SUPT3_HUMAN
ID SUPT3_HUMAN Reviewed; 317 AA.
AC O75486; A6NKG9; B2R9Q5; O76066; Q5TAV9; Q86VN7;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transcription initiation protein SPT3 homolog;
DE AltName: Full=SPT3-like protein;
GN Name=SUPT3H; Synonyms=SPT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Craniofacial;
RX PubMed=9787080; DOI=10.1006/geno.1998.5500;
RA Yu J., Madison J.M., Mundlos S., Winston F., Olsen B.R.;
RT "Characterization of a human homologue of the Saccharomyces cerevisiae
RT transcription factor Spt3 (SUPT3H).";
RL Genomics 53:90-96(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 77-88 AND
RP 297-308.
RC TISSUE=Cervix carcinoma;
RX PubMed=9674425; DOI=10.1016/s0092-8674(00)81219-2;
RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J.,
RA Howard B.H., Qin J., Nakatani Y.;
RT "Histone-like TAFs within the PCAF histone acetylase complex.";
RL Cell 94:35-44(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TAFII31 AND GCN5L2.
RC TISSUE=Cervix carcinoma;
RX PubMed=9726987; DOI=10.1074/jbc.273.37.23781;
RA Martinez E., Kundu T.K., Fu J., Roeder R.G.;
RT "A human SPT3-TAFII31-GCN5-L acetylase complex distinct from transcription
RT factor IID.";
RL J. Biol. Chem. 273:23781-23785(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 [8]
RP IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; TAF6L;
RP TAF10; TAF12; TRRAP AND TAF9.
RC TISSUE=Fetal heart;
RX PubMed=9885574; DOI=10.1016/s1097-2765(00)80301-9;
RA Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J.,
RA Nakatani Y.;
RT "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the
RT ATM superfamily.";
RL Mol. Cell 2:869-875(1998).
RN [9]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; TAF2;
RP TAF4; TAF5; TRRAP; GCN5L2 AND TAF10.
RX PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
RA Brand M., Yamamoto K., Staub A., Tora L.;
RT "Identification of TATA-binding protein-free TAFII-containing complex
RT subunits suggests a role in nucleosome acetylation and signal
RT transduction.";
RL J. Biol. Chem. 274:18285-18289(1999).
RN [10]
RP IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [11]
RP IDENTIFICATION IN STAGA COMPLEX.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-123 AND LYS-163, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Probable transcriptional activator.
CC {ECO:0000269|PubMed:9787080}.
CC -!- SUBUNIT: Component of the PCAF complex, at least composed of
CC TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha,
CC TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Associates with
CC TAFII31 and GCN5L2. Component of the TFTC-HAT complex, at least
CC composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150,
CC TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP. Component
CC of the STAGA transcription coactivator-HAT complex, at least composed
CC of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12,
CC TRRAP and TAF9. The STAGA core complex is associated with a subcomplex
CC required for histone deubiquitination composed of ATXN7L3, ENY2 and
CC USP22. {ECO:0000269|PubMed:10373431, ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:9885574}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:9726987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75486-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75486-4; Sequence=VSP_059496;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including pancreas,
CC kidney, skeletal muscle, liver, lung, placenta, brain and heart.
CC -!- SIMILARITY: Belongs to the SPT3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC70014.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC70014.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC70014.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AF064804; AAC70014.1; ALT_SEQ; mRNA.
DR EMBL; AF069734; AAC39904.1; -; mRNA.
DR EMBL; AF073930; AAC36098.1; -; mRNA.
DR EMBL; AK313874; BAG36602.1; -; mRNA.
DR EMBL; AL096865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL499610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04274.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04275.1; -; Genomic_DNA.
DR EMBL; BC050384; AAH50384.1; -; mRNA.
DR CCDS; CCDS34465.1; -. [O75486-1]
DR CCDS; CCDS34466.1; -. [O75486-4]
DR RefSeq; NP_003590.1; NM_003599.3. [O75486-1]
DR RefSeq; NP_852001.1; NM_181356.2. [O75486-4]
DR RefSeq; XP_016866860.1; XM_017011371.1. [O75486-1]
DR RefSeq; XP_016866861.1; XM_017011372.1.
DR PDB; 7KTR; EM; 2.93 A; I=1-317.
DR PDB; 7KTS; EM; 19.09 A; I=1-317.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; O75486; -.
DR SMR; O75486; -.
DR BioGRID; 114042; 59.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR CORUM; O75486; -.
DR DIP; DIP-28148N; -.
DR IntAct; O75486; 14.
DR MINT; O75486; -.
DR STRING; 9606.ENSP00000360515; -.
DR iPTMnet; O75486; -.
DR PhosphoSitePlus; O75486; -.
DR BioMuta; SUPT3H; -.
DR EPD; O75486; -.
DR jPOST; O75486; -.
DR MassIVE; O75486; -.
DR MaxQB; O75486; -.
DR PaxDb; O75486; -.
DR PeptideAtlas; O75486; -.
DR PRIDE; O75486; -.
DR ProteomicsDB; 50042; -. [O75486-1]
DR Antibodypedia; 16814; 207 antibodies from 28 providers.
DR DNASU; 8464; -.
DR Ensembl; ENST00000371459.6; ENSP00000360514.1; ENSG00000196284.17. [O75486-1]
DR Ensembl; ENST00000371460.5; ENSP00000360515.1; ENSG00000196284.17. [O75486-4]
DR Ensembl; ENST00000475057.5; ENSP00000436411.1; ENSG00000196284.17. [O75486-1]
DR GeneID; 8464; -.
DR KEGG; hsa:8464; -.
DR MANE-Select; ENST00000371459.6; ENSP00000360514.1; NM_003599.4; NP_003590.1.
DR UCSC; uc003oxn.3; human. [O75486-1]
DR CTD; 8464; -.
DR DisGeNET; 8464; -.
DR GeneCards; SUPT3H; -.
DR HGNC; HGNC:11466; SUPT3H.
DR HPA; ENSG00000196284; Low tissue specificity.
DR MalaCards; SUPT3H; -.
DR MIM; 602947; gene.
DR neXtProt; NX_O75486; -.
DR OpenTargets; ENSG00000196284; -.
DR PharmGKB; PA36252; -.
DR VEuPathDB; HostDB:ENSG00000196284; -.
DR eggNOG; KOG3902; Eukaryota.
DR GeneTree; ENSGT00390000010738; -.
DR HOGENOM; CLU_061312_0_0_1; -.
DR InParanoid; O75486; -.
DR OMA; QFMFNEQ; -.
DR OrthoDB; 1552679at2759; -.
DR PhylomeDB; O75486; -.
DR TreeFam; TF323574; -.
DR PathwayCommons; O75486; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; O75486; -.
DR BioGRID-ORCS; 8464; 44 hits in 1079 CRISPR screens.
DR ChiTaRS; SUPT3H; human.
DR GeneWiki; Transcription_initiation_protein_SPT3_homolog; -.
DR GenomeRNAi; 8464; -.
DR Pharos; O75486; Tbio.
DR PRO; PR:O75486; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O75486; protein.
DR Bgee; ENSG00000196284; Expressed in sperm and 129 other tissues.
DR ExpressionAtlas; O75486; baseline and differential.
DR Genevisible; O75486; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR11380; PTHR11380; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..317
FT /note="Transcription initiation protein SPT3 homolog"
FT /id="PRO_0000072313"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..34
FT /note="MNNTAASPMSTATSSSGRSTGKSISFATELQSMM -> MVVFGTTFFNFDSF
FT IGKTDSIEIIGKSVFPYCYHNILPLLNDSGR (in isoform 2)"
FT /id="VSP_059496"
FT VARIANT 242
FT /note="D -> A (in dbSNP:rs16872923)"
FT /id="VAR_057000"
FT CONFLICT 42..46
FT /note="RPLHE -> SLFMR (in Ref. 1; AAC70014)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..175
FT /note="QTR -> HNS (in Ref. 1; AAC70014)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="L -> S (in Ref. 4; BAG36602)"
FT /evidence="ECO:0000305"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 45..73
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 215..243
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 317 AA; 35793 MW; AF339954A57DB5A6 CRC64;
MNNTAASPMS TATSSSGRST GKSISFATEL QSMMYSLGDA RRPLHETAVL VEDVVHTQLI
NLLQQAAEVS QLRGARVITP EDLLFLMRKD KKKLRRLLKY MFIRDYKSKI VKGIDEDDLL
EDKLSGSNNA NKRQKIAQDF LNSIDQTGEL LAMFEDDEID EVKQERMERA ERQTRIMDSA
QYAEFCESRQ LSFSKKASKF RDWLDCSSME IKPNVVAMEI LAYLAYETVA QLVDLALLVR
QDMVTKAGDP FSHAISATFI QYHNSAESTA ACGVEAHSDA IQPCHIREAI RRYSHRIGPL
SPFTNAYRRN GMAFLAC
