). Plays a role in cardiomyocyte growth and cardiac
hypertrophy in response to activation of the beta-adrenergic
receptor by phenylephrine or isoproterenol (PubMed:17537920,
PubMed:23090968). Required for normal adaptive cardiac hypertrophy
in response to pressure overload (PubMed:23716597). Plays a role
in osteogenesis (By similarity). {ECO:0000250|UniProtKB:E9Q394,
ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:11579095,
ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:21224381,
ECO:0000269|PubMed:23716597, ECO:0000269|PubMed:24993829,
ECO:0000269|PubMed:25186459, ECO:0000269|PubMed:9627117,
ECO:0000269|PubMed:9891067}.
-!- SUBUNIT: Interacts with the cAMP-dependent protein kinase (PKA)
holoenzyme and with the regulatory subunit PRKAR2A
(PubMed:11546812, PubMed:1618839, PubMed:15229649,
PubMed:21102438, PubMed:11285229). Interacts with RHOA
(PubMed:11546812, PubMed:17537920, PubMed:25186459,
PubMed:24993829). Interacts also with RHOB and RHOC
(PubMed:11546812). Identified in a ternary complex with RHOA and
PRKAR2A (PubMed:11546812). Identified in a complex with NR3C1 and
RHOA (PubMed:16469733). Interacts with BRAF and KSR1
(PubMed:21102438). Identified in a complex with BRAF and KSR1
(PubMed:21102438). Component of a signaling complex containing at
least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex,
AKAP13 interacts directly with PKN1, which in turn recruits
MAPK14, MAP2K3 and ZAK (PubMed:21224381). Interacts
(phosphorylated form) with YWHAB and YWHAZ (PubMed:15229649,
PubMed:21224381). Interaction with YWHAB inhibits activation of
RHOA, interferes with PKN1 binding and activation of MAP kinases
(PubMed:15229649, PubMed:21224381). Interacts with GNA12
(PubMed:11546812). Interacts with IKBKB (PubMed:23090968).
Interacts with ESR1, THRA, PPARA and NME2 (PubMed:9627117,
PubMed:15249197). Interacts (via the C-terminal domain after the
PH domain) with MEF2C and RXRB. Interacts (via the C-terminal
domain after the PH domain) with PRKD1 (By similarity).
{ECO:0000250|UniProtKB:E9Q394, ECO:0000269|PubMed:11285229,
ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:11579095,
ECO:0000269|PubMed:15229649, ECO:0000269|PubMed:15249197,
ECO:0000269|PubMed:1618839, ECO:0000269|PubMed:17537920,
ECO:0000269|PubMed:21102438, ECO:0000269|PubMed:21224381,
ECO:0000269|PubMed:24993829, ECO:0000269|PubMed:25186459,
ECO:0000269|PubMed:9627117}.
-!- INTERACTION:
P03372:ESR1; NbExp=3; IntAct=EBI-1373806, EBI-78473;
P21980:TGM2; NbExp=4; IntAct=EBI-1373806, EBI-727668;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:9891067}.
Cytoplasm {ECO:0000269|PubMed:9627117}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:11546812}. Nucleus
{ECO:0000269|PubMed:9627117}. Membrane
{ECO:0000269|PubMed:11696353, ECO:0000269|PubMed:9891067};
Peripheral membrane protein {ECO:0000269|PubMed:11696353,
ECO:0000305|PubMed:9891067}. Note=Colocalizes with the actin
cytoskeleton at the cell cortex. {ECO:0000269|PubMed:11546812}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q12802-1; Sequence=Displayed;
Name=2;
IsoId=Q12802-2; Sequence=VSP_023490;
Name=3;
IsoId=Q12802-4; Sequence=VSP_023489, VSP_023491;
Name=4;
IsoId=Q12802-5; Sequence=VSP_023486, VSP_023487;
-!- TISSUE SPECIFICITY: Detected in mammary gland (PubMed:9627117).
Detected in heart (at protein level) (PubMed:11546812). Expressed
as a 5.3 kb transcript in hematopoietic cells, skeletal muscle,
lung, heart, estrogen-responsive reproductive tissues, including
breast ductal epithelium. Also found in testis and breast cancer
cell lines. Predominantly expressed as a 10 kb transcript in the
heart and at lower levels in the lung, placenta, kidney, pancreas,
skeletal muscle and liver. Transcripts of between 6-9 kb are also
expressed in myeloid and lymphoid lineages, a variety of
epithelial tissues, and in skeletal muscle.
{ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:9627117,
ECO:0000269|PubMed:9891067}.
-!- DOMAIN: The DH domain is sufficient for interaction with RHOA, and
for guanine nucleotide exchange (GEF) activity with RHOA
(PubMed:24993829). Forms that lack C-terminal regulatory domains
have transforming activity and function as oncogenes
(PubMed:9891067). {ECO:0000269|PubMed:24993829,
ECO:0000269|PubMed:9891067, ECO:0000305|PubMed:25186459}.
-!- DOMAIN: The PH domain does not play a role in lipid-binding.
Instead, it inhibits the guanine nucleotide exchange (GEF)
activity of the isolated DH domain (in vitro).
{ECO:0000269|PubMed:24993829}.
-!- DOMAIN: The C-terminal domain after the PH domain is involved in
protein-protein interactions that are required for normal,
compensatory cardiac hypertrophy in response to pressure overload.
{ECO:0000250|UniProtKB:E9Q394}.
-!- SEQUENCE CAUTION:
Sequence=AAC50065.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC50065.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=AAD21311.1; Type=Frameshift; Positions=2614, 2647; Evidence={ECO:0000305};
Sequence=AAD40799.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD40799.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAL40923.1; Type=Frameshift; Positions=2614, 2647; Evidence={ECO:0000305};
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EMBL; AF387101; AAL40923.1; ALT_FRAME; mRNA.
EMBL; AF406992; AAL11723.1; -; mRNA.
EMBL; AB055890; BAB62913.1; -; mRNA.
EMBL; BC050312; AAH50312.1; -; mRNA.
EMBL; AF126008; AAD21311.1; ALT_FRAME; mRNA.
EMBL; AF127481; AAD40799.1; ALT_SEQ; mRNA.
EMBL; U03634; AAC50065.1; ALT_SEQ; mRNA.
EMBL; M90360; AAA58670.1; ALT_TERM; mRNA.
EMBL; AB209414; BAD92651.1; -; mRNA.
CCDS; CCDS32319.1; -. [Q12802-1]
CCDS; CCDS32320.1; -. [Q12802-2]
PIR; A42915; A42915.
PIR; I38434; I38434.
RefSeq; NP_001257475.1; NM_001270546.1.
RefSeq; NP_006729.4; NM_006738.5. [Q12802-2]
RefSeq; NP_009131.2; NM_007200.4. [Q12802-1]
UniGene; Hs.459211; -.
UniGene; Hs.710656; -.
PDB; 2DRN; NMR; -; C=1246-1269.
PDB; 2LG1; NMR; -; A=2164-2346.
PDB; 4D0N; X-ray; 2.10 A; B=1968-2338.
PDB; 4D0O; X-ray; 2.75 A; A/B=1972-2207.
PDB; 6BCA; X-ray; 2.00 A; A/B=2193-2333.
PDBsum; 2DRN; -.
PDBsum; 2LG1; -.
PDBsum; 4D0N; -.
PDBsum; 4D0O; -.
PDBsum; 6BCA; -.
ProteinModelPortal; Q12802; -.
SMR; Q12802; -.
BioGrid; 116383; 36.
CORUM; Q12802; -.
DIP; DIP-180N; -.
IntAct; Q12802; 28.
MINT; Q12802; -.
STRING; 9606.ENSP00000354718; -.
iPTMnet; Q12802; -.
PhosphoSitePlus; Q12802; -.
BioMuta; AKAP13; -.
DMDM; 134048676; -.
EPD; Q12802; -.
jPOST; Q12802; -.
MaxQB; Q12802; -.
PaxDb; Q12802; -.
PeptideAtlas; Q12802; -.
PRIDE; Q12802; -.
ProteomicsDB; 58955; -.
ProteomicsDB; 58956; -. [Q12802-2]
ProteomicsDB; 58957; -. [Q12802-4]
ProteomicsDB; 58958; -. [Q12802-5]
Ensembl; ENST00000361243; ENSP00000354718; ENSG00000170776. [Q12802-2]
Ensembl; ENST00000394518; ENSP00000378026; ENSG00000170776. [Q12802-1]
Ensembl; ENST00000560302; ENSP00000453634; ENSG00000170776. [Q12802-5]
GeneID; 11214; -.
KEGG; hsa:11214; -.
UCSC; uc002bls.5; human. [Q12802-1]
CTD; 11214; -.
DisGeNET; 11214; -.
EuPathDB; HostDB:ENSG00000170776.19; -.
GeneCards; AKAP13; -.
H-InvDB; HIX0021561; -.
H-InvDB; HIX0172808; -.
HGNC; HGNC:371; AKAP13.
HPA; HPA019773; -.
MIM; 604686; gene.
neXtProt; NX_Q12802; -.
OpenTargets; ENSG00000170776; -.
PharmGKB; PA24665; -.
eggNOG; KOG3520; Eukaryota.
eggNOG; COG5422; LUCA.
GeneTree; ENSGT00940000154146; -.
HOVERGEN; HBG080828; -.
InParanoid; Q12802; -.
KO; K16529; -.
OMA; HRELDVY; -.
OrthoDB; 69816at2759; -.
PhylomeDB; Q12802; -.
TreeFam; TF325887; -.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
SignaLink; Q12802; -.
SIGNOR; Q12802; -.
ChiTaRS; AKAP13; human.
EvolutionaryTrace; Q12802; -.
GeneWiki; AKAP13; -.
GenomeRNAi; 11214; -.
PRO; PR:Q12802; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000170776; Expressed in 242 organ(s), highest expression level in tendon of biceps brachii.
ExpressionAtlas; Q12802; baseline and differential.
Genevisible; Q12802; HS.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:InterPro.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
GO; GO:0032947; F:protein-containing complex scaffold activity; IDA:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; IPI:UniProtKB.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0086023; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISS:UniProtKB.
GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060348; P:bone development; ISS:UniProtKB.
GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEA:Ensembl.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0051168; P:nuclear export; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
GO; GO:1900169; P:regulation of glucocorticoid mediated signaling pathway; IEA:Ensembl.
GO; GO:0060297; P:regulation of sarcomere organization; ISS:UniProtKB.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR028852; AKAP13.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR018459; RII_binding_1.
PANTHER; PTHR13944:SF18; PTHR13944:SF18; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF10522; RII_binding_1; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 2813 A-kinase anchor protein 13.
/FTId=PRO_0000080963.
DOMAIN 1994 2191 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 2231 2333 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 1791 1838 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 494 516 Important for interaction with PRKAR2A.
REGION 1585 1715 Important for interaction with MAP2K3.
{ECO:0000269|PubMed:21224381}.
REGION 1919 2813 Interaction with ESR1.
{ECO:0000269|PubMed:9627117}.
COILED 1758 1790 {ECO:0000255}.
COILED 2345 2381 {ECO:0000255}.
COILED 2568 2683 {ECO:0000255}.
COMPBIAS 1471 1474 Poly-Ser.
COMPBIAS 1534 1537 Poly-Glu.
COMPBIAS 2778 2790 Poly-Lys.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 815 815 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 953 953 Phosphothreonine.
{ECO:0000250|UniProtKB:E9Q394}.
MOD_RES 983 983 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1489 1489 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1507 1507 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1540 1540 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1565 1565 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000269|PubMed:15229649}.
MOD_RES 1602 1602 Phosphoserine.
{ECO:0000250|UniProtKB:F1M3G7}.
MOD_RES 1642 1642 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1645 1645 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1647 1647 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1670 1670 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1876 1876 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1895 1895 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1929 1929 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1930 1930 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1932 1932 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1945 1945 Phosphoserine.
{ECO:0000250|UniProtKB:F1M3G7}.
MOD_RES 2345 2345 Phosphoserine.
{ECO:0000250|UniProtKB:F1M3G7}.
MOD_RES 2398 2398 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2467 2467 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2473 2473 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2563 2563 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 2566 2566 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q394}.
MOD_RES 2703 2703 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2709 2709 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2728 2728 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 160 179 DAGPRETLMHFAVRLGLLRL -> GENLYDLQTHFKFVIFL
LFF (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023486.
VAR_SEQ 180 2813 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023487.
VAR_SEQ 1581 1598 Missing (in isoform 3).
{ECO:0000303|PubMed:8290273,
ECO:0000303|PubMed:9891067,
ECO:0000303|Ref.10}.
/FTId=VSP_023489.
VAR_SEQ 1583 1598 SMRVLGDVVRRPPIHR -> MSWCPSGVQYSAGLSADFNY
(in isoform 2).
{ECO:0000303|PubMed:11546812}.
/FTId=VSP_023490.
VAR_SEQ 1950 1951 Missing (in isoform 3).
{ECO:0000303|PubMed:8290273,
ECO:0000303|PubMed:9891067,
ECO:0000303|Ref.10}.
/FTId=VSP_023491.
VARIANT 452 452 M -> T (in dbSNP:rs2061821).
{ECO:0000269|Ref.3}.
/FTId=VAR_030925.
VARIANT 494 494 W -> R (in dbSNP:rs2061822).
{ECO:0000269|Ref.3}.
/FTId=VAR_030926.
VARIANT 526 526 K -> Q (in dbSNP:rs34434221).
/FTId=VAR_051986.
VARIANT 574 574 R -> C (in dbSNP:rs2061824).
{ECO:0000269|PubMed:11696353,
ECO:0000269|Ref.3}.
/FTId=VAR_030927.
VARIANT 624 624 G -> V (in dbSNP:rs745191).
{ECO:0000269|PubMed:11546812}.
/FTId=VAR_030928.
VARIANT 689 689 E -> K (in dbSNP:rs7177107).
{ECO:0000269|Ref.3}.
/FTId=VAR_030929.
VARIANT 845 845 V -> A (in dbSNP:rs4075256).
{ECO:0000269|Ref.3}.
/FTId=VAR_030930.
VARIANT 897 897 V -> M (in dbSNP:rs4075254).
{ECO:0000269|PubMed:11546812,
ECO:0000269|Ref.3}.
/FTId=VAR_030931.
VARIANT 1062 1062 P -> A (in dbSNP:rs4843074).
{ECO:0000269|Ref.3}.
/FTId=VAR_030932.
VARIANT 1086 1086 D -> N (in dbSNP:rs4843075).
{ECO:0000269|Ref.3}.
/FTId=VAR_030933.
VARIANT 1216 1216 M -> T (in dbSNP:rs7162168).
{ECO:0000269|Ref.3}.
/FTId=VAR_030934.
VARIANT 1525 1525 S -> G (in dbSNP:rs35079107).
/FTId=VAR_051987.
VARIANT 2457 2457 G -> S (in dbSNP:rs2241268).
{ECO:0000269|PubMed:11546812,
ECO:0000269|PubMed:11696353,
ECO:0000269|PubMed:9627117,
ECO:0000269|Ref.10}.
/FTId=VAR_030935.
VARIANT 2801 2801 A -> T (in dbSNP:rs2614668).
/FTId=VAR_030936.
MUTAGEN 1251 1251 A->P: Abolishes interaction with PRKAR2A
and leads to constitutive activation of
RHOA; when associated with P-1260.
{ECO:0000269|PubMed:11546812,
ECO:0000269|PubMed:15229649}.
MUTAGEN 1260 1260 I->P: Abolishes interaction with
PRKAR2Aand leads to constitutive
activation of RHOA; when associated with
P-1251. {ECO:0000269|PubMed:11546812,
ECO:0000269|PubMed:15229649}.
MUTAGEN 1265 1265 A->P: Abolishes interaction with PRKAR2A.
{ECO:0000269|PubMed:1618839}.
MUTAGEN 1565 1565 S->A: Abolishes interaction with YWHAB,
leading to constitutive activation of
RHOA and MAPK14.
{ECO:0000269|PubMed:15229649,
ECO:0000269|PubMed:21224381}.
MUTAGEN 2001 2001 E->A: Decreases guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:24993829}.
MUTAGEN 2136 2136 R->G: Decreases guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:24993829}.
MUTAGEN 2148 2148 Q->Y: Abolishes guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:25186459}.
MUTAGEN 2152 2152 K->Y: Abolishes guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:25186459}.
MUTAGEN 2153 2153 Y->F: Loss of guanyl nucleotide exchange
activity toward RHOA.
{ECO:0000269|PubMed:11546812}.
MUTAGEN 2189 2189 D->A: Reduces guanyl nucleotide exchange
activity toward RHOA.
{ECO:0000269|PubMed:25186459}.
MUTAGEN 2189 2189 D->Y: Abolishes guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:25186459}.
MUTAGEN 2289 2289 R->A: Decreases guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:24993829}.
MUTAGEN 2299 2299 F->A: Decreases guanyl nucleotide
exchange activity toward RHOA.
{ECO:0000269|PubMed:24993829}.
MUTAGEN 2324 2324 W->L: Impairs interaction with IKBKB.
{ECO:0000269|PubMed:23090968}.
CONFLICT 191 191 G -> R (in Ref. 1; AAL40923).
{ECO:0000305}.
CONFLICT 354 354 C -> R (in Ref. 1; AAL40923).
{ECO:0000305}.
CONFLICT 609 609 A -> V (in Ref. 1; AAL40923).
{ECO:0000305}.
CONFLICT 614 614 A -> T (in Ref. 1; AAL40923).
{ECO:0000305}.
CONFLICT 618 618 S -> P (in Ref. 1; AAL40923).
{ECO:0000305}.
CONFLICT 619 619 D -> A (in Ref. 2; AAL11723).
{ECO:0000305}.
CONFLICT 755 755 M -> S (in Ref. 9; AAA58670).
{ECO:0000305}.
CONFLICT 1385 1387 TQA -> MLY (in Ref. 5; AAD21311).
{ECO:0000305}.
CONFLICT 1547 1547 N -> H (in Ref. 10; BAD92651).
{ECO:0000305}.
CONFLICT 1766 1768 EKE -> KKK (in Ref. 9; AAA58670).
{ECO:0000305}.
CONFLICT 1877 1877 A -> G (in Ref. 6; AAD40799).
{ECO:0000305}.
CONFLICT 1897 1897 Q -> E (in Ref. 6; AAD40799).
{ECO:0000305}.
CONFLICT 2035 2035 V -> D (in Ref. 5; AAD21311).
{ECO:0000305}.
CONFLICT 2488 2488 D -> G (in Ref. 5; AAD21311).
{ECO:0000305}.
CONFLICT 2667 2668 QL -> HV (in Ref. 3; BAB62913 and 5;
AAD21311). {ECO:0000305}.
HELIX 1248 1263 {ECO:0000244|PDB:2DRN}.
TURN 1264 1268 {ECO:0000244|PDB:2DRN}.
STRAND 1973 1975 {ECO:0000244|PDB:4D0N}.
HELIX 1976 1979 {ECO:0000244|PDB:4D0N}.
HELIX 1982 1986 {ECO:0000244|PDB:4D0N}.
HELIX 1990 2018 {ECO:0000244|PDB:4D0N}.
HELIX 2020 2027 {ECO:0000244|PDB:4D0N}.
HELIX 2032 2038 {ECO:0000244|PDB:4D0N}.
HELIX 2042 2061 {ECO:0000244|PDB:4D0N}.
HELIX 2078 2084 {ECO:0000244|PDB:4D0N}.
HELIX 2087 2117 {ECO:0000244|PDB:4D0N}.
HELIX 2119 2131 {ECO:0000244|PDB:4D0N}.
HELIX 2135 2137 {ECO:0000244|PDB:4D0N}.
HELIX 2139 2149 {ECO:0000244|PDB:4D0N}.
HELIX 2150 2152 {ECO:0000244|PDB:4D0N}.
HELIX 2153 2163 {ECO:0000244|PDB:4D0N}.
TURN 2166 2168 {ECO:0000244|PDB:2LG1}.
STRAND 2177 2181 {ECO:0000244|PDB:2LG1}.
TURN 2182 2184 {ECO:0000244|PDB:2LG1}.
HELIX 2186 2191 {ECO:0000244|PDB:2LG1}.
HELIX 2194 2207 {ECO:0000244|PDB:6BCA}.
STRAND 2213 2215 {ECO:0000244|PDB:6BCA}.
STRAND 2221 2223 {ECO:0000244|PDB:6BCA}.
HELIX 2224 2227 {ECO:0000244|PDB:6BCA}.
STRAND 2232 2241 {ECO:0000244|PDB:6BCA}.
STRAND 2247 2265 {ECO:0000244|PDB:6BCA}.
STRAND 2268 2271 {ECO:0000244|PDB:6BCA}.
STRAND 2275 2277 {ECO:0000244|PDB:2LG1}.
STRAND 2279 2283 {ECO:0000244|PDB:6BCA}.
STRAND 2286 2290 {ECO:0000244|PDB:6BCA}.
STRAND 2297 2302 {ECO:0000244|PDB:6BCA}.
STRAND 2304 2307 {ECO:0000244|PDB:4D0N}.
STRAND 2309 2314 {ECO:0000244|PDB:6BCA}.
HELIX 2318 2332 {ECO:0000244|PDB:6BCA}.
SEQUENCE 2813 AA; 307550 MW; 6A8FDAC9A3D3B1F2 CRC64;
MKLNPQQAPL YGDCVVTVLL AEEDKAEDDV VFYLVFLGST LRHCTSTRKV SSDTLETIAP
GHDCCETVKV QLCASKEGLP VFVVAEEDFH FVQDEAYDAA QFLATSAGNQ QALNFTRFLD
QSGPPSGDVN SLDKKLVLAF RHLKLPTEWN VLGTDQSLHD AGPRETLMHF AVRLGLLRLT
WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG
DCSVRHHREL DIYTLTSESD SHHEHPFPGD GCTGPIFKLM NIQQQLMKTN LKQMDSLMPL
MMTAQDPSSA PETDGQFLPC APEPTDPQRL SSSEETESTQ CCPGSPVAQT ESPCDLSSIV
EEENTDRSCR KKNKGVERKG EEVEPAPIVD SGTVSDQDSC LQSLPDCGVK GTEGLSSCGN
RNEETGTKSS GMPTDQESLS SGDAVLQRDL VMEPGTAQYS SGGELGGIST TNVSTPDTAG
EMEHGLMNPD ATVWKNVLQG GESTKERFEN SNIGTAGASD VHVTSKPVDK ISVPNCAPAA
SSLDGNKPAE SSLAFSNEET STEKTAETET SRSREESADA PVDQNSVVIP AAAKDKISDG
LEPYTLLAAG IGEAMSPSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS PICSTTGDDK
LCADSACQQN TVTSSGDLVA KLCDNIVSES ESTTARQPSS QDPPDASHCE DPQAHTVTSD
PVRDTQERAD FCPFKVVDNK GQRKDVKLDK PLTNMLEVVS HPHPVVPKME KELVPDQAVI
SDSTFSLANS PGSESVTKDD ALSFVPSQKE KGTATPELHT ATDYRDGPDG NSNEPDTRPL
EDRAVGLSTS STAAELQHGM GNTSLTGLGG EHEGPAPPAI PEALNIKGNT DSSLQSVGKA
TLALDSVLTE EGKLLVVSES SAAQEQDKDK AVTCSSIKEN ALSSGTLQEE QRTPPPGQDT
QQFHEKSISA DCAKDKALQL SNSPGASSAF LKAETEHNKE VAPQVSLLTQ GGAAQSLVPP
GASLATESRQ EALGAEHNSS ALLPCLLPDG SDGSDALNCS QPSPLDVGVK NTQSQGKTSA
CEVSGDVTVD VTGVNALQGM AEPRRENISH NTQDILIPNV LLSQEKNAVL GLPVALQDKA
VTDPQGVGTP EMIPLDWEKG KLEGADHSCT MGDAEEAQID DEAHPVLLQP VAKELPTDME
LSAHDDGAPA GVREVMRAPP SGRERSTPSL PCMVSAQDAP LPKGADLIEE AASRIVDAVI
EQVKAAGALL TEGEACHMSL SSPELGPLTK GLESAFTEKV STFPPGESLP MGSTPEEATG
SLAGCFAGRE EPEKIILPVQ GPEPAAEMPD VKAEDEVDFR ASSISEEVAV GSIAATLKMK
QGPMTQAINR ENWCTIEPCP DAASLLASKQ SPECENFLDV GLGRECTSKQ GVLKRESGSD
SDLFHSPSDD MDSIIFPKPE EEHLACDITG SSSSTDDTAS LDRHSSHGSD VSLSQILKPN
RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS ITEVPANCSV LRSSMRSLSP
FRRHSWGPGK NAASDAEMNH RSSMRVLGDV VRRPPIHRRS FSLEGLTGGA GVGNKPSSSL
EVSSANAEEL RHPFSGEERV DSLVSLSEED LESDQREHRM FDQQICHRSK QQGFNYCTSA
ISSPLTKSIS LMTISHPGLD NSRPFHSTFH NTSANLTESI TEENYNFLPH SPSKKDSEWK
SGTKVSRTFS YIKNKMSSSK KSKEKEKEKD KIKEKEKDSK DKEKDKKTVN GHTFSSIPVV
GPISCSQCMK PFTNKDAYTC ANCSAFVHKG CRESLASCAK VKMKQPKGSL QAHDTSSLPT
VIMRNKPSQP KERPRSAVLL VDETATTPIF ANRRSQQSVS LSKSVSIQNI TGVGNDENMS
NTWKFLSHST DSLNKISKVN ESTESLTDEG VGTDMNEGQL LGDFEIESKQ LEAESWSRII
DSKFLKQQKK DVVKRQEVIY ELMQTEFHHV RTLKIMSGVY SQGMMADLLF EQQMVEKLFP
CLDELISIHS QFFQRILERK KESLVDKSEK NFLIKRIGDV LVNQFSGENA ERLKKTYGKF
CGQHNQSVNY FKDLYAKDKR FQAFVKKKMS SSVVRRLGIP ECILLVTQRI TKYPVLFQRI
LQCTKDNEVE QEDLAQSLSL VKDVIGAVDS KVASYEKKVR LNEIYTKTDS KSIMRMKSGQ
MFAKEDLKRK KLVRDGSVFL KNAAGRLKEV QAVLLTDILV FLQEKDQKYI FASLDQKSTV
ISLKKLIVRE VAHEEKGLFL ISMGMTDPEM VEVHASSKEE RNSWIQIIQD TINTLNRDED
EGIPSENEEE KKMLDTRARE LKEQLHQKDQ KILLLLEEKE MIFRDMAECS TPLPEDCSPT
HSPRVLFRSN TEEALKGGPL MKSAINEVEI LQGLVSGNLG GTLGPTVSSP IEQDVVGPVS
LPRRAETFGG FDSHQMNASK GGEKEEGDDG QDLRRTESDS GLKKGGNANL VFMLKRNSEQ
VVQSVVHLYE LLSALQGVVL QQDSYIEDQK LVLSERALTR SLSRPSSLIE QEKQRSLEKQ
RQDLANLQKQ QAQYLEEKRR REREWEARER ELREREALLA QREEEVQQGQ QDLEKEREEL
QQKKGTYQYD LERLRAAQKQ LEREQEQLRR EAERLSQRQT ERDLCQVSHP HTKLMRIPSF
FPSPEEPPSP SAPSIAKSGS LDSELSVSPK RNSISRTHKD KGPFHILSST SQTNKGPEGQ
SQAPASTSAS TRLFGLTKPK EKKEKKKKNK TSRSQPGDGP ASEVSAEGEE IFC


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Kits Elisa; taq POLYMERASE

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