GTF2I_MOUSE
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 03-AUG-2022, entry version 169.
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 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};
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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; 15.
DR IntAct; Q9ESZ8; 6.
DR MINT; Q9ESZ8; -.
DR STRING; 10090.ENSMUSP00000049625; -.
DR iPTMnet; Q9ESZ8; -.
DR PhosphoSitePlus; Q9ESZ8; -.
DR EPD; Q9ESZ8; -.
DR jPOST; Q9ESZ8; -.
DR MaxQB; Q9ESZ8; -.
DR PaxDb; Q9ESZ8; -.
DR PeptideAtlas; Q9ESZ8; -.
DR PRIDE; 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 Antibodypedia; 73029; 445 antibodies from 34 providers.
DR DNASU; 14886; -.
DR Ensembl; ENSMUST00000059042; ENSMUSP00000049625; ENSMUSG00000060261. [Q9ESZ8-1]
DR Ensembl; ENSMUST00000082057; ENSMUSP00000080714; ENSMUSG00000060261. [Q9ESZ8-6]
DR Ensembl; ENSMUST00000111261; ENSMUSP00000106892; ENSMUSG00000060261. [Q9ESZ8-2]
DR Ensembl; ENSMUST00000173888; ENSMUSP00000133969; ENSMUSG00000060261. [Q9ESZ8-5]
DR Ensembl; ENSMUST00000174155; ENSMUSP00000133566; ENSMUSG00000060261. [Q9ESZ8-1]
DR Ensembl; ENSMUST00000174354; ENSMUSP00000134440; ENSMUSG00000060261. [Q9ESZ8-2]
DR Ensembl; ENSMUST00000174513; ENSMUSP00000133489; ENSMUSG00000060261. [Q9ESZ8-4]
DR Ensembl; ENSMUST00000174772; ENSMUSP00000133740; ENSMUSG00000060261. [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 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; VEVTIEX; -.
DR OrthoDB; 115381at2759; -.
DR PhylomeDB; Q9ESZ8; -.
DR TreeFam; TF352524; -.
DR BioGRID-ORCS; 14886; 1 hit in 78 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 281 other tissues.
DR ExpressionAtlas; Q9ESZ8; baseline and differential.
DR Genevisible; Q9ESZ8; MM.
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:0100026; P:positive regulation of DNA repair by transcription from RNA polymerase II promoter; ISO:MGI.
DR Gene3D; 3.90.1460.10; -; 6.
DR InterPro; IPR004212; GTF2I.
DR InterPro; IPR036647; GTF2I-like_rpt_sf.
DR InterPro; IPR016659; TF_II-I.
DR Pfam; PF02946; GTF2I; 6.
DR PIRSF; PIRSF016441; TF_II-I; 1.
DR SUPFAM; SSF117773; SSF117773; 6.
DR PROSITE; PS51139; GTF2I; 6.
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
