AP2C_HUMAN
ID AP2C_HUMAN Reviewed; 450 AA.
AC Q92754; B4DWK3; O00685; O00730; Q86V30; Q8IVB6; Q9P1X2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Transcription factor AP-2 gamma;
DE Short=AP2-gamma;
DE AltName: Full=Activating enhancer-binding protein 2 gamma;
DE AltName: Full=Transcription factor ERF-1;
GN Name=TFAP2C;
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=Mammary tumor;
RX PubMed=8661133; DOI=10.1006/geno.1996.0351;
RA Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T.,
RA Hurst H.C.;
RT "Chromosomal mapping of the human and mouse homologues of two new members
RT of the AP-2 family of transcription factors.";
RL Genomics 35:262-264(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 203-211 AND
RP 361-370.
RC TISSUE=Mammary tumor;
RX PubMed=9113991; DOI=10.1073/pnas.94.9.4342;
RA McPherson L.A., Baichwal V.R., Weigel R.J.;
RT "Identification of ERF-1 as a member of the AP2 transcription factor
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4342-4347(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Haselton M.D., Ibbitt C.J., Hurst H.C.;
RT "Characterisation of the human AP-2gamma and AP-2beta genes.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary, and Skin;
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 [GENOMIC DNA] OF 17-450.
RC TISSUE=Liver;
RA Nishizawa M., Ito S.;
RT "Structure of human AP-2gamma gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND INTERACTION WITH CITED2.
RX PubMed=11694877; DOI=10.1038/ng768;
RA Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I.,
RA Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.;
RT "Cardiac malformations, adrenal agenesis, neural crest defects and
RT exencephaly in mice lacking Cited2, a new Tfap2 co-activator.";
RL Nat. Genet. 29:469-474(2001).
RN [9]
RP INTERACTION WITH CITED4.
RX PubMed=11744733; DOI=10.1074/jbc.m110850200;
RA Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J.,
RA Hurst H.C., Shioda T., Bhattacharya S.;
RT "Human CREB-binding protein/p300-interacting transactivator with ED-rich
RT tail (CITED) 4, a new member of the CITED family, functions as a co-
RT activator for transcription factor AP-2.";
RL J. Biol. Chem. 277:8559-8565(2002).
RN [10]
RP INTERACTION WITH UBE2I, AND SUMOYLATION AT LYS-10.
RX PubMed=12072434; DOI=10.1074/jbc.m202780200;
RA Eloranta J.J., Hurst H.C.;
RT "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9
RT and is sumolated in vivo.";
RL J. Biol. Chem. 277:30798-30804(2002).
RN [11]
RP INTERACTION WITH CITED2.
RX PubMed=12586840; DOI=10.1074/jbc.m208144200;
RA Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
RA Bhattacharya S.;
RT "Physical and functional interactions among AP-2 transcription factors,
RT p300/CREB-binding protein, and CITED2.";
RL J. Biol. Chem. 278:16021-16029(2003).
RN [12]
RP INTERACTION WITH WWOX, DOMAIN, AND MUTAGENESIS OF TYR-59 AND TYR-64.
RX PubMed=15548692; DOI=10.1158/0008-5472.can-04-2055;
RA Aqeilan R.I., Palamarchuk A., Weigel R.J., Herrero J.J., Pekarsky Y.,
RA Croce C.M.;
RT "Physical and functional interactions between the Wwox tumor suppressor
RT protein and the AP-2gamma transcription factor.";
RL Cancer Res. 64:8256-8261(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP INTERACTION WITH KCTD1.
RX PubMed=19115315; DOI=10.1002/jcb.22002;
RA Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L., He A.,
RA Zhu J., Gao X., Zhang J.;
RT "The interaction of KCTD1 with transcription factor AP-2alpha inhibits its
RT transactivation.";
RL J. Cell. Biochem. 106:285-295(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, INTERACTION WITH MTA1, AND SUBCELLULAR LOCATION.
RX PubMed=24413532; DOI=10.1158/0008-5472.can-13-2020;
RA Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA Kim Y.N., Seong J.K., Lee M.O.;
RT "Differential regulation of estrogen receptor alpha expression in breast
RT cancer cells by metastasis-associated protein 1.";
RL Cancer Res. 74:1484-1494(2014).
CC -!- FUNCTION: Sequence-specific DNA-binding protein that interacts with
CC inducible viral and cellular enhancer elements to regulate
CC transcription of selected genes. AP-2 factors bind to the consensus
CC sequence 5'-GCCNNNGGC-3' and activate genes involved in a large
CC spectrum of important biological functions including proper eye, face,
CC body wall, limb and neural tube development. They also suppress a
CC number of genes including MCAM/MUC18, C/EBP alpha and MYC. Involved in
CC the MTA1-mediated epigenetic regulation of ESR1 expression in breast
CC cancer. {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:24413532}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members (By similarity). Interacts with WWOX.
CC Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this
CC interaction represses transcription activation. Interacts with CITED2
CC (via C-terminus); the interaction stimulates TFAP2B-transcriptional
CC activity. Interacts with MTA1. {ECO:0000250,
CC ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:11744733,
CC ECO:0000269|PubMed:12072434, ECO:0000269|PubMed:12586840,
CC ECO:0000269|PubMed:15548692, ECO:0000269|PubMed:19115315,
CC ECO:0000269|PubMed:24413532}.
CC -!- INTERACTION:
CC Q92754; Q99967: CITED2; NbExp=2; IntAct=EBI-937309, EBI-937732;
CC Q92754; P63279: UBE2I; NbExp=5; IntAct=EBI-937309, EBI-80168;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24413532}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92754-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92754-2; Sequence=VSP_056501;
CC -!- INDUCTION: During retinoic acid-mediated differentiation.
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX.
CC {ECO:0000269|PubMed:15548692}.
CC -!- PTM: Sumoylated on Lys-10; which inhibits transcriptional activity.
CC {ECO:0000269|PubMed:12072434}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Activating protein 2 entry;
CC URL="https://en.wikipedia.org/wiki/Activating_protein_2";
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DR EMBL; X95693; CAA64989.1; -; mRNA.
DR EMBL; U85658; AAC51305.1; -; mRNA.
DR EMBL; AJ315934; CAC86997.1; -; Genomic_DNA.
DR EMBL; AK301572; BAG63065.1; -; mRNA.
DR EMBL; AL121920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035664; AAH35664.2; -; mRNA.
DR EMBL; BC051829; AAH51829.2; -; mRNA.
DR EMBL; AB041717; BAC11805.1; -; Genomic_DNA.
DR CCDS; CCDS13454.1; -. [Q92754-1]
DR RefSeq; NP_003213.1; NM_003222.3. [Q92754-1]
DR AlphaFoldDB; Q92754; -.
DR BioGRID; 112880; 29.
DR CORUM; Q92754; -.
DR ELM; Q92754; -.
DR IntAct; Q92754; 80.
DR STRING; 9606.ENSP00000201031; -.
DR iPTMnet; Q92754; -.
DR PhosphoSitePlus; Q92754; -.
DR BioMuta; TFAP2C; -.
DR DMDM; 12643310; -.
DR EPD; Q92754; -.
DR jPOST; Q92754; -.
DR MassIVE; Q92754; -.
DR MaxQB; Q92754; -.
DR PaxDb; Q92754; -.
DR PeptideAtlas; Q92754; -.
DR PRIDE; Q92754; -.
DR ProteomicsDB; 5349; -.
DR ProteomicsDB; 75446; -. [Q92754-1]
DR Antibodypedia; 4230; 434 antibodies from 42 providers.
DR DNASU; 7022; -.
DR Ensembl; ENST00000201031.3; ENSP00000201031.2; ENSG00000087510.7. [Q92754-1]
DR GeneID; 7022; -.
DR KEGG; hsa:7022; -.
DR MANE-Select; ENST00000201031.3; ENSP00000201031.2; NM_003222.4; NP_003213.1.
DR UCSC; uc002xya.4; human. [Q92754-1]
DR CTD; 7022; -.
DR DisGeNET; 7022; -.
DR GeneCards; TFAP2C; -.
DR HGNC; HGNC:11744; TFAP2C.
DR HPA; ENSG00000087510; Tissue enhanced (esophagus, skin).
DR MIM; 601602; gene.
DR neXtProt; NX_Q92754; -.
DR OpenTargets; ENSG00000087510; -.
DR PharmGKB; PA36461; -.
DR VEuPathDB; HostDB:ENSG00000087510; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR HOGENOM; CLU_035175_4_1_1; -.
DR InParanoid; Q92754; -.
DR OMA; EDRHDGN; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; Q92754; -.
DR TreeFam; TF313718; -.
DR PathwayCommons; Q92754; -.
DR Reactome; R-HSA-3232118; SUMOylation of transcription factors.
DR Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-HSA-8866906; TFAP2 (AP-2) family regulates transcription of other transcription factors.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR SignaLink; Q92754; -.
DR SIGNOR; Q92754; -.
DR BioGRID-ORCS; 7022; 66 hits in 1101 CRISPR screens.
DR ChiTaRS; TFAP2C; human.
DR GeneWiki; TFAP2C; -.
DR GenomeRNAi; 7022; -.
DR Pharos; Q92754; Tbio.
DR PRO; PR:Q92754; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q92754; protein.
DR Bgee; ENSG00000087510; Expressed in endometrium epithelium and 130 other tissues.
DR ExpressionAtlas; Q92754; baseline and differential.
DR Genevisible; Q92754; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004979; TF_AP2.
DR InterPro; IPR013854; TF_AP2_C.
DR InterPro; IPR008123; TF_AP2_gamma.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01751; AP2CTNSCPFCT.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..450
FT /note="Transcription factor AP-2 gamma"
FT /id="PRO_0000184803"
FT REGION 13..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..424
FT /note="H-S-H (helix-span-helix), dimerization"
FT REGION 431..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..64
FT /note="PPxY motif"
FT COMPBIAS 92..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12072434"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056501"
FT MUTAGEN 59
FT /note="Y->A: Loss of interaction with WWOX; when associated
FT with A-64."
FT /evidence="ECO:0000269|PubMed:15548692"
FT MUTAGEN 64
FT /note="Y->A: Loss of interaction with WWOX; when associated
FT with A-59."
FT /evidence="ECO:0000269|PubMed:15548692"
SQ SEQUENCE 450 AA; 49177 MW; 2D4F5FBC269A34A8 CRC64;
MLWKITDNVK YEEDCEDRHD GSSNGNPRVP HLSSAGQHLY SPAPPLSHTG VAEYQPPPYF
PPPYQQLAYS QSADPYSHLG EAYAAAINPL HQPAPTGSQQ QAWPGRQSQE GAGLPSHHGR
PAGLLPHLSG LEAGAVSARR DAYRRSDLLL PHAHALDAAG LAENLGLHDM PHQMDEVQNV
DDQHLLLHDQ TVIRKGPISM TKNPLNLPCQ KELVGAVMNP TEVFCSVPGR LSLLSSTSKY
KVTVAEVQRR LSPPECLNAS LLGGVLRRAK SKNGGRSLRE KLDKIGLNLP AGRRKAAHVT
LLTSLVEGEA VHLARDFAYV CEAEFPSKPV AEYLTRPHLG GRNEMAARKN MLLAAQQLCK
EFTELLSQDR TPHGTSRLAP VLETNIQNCL SHFSLITHGF GSQAICAAVS ALQNYIKEAL
IVIDKSYMNP GDQSPADSNK TLEKMEKHRK
