ID GTF2I_MOUSE Reviewed; 998 AA. AC Q9ESZ8; O54700; O55030; O55031; Q8VHD1; Q8VHD2; Q8VHD3; Q8VHD4; Q9CSB5; AC Q9D9K9; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 3. DT 24-JAN-2024, entry version 177. DE RecName: Full=General transcription factor II-I; DE Short=GTFII-I; DE Short=TFII-I; DE AltName: Full=Bruton tyrosine kinase-associated protein 135; DE Short=BAP-135; DE Short=BTK-associated protein 135; GN Name=Gtf2i; Synonyms=Bap135, Diws1t; 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] (ISOFORMS 1; 2; 3; 4 AND 5). RC TISSUE=Brain; RX PubMed=9521869; DOI=10.1006/geno.1997.5182; RA Wang Y.-K., Perez-Jurado L.A., Francke U.; RT "A mouse single-copy gene, Gtf2i, the homolog of human GTF2I, that is RT duplicated in the Williams-Beuren syndrome deletion region."; RL Genomics 48:163-170(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4). RC STRAIN=C57BL/Kaplan; TISSUE=T-cell lymphoma; RA Johansson E., Hjortsberg K., Roy A.L., Thelander L.; RT "Cloning and expression of two forms of mouse TFII-I."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 6). RC STRAIN=129/SvJ; RX PubMed=11827466; DOI=10.1006/geno.2001.6674; RA Bayarsaihan D., Dunai J., Greally J.M., Kawasaki K., Sumiyama K., RA Enkhmandakh B., Shimizu N., Ruddle F.H.; RT "Genomic organization of the genes Gtf2ird1, Gtf2i, and Ncf1 at the mouse RT chromosome 5 region syntenic to the human chromosome 7q11.23 Williams RT syndrome critical region."; RL Genomics 79:137-143(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-130 AND 719-998. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis; 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 [6] RP NUCLEOTIDE SEQUENCE OF 1-314 (ISOFORM 2). RC STRAIN=129/Sv; RA Green E.D.; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH ARID3A AND BTK, AND FUNCTION. RX PubMed=16738337; DOI=10.1128/mcb.02009-05; RA Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F.; RT "Induction of immunoglobulin heavy-chain transcription through the RT transcription factor Bright requires TFII-I."; RL Mol. Cell. Biol. 26:4758-4768(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556 AND THR-558, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and RC 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-353; LYS-450 AND RP LYS-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP STRUCTURE BY NMR OF 733-818. RX PubMed=17600150; DOI=10.1110/ps.072792007; RA Doi-Katayama Y., Hayashi F., Inoue M., Yabuki T., Aoki M., Seki E., RA Matsuda T., Kigawa T., Yoshida M., Shirouzu M., Terada T., Hayashizaki Y., RA Yokoyama S., Hirota H.; RT "Solution structure of the general transcription factor 2I domain in mouse RT TFII-I protein."; RL Protein Sci. 16:1788-1792(2007). CC -!- FUNCTION: Interacts with the basal transcription machinery by CC coordinating the formation of a multiprotein complex at the C-FOS CC promoter, and linking specific signal responsive activator complexes. CC Promotes the formation of stable high-order complexes of SRF and PHOX1 CC and interacts cooperatively with PHOX1 to promote serum-inducible CC transcription of a reporter gene deriven by the C-FOS serum response CC element (SRE). Acts as a coregulator for USF1 by binding independently CC two promoter elements, a pyrimidine-rich initiator (Inr) and an CC upstream E-box (By similarity). Required for the formation of CC functional ARID3A DNA-binding complexes and for activation of CC immunoglobulin heavy-chain transcription upon B-lymphocyte activation. CC {ECO:0000250, ECO:0000269|PubMed:16738337}. CC -!- SUBUNIT: Homodimer (Potential). Interacts with SRF and PHOX1. Binds a CC pyrimidine-rich initiator (Inr) and a recognition site (E-box) for CC upstream stimulatory factor 1 (USF1). Associates with the PH domain of CC Bruton's tyrosine kinase (BTK) (By similarity). May be a component of a CC BHC histone deacetylase complex that contains HDAC1, HDAC2, CC HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, CC GSE1 and GTF2I. Interacts with BTK and ARID3A. Interacts with isoform CC beta of PRKG1 (By similarity). {ECO:0000250, ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with BTK in CC the cytoplasm. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=Gamma; CC IsoId=Q9ESZ8-1; Sequence=Displayed; CC Name=2; Synonyms=Beta, Long; CC IsoId=Q9ESZ8-2; Sequence=VSP_003869; CC Name=3; CC IsoId=Q9ESZ8-3; Sequence=VSP_003870; CC Name=4; Synonyms=Delta, Short; CC IsoId=Q9ESZ8-4; Sequence=VSP_003869, VSP_003872; CC Name=5; CC IsoId=Q9ESZ8-5; Sequence=VSP_003871; CC Name=6; Synonyms=Alpha; CC IsoId=Q9ESZ8-6; Sequence=VSP_003872; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Transiently phosphorylated on tyrosine residues by BTK in response CC to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-398, CC and perhaps, on Tyr-503 contributes to BTK-mediated transcriptional CC activation (By similarity). {ECO:0000250}. CC -!- PTM: Sumoylated. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TFII-I family. {ECO:0000255|PROSITE- CC ProRule:PRU00484}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB28803.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF017085; AAC53569.1; -; mRNA. DR EMBL; AF043219; AAC02990.1; -; mRNA. DR EMBL; AF043220; AAC02991.1; -; mRNA. DR EMBL; AF325177; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY030290; AAK49785.1; -; mRNA. DR EMBL; AY030291; AAK49786.1; -; mRNA. DR EMBL; AY030292; AAK49787.1; -; mRNA. DR EMBL; AY030293; AAK49788.1; -; mRNA. DR EMBL; BC053044; AAH53044.1; -; mRNA. DR EMBL; AK006796; BAB24743.1; -; mRNA. DR EMBL; AK013348; BAB28803.2; ALT_INIT; mRNA. DR EMBL; AF289666; AAF99338.1; -; Genomic_DNA. DR CCDS; CCDS39299.1; -. [Q9ESZ8-2] DR CCDS; CCDS39300.1; -. [Q9ESZ8-6] DR CCDS; CCDS39301.1; -. [Q9ESZ8-1] DR CCDS; CCDS57386.1; -. [Q9ESZ8-4] DR PIR; T03763; T03763. DR RefSeq; NP_001074215.1; NM_001080746.2. [Q9ESZ8-1] DR RefSeq; NP_001074216.1; NM_001080747.2. [Q9ESZ8-6] DR RefSeq; NP_001074217.1; NM_001080748.2. [Q9ESZ8-4] DR RefSeq; NP_034495.2; NM_010365.4. [Q9ESZ8-2] DR RefSeq; XP_017176169.1; XM_017320680.1. DR RefSeq; XP_017176170.1; XM_017320681.1. [Q9ESZ8-4] DR PDB; 1Q60; NMR; -; A=733-818. DR PDBsum; 1Q60; -. DR AlphaFoldDB; Q9ESZ8; -. DR SMR; Q9ESZ8; -. DR BioGRID; 200113; 16. DR IntAct; Q9ESZ8; 6. DR MINT; Q9ESZ8; -. DR STRING; 10090.ENSMUSP00000049625; -. DR GlyGen; Q9ESZ8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9ESZ8; -. DR PhosphoSitePlus; Q9ESZ8; -. DR SwissPalm; Q9ESZ8; -. DR EPD; Q9ESZ8; -. DR jPOST; Q9ESZ8; -. DR MaxQB; Q9ESZ8; -. DR PaxDb; 10090-ENSMUSP00000049625; -. DR PeptideAtlas; Q9ESZ8; -. DR ProteomicsDB; 271483; -. [Q9ESZ8-1] DR ProteomicsDB; 271484; -. [Q9ESZ8-2] DR ProteomicsDB; 271485; -. [Q9ESZ8-3] DR ProteomicsDB; 271486; -. [Q9ESZ8-4] DR ProteomicsDB; 271487; -. [Q9ESZ8-5] DR ProteomicsDB; 271488; -. [Q9ESZ8-6] DR Pumba; Q9ESZ8; -. DR Antibodypedia; 73029; 488 antibodies from 34 providers. DR DNASU; 14886; -. DR Ensembl; ENSMUST00000059042.15; ENSMUSP00000049625.8; ENSMUSG00000060261.17. [Q9ESZ8-1] DR Ensembl; ENSMUST00000082057.10; ENSMUSP00000080714.4; ENSMUSG00000060261.17. [Q9ESZ8-6] DR Ensembl; ENSMUST00000111261.12; ENSMUSP00000106892.5; ENSMUSG00000060261.17. [Q9ESZ8-2] DR Ensembl; ENSMUST00000173888.8; ENSMUSP00000133969.2; ENSMUSG00000060261.17. [Q9ESZ8-5] DR Ensembl; ENSMUST00000174155.8; ENSMUSP00000133566.2; ENSMUSG00000060261.17. [Q9ESZ8-1] DR Ensembl; ENSMUST00000174354.8; ENSMUSP00000134440.2; ENSMUSG00000060261.17. [Q9ESZ8-2] DR Ensembl; ENSMUST00000174513.8; ENSMUSP00000133489.2; ENSMUSG00000060261.17. [Q9ESZ8-4] DR Ensembl; ENSMUST00000174772.8; ENSMUSP00000133740.2; ENSMUSG00000060261.17. [Q9ESZ8-6] DR GeneID; 14886; -. DR KEGG; mmu:14886; -. DR UCSC; uc008zvj.3; mouse. [Q9ESZ8-1] DR UCSC; uc008zvk.3; mouse. [Q9ESZ8-2] DR UCSC; uc008zvl.3; mouse. [Q9ESZ8-6] DR UCSC; uc008zvm.3; mouse. [Q9ESZ8-4] DR AGR; MGI:1202722; -. DR CTD; 2969; -. DR MGI; MGI:1202722; Gtf2i. DR VEuPathDB; HostDB:ENSMUSG00000060261; -. DR eggNOG; ENOG502QWD0; Eukaryota. DR GeneTree; ENSGT00940000160349; -. DR HOGENOM; CLU_011773_0_0_1; -. DR InParanoid; Q9ESZ8; -. DR OMA; TEAWNAK; -. DR OrthoDB; 5308582at2759; -. DR PhylomeDB; Q9ESZ8; -. DR TreeFam; TF352524; -. DR BioGRID-ORCS; 14886; 1 hit in 84 CRISPR screens. DR ChiTaRS; Gtf2i; mouse. DR EvolutionaryTrace; Q9ESZ8; -. DR PRO; PR:Q9ESZ8; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9ESZ8; Protein. DR Bgee; ENSMUSG00000060261; Expressed in utricle of membranous labyrinth and 285 other cell types or tissues. DR ExpressionAtlas; Q9ESZ8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 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; IBA:GO_Central. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI. DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro. DR Gene3D; 3.90.1460.10; GTF2I-like; 6. DR InterPro; IPR004212; GTF2I. DR InterPro; IPR036647; GTF2I-like_rpt_sf. DR InterPro; IPR016659; TF_II-I. DR PANTHER; PTHR46304:SF2; GENERAL TRANSCRIPTION FACTOR II-I; 1. DR PANTHER; PTHR46304; GENERAL TRANSCRIPTION FACTOR II-I REPEAT DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF02946; GTF2I; 6. DR PIRSF; PIRSF016441; TF_II-I; 1. DR SUPFAM; SSF117773; GTF2I-like repeat; 6. DR PROSITE; PS51139; GTF2I; 6. DR Genevisible; Q9ESZ8; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CHAIN 2..998 FT /note="General transcription factor II-I" FT /id="PRO_0000083873" FT REPEAT 103..197 FT /note="GTF2I-like 1" FT REPEAT 352..446 FT /note="GTF2I-like 2" FT REPEAT 457..551 FT /note="GTF2I-like 3" FT REPEAT 562..656 FT /note="GTF2I-like 4" FT REPEAT 724..818 FT /note="GTF2I-like 5" FT REPEAT 859..953 FT /note="GTF2I-like 6" FT REGION 241..341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 661..714 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 816..836 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 960..998 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 319..326 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 324..339 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 661..675 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 688..713 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 130 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 248 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 353 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 398 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 412 FT /note="Phosphoserine; by PKG/PRKG1" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 450 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 503 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 517 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 556 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 558 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 668 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 674 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 715 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 722 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 784 FT /note="Phosphoserine; by PKG/PRKG1" FT /evidence="ECO:0000250|UniProtKB:P78347" FT MOD_RES 823 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 35 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 86 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 92 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 94 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 130 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 140 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 185 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 219 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 221 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 221 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 325 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 343 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 353 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 380 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 435 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 450 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 456 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 488 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 494 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 526 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 561 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 660 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 664 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 670 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 680 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 715 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 816 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 827 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 861 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 864 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 879 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 891 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 991 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT CROSSLNK 991 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P78347" FT VAR_SEQ 255..313 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:9521869" FT /id="VSP_003871" FT VAR_SEQ 255..292 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9521869" FT /id="VSP_003870" FT VAR_SEQ 255..273 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11827466, FT ECO:0000303|PubMed:9521869, ECO:0000303|Ref.2" FT /id="VSP_003869" FT VAR_SEQ 293..313 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:11827466, FT ECO:0000303|PubMed:9521869, ECO:0000303|Ref.2" FT /id="VSP_003872" FT CONFLICT 5 FT /note="V -> A (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="G -> R (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 127..130 FT /note="ALGK -> NTAL (in Ref. 5; BAB24743)" FT /evidence="ECO:0000305" FT CONFLICT 254 FT /note="Q -> QA (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 261 FT /note="G -> D (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="L -> Q (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 271..272 FT /note="AL -> PM (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 314 FT /note="D -> G (in Ref. 6)" FT /evidence="ECO:0000305" FT CONFLICT 334 FT /note="Missing (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 538 FT /note="I -> T (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 607 FT /note="L -> C (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 621 FT /note="P -> L (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 691 FT /note="P -> L (in Ref. 2; AAC02990/AAC02991)" FT /evidence="ECO:0000305" FT CONFLICT 748 FT /note="A -> T (in Ref. 1; AAC53569)" FT /evidence="ECO:0000305" FT CONFLICT 826 FT /note="R -> IFLSG (in Ref. 5; BAB28803)" FT /evidence="ECO:0000305" FT CONFLICT 966 FT /note="E -> Q (in Ref. 5; BAB28803)" FT /evidence="ECO:0000305" FT HELIX 733..749 FT /evidence="ECO:0007829|PDB:1Q60" FT HELIX 759..764 FT /evidence="ECO:0007829|PDB:1Q60" FT TURN 766..768 FT /evidence="ECO:0007829|PDB:1Q60" FT STRAND 769..773 FT /evidence="ECO:0007829|PDB:1Q60" FT TURN 783..785 FT /evidence="ECO:0007829|PDB:1Q60" FT HELIX 788..796 FT /evidence="ECO:0007829|PDB:1Q60" FT TURN 797..800 FT /evidence="ECO:0007829|PDB:1Q60" FT STRAND 802..806 FT /evidence="ECO:0007829|PDB:1Q60" FT HELIX 808..810 FT /evidence="ECO:0007829|PDB:1Q60" FT HELIX 812..817 FT /evidence="ECO:0007829|PDB:1Q60" SQ SEQUENCE 998 AA; 112265 MW; 3BC228A2F4F880CF CRC64; MAQVVMSALP AEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPEHYDLATL KWILENKAGI SFIIKRPFLE PKKHLGGRVL AAEAERSMLS PSGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ YNIQGPSETD GVDEKLPLSK ALQGSHHSSE GNEGTEVEVP AEDSTQHVPS ETSEDPEVEV TIEDDDYSPP TKRLKSTEPP PPPPVPEPAN AGKRKVREFN FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVV SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNSSPQTSA VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQNESE GPVIQESAEA SQLEVPVTEE IKETDGSSQI KQEPDPTW //