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   27-MAR-2024, entry version 192.
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   PDB; 8I17; X-ray; 1.98 A; C/F/I=926-965.
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   PDBsum; 8I17; -.
DR   AlphaFoldDB; Q9Y5B9; -.
DR   EMDB; EMD-20840; -.
DR   EMDB; EMD-20841; -.
DR   SMR; Q9Y5B9; -.
DR   BioGRID; 116367; 440.
DR   ComplexPortal; CPX-419; FACT complex.
DR   CORUM; Q9Y5B9; -.
DR   DIP; DIP-42757N; -.
DR   IntAct; Q9Y5B9; 118.
DR   MINT; Q9Y5B9; -.
DR   STRING; 9606.ENSP00000216297; -.
DR   MEROPS; M24.974; -.
DR   GlyCosmos; Q9Y5B9; 1 site, 2 glycans.
DR   GlyGen; Q9Y5B9; 6 sites, 2 O-linked glycans (6 sites).
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; 9606-ENSP00000216297; -.
DR   PeptideAtlas; Q9Y5B9; -.
DR   ProteomicsDB; 86338; -.
DR   Pumba; Q9Y5B9; -.
DR   Antibodypedia; 22129; 477 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   AGR; HGNC:11465; -.
DR   CTD; 11198; -.
DR   DisGeNET; 11198; -.
DR   GeneCards; SUPT16H; -.
DR   HGNC; HGNC:11465; SUPT16H.
DR   HPA; ENSG00000092201; Low tissue specificity.
DR   MalaCards; SUPT16H; -.
DR   MIM; 605012; gene.
DR   MIM; 619480; phenotype.
DR   neXtProt; NX_Q9Y5B9; -.
DR   OpenTargets; ENSG00000092201; -.
DR   Orphanet; 261229; 14q11.2 microduplication syndrome.
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; YHINTIP; -.
DR   OrthoDB; 169847at2759; -.
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; 799 hits in 1141 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 132 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5B9; baseline and differential.
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:0006334; P:nucleosome assembly; NAS: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:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd01091; CDC68-like; 1.
DR   Gene3D; 2.30.29.150; -; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR   Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
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; IPR013719; RTT106/SPT16-like_middle_dom.
DR   InterPro; IPR040258; Spt16.
DR   InterPro; IPR048969; SPT16_C.
DR   InterPro; IPR033825; Spt16_M24.
DR   PANTHER; PTHR13980; CDC68 RELATED; 1.
DR   PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR   Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   Pfam; PF08644; SPT16; 1.
DR   Pfam; PF21091; SPT16_C; 1.
DR   SMART; SM01285; FACT-Spt16_Nlob; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SMART; SM01286; SPT16; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   Genevisible; Q9Y5B9; HS.
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; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:31924697"
FT                   /id="VAR_086185"
FT   VARIANT         432
FT                   /note="L -> P (in NEDDFAC; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:31924697"
FT                   /id="VAR_086186"
FT   VARIANT         571
FT                   /note="N -> S (in NEDDFAC; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:31924697"
FT                   /id="VAR_086187"
FT   VARIANT         734
FT                   /note="R -> W (in NEDDFAC; uncertain 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"
FT   HELIX           941..944
FT                   /evidence="ECO:0007829|PDB:8I17"
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
//