RREB1_MOUSE
ID RREB1_MOUSE Reviewed; 1700 AA.
AC Q3UH06; B8JJE2; B8JJE3; Q3TB97; Q4ZE88; Q66JZ8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ras-responsive element-binding protein 1;
DE Short=RREB-1;
DE AltName: Full=RAS-responsive zinc finger transcription factor RREB;
GN Name=Rreb1;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-1700 (ISOFORM 3).
RC STRAIN=BALB/cJ;
RA Zhang S., Bliskovsky V., Mock B.;
RT "Role of mouse RREB gene in cancer susceptibility/resistance.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12700664; DOI=10.1038/sj.onc.1206257;
RA Zhang S., Qian X., Redman C., Bliskovski V., Ramsay E.S., Lowy D.R.,
RA Mock B.A.;
RT "p16 INK4a gene promoter variation and differential binding of a repressor,
RT the ras-responsive zinc-finger transcription factor, RREB.";
RL Oncogene 22:2285-2295(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137; SER-1138; SER-1179 AND
RP SER-1180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-970; SER-1137;
RP SER-1138; SER-1450; SER-1452; SER-1593 AND SER-1606, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION.
RX PubMed=27923061; DOI=10.1371/journal.pgen.1006474;
RA Brunmeir R., Wu J., Peng X., Kim S.Y., Julien S.G., Zhang Q., Xie W.,
RA Xu F.;
RT "Comparative Transcriptomic and Epigenomic Analyses Reveal New Regulators
RT of Murine Brown Adipogenesis.";
RL PLoS Genet. 12:E1006474-E1006474(2016).
CC -!- FUNCTION: Transcription factor that binds specifically to the RAS-
CC responsive elements (RRE) of gene promoters (PubMed:12700664).
CC Represses the angiotensinogen gene (By similarity). Negatively
CC regulates the transcriptional activity of AR (By similarity).
CC Potentiates the transcriptional activity of NEUROD1 (By similarity).
CC Binds specifically to the allelic variant of the CDKN2A promoter
CC present in Balb/c mice, which leads to a down-regulation of CDKN2A
CC expression in this strain, and, as a consequence, to an elevated
CC susceptibility to pristane-induced tumors (PubMed:12700664). Promotes
CC brown adipocyte differentiation (PubMed:27923061). May be involved in
CC Ras/Raf-mediated cell differentiation by enhancing calcitonin
CC expression (By similarity). {ECO:0000250|UniProtKB:Q92766,
CC ECO:0000269|PubMed:12700664, ECO:0000269|PubMed:27923061}.
CC -!- SUBUNIT: Interacts with NEUROD1 (By similarity). Interacts with AR (By
CC similarity). {ECO:0000250|UniProtKB:Q92766}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3UH06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UH06-2; Sequence=VSP_026765;
CC Name=3;
CC IsoId=Q3UH06-3; Sequence=VSP_026766;
CC Name=4;
CC IsoId=Q3UH06-4; Sequence=VSP_026767, VSP_026768;
CC -!- TISSUE SPECIFICITY: Expressed in splenic B-cells.
CC {ECO:0000269|PubMed:12700664}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK147653; BAE28051.1; -; mRNA.
DR EMBL; AK154980; BAE32969.1; -; mRNA.
DR EMBL; AK171375; BAE42417.1; -; mRNA.
DR EMBL; CT010477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080680; AAH80680.1; -; mRNA.
DR EMBL; AY946044; AAX83010.1; -; mRNA.
DR CCDS; CCDS36634.1; -. [Q3UH06-4]
DR CCDS; CCDS49238.1; -. [Q3UH06-3]
DR RefSeq; NP_001034277.1; NM_001039188.1. [Q3UH06-4]
DR RefSeq; NP_001171339.1; NM_001177868.1. [Q3UH06-4]
DR RefSeq; NP_001171340.1; NM_001177869.1. [Q3UH06-3]
DR RefSeq; NP_081106.1; NM_026830.2. [Q3UH06-4]
DR RefSeq; XP_006516812.1; XM_006516749.1. [Q3UH06-3]
DR RefSeq; XP_006516813.1; XM_006516750.2. [Q3UH06-3]
DR RefSeq; XP_006516814.1; XM_006516751.2. [Q3UH06-3]
DR RefSeq; XP_006516815.1; XM_006516752.2. [Q3UH06-3]
DR RefSeq; XP_006516816.1; XM_006516753.3. [Q3UH06-3]
DR RefSeq; XP_006516817.1; XM_006516754.3. [Q3UH06-3]
DR RefSeq; XP_006516819.1; XM_006516756.2. [Q3UH06-3]
DR RefSeq; XP_006516820.1; XM_006516757.3. [Q3UH06-3]
DR RefSeq; XP_006516822.1; XM_006516759.1. [Q3UH06-1]
DR BioGRID; 213031; 9.
DR STRING; 10090.ENSMUSP00000105867; -.
DR iPTMnet; Q3UH06; -.
DR PhosphoSitePlus; Q3UH06; -.
DR SwissPalm; Q3UH06; -.
DR EPD; Q3UH06; -.
DR jPOST; Q3UH06; -.
DR MaxQB; Q3UH06; -.
DR PaxDb; Q3UH06; -.
DR PeptideAtlas; Q3UH06; -.
DR PRIDE; Q3UH06; -.
DR ProteomicsDB; 260838; -. [Q3UH06-1]
DR ProteomicsDB; 260839; -. [Q3UH06-2]
DR ProteomicsDB; 260840; -. [Q3UH06-3]
DR ProteomicsDB; 260841; -. [Q3UH06-4]
DR Antibodypedia; 9691; 207 antibodies from 31 providers.
DR DNASU; 68750; -.
DR Ensembl; ENSMUST00000037232; ENSMUSP00000049265; ENSMUSG00000039087. [Q3UH06-3]
DR Ensembl; ENSMUST00000110237; ENSMUSP00000105866; ENSMUSG00000039087. [Q3UH06-4]
DR Ensembl; ENSMUST00000110238; ENSMUSP00000105867; ENSMUSG00000039087. [Q3UH06-4]
DR Ensembl; ENSMUST00000128570; ENSMUSP00000115599; ENSMUSG00000039087. [Q3UH06-3]
DR Ensembl; ENSMUST00000149745; ENSMUSP00000121211; ENSMUSG00000039087. [Q3UH06-4]
DR GeneID; 68750; -.
DR KEGG; mmu:68750; -.
DR UCSC; uc007qcw.2; mouse. [Q3UH06-4]
DR UCSC; uc007qda.2; mouse. [Q3UH06-1]
DR UCSC; uc007qdb.2; mouse. [Q3UH06-3]
DR CTD; 6239; -.
DR MGI; MGI:2443664; Rreb1.
DR VEuPathDB; HostDB:ENSMUSG00000039087; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157533; -.
DR HOGENOM; CLU_002702_0_0_1; -.
DR InParanoid; Q3UH06; -.
DR OMA; VHMRTHC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q3UH06; -.
DR TreeFam; TF332503; -.
DR BioGRID-ORCS; 68750; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Rreb1; mouse.
DR PRO; PR:Q3UH06; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UH06; protein.
DR Bgee; ENSMUSG00000039087; Expressed in left lung lobe and 264 other tissues.
DR ExpressionAtlas; Q3UH06; baseline and differential.
DR Genevisible; Q3UH06; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:MGI.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1700
FT /note="Ras-responsive element-binding protein 1"
FT /id="PRO_0000295155"
FT ZN_FING 66..88
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 97..119
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 125..147
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 206..228
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..256
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..663
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 669..691
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..720
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 751..782
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 788..813
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1251..1273
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1400..1422
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1520..1542
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1548..1570
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 31..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1344
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1578
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 1137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 564
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 855
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 883
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT CROSSLNK 911
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92766"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026765"
FT VAR_SEQ 1274
FT /note="T -> TGQKPFPCQKCDAFFSTKSNCERHQLRKHGVTTCSLRRNGLIPPKES
FT DVGSHDST (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_026766"
FT VAR_SEQ 1275..1291
FT /note="DSQSDTDTLTTPGEVLD -> GKKALTAHQAVSLERKE (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026767"
FT VAR_SEQ 1292..1700
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026768"
FT CONFLICT 834
FT /note="D -> G (in Ref. 1; BAE28051)"
FT /evidence="ECO:0000305"
FT CONFLICT 1113
FT /note="I -> T (in Ref. 4; AAH80680)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="D -> G (in Ref. 1; BAE28051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1700 AA; 184154 MW; DAB9246A566B1BC9 CRC64;
MTSNSPIGLE GSDLSSINTM MSAVMSVASV TENGGSPQGI KSPMKPPGPN RIGRRNQETK
EEKSSYNCPL CEKICTTQHQ LTMHIRQHNT DTGGADHACS ICGKSLSSAS SLDRHMLVHS
GERPYKCTVC GQSFTTNGNM HRHMKIHEKD TNSTTAAAPP SPLKRRRLSS KRKLSHDAES
EDPGPAKKMV EDGQSGDLDK MSDEIFHCPV CFKEFVCKYE LETHMETHSD NPLRCDICCV
TFRTHRGLLR HNALVHKQLP RDAMGRPFIQ NNPSIPAGFH DLGFTDFSCR KFPRISQAWC
ETNLRRCISE QHRFVCDTCD KAFPMLSSLI LHRQSHIPAD QGREKLQTKT LAAESLEQKA
FLALLGLQHT KDVKPAPAEE LLPDDNQAIQ LQTLKYQLPQ EPGCPTVLSV SPLDAASLGG
SLTVLPATKE NMKHLSLQPF QKGFIIQPDS SIVVKPISGE SAIELADIQQ ILKMAASAPP
QISLPPLSKA PATPLQAIFK HMPPLKPKPL VTPRTVVAAS TPPPLINAQQ ASPGCISPSL
PPQSLKFLKG SVEAVSNVHL LQSKSGIQPS TTTQLFLQQA GVELPGQPEM KTQLEQESII
EALLPLNMEA KIKQEITEGD LKAIMTGPSG KKTPAMRKVL YPCRFCNQVF AFSGVLRAHV
RSHLGISPYQ CNICDYIAAD KAALIRHIRT HSGERPYICK ICHYPFTVKA NCERHLRKKH
LKATRKDIEK NIEYVSSPTA ELVDAFCAPE TVCRLCGEDL KHYRALRIHM RTHCSRGLGG
CHKGRKPFEC KECNAPFVAK RNCIHHILKQ HLHVPEKDIE SYVLATNSGL GPADTPTDAA
SRGEEGSCVT FAECKPLATF LEPQNGFLHS SPTQPLPSHI SVKLEPASSF AMDFNEPLDF
SQKGLALVQV KQENVSSLLT SSSSSALYDC SMEPIDLSIP KSVKKGDKDT VVPSDAKKPE
PEAGQAEPLS PRPPPCPTLS VTVEPKGSLE TPTGTVVAVT TAAKLEPHTQ PLQGSVQLAV
PIYSPALVSN TPLLGNSAAL LNNPALLRPL RPKPPLLLPK PSMTEELPPL ASIAQIISSV
SSAPTLLKTK VADPGPSITS SNTVATDSPG SSIPKAAATP TDTTSSKESS EPPPAASSPE
EALPTEQGPA ATSSSRKRGR KRGLRNRPLP NSSAVDLDSS GEFASIEKML ATTDTNKFSP
FLQTAEDDTQ EEVAGAPADQ HGPADEEQGS PAEDRLLRAK RNSYANCLQK INCPHCPRVF
PWASSLQRHM LTHTDSQSDT DTLTTPGEVL DLTAQAKEQP PAEGASEISP ASQDLAIKEA
KAAAAPSEEE EEKETEENPE PEEECRVEES TGAADAPEED TASNQSLDLD FATKLMDFKL
AESEAGSVDS QGPAQQEPKH ACDTCGKNFK FLGTLSRHKK AHSCQEPKEE EAAAPSLENE
GVGRAVEGPS PSPEPEEKPA ESLAIDPTPG TREASVAKQN EETEGPTDGE GTAEKRGDGD
KRPKTDSPKS MASKADKRKK VCSVCNKRFW SLQDLTRHMR SHTGERPYKC QTCERTFTLK
HSLVRHQRIH QKARHSKHHG KDSDKDERAE EDSEDESTHS ATNPASENEA ESAPSTSNHV
AVTRSRKESL STSGKECSPE ERAAAEQAAE PSAPKEQASP GETDPQSPAA IVQDLLELCG
KRPAPILAAT DGASQLLGME
