SP16H_HUMAN
ID SP16H_HUMAN Reviewed; 1047 AA.
AC Q9Y5B9; Q6GMT8; Q6P2F1; Q6PJM1; Q9NRX0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Chromatin-specific transcription elongation factor 140 kDa subunit;
DE AltName: Full=FACT 140 kDa subunit;
DE AltName: Full=FACTp140;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
DE Short=hSPT16;
GN Name=SUPT16H; Synonyms=FACT140, FACTP140;
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], IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SSRP1; H2A AND H2B.
RX PubMed=10421373; DOI=10.1038/22350;
RA Orphanides G., Wu W.-H., Lane W.S., Hampsey M., Reinberg D.;
RT "The chromatin-specific transcription elongation factor FACT comprises
RT human SPT16 and SSRP1 proteins.";
RL Nature 400:284-288(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-638.
RC TISSUE=Brain, Eye, and Testis;
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 [3]
RP PROTEIN SEQUENCE OF 2-12 AND 480-490, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 2-12; 93-108 AND 582-596, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 801-1047, TISSUE SPECIFICITY, AND INTERACTION
RP WITH GTF2E2.
RX PubMed=10792464; DOI=10.1046/j.1365-2443.2000.00323.x;
RA Kang S.-W., Kuzuhara T., Horikoshi M.;
RT "Functional interaction of general transcription initiation factor TFIIE
RT with general chromatin factor SPT16/CDC68.";
RL Genes Cells 5:251-263(2000).
RN [6]
RP FUNCTION.
RX PubMed=9489704; DOI=10.1016/s0092-8674(00)80903-4;
RA Orphanides G., LeRoy G., Chang C.-H., Luse D.S., Reinberg D.;
RT "FACT, a factor that facilitates transcript elongation through
RT nucleosomes.";
RL Cell 92:105-116(1998).
RN [7]
RP FUNCTION.
RX PubMed=9836642; DOI=10.1126/science.282.5395.1900;
RA LeRoy G., Orphanides G., Lane W.S., Reinberg D.;
RT "Requirement of RSF and FACT for transcription of chromatin templates in
RT vitro.";
RL Science 282:1900-1904(1998).
RN [8]
RP FUNCTION.
RX PubMed=10912001; DOI=10.1016/s1097-2765(00)80272-5;
RA Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y.,
RA Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.;
RT "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation
RT and reveals functional differences between P-TEFb and TFIIH.";
RL Mol. Cell 5:1067-1072(2000).
RN [9]
RP FUNCTION, AND INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
RX PubMed=11239457; DOI=10.1016/s1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R.,
RA Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16,
RT and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [10]
RP INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
RX PubMed=12393879; DOI=10.1074/jbc.m209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction of the
RT assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [11]
RP FUNCTION, AND DOMAIN.
RX PubMed=12934006; DOI=10.1126/science.1085703;
RA Belotserkovskaya R., Oh S., Bondarenko V.A., Orphanides G., Studitsky V.M.,
RA Reinberg D.;
RT "FACT facilitates transcription-dependent nucleosome alteration.";
RL Science 301:1090-1093(2003).
RN [12]
RP INTERACTION WITH NEK9.
RX PubMed=14660563; DOI=10.1074/jbc.m311477200;
RA Tan B.C.-M., Lee S.-C.;
RT "Nek9, a novel FACT-associated protein, modulates interphase progression.";
RL J. Biol. Chem. 279:9321-9330(2004).
RN [13]
RP FUNCTION.
RX PubMed=16713563; DOI=10.1016/j.cell.2006.04.029;
RA Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.;
RT "Histone H2B monoubiquitination functions cooperatively with FACT to
RT regulate elongation by RNA polymerase II.";
RL Cell 125:703-717(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 AND SER-982, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP ADP-RIBOSYLATION.
RX PubMed=16682447; DOI=10.1093/nar/gkl241;
RA Huang J.-Y., Chen W.-H., Chang Y.-L., Wang H.-T., Chuang W.-T., Lee S.-C.;
RT "Modulation of nucleosome-binding activity of FACT by poly(ADP-
RT ribosyl)ation.";
RL Nucleic Acids Res. 34:2398-2407(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 AND SER-1015, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-196; LYS-223; LYS-513;
RP LYS-732; LYS-786 AND LYS-904, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650; THR-903; SER-979 AND
RP SER-982, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-650; SER-979;
RP SER-982 AND SER-986, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-455; SER-508;
RP SER-650; SER-658; THR-903; SER-982 AND SER-1015, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-647, 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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [27]
RP SUBUNIT.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [28]
RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN ICP22.
RX PubMed=28611249; DOI=10.1128/mbio.00745-17;
RA Fox H.L., Dembowski J.A., DeLuca N.A.;
RT "A Herpesviral Immediate Early Protein Promotes Transcription Elongation of
RT Viral Transcripts.";
RL MBio 8:0-0(2017).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-497; LYS-513 AND LYS-647, 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).
RN [30]
RP VARIANTS NEDDFAC VAL-162; PRO-432; SER-571 AND TRP-734, AND INVOLVEMENT IN
RP NEDDFAC.
RX PubMed=31924697; DOI=10.1136/jmedgenet-2019-106193;
RA Bina R., Matalon D., Fregeau B., Tarsitano J.J., Aukrust I., Houge G.,
RA Bend R., Warren H., Stevenson R.E., Stuurman K.E., Barkovich A.J.,
RA Sherr E.H.;
RT "De novo variants in SUPT16H cause neurodevelopmental disorders associated
RT with corpus callosum abnormalities.";
RL J. Med. Genet. 57:461-465(2020).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. The FACT complex is probably also
CC involved in phosphorylation of 'Ser-392' of p53/TP53 via its
CC association with CK2 (casein kinase II). {ECO:0000269|PubMed:10912001,
CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12934006,
CC ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704,
CC ECO:0000269|PubMed:9836642}.
CC -!- SUBUNIT: Interacts with MYOG (via C-terminal region) (By similarity).
CC Component of the FACT complex, a stable heterodimer of SSRP1 and
CC SUPT16H (PubMed:10421373). Also a component of a CK2-SPT16-SSRP1
CC complex which forms following UV irradiation, composed of SSRP1,
CC SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (PubMed:11239457,
CC PubMed:12393879). Interacts with NEK9 (PubMed:14660563). Binds to
CC histone H2A-H2B (PubMed:10421373). Identified in a centromere complex
CC containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC,
CC CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292).
CC Interacts with GTF2E2 (PubMed:10792464). {ECO:0000250|UniProtKB:Q920B9,
CC ECO:0000269|PubMed:10421373, ECO:0000269|PubMed:10792464,
CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12393879,
CC ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:27499292}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Herpes simplex virus 1
CC (HHV-1) protein ICP22; this interaction relocalizes the FACT complex to
CC viral genomes in infected cells. {ECO:0000269|PubMed:28611249}.
CC -!- INTERACTION:
CC Q9Y5B9; P05067: APP; NbExp=3; IntAct=EBI-1046849, EBI-77613;
CC Q9Y5B9; P33991: MCM4; NbExp=3; IntAct=EBI-1046849, EBI-374938;
CC Q9Y5B9; Q08945: SSRP1; NbExp=6; IntAct=EBI-1046849, EBI-353771;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10421373}. Chromosome
CC {ECO:0000269|PubMed:10421373}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10792464}.
CC -!- DOMAIN: The C-terminal Glu-rich acidic region is essential for FACT
CC activity. {ECO:0000269|PubMed:12934006}.
CC -!- PTM: ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic
CC stress and correlates with dissociation of FACT from chromatin.
CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic facies and thin
CC corpus callosum (NEDDFAC) [MIM:619480]: An autosomal dominant disorder
CC characterized by global developmental delay, impaired intellectual
CC development with poor or absent speech and language, and autistic-like
CC behaviors. Corpus callosum anomalies are visible on brain imaging. Most
CC patients have dysmorphic features including tall forehead, down-
CC slanting palpebral fissures, ear anomalies and broad nasal bridge.
CC Other variably present clinical features include seizures, sleeping
CC difficulties and precocious puberty. {ECO:0000269|PubMed:31924697}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64561.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH73849.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF152961; AAD43978.1; -; mRNA.
DR EMBL; BC000565; AAH00565.1; -; mRNA.
DR EMBL; BC014046; AAH14046.1; -; mRNA.
DR EMBL; BC064561; AAH64561.1; ALT_SEQ; mRNA.
DR EMBL; BC073849; AAH73849.1; ALT_SEQ; mRNA.
DR EMBL; AF164924; AAF28231.1; -; mRNA.
DR CCDS; CCDS9569.1; -.
DR RefSeq; NP_009123.1; NM_007192.3.
DR PDB; 4Z2M; X-ray; 2.98 A; B=644-930.
DR PDB; 4Z2N; X-ray; 1.92 A; A=644-930.
DR PDB; 5E5B; X-ray; 1.84 A; A=2-432.
DR PDB; 5UMT; X-ray; 2.09 A; A=1-434.
DR PDB; 5UMU; X-ray; 1.90 A; A/B=649-926.
DR PDB; 5XM2; X-ray; 2.19 A; A/B=1-437.
DR PDB; 6UPK; EM; 4.90 A; G=2-925.
DR PDB; 6UPL; EM; 7.40 A; G=2-925.
DR PDBsum; 4Z2M; -.
DR PDBsum; 4Z2N; -.
DR PDBsum; 5E5B; -.
DR PDBsum; 5UMT; -.
DR PDBsum; 5UMU; -.
DR PDBsum; 5XM2; -.
DR PDBsum; 6UPK; -.
DR PDBsum; 6UPL; -.
DR AlphaFoldDB; Q9Y5B9; -.
DR SMR; Q9Y5B9; -.
DR BioGRID; 116367; 345.
DR ComplexPortal; CPX-419; FACT complex.
DR CORUM; Q9Y5B9; -.
DR DIP; DIP-42757N; -.
DR IntAct; Q9Y5B9; 111.
DR MINT; Q9Y5B9; -.
DR STRING; 9606.ENSP00000216297; -.
DR MEROPS; M24.974; -.
DR GlyGen; Q9Y5B9; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9Y5B9; -.
DR MetOSite; Q9Y5B9; -.
DR PhosphoSitePlus; Q9Y5B9; -.
DR SwissPalm; Q9Y5B9; -.
DR BioMuta; SUPT16H; -.
DR DMDM; 74753511; -.
DR EPD; Q9Y5B9; -.
DR jPOST; Q9Y5B9; -.
DR MassIVE; Q9Y5B9; -.
DR MaxQB; Q9Y5B9; -.
DR PaxDb; Q9Y5B9; -.
DR PeptideAtlas; Q9Y5B9; -.
DR PRIDE; Q9Y5B9; -.
DR ProteomicsDB; 86338; -.
DR Antibodypedia; 22129; 441 antibodies from 40 providers.
DR DNASU; 11198; -.
DR Ensembl; ENST00000216297.7; ENSP00000216297.2; ENSG00000092201.10.
DR GeneID; 11198; -.
DR KEGG; hsa:11198; -.
DR MANE-Select; ENST00000216297.7; ENSP00000216297.2; NM_007192.4; NP_009123.1.
DR UCSC; uc001wao.2; human.
DR CTD; 11198; -.
DR DisGeNET; 11198; -.
DR GeneCards; SUPT16H; -.
DR HGNC; HGNC:11465; SUPT16H.
DR HPA; ENSG00000092201; Low tissue specificity.
DR MIM; 605012; gene.
DR MIM; 619480; phenotype.
DR neXtProt; NX_Q9Y5B9; -.
DR OpenTargets; ENSG00000092201; -.
DR PharmGKB; PA36251; -.
DR VEuPathDB; HostDB:ENSG00000092201; -.
DR eggNOG; KOG1189; Eukaryota.
DR GeneTree; ENSGT00390000014495; -.
DR HOGENOM; CLU_004627_0_0_1; -.
DR InParanoid; Q9Y5B9; -.
DR OMA; HQFFLDG; -.
DR OrthoDB; 145488at2759; -.
DR PhylomeDB; Q9Y5B9; -.
DR TreeFam; TF300341; -.
DR PathwayCommons; Q9Y5B9; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q9Y5B9; -.
DR BioGRID-ORCS; 11198; 766 hits in 1063 CRISPR screens.
DR ChiTaRS; SUPT16H; human.
DR GeneWiki; SUPT16H; -.
DR GenomeRNAi; 11198; -.
DR Pharos; Q9Y5B9; Tbio.
DR PRO; PR:Q9Y5B9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y5B9; protein.
DR Bgee; ENSG00000092201; Expressed in ventricular zone and 130 other tissues.
DR ExpressionAtlas; Q9Y5B9; baseline and differential.
DR Genevisible; Q9Y5B9; HS.
DR GO; GO:0035101; C:FACT complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:ComplexPortal.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; TAS:ProtInc.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; PTHR13980; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; Coiled coil;
KW Direct protein sequencing; DNA damage; DNA repair; DNA replication;
KW Host-virus interaction; Intellectual disability; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1047
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000245169"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..507
FT /evidence="ECO:0000255"
FT COMPBIAS 929..971
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 513
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 732
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 786
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 903
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 904
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VARIANT 162
FT /note="I -> V (in NEDDFAC; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31924697"
FT /id="VAR_086185"
FT VARIANT 432
FT /note="L -> P (in NEDDFAC; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31924697"
FT /id="VAR_086186"
FT VARIANT 571
FT /note="N -> S (in NEDDFAC; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31924697"
FT /id="VAR_086187"
FT VARIANT 734
FT /note="R -> W (in NEDDFAC; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31924697"
FT /id="VAR_086188"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:5E5B"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5UMT"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 177..196
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5E5B"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 296..315
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 322..336
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:5E5B"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5UMT"
FT STRAND 376..387
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 398..408
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:5E5B"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:5E5B"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:4Z2N"
FT STRAND 661..669
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 684..691
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 696..700
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 704..710
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 715..730
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 733..743
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:4Z2M"
FT HELIX 770..790
FT /evidence="ECO:0007829|PDB:5UMU"
FT TURN 791..793
FT /evidence="ECO:0007829|PDB:4Z2N"
FT HELIX 802..804
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 806..813
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 821..826
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 833..836
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 837..839
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 840..847
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 853..863
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 869..875
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 876..878
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 879..888
FT /evidence="ECO:0007829|PDB:5UMU"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 902..911
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 913..918
FT /evidence="ECO:0007829|PDB:5UMU"
FT HELIX 921..925
FT /evidence="ECO:0007829|PDB:5UMU"
SQ SEQUENCE 1047 AA; 119914 MW; 3E1B23C45BDC61C2 CRC64;
MAVTLDKDAY YRRVKRLYSN WRKGEDEYAN VDAIVVSVGV DEEIVYAKST ALQTWLFGYE
LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA PAITLLIREK NESNKSSFDK
MIEAIKESKN GKKIGVFSKD KFPGEFMKSW NDCLNKEGFD KIDISAVVAY TIAVKEDGEL
NLMKKAASIT SEVFNKFFKE RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE
MCYPPIIQSG GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPSQEVQE
NYNFLLQLQE ELLKELRHGV KICDVYNAVM DVVKKQKPEL LNKITKNLGF GMGIEFREGS
LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA LFIGDTVLVD EDGPATVLTS
VKKKVKNVGI FLKNEDEEEE EEEKDEAEDL LGRGSRAALL TERTRNEMTA EEKRRAHQKE
LAAQLNEEAK RRLTEQKGEQ QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM
PVFGIATPFH IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY
RASNIKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS LVINLNRSNP
KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMIIVL
HFHLKNAIMF GKKRHTDVQF YTEVGEITTD LGKHQHMHDR DDLYAEQMER EMRHKLKTAF
KNFIEKVEAL TKEELEFEVP FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV
ELIHFERVQF HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL
NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEEGDSE SEIEDETFNP SEDDYEEEEE
DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA DRESRYEEEE EQSRSMSRKR
KASVHSSGRG SNRGSRHSSA PPKKKRK
