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Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein)

 AEBP1_MOUSE             Reviewed;        1128 AA.
Q640N1; O88442; Q3TVV5; Q3TWA7; Q3TX56; Q3TXB2; Q5NCI9; Q61281;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
05-JUL-2017, entry version 117.
RecName: Full=Adipocyte enhancer-binding protein 1;
Short=AE-binding protein 1;
AltName: Full=Aortic carboxypeptidase-like protein;
Flags: Precursor;
Name=Aebp1; Synonyms=Aclp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=7477299; DOI=10.1038/378092a0;
He G.-P., Muise A.M., Li A.W., Ro H.-S.;
"A eukaryotic transcriptional repressor with carboxypeptidase
activity.";
Nature 378:92-96(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9624159; DOI=10.1074/jbc.273.25.15654;
Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T.,
Perrella M.A., Blanar M.A., Haber E., Lee M.-E.;
"Aortic carboxypeptidase-like protein, a novel protein with discoidin
and carboxypeptidase-like domains, is up-regulated during vascular
smooth muscle cell differentiation.";
J. Biol. Chem. 273:15654-15660(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Eye;
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).
[6]
DEVELOPMENTAL STAGE.
PubMed=8920928; DOI=10.1006/bbrc.1996.1675;
Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K.,
Okubo K.;
"A cDNA cloning of human AEBP1 from primary cultured osteoblasts and
its expression in a differentiating osteoblastic cell line.";
Biochem. Biophys. Res. Commun. 228:411-414(1996).
[7]
FUNCTION, DNA-BINDING, AND INTERACTION WITH GNG5.
PubMed=10406805; DOI=10.1093/emboj/18.14.4004;
Park J.-G., Muise A.M., He G.-P., Kim S.-W., Ro H.-S.;
"Transcriptional regulation by the gamma5 subunit of a heterotrimeric
G protein during adipogenesis.";
EMBO J. 18:4004-4012(1999).
[8]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=11738825; DOI=10.1016/S0378-1119(01)00771-5;
Ro H.-S., Kim S.-W., Wu D., Webber C., Nicholson T.E.;
"Gene structure and expression of the mouse adipocyte enhancer-binding
protein.";
Gene 280:123-133(2001).
[9]
FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, AND DEVELOPMENTAL STAGE.
PubMed=11152475; DOI=10.1074/jbc.M010640200;
Kim S.-W., Muise A.M., Lyons P.J., Ro H.-S.;
"Regulation of adipogenesis by a transcriptional repressor that
modulates MAPK activation.";
J. Biol. Chem. 276:10199-10206(2001).
[10]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL
STAGE, AND TISSUE SPECIFICITY.
PubMed=11438679; DOI=10.1128/MCB.21.15.5256-5261.2001;
Layne M.D., Yet S.-F., Maemura K., Hsieh C.-M., Bernfield M.,
Perrella M.A., Lee M.-E.;
"Impaired abdominal wall development and deficient wound healing in
mice lacking aortic carboxypeptidase-like protein.";
Mol. Cell. Biol. 21:5256-5261(2001).
[11]
DEVELOPMENTAL STAGE.
PubMed=12072377; DOI=10.1210/endo.143.7.8875;
Gagnon A., Abaiian K.J., Crapper T., Layne M.D., Sorisky A.;
"Down-regulation of aortic carboxypeptidase-like protein during the
early phase of 3T3-L1 adipogenesis.";
Endocrinology 143:2478-2485(2002).
[12]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=14729459; DOI=10.1016/j.yexcr.2003.10.020;
Abderrahim-Ferkoune A., Bezy O., Astri-Roques S., Elabd C.,
Ailhaud G., Amri E.-Z.;
"Transdifferentiation of preadipose cells into smooth muscle-like
cells: role of aortic carboxypeptidase-like protein.";
Exp. Cell Res. 293:219-228(2004).
[13]
DNA-BINDING, MUTAGENESIS OF THR-1003, AND PHOSPHORYLATION.
PubMed=15654748; DOI=10.1021/bi0480178;
Lyons P.J., Muise A.M., Ro H.-S.;
"MAPK modulates the DNA binding of adipocyte enhancer-binding protein
1.";
Biochemistry 44:926-931(2005).
[14]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=15927179; DOI=10.1016/j.yexcr.2005.04.031;
Gagnon A., Landry A., Proulx J., Layne M.D., Sorisky A.;
"Aortic carboxypeptidase-like protein is regulated by transforming
growth factor beta in 3T3-L1 preadipocytes.";
Exp. Cell Res. 308:265-272(2005).
[15]
DEVELOPMENTAL STAGE.
PubMed=15749083; DOI=10.1016/j.modgep.2004.11.002;
Ith B., Wei J., Yet S.-F., Perrella M.A., Layne M.D.;
"Aortic carboxypeptidase-like protein is expressed in collagen-rich
tissues during mouse embryonic development.";
Gene Expr. Patterns 5:533-537(2005).
[16]
FUNCTION, AND INDUCTION.
PubMed=16307171; DOI=10.2119/2006-00021.Ro;
Zhang L., Reidy S.P., Nicholson T.E., Lee H.-J., Majdalawieh A.,
Webber C., Stewart B.R., Dolphin P., Ro H.-S.;
"The role of AEBP1 in sex-specific diet-induced obesity.";
Mol. Med. 11:39-47(2005).
[17]
FUNCTION, AND DNA-BINDING.
PubMed=16461908; DOI=10.1073/pnas.0508139103;
Majdalawieh A., Zhang L., Fuki I.V., Rader D.J., Ro H.-S.;
"Adipocyte enhancer-binding protein 1 is a potential novel atherogenic
factor involved in macrophage cholesterol homeostasis and
inflammation.";
Proc. Natl. Acad. Sci. U.S.A. 103:2346-2351(2006).
[18]
FUNCTION, DNA-BINDING, AND INTERACTION WITH CALMODULIN.
PubMed=16538615; DOI=10.1002/prot.20946;
Lyons P.J., Mattatall N.R., Ro H.-S.;
"Modeling and functional analysis of AEBP1, a transcriptional
repressor.";
Proteins 63:1069-1083(2006).
[19]
FUNCTION, INTERACTION WITH NFKBIA, AND SUBCELLULAR LOCATION.
PubMed=17202411; DOI=10.1091/mbc.E06-03-0217;
Majdalawieh A., Zhang L., Ro H.-S.;
"Adipocyte enhancer-binding protein-1 promotes macrophage inflammatory
responsiveness by up-regulating NF-kappaB via IkappaBalpha negative
regulation.";
Mol. Biol. Cell 18:930-942(2007).
[20]
DISRUPTION PHENOTYPE, AND INTERACTION WITH PTEN.
PubMed=17299101; DOI=10.1038/oby.2007.569;
Ro H.-S., Zhang L., Majdalawieh A., Kim S.-W., Wu X., Lyons P.J.,
Webber C., Ma H., Reidy S.P., Boudreau A., Miller J.R., Mitchell P.,
McLeod R.S.;
"Adipocyte enhancer-binding protein 1 modulates adiposity and energy
homeostasis.";
Obesity 15:288-302(2007).
-!- FUNCTION: Isoform 2 may positively regulate MAP-kinase activity in
adipocytes, leading to enhanced adipocyte proliferation and
reduced adipocyte differentiation. Isoform 2 may also positively
regulate NF-kappa-B activity in macrophages by promoting the
phosphorylation and subsequent degradation of I-kappa-B-alpha
(NFKBIA), leading to enhanced macrophage inflammatory
responsiveness. Can act as a transcriptional repressor.
{ECO:0000269|PubMed:10406805, ECO:0000269|PubMed:11152475,
ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:14729459,
ECO:0000269|PubMed:16307171, ECO:0000269|PubMed:16461908,
ECO:0000269|PubMed:16538615, ECO:0000269|PubMed:17202411,
ECO:0000269|PubMed:7477299}.
-!- SUBUNIT: Isoform 2 interacts with GNG5, NFKBIA, MAPK1, MAPK3 and
PTEN. Interaction with MAPK1 may stimulate DNA-binding. May
interact with calmodulin. Binds to DNA in vitro.
{ECO:0000269|PubMed:10406805, ECO:0000269|PubMed:11152475,
ECO:0000269|PubMed:16538615, ECO:0000269|PubMed:17202411,
ECO:0000269|PubMed:17299101}.
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted
{ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:15927179}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:9624159}. Nucleus
{ECO:0000269|PubMed:17202411}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Aclp;
IsoId=Q640N1-1; Sequence=Displayed;
Name=2; Synonyms=Aebp1;
IsoId=Q640N1-2; Sequence=VSP_033470;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
adipose tissue, brain, heart, kidney, liver, lung, skeletal
muscle, small intestine, spleen and testis. Isoform 2 is expressed
in macrophages. Expressed in aorta, preadipocytes, adipocyte
tissue, brain, heart, liver, lung, skeletal muscle, skin and
spleen (at protein level). {ECO:0000269|PubMed:11438679,
ECO:0000269|PubMed:11738825, ECO:0000269|PubMed:9624159}.
-!- DEVELOPMENTAL STAGE: Expressed in the somites and dorsa from E9.5
and in the yolk sac and embryonic vasculature from E10.5.
Expression within the large and small blood vessels increases at
E11.5 and E13.5, with high expression in the vascular smooth
muscle at E16.5. Also expressed later in development in
mesenchymal cells in the dermal layer, the developing skeleton,
connective tissue and the umbilical ring and vessels. Up-regulated
during vascular smooth muscle cell differentiation and down-
regulated during adipocyte differentiation and osteoblast
differentiation. {ECO:0000269|PubMed:11152475,
ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:12072377,
ECO:0000269|PubMed:14729459, ECO:0000269|PubMed:15749083,
ECO:0000269|PubMed:15927179, ECO:0000269|PubMed:7477299,
ECO:0000269|PubMed:8920928, ECO:0000269|PubMed:9624159}.
-!- INDUCTION: By TGF-beta. Expression is also induced by a high fat
diet. {ECO:0000269|PubMed:15927179, ECO:0000269|PubMed:16307171}.
-!- PTM: Phosphorylated by MAPK1 in vitro.
{ECO:0000269|PubMed:15654748}.
-!- DISRUPTION PHENOTYPE: Two independent knockout mice have been
generated for the gene encoding this protein, and these exhibit
different phenotypes. Mice lacking exons 7-12 exhibit reduced
growth rate and body weight and resistance to dietary-induced
obesity. Individual adipocytes from these animals are
hypoproliferative while the adipose tissue is prone to apoptosis.
Mice lacking exons 7-16 die perinatally from gastroschisis, in
which abdominal viscera are extruded through the ventral body
wall. Surviving mice exhibit deficient wound healing, having
dermal fibroblasts with reduced proliferative capacity. Mice
lacking exons 7-16 may exhibit phenotypes arising from effects on
the locus encoding Pold2, which lies immediately downstream of
this locus. {ECO:0000269|PubMed:11438679,
ECO:0000269|PubMed:17299101}.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
-!- CAUTION: Although related to peptidase M14 family, lacks the
active site residues and zinc-binding sites, suggesting that it
has no carboxypeptidase activity. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA56648.1; Type=Frameshift; Positions=406; Evidence={ECO:0000305};
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EMBL; X80478; CAA56648.1; ALT_FRAME; mRNA.
EMBL; AF053943; AAC25584.1; -; mRNA.
EMBL; AK159330; BAE34995.1; -; mRNA.
EMBL; AK159342; BAE35004.1; -; mRNA.
EMBL; AK159377; BAE35033.1; -; mRNA.
EMBL; AK159409; BAE35060.1; -; mRNA.
EMBL; AK159774; BAE35359.1; -; mRNA.
EMBL; AK159957; BAE35513.1; -; mRNA.
EMBL; AL627069; CAI25440.1; -; Genomic_DNA.
EMBL; AL627069; CAI25441.1; -; Genomic_DNA.
EMBL; BC082577; AAH82577.1; -; mRNA.
CCDS; CCDS24406.1; -. [Q640N1-1]
PIR; S60227; S51739.
RefSeq; NP_001278786.1; NM_001291857.2.
RefSeq; NP_033766.2; NM_009636.3. [Q640N1-1]
UniGene; Mm.271178; -.
UniGene; Mm.3317; -.
UniGene; Mm.4665; -.
ProteinModelPortal; Q640N1; -.
SMR; Q640N1; -.
BioGrid; 198013; 2.
STRING; 10090.ENSMUSP00000099987; -.
MEROPS; M14.951; -.
iPTMnet; Q640N1; -.
PhosphoSitePlus; Q640N1; -.
PaxDb; Q640N1; -.
PeptideAtlas; Q640N1; -.
PRIDE; Q640N1; -.
Ensembl; ENSMUST00000102923; ENSMUSP00000099987; ENSMUSG00000020473. [Q640N1-1]
Ensembl; ENSMUST00000109829; ENSMUSP00000105454; ENSMUSG00000020473. [Q640N1-2]
GeneID; 11568; -.
KEGG; mmu:11568; -.
UCSC; uc007hxg.3; mouse. [Q640N1-1]
CTD; 165; -.
MGI; MGI:1197012; Aebp1.
eggNOG; KOG2649; Eukaryota.
eggNOG; ENOG410XX0H; LUCA.
GeneTree; ENSGT00760000119124; -.
HOVERGEN; HBG003410; -.
InParanoid; Q640N1; -.
KO; K21392; -.
OMA; GINHGVK; -.
OrthoDB; EOG091G06A9; -.
PhylomeDB; Q640N1; -.
TreeFam; TF315592; -.
ChiTaRS; Aebp1; mouse.
PRO; PR:Q640N1; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020473; -.
Genevisible; Q640N1; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004180; F:carboxypeptidase activity; IDA:MGI.
GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
GO; GO:0016485; P:protein processing; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd03869; M14_CPX_like; 1.
Gene3D; 2.60.120.260; -; 1.
InterPro; IPR034243; AEBP1/CPX_M14_CPD.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR000421; FA58C.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR000834; Peptidase_M14.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF00246; Peptidase_M14; 1.
PRINTS; PR00765; CRBOXYPTASEA.
SMART; SM00231; FA58C; 1.
SMART; SM00631; Zn_pept; 1.
SUPFAM; SSF49464; SSF49464; 1.
SUPFAM; SSF49785; SSF49785; 1.
PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PROSITE; PS01285; FA58C_1; 1.
PROSITE; PS01286; FA58C_2; 1.
PROSITE; PS50022; FA58C_3; 1.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Complete proteome;
Cytoplasm; DNA-binding; Glycoprotein; Nucleus; Reference proteome;
Repressor; Secreted; Signal; Transcription; Transcription regulation.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1128 Adipocyte enhancer-binding protein 1.
/FTId=PRO_0000333190.
DOMAIN 374 531 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
REGION 381 546 Required for DNA-binding and interaction
with NFKBIA.
{ECO:0000269|PubMed:17202411}.
REGION 412 615 Interaction with MAPK1 and MAPK3.
{ECO:0000269|PubMed:11152475}.
REGION 546 976 Interaction with PTEN.
{ECO:0000269|PubMed:17299101}.
REGION 932 1128 Required for transcriptional repression.
REGION 997 1128 Interaction with MAPK1 and MAPK3.
{ECO:0000269|PubMed:11152475}.
COMPBIAS 70 166 Lys-rich.
COMPBIAS 625 629 Poly-Leu.
COMPBIAS 1069 1106 Glu-rich.
CARBOHYD 519 519 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 380 Missing (in isoform 2).
{ECO:0000303|PubMed:7477299}.
/FTId=VSP_033470.
MUTAGEN 1003 1003 T->A: Impairs DNA-binding and
phosphorylation by MAPK1.
{ECO:0000269|PubMed:15654748}.
MUTAGEN 1003 1003 T->D: Impairs DNA-binding.
{ECO:0000269|PubMed:15654748}.
CONFLICT 333 333 K -> E (in Ref. 3; BAE34995/BAE35004).
{ECO:0000305}.
CONFLICT 356 356 K -> KA (in Ref. 3; BAE35359/BAE35513/
BAE34995/BAE35004/BAE35033/BAE35060).
{ECO:0000305}.
CONFLICT 792 792 S -> F (in Ref. 3; BAE35359/BAE35513).
{ECO:0000305}.
CONFLICT 917 917 S -> C (in Ref. 3; BAE35359).
{ECO:0000305}.
CONFLICT 995 995 R -> G (in Ref. 2; AAC25584).
{ECO:0000305}.
CONFLICT 1096 1096 I -> IEE (in Ref. 3; BAE35359/BAE35513/
BAE34995/BAE35004/BAE35033/BAE35060).
{ECO:0000305}.
CONFLICT 1115 1115 L -> F (in Ref. 3; BAE35359/BAE35513/
BAE34995/BAE35004/BAE35033/BAE35060).
{ECO:0000305}.
SEQUENCE 1128 AA; 128365 MW; C24F46B893C02DC9 CRC64;
MAPVRTASLL CGLLALLTLC PEGNPQTVLT DDEIEEFLEG FLSELETQSP PREDDVEVQP
LPEPTQRPRK SKAGGKQRAD VEVPPEKNKD KEKKGKKDKG PKATKPLEGS TRPTKKPKEK
PPKATKKPKE KPPKATKKPK EKPPKATKKP KEKPPKATKR PSAGKKFSTV APLETLDRLL
PSPSNPSAQE LPQKRDTPFP NAWQGQGEET QVEAKQPRPE PEEETEMPTL DYNDQIEKED
YEDFEYIRRQ KQPRPTPSRR RLWPERPEEK TEEPEERKEV EPPLKPLLPP DYGDSYVIPN
YDDLDYYFPH PPPQKPDVGQ EVDEEKEEMK KPKKEGSSPK EDTEDKWTVE KNKDHKGPRK
GEELEEEWAP VEKIKCPPIG MESHRIEDNQ IRASSMLRHG LGAQRGRLNM QAGANEDDYY
DGAWCAEDES QTQWIEVDTR RTTRFTGVIT QGRDSSIHDD FVTTFFVGFS NDSQTWVMYT
NGYEEMTFYG NVDKDTPVLS ELPEPVVARF IRIYPLTWNG SLCMRLEVLG CPVTPVYSYY
AQNEVVTTDS LDFRHHSYKD MRQLMKAVNE ECPTITRTYS LGKSSRGLKI YAMEISDNPG
DHELGEPEFR YTAGIHGNEV LGRELLLLLM QYLCQEYRDG NPRVRNLVQD TRIHLVPSLN
PDGYEVAAQM GSEFGNWALG LWTEEGFDIF EDFPDLNSVL WAAEEKKWVP YRVPNNNLPI
PERYLSPDAT VSTEVRAIIS WMEKNPFVLG ANLNGGERLV SYPYDMARTP SQEQLLAEAL
AAARGEDDDG VSEAQETPDH AIFRWLAISF ASAHLTMTEP YRGGCQAQDY TSGMGIVNGA
KWNPRSGTFN DFSYLHTNCL ELSVYLGCDK FPHESELPRE WENNKEALLT FMEQVHRGIK
GVVTDEQGIP IANATISVSG INHGVKTASG GDYWRILNPG EYRVTAHAEG YTSSAKICNV
DYDIGATQCN FILARSNWKR IREILAMNGN RPILRVDPSR PMTPQQRRMQ QRRLQYRLRM
REQMRLRRLN STAGPATSPT PALMPPPSPT PAITLRPWEV LPTTTAGWEE SETETYTEVV
TEFETEYGTD LEVEEIEEEE EEEEEEMDTG LTFPLTTVET YTVNFGDF


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