SPT5H_MOUSE
ID SPT5H_MOUSE Reviewed; 1082 AA.
AC O55201; Q3UJ77; Q3UJH1; Q3UKD7; Q3UM54; Q6PB73; Q6PDP0; Q6PFR4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
GN Name=Supt5h; Synonyms=Supt5;
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] (ISOFORM 1).
RX PubMed=9480761; DOI=10.1006/geno.1997.5137;
RA Chiang P.-W., Stubbs L., Zhang L., Kurnit D.M.;
RT "Isolation of murine SPT5 homologue: completion of the isolation and
RT characterization of human and murine homologues of yeast chromatin
RT structural protein complex SPT4, SPT5, and SPT6.";
RL Genomics 47:426-428(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart, Mammary gland, and Placenta;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Mammary tumor, Olfactory epithelium, and Salivary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-36; THR-661 AND
RP SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-712, AND IDENTIFICATION BY MASS
RP 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-690, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the DRB sensitivity-inducing factor complex
CC (DSIF complex), which regulates mRNA processing and transcription
CC elongation by RNA polymerase II. DSIF positively regulates mRNA capping
CC by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A.
CC DSIF also acts cooperatively with the negative elongation factor
CC complex (NELF complex) to enhance transcriptional pausing at sites
CC proximal to the promoter. Transcriptional pausing may facilitate the
CC assembly of an elongation competent RNA polymerase II complex. DSIF and
CC NELF promote pausing by inhibition of the transcription elongation
CC factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at
CC transcription pause sites and stimulates the weak intrinsic nuclease
CC activity of the enzyme. Cleavage of blocked transcripts by RNA
CC polymerase II promotes the resumption of transcription from the new 3'
CC terminus and may allow repeated attempts at transcription through
CC natural pause sites (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SUPT4H1 to form DSIF. DSIF interacts with the
CC positive transcription elongation factor b complex (P-TEFb complex),
CC which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts
CC with RNA polymerase II, and this interaction is reduced by
CC phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb.
CC DSIF also interacts with the NELF complex, which is composed of NELFA,
CC NELFB, NELFD and NELFE, and this interaction occurs following prior
CC binding of DSIF to RNA polymerase II. Also interacts with
CC PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can
CC interact with PIN1. Component of a complex which is at least composed
CC of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin (By similarity). Interacts
CC with MCM3AP (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O00267}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O55201-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O55201-2; Sequence=VSP_016283;
CC -!- PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively
CC regulates interaction with P-TEFb and RNA polymerase II (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb
CC alleviates transcriptional pausing. Phosphorylation may also stimulate
CC interaction with PIN1. Bulk phosphorylation occurs predominantly in
CC mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57449.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U88539; AAC40052.1; -; mRNA.
DR EMBL; AK145117; BAE26244.1; -; mRNA.
DR EMBL; AK146055; BAE26864.1; -; mRNA.
DR EMBL; AK146453; BAE27184.1; -; mRNA.
DR EMBL; AK146583; BAE27278.1; -; mRNA.
DR EMBL; AK146650; BAE27330.1; -; mRNA.
DR EMBL; BC007132; AAH07132.1; -; mRNA.
DR EMBL; BC057449; AAH57449.1; ALT_INIT; mRNA.
DR EMBL; BC058598; AAH58598.1; -; mRNA.
DR EMBL; BC059849; AAH59849.1; -; mRNA.
DR CCDS; CCDS39857.1; -. [O55201-1]
DR PIR; T42204; T42204.
DR RefSeq; NP_038704.1; NM_013676.1. [O55201-1]
DR AlphaFoldDB; O55201; -.
DR SMR; O55201; -.
DR BioGRID; 203575; 30.
DR IntAct; O55201; 2.
DR STRING; 10090.ENSMUSP00000003527; -.
DR iPTMnet; O55201; -.
DR PhosphoSitePlus; O55201; -.
DR SwissPalm; O55201; -.
DR EPD; O55201; -.
DR jPOST; O55201; -.
DR MaxQB; O55201; -.
DR PaxDb; O55201; -.
DR PeptideAtlas; O55201; -.
DR PRIDE; O55201; -.
DR ProteomicsDB; 254549; -. [O55201-1]
DR ProteomicsDB; 254550; -. [O55201-2]
DR Antibodypedia; 16797; 188 antibodies from 29 providers.
DR DNASU; 20924; -.
DR Ensembl; ENSMUST00000003527; ENSMUSP00000003527; ENSMUSG00000003435. [O55201-1]
DR Ensembl; ENSMUST00000209141; ENSMUSP00000147164; ENSMUSG00000003435. [O55201-1]
DR GeneID; 20924; -.
DR KEGG; mmu:20924; -.
DR UCSC; uc009fyh.1; mouse. [O55201-1]
DR CTD; 20924; -.
DR MGI; MGI:1202400; Supt5.
DR VEuPathDB; HostDB:ENSMUSG00000003435; -.
DR eggNOG; KOG1999; Eukaryota.
DR GeneTree; ENSGT00440000037640; -.
DR HOGENOM; CLU_003537_0_0_1; -.
DR InParanoid; O55201; -.
DR OMA; VGYMNTP; -.
DR OrthoDB; 828863at2759; -.
DR PhylomeDB; O55201; -.
DR TreeFam; TF105730; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-72086; mRNA Capping.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR BioGRID-ORCS; 20924; 26 hits in 112 CRISPR screens.
DR ChiTaRS; Supt5; mouse.
DR PRO; PR:O55201; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O55201; protein.
DR Bgee; ENSMUSG00000003435; Expressed in placenta labyrinth and 275 other tissues.
DR ExpressionAtlas; O55201; baseline and differential.
DR Genevisible; O55201; MM.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1082
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208469"
FT DOMAIN 271..304
FT /note="KOW 1"
FT DOMAIN 418..449
FT /note="KOW 2"
FT DOMAIN 470..501
FT /note="KOW 3"
FT DOMAIN 592..625
FT /note="KOW 4"
FT DOMAIN 698..731
FT /note="KOW 5"
FT REPEAT 748..753
FT /note="CTR1-1; approximate"
FT REPEAT 754..759
FT /note="CTR1-2"
FT REPEAT 760..765
FT /note="CTR1-3"
FT REPEAT 766..772
FT /note="CTR1-4"
FT REPEAT 775..781
FT /note="CTR1-5"
FT REPEAT 782..788
FT /note="CTR1-6"
FT REPEAT 790..796
FT /note="CTR1-7"
FT REPEAT 797..803
FT /note="CTR1-8"
FT REPEAT 805..811
FT /note="CTR1-9"
FT REPEAT 838..845
FT /note="CTR2-1"
FT REPEAT 848..856
FT /note="CTR2-2; approximate"
FT REPEAT 857..863
FT /note="CTR2-3; approximate"
FT REPEAT 875..879
FT /note="CTR2-4; half-length"
FT REPEAT 890..896
FT /note="CTR2-5; approximate"
FT REPEAT 898..905
FT /note="CTR2-6"
FT REPEAT 910..915
FT /note="CTR2-7; approximate"
FT REPEAT 918..924
FT /note="CTR2-8"
FT REPEAT 926..933
FT /note="CTR2-9"
FT REPEAT 937..944
FT /note="CTR2-10"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..268
FT /note="Interaction with SUPT4H1 and SUPT4H2"
FT /evidence="ECO:0000250"
FT REGION 311..418
FT /note="Interaction with RNA polymerase II"
FT /evidence="ECO:0000250"
FT REGION 669..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..811
FT /note="9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-
FT X-[YQ], motif CTR1"
FT REGION 838..944
FT /note="10 X 8 AA approximate tandem repeats of P-[TS]-P-S-
FT P-[QA]-[SG]-Y, motif CTR2"
FT COMPBIAS 1..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 690
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 690
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 692
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 692
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 692
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 712
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 769
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 778
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 785
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 800
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT MOD_RES 1028
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT CROSSLNK 1031
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00267"
FT VAR_SEQ 1..194
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016283"
FT CONFLICT 30
FT /note="Q -> R (in Ref. 2; BAE26244)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="E -> EE (in Ref. 2; BAE26244)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="V -> L (in Ref. 2; BAE27278)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="K -> E (in Ref. 2; BAE27184)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="V -> E (in Ref. 2; BAE26864)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="H -> N (in Ref. 3; AAH58598)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="G -> D (in Ref. 2; BAE26864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="L -> I (in Ref. 2; BAE26864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1082 AA; 120664 MW; 109D0D8D2D71DDE7 CRC64;
MSDSEDSNFS EEEDSERSSE AEEAEVEEDQ RSAAGSEKEE EPEEEEEEEE EYDEEEEEED
DDRPPKKPRH GGFILDEADV DDEYEDEDQW EDGAEDILEK EEIEASNIDN VVLDEDRSGA
RRLQNLWRDQ REEELGEYYM KKYAKSSVGE TVYGGSDELS DDITQQQLLP GVKDPNLWTV
KCKIGEERAT AISLMRKFIA YQFTDTPLQI KSVVAPEHVK GYIYVEAYKQ THVKQAIEGV
GNLRLGYWNQ QMVPIKEMTD VLKVVKEVAN LKPKSWVRLK RGIYKDDIAQ VDYVEPSQNT
ISLKMIPRID YDRIKARMSL KDWFAKRKKF KRPPQRLFDA EKIRSLGGDV ASDGDFLIFE
GNRYSRKGFL FKSFAMSAVI TEGVKPTLSE LEKFEDQPEG IDLEVVTEST GKEREHNFQP
GDNVEVCEGE LINLQGKVLS VDGNKITIMP KHEDLKDMLE FPAQELRKYF KMGDHVKVIA
GRFEGDTGLI VRVEENFVIL FSDLTMHELK VLPRDLQLCS ETASGVDVGG QHEWGELVQL
DPRTVGVIVR LERETFQVLN MHGKVVTVRH QAVTQKKDNR FAVALDSDQN NIHVKDIVKV
IDGPHSGREG EIRHLYRSFA FLHCKKLVEN GGMFVCKARH LVLAGGSKPR DVTNLTVGGF
TPMSPRISSP MHPSAEGQHG GFGSPGGMSR GRGRRDNELI GQTVRISQGP YKGYIGVVKD
ATESTARVEL HSTCQTISVD RQRLTTVDSQ RPGGMTSTYG RTPMYGSQTP MYGSGSRTPM
YGSQTPLQDG SRTPHYGSQT PLHDGSRTPA QSGAWDPNNP NTPSRAEEEY EYAFDDEPTP
SPQAYGGTPN PQTPGYPDPS SPQVNPQYNP QTPGTPAMYN TDQFSPYAAP SPQGSYQPSP
SPQSYHQVAP SPAGYQNTHS PASYHPTPSP MAYQASPSPS PVGYSPMTPG APSPGGYNPH
TPGSGIEQNS SDWVTTDIQV KVRDTYLDTQ IVGQTGVIRS VTGGMCSVYL KDSEKVVSIS
SEHLEPITPT KNNKVKVILG EDREATGVLL SIDGEDGIIR MDLEDQQIKI LNLRFLGKLL
EA
