ID   AEBP1_HUMAN             Reviewed;        1158 AA.
AC   Q8IUX7; Q14113; Q59ER7; Q6ZSC7; Q7KZ79;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Adipocyte enhancer-binding protein 1;
DE            Short=AE-binding protein 1;
DE   AltName: Full=Aortic carboxypeptidase-like protein;
DE   Flags: Precursor;
GN   Name=AEBP1; Synonyms=ACLP;
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).
RC   TISSUE=Aortic smooth muscle;
RX   PubMed=9624159; DOI=10.1074/jbc.273.25.15654;
RA   Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T.,
RA   Perrella M.A., Blanar M.A., Haber E., Lee M.-E.;
RT   "Aortic carboxypeptidase-like protein, a novel protein with discoidin and
RT   carboxypeptidase-like domains, is up-regulated during vascular smooth
RT   muscle cell differentiation.";
RL   J. Biol. Chem. 273:15654-15660(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-1133.
RC   TISSUE=Aortic endothelium;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 314-1158 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Cancellous bone;
RX   PubMed=8920928; DOI=10.1006/bbrc.1996.1675;
RA   Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K.,
RA   Okubo K.;
RT   "A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its
RT   expression in a differentiating osteoblastic cell line.";
RL   Biochem. Biophys. Res. Commun. 228:411-414(1996).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-922.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [9]
RP   IDENTIFICATION BY MASS 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   [10]
RP   INVOLVEMENT IN EDSCLL2.
RX   PubMed=27023906; DOI=10.1007/s00439-016-1660-z;
RA   Alazami A.M., Al-Qattan S.M., Faqeih E., Alhashem A., Alshammari M.,
RA   Alzahrani F., Al-Dosari M.S., Patel N., Alsagheir A., Binabbas B.,
RA   Alzaidan H., Alsiddiky A., Alharbi N., Alfadhel M., Kentab A., Daza R.M.,
RA   Kircher M., Shendure J., Hashem M., Alshahrani S., Rahbeeni Z., Khalifa O.,
RA   Shaheen R., Alkuraya F.S.;
RT   "Expanding the clinical and genetic heterogeneity of hereditary disorders
RT   of connective tissue.";
RL   Hum. Genet. 135:525-540(2016).
RN   [11]
RP   FUNCTION, INTERACTION WITH COLLAGEN, DOMAIN, INVOLVEMENT IN EDSCLL2, AND
RP   VARIANT EDSCLL2 581-CYS--PHE-1158 DEL.
RX   PubMed=29606302; DOI=10.1016/j.ajhg.2018.02.018;
RA   Blackburn P.R., Xu Z., Tumelty K.E., Zhao R.W., Monis W.J., Harris K.G.,
RA   Gass J.M., Cousin M.A., Boczek N.J., Mitkov M.V., Cappel M.A.,
RA   Francomano C.A., Parisi J.E., Klee E.W., Faqeih E., Alkuraya F.S.,
RA   Layne M.D., McDonnell N.B., Atwal P.S.;
RT   "Bi-allelic alterations in AEBP1 lead to defective collagen assembly and
RT   connective tissue structure resulting in a variant of Ehlers-Danlos
RT   syndrome.";
RL   Am. J. Hum. Genet. 102:696-705(2018).
CC   -!- FUNCTION: [Isoform 1]: As a positive regulator of collagen
CC       fibrillogenesis, it is probably involved in the organization and
CC       remodeling of the extracellular matrix. {ECO:0000269|PubMed:29606302}.
CC   -!- FUNCTION: [Isoform 2]: May positively regulate MAP-kinase activity in
CC       adipocytes, leading to enhanced adipocyte proliferation and reduced
CC       adipocyte differentiation. May also positively regulate NF-kappa-B
CC       activity in macrophages by promoting the phosphorylation and subsequent
CC       degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage
CC       inflammatory responsiveness. Can act as a transcriptional repressor.
CC       {ECO:0000250|UniProtKB:Q640N1}.
CC   -!- SUBUNIT: Isoform 1: Interacts with different types of collagen,
CC       including collagens I, III, and V (PubMed:29606302). Isoform 2:
CC       Interacts with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN. Interaction with
CC       MAPK1 may stimulate DNA-binding. May interact with calmodulin. Binds to
CC       DNA in vitro. {ECO:0000250|UniProtKB:Q640N1,
CC       ECO:0000269|PubMed:29606302}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC       {ECO:0000250|UniProtKB:Q640N1}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q640N1}. Nucleus {ECO:0000250|UniProtKB:Q640N1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IUX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IUX7-2; Sequence=VSP_033467, VSP_033468, VSP_033469;
CC   -!- TISSUE SPECIFICITY: Expressed in osteoblast and visceral fat.
CC       {ECO:0000269|PubMed:8920928}.
CC   -!- DOMAIN: [Isoform 1]: The F5/8 type C domain binds to different types of
CC       collagen, including collagens I, III, and V.
CC       {ECO:0000269|PubMed:29606302}.
CC   -!- PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000250}.
CC   -!- DISEASE: Ehlers-Danlos syndrome, classic-like, 2 (EDSCLL2)
CC       [MIM:618000]: A variant form of Ehlers-Danlos syndrome, a connective
CC       tissue disorder. EDSCLL2 patients show severe joint and skin laxity,
CC       osteoporosis affecting the hips and spine, osteoarthritis, soft
CC       redundant skin that can be acrogeria-like, delayed wound healing with
CC       abnormal atrophic scarring, and shoulder, hip, knee, and ankle
CC       dislocations. Additional variable features include gastrointestinal and
CC       genitourinary manifestations (bowel rupture, gut dysmotility,
CC       cryptorchidism, and hernias), vascular complications (mitral valve
CC       prolapse and aortic root dilation), and skeletal anomalies. EDSCLL2
CC       inheritance is autosomal recessive. {ECO:0000269|PubMed:27023906,
CC       ECO:0000269|PubMed:29606302}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   -!- CAUTION: Although related to peptidase M14 family, lacks the active
CC       site residues and zinc-binding sites, suggesting that it has no
CC       carboxypeptidase activity. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF053944; AAC25585.1; -; mRNA.
DR   EMBL; AK127541; BAC87026.1; -; mRNA.
DR   EMBL; AB209744; BAD92981.1; ALT_INIT; mRNA.
DR   EMBL; CH236960; EAL23768.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW61119.1; -; Genomic_DNA.
DR   EMBL; BC038588; AAH38588.1; -; mRNA.
DR   EMBL; D86479; BAA13094.1; -; mRNA.
DR   CCDS; CCDS5476.1; -. [Q8IUX7-1]
DR   PIR; JC5256; JC5256.
DR   RefSeq; NP_001120.3; NM_001129.4. [Q8IUX7-1]
DR   AlphaFoldDB; Q8IUX7; -.
DR   SMR; Q8IUX7; -.
DR   BioGRID; 106674; 4.
DR   IntAct; Q8IUX7; 3.
DR   STRING; 9606.ENSP00000223357; -.
DR   MEROPS; M14.951; -.
DR   GlyConnect; 995; 18 N-Linked glycans (3 sites).
DR   GlyCosmos; Q8IUX7; 15 sites, 22 glycans.
DR   GlyGen; Q8IUX7; 15 sites, 18 N-linked glycans (3 sites), 4 O-linked glycans (12 sites).
DR   iPTMnet; Q8IUX7; -.
DR   PhosphoSitePlus; Q8IUX7; -.
DR   BioMuta; AEBP1; -.
DR   DMDM; 74728002; -.
DR   EPD; Q8IUX7; -.
DR   jPOST; Q8IUX7; -.
DR   MassIVE; Q8IUX7; -.
DR   MaxQB; Q8IUX7; -.
DR   PaxDb; 9606-ENSP00000223357; -.
DR   PeptideAtlas; Q8IUX7; -.
DR   ProteomicsDB; 70626; -. [Q8IUX7-1]
DR   ProteomicsDB; 70627; -. [Q8IUX7-2]
DR   Antibodypedia; 4099; 212 antibodies from 29 providers.
DR   DNASU; 165; -.
DR   Ensembl; ENST00000223357.8; ENSP00000223357.3; ENSG00000106624.11. [Q8IUX7-1]
DR   Ensembl; ENST00000450684.2; ENSP00000398878.2; ENSG00000106624.11. [Q8IUX7-2]
DR   GeneID; 165; -.
DR   KEGG; hsa:165; -.
DR   MANE-Select; ENST00000223357.8; ENSP00000223357.3; NM_001129.5; NP_001120.3.
DR   UCSC; uc003tkb.5; human. [Q8IUX7-1]
DR   AGR; HGNC:303; -.
DR   CTD; 165; -.
DR   DisGeNET; 165; -.
DR   GeneCards; AEBP1; -.
DR   HGNC; HGNC:303; AEBP1.
DR   HPA; ENSG00000106624; Low tissue specificity.
DR   MalaCards; AEBP1; -.
DR   MIM; 602981; gene.
DR   MIM; 618000; phenotype.
DR   neXtProt; NX_Q8IUX7; -.
DR   OpenTargets; ENSG00000106624; -.
DR   Orphanet; 536532; Classical-like Ehlers-Danlos syndrome type 2.
DR   PharmGKB; PA24604; -.
DR   VEuPathDB; HostDB:ENSG00000106624; -.
DR   eggNOG; KOG2649; Eukaryota.
DR   GeneTree; ENSGT00940000158323; -.
DR   HOGENOM; CLU_006722_0_1_1; -.
DR   InParanoid; Q8IUX7; -.
DR   OMA; YIRRQKR; -.
DR   OrthoDB; 5490979at2759; -.
DR   PhylomeDB; Q8IUX7; -.
DR   TreeFam; TF315592; -.
DR   PathwayCommons; Q8IUX7; -.
DR   SignaLink; Q8IUX7; -.
DR   SIGNOR; Q8IUX7; -.
DR   BioGRID-ORCS; 165; 15 hits in 1158 CRISPR screens.
DR   ChiTaRS; AEBP1; human.
DR   GenomeRNAi; 165; -.
DR   Pharos; Q8IUX7; Tbio.
DR   PRO; PR:Q8IUX7; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q8IUX7; Protein.
DR   Bgee; ENSG00000106624; Expressed in tendon of biceps brachii and 186 other cell types or tissues.
DR   ExpressionAtlas; Q8IUX7; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   GO; GO:1904026; P:regulation of collagen fibril organization; IDA:UniProtKB.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF48; ADIPOCYTE ENHANCER-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS52035; PEPTIDASE_M14; 1.
DR   Genevisible; Q8IUX7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Cytoplasm; Disease variant;
KW   DNA-binding; Ehlers-Danlos syndrome; Glycoprotein; Nucleus;
KW   Reference proteome; Repressor; Secreted; Signal; Transcription;
KW   Transcription regulation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1158
FT                   /note="Adipocyte enhancer-binding protein 1"
FT                   /id="PRO_0000333189"
FT   DOMAIN          383..540
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          563..904
FT                   /note="Peptidase M14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   REGION          40..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..555
FT                   /note="Required for DNA-binding and interaction with
FT                   NFKBIA"
FT                   /evidence="ECO:0000250"
FT   REGION          421..624
FT                   /note="Interaction with MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250"
FT   REGION          555..985
FT                   /note="Interaction with PTEN"
FT                   /evidence="ECO:0000250"
FT   REGION          941..1158
FT                   /note="Required for transcriptional repression"
FT                   /evidence="ECO:0000250"
FT   REGION          1006..1158
FT                   /note="Interaction with MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250"
FT   REGION          1108..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..194
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..303
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1136
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        922
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   VAR_SEQ         1..457
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033467"
FT   VAR_SEQ         458..495
FT                   /note="ITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEM -> MRKWWAPCPG
FT                   SWLCSHCLGEGWALRGAGSTALRPASPQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033468"
FT   VAR_SEQ         543..544
FT                   /note="AP -> ARECGGLAGALSGGGVLGWASRHPAKDNPASLAA (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033469"
FT   VARIANT         273
FT                   /note="P -> T (in dbSNP:rs2537188)"
FT                   /id="VAR_043118"
FT   VARIANT         581..1158
FT                   /note="Missing (in EDSCLL2)"
FT                   /evidence="ECO:0000269|PubMed:29606302"
FT                   /id="VAR_080664"
FT   VARIANT         648
FT                   /note="D -> E (in dbSNP:rs11770649)"
FT                   /id="VAR_043119"
FT   VARIANT         1001
FT                   /note="P -> L (in dbSNP:rs4724285)"
FT                   /id="VAR_043120"
FT   VARIANT         1133
FT                   /note="K -> E (in dbSNP:rs13928)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_043121"
FT   VARIANT         1148
FT                   /note="V -> I (in dbSNP:rs13898)"
FT                   /id="VAR_043122"
FT   CONFLICT        145
FT                   /note="K -> E (in Ref. 1; AAC25585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="R -> Q (in Ref. 1; AAC25585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="D -> G (in Ref. 2; BAC87026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        715
FT                   /note="R -> G (in Ref. 2; BAC87026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        884
FT                   /note="S -> G (in Ref. 2; BAC87026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1079
FT                   /note="E -> G (in Ref. 3; BAD92981)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1158 AA;  130929 MW;  1D7F4A20451646AE CRC64;
     MAAVRGAPLL SCLLALLALC PGGRPQTVLT DDEIEEFLEG FLSELEPEPR EDDVEAPPPP
     EPTPRVRKAQ AGGKPGKRPG TAAEVPPEKT KDKGKKGKKD KGPKVPKESL EGSPRPPKKG
     KEKPPKATKK PKEKPPKATK KPKEKPPKAT KKPKEKPPKA TKKPPSGKRP PILAPSETLE
     WPLPPPPSPG PEELPQEGGA PLSNNWQNPG EETHVEAREH QPEPEEETEQ PTLDYNDQIE
     REDYEDFEYI RRQKQPRPPP SRRRRPERVW PEPPEEKAPA PAPEERIEPP VKPLLPPLPP
     DYGDGYVIPN YDDMDYYFGP PPPQKPDAER QTDEEKEELK KPKKEDSSPK EETDKWAVEK
     GKDHKEPRKG EELEEEWTPT EKVKCPPIGM ESHRIEDNQI RASSMLRHGL GAQRGRLNMQ
     TGATEDDYYD GAWCAEDDAR TQWIEVDTRR TTRFTGVITQ GRDSSIHDDF VTTFFVGFSN
     DSQTWVMYTN GYEEMTFHGN VDKDTPVLSE LPEPVVARFI RIYPLTWNGS LCMRLEVLGC
     SVAPVYSYYA QNEVVATDDL DFRHHSYKDM RQLMKVVNEE CPTITRTYSL GKSSRGLKIY
     AMEISDNPGE HELGEPEFRY TAGIHGNEVL GRELLLLLMQ YLCREYRDGN PRVRSLVQDT
     RIHLVPSLNP DGYEVAAQMG SEFGNWALGL WTEEGFDIFE DFPDLNSVLW GAEERKWVPY
     RVPNNNLPIP ERYLSPDATV STEVRAIIAW MEKNPFVLGA NLNGGERLVS YPYDMARTPT
     QEQLLAAAMA AARGEDEDEV SEAQETPDHA IFRWLAISFA SAHLTLTEPY RGGCQAQDYT
     GGMGIVNGAK WNPRTGTIND FSYLHTNCLE LSFYLGCDKF PHESELPREW ENNKEALLTF
     MEQVHRGIKG VVTDEQGIPI ANATISVSGI NHGVKTASGG DYWRILNPGE YRVTAHAEGY
     TPSAKTCNVD YDIGATQCNF ILARSNWKRI REIMAMNGNR PIPHIDPSRP MTPQQRRLQQ
     RRLQHRLRLR AQMRLRRLNA TTTLGPHTVP PTLPPAPATT LSTTIEPWGL IPPTTAGWEE
     SETETYTEVV TEFGTEVEPE FGTKVEPEFE TQLEPEFETQ LEPEFEEEEE EEKEEEIATG
     QAFPFTTVET YTVNFGDF
//