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AP2C_MOUSE
ID   AP2C_MOUSE              Reviewed;         449 AA.
AC   Q61312; Q99L72;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Transcription factor AP-2 gamma;
DE            Short=AP2-gamma;
DE   AltName: Full=AP-2.2;
DE   AltName: Full=Activating enhancer-binding protein 2 gamma;
GN   Name=Tfap2c; Synonyms=Tcfap2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryonic carcinoma;
RX   PubMed=8660922; DOI=10.1006/excr.1996.0184;
RA   Oulad-Abdelghani M., Bouillet P., Chazaud C., Dolle P., Chambon P.;
RT   "AP-2.2: a novel AP-2-related transcription factor induced by retinoic acid
RT   during differentiation of P19 embryonal carcinoma cells.";
RL   Exp. Cell Res. 225:338-347(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [6]
RP   INTERACTION WITH CITED4.
RX   PubMed=12504852; DOI=10.1006/geno.2002.7005;
RA   Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T.,
RA   Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S.,
RA   Shioda T.;
RT   "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding
RT   transcriptional coactivators: induced expression in mammary epithelial
RT   cells.";
RL   Genomics 80:601-613(2002).
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.
CC   -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC       other AP-2 family members. Interacts with WWOX. Interacts with UBE2I
CC       (By similarity). Interacts with CITED4. 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, ovary and testis. Expressed in
CC       most squamous epithelia. Also, detected in several exocrine glands
CC       including the prostate, the preputial and salivary glands, serous
CC       glands of the tongue and ocular harderian glands.
CC   -!- INDUCTION: During retinoic acid-mediated differentiation.
CC   -!- DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}.
CC   -!- PTM: Sumoylated on Lys-10; which inhibits transcriptional activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
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DR   EMBL; X94694; CAA64357.1; -; mRNA.
DR   EMBL; AK145166; BAE26271.1; -; mRNA.
DR   EMBL; AL833787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466551; EDL06609.1; -; Genomic_DNA.
DR   EMBL; BC003778; AAH03778.1; -; mRNA.
DR   CCDS; CCDS17135.1; -.
DR   RefSeq; NP_001153168.1; NM_001159696.1.
DR   RefSeq; NP_033361.2; NM_009335.2.
DR   AlphaFoldDB; Q61312; -.
DR   BioGRID; 204013; 6.
DR   STRING; 10090.ENSMUSP00000030391; -.
DR   iPTMnet; Q61312; -.
DR   PhosphoSitePlus; Q61312; -.
DR   MaxQB; Q61312; -.
DR   PaxDb; Q61312; -.
DR   PRIDE; Q61312; -.
DR   ProteomicsDB; 296264; -.
DR   Antibodypedia; 4230; 434 antibodies from 42 providers.
DR   DNASU; 21420; -.
DR   Ensembl; ENSMUST00000030391; ENSMUSP00000030391; ENSMUSG00000028640.
DR   GeneID; 21420; -.
DR   KEGG; mmu:21420; -.
DR   UCSC; uc008ocz.2; mouse.
DR   CTD; 7022; -.
DR   MGI; MGI:106032; Tfap2c.
DR   VEuPathDB; HostDB:ENSMUSG00000028640; -.
DR   eggNOG; KOG3811; Eukaryota.
DR   GeneTree; ENSGT00950000182848; -.
DR   HOGENOM; CLU_035175_4_1_1; -.
DR   InParanoid; Q61312; -.
DR   OMA; EDRHDGN; -.
DR   OrthoDB; 641707at2759; -.
DR   TreeFam; TF313718; -.
DR   Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR   Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR   Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR   Reactome; R-MMU-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR   BioGRID-ORCS; 21420; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Tfap2c; mouse.
DR   PRO; PR:Q61312; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q61312; protein.
DR   Bgee; ENSMUSG00000028640; Expressed in ectoplacental cone and 235 other tissues.
DR   ExpressionAtlas; Q61312; baseline and differential.
DR   Genevisible; Q61312; MM.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0060598; P:dichotomous subdivision of terminal units involved in mammary gland duct morphogenesis; IMP:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IMP:MGI.
DR   GO; GO:0021877; P:forebrain neuron fate commitment; IMP:MGI.
DR   GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IGI:MGI.
DR   GO; GO:0003334; P:keratinocyte development; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0045682; P:regulation of epidermis development; IMP:MGI.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR   GO; GO:0048733; P:sebaceous gland development; IGI:MGI.
DR   GO; GO:0043588; P:skin development; IGI:MGI.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR   GO; GO:0019827; P:stem cell population maintenance; IDA:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
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; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..449
FT                   /note="Transcription factor AP-2 gamma"
FT                   /id="PRO_0000184804"
FT   REGION          13..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..423
FT                   /note="H-S-H (helix-span-helix), dimerization"
FT   REGION          426..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..64
FT                   /note="PPxY motif"
FT   COMPBIAS        94..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         251
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92754"
FT   CROSSLNK        10
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        67..68
FT                   /note="LA -> VV (in Ref. 1; CAA64357)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   449 AA;  49137 MW;  92490E234697B6A3 CRC64;
     MLWKITDNVK YEEDCEDRHD SSSNGNPRIP HLSSPGQHLY SPAPPLSHTG VAEYQPPPYF
     PPPYQQLAYS QSADHYSHLG EAYAAAMNPL HQPAATGSQQ QAWPGRQSQE GSSLASHHSR
     SASLIPHISG LEGGSVSARR EVYRRSDLLL PHAHALEAGL AENLGLHEMA HPIEEVQNVD
     DAHLLLHDQT VIRKGPISMT KNPLGLPCQK DLVGVVMNPS EVFCSVPGRL SLLSSTSKYK
     VTVAEVQRRL SPPECLNASL LGGVLRRAKS KNGGRSLREK LDKIGLNLPA GRRKAAHVTL
     LTSLVEGEAV HLARDFAYVC EAEFPSKAVA DYLTRPHLGG RNEMATRKSM LLAAQQVCKE
     FTDLLHQDRT PNGNNRPAQV LEPNIQNCLS HFSLITHGFG SQAICAAVSA VQNYIKEALI
     AIDKSYMNPG DQSPADSSKT MEKMEKHRK
 
 
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