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FACT complex subunit SPT16 (Chromatin-specific transcription elongation factor 140 kDa subunit) (FACT 140 kDa subunit) (FACTp140) (Facilitates chromatin transcription complex subunit SPT16) (hSPT16)

 SP16H_HUMAN             Reviewed;        1047 AA.
Q9Y5B9; Q6GMT8; Q6P2F1; Q6PJM1; Q9NRX0;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=FACT complex subunit SPT16;
AltName: Full=Chromatin-specific transcription elongation factor 140 kDa subunit;
AltName: Full=FACT 140 kDa subunit;
AltName: Full=FACTp140;
AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
Short=hSPT16;
Name=SUPT16H; Synonyms=FACT140, FACTP140;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, AND INTERACTION WITH SSRP1; H2A AND H2B.
PubMed=10421373; DOI=10.1038/22350;
Orphanides G., Wu W.-H., Lane W.S., Hampsey M., Reinberg D.;
"The chromatin-specific transcription elongation factor FACT comprises
human SPT16 and SSRP1 proteins.";
Nature 400:284-288(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-638.
TISSUE=Brain, Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-12 AND 480-490, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 2-12; 93-108 AND 582-596, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 801-1047, TISSUE SPECIFICITY, AND
INTERACTION WITH GTF2E2.
PubMed=10792464; DOI=10.1046/j.1365-2443.2000.00323.x;
Kang S.-W., Kuzuhara T., Horikoshi M.;
"Functional interaction of general transcription initiation factor
TFIIE with general chromatin factor SPT16/CDC68.";
Genes Cells 5:251-263(2000).
[6]
FUNCTION.
PubMed=9489704; DOI=10.1016/S0092-8674(00)80903-4;
Orphanides G., LeRoy G., Chang C.-H., Luse D.S., Reinberg D.;
"FACT, a factor that facilitates transcript elongation through
nucleosomes.";
Cell 92:105-116(1998).
[7]
FUNCTION.
PubMed=9836642; DOI=10.1126/science.282.5395.1900;
LeRoy G., Orphanides G., Lane W.S., Reinberg D.;
"Requirement of RSF and FACT for transcription of chromatin templates
in vitro.";
Science 282:1900-1904(1998).
[8]
FUNCTION.
PubMed=10912001; DOI=10.1016/S1097-2765(00)80272-5;
Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D.,
Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.;
"FACT relieves DSIF/NELF-mediated inhibition of transcriptional
elongation and reveals functional differences between P-TEFb and
TFIIH.";
Mol. Cell 5:1067-1072(2000).
[9]
FUNCTION, AND INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9;
Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H.,
Goodman R., Lozano G., Zhao Y., Lu H.;
"A DNA damage-induced p53 serine 392 kinase complex contains CK2,
hSpt16, and SSRP1.";
Mol. Cell 7:283-292(2001).
[10]
INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
PubMed=12393879; DOI=10.1074/jbc.M209820200;
Keller D.M., Lu H.;
"p53 serine 392 phosphorylation increases after UV through induction
of the assembly of the CK2.hSPT16.SSRP1 complex.";
J. Biol. Chem. 277:50206-50213(2002).
[11]
FUNCTION, AND DOMAIN.
PubMed=12934006; DOI=10.1126/science.1085703;
Belotserkovskaya R., Oh S., Bondarenko V.A., Orphanides G.,
Studitsky V.M., Reinberg D.;
"FACT facilitates transcription-dependent nucleosome alteration.";
Science 301:1090-1093(2003).
[12]
INTERACTION WITH NEK9.
PubMed=14660563; DOI=10.1074/jbc.M311477200;
Tan B.C.-M., Lee S.-C.;
"Nek9, a novel FACT-associated protein, modulates interphase
progression.";
J. Biol. Chem. 279:9321-9330(2004).
[13]
FUNCTION.
PubMed=16713563; DOI=10.1016/j.cell.2006.04.029;
Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A.,
Reinberg D.;
"Histone H2B monoubiquitination functions cooperatively with FACT to
regulate elongation by RNA polymerase II.";
Cell 125:703-717(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 AND SER-982, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
ADP-RIBOSYLATION.
PubMed=16682447; DOI=10.1093/nar/gkl241;
Huang J.-Y., Chen W.-H., Chang Y.-L., Wang H.-T., Chuang W.-T.,
Lee S.-C.;
"Modulation of nucleosome-binding activity of FACT by poly(ADP-
ribosyl)ation.";
Nucleic Acids Res. 34:2398-2407(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 AND SER-1015, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-196; LYS-223;
LYS-513; LYS-732; LYS-786 AND LYS-904, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650; THR-903; SER-979
AND SER-982, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-650; SER-979;
SER-982 AND SER-986, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-455; SER-508;
SER-650; SER-658; THR-903; SER-982 AND SER-1015, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[27]
SUBUNIT.
PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M.,
Syed S.H., Lone I.N., Boopathi R., Fontaine E., Papai G.,
Tachiwana H., Gautier T., Skoufias D., Padmanabhan K., Bednar J.,
Kurumizaka H., Schultz P., Angelov D., Hamiche A., Dimitrov S.;
"The flexible ends of CENP-A nucleosome are required for mitotic
fidelity.";
Mol. Cell 63:674-685(2016).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-497; LYS-513 AND LYS-647,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Component of the FACT complex, a general chromatin
factor that acts to reorganize nucleosomes. The FACT complex is
involved in multiple processes that require DNA as a template such
as mRNA elongation, DNA replication and DNA repair. During
transcription elongation the FACT complex acts as a histone
chaperone that both destabilizes and restores nucleosomal
structure. It facilitates the passage of RNA polymerase II and
transcription by promoting the dissociation of one histone H2A-H2B
dimer from the nucleosome, then subsequently promotes the
reestablishment of the nucleosome following the passage of RNA
polymerase II. The FACT complex is probably also involved in
phosphorylation of 'Ser-392' of p53/TP53 via its association with
CK2 (casein kinase II). {ECO:0000269|PubMed:10912001,
ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12934006,
ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704,
ECO:0000269|PubMed:9836642}.
-!- SUBUNIT: Interacts with MYOG (via C-terminal region) (By
similarity). Component of the FACT complex, a stable heterodimer
of SSRP1 and SUPT16H (PubMed:10421373). Also component of a CK2-
SPT16-SSRP1 complex which forms following UV irradiation, composed
of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (PubMed:11239457,
PubMed:12393879). Interacts with NEK9 (PubMed:14660563). Binds to
histone H2A-H2B (PubMed:10421373). Identified in a centromere
complex containing histones H2A, H2B and H4, and at least CENPA,
CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
(PubMed:27499292). Interacts with GTF2E2 (PubMed:10792464).
{ECO:0000250|UniProtKB:Q920B9, ECO:0000269|PubMed:10421373,
ECO:0000269|PubMed:10792464, ECO:0000269|PubMed:11239457,
ECO:0000269|PubMed:12393879, ECO:0000269|PubMed:14660563,
ECO:0000269|PubMed:27499292}.
-!- INTERACTION:
P33991:MCM4; NbExp=3; IntAct=EBI-1046849, EBI-374938;
Q08945:SSRP1; NbExp=3; IntAct=EBI-1046849, EBI-353771;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10421373}.
Chromosome {ECO:0000269|PubMed:10421373}. Note=Colocalizes with
RNA polymerase II on chromatin. Recruited to actively transcribed
loci.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10792464}.
-!- DOMAIN: The C-terminal Glu-rich acidic region is essential for
FACT activity. {ECO:0000269|PubMed:12934006}.
-!- PTM: ADP-ribosylated. ADP-ribosylation by PARP1 is induced by
genotoxic stress and correlates with dissociation of FACT from
chromatin.
-!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
{ECO:0000305}.
-!- CAUTION: Although related to the peptidase M24 family, this
protein lacks conserved active site residues suggesting that it
may lack peptidase activity. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH64561.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH73849.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF152961; AAD43978.1; -; mRNA.
EMBL; BC000565; AAH00565.1; -; mRNA.
EMBL; BC014046; AAH14046.1; -; mRNA.
EMBL; BC064561; AAH64561.1; ALT_SEQ; mRNA.
EMBL; BC073849; AAH73849.1; ALT_SEQ; mRNA.
EMBL; AF164924; AAF28231.1; -; mRNA.
CCDS; CCDS9569.1; -.
RefSeq; NP_009123.1; NM_007192.3.
UniGene; Hs.213724; -.
PDB; 4Z2M; X-ray; 2.98 A; B=644-930.
PDB; 4Z2N; X-ray; 1.92 A; A=644-930.
PDB; 5E5B; X-ray; 1.84 A; A=2-432.
PDBsum; 4Z2M; -.
PDBsum; 4Z2N; -.
PDBsum; 5E5B; -.
ProteinModelPortal; Q9Y5B9; -.
SMR; Q9Y5B9; -.
BioGrid; 116367; 158.
CORUM; Q9Y5B9; -.
DIP; DIP-42757N; -.
IntAct; Q9Y5B9; 53.
MINT; MINT-2823866; -.
STRING; 9606.ENSP00000216297; -.
MEROPS; M24.974; -.
iPTMnet; Q9Y5B9; -.
PhosphoSitePlus; Q9Y5B9; -.
SwissPalm; Q9Y5B9; -.
BioMuta; SUPT16H; -.
DMDM; 74753511; -.
EPD; Q9Y5B9; -.
MaxQB; Q9Y5B9; -.
PaxDb; Q9Y5B9; -.
PeptideAtlas; Q9Y5B9; -.
PRIDE; Q9Y5B9; -.
Ensembl; ENST00000216297; ENSP00000216297; ENSG00000092201.
GeneID; 11198; -.
KEGG; hsa:11198; -.
UCSC; uc001wao.2; human.
CTD; 11198; -.
DisGeNET; 11198; -.
EuPathDB; HostDB:ENSG00000092201.9; -.
GeneCards; SUPT16H; -.
HGNC; HGNC:11465; SUPT16H.
HPA; CAB022551; -.
HPA; HPA049787; -.
MIM; 605012; gene.
neXtProt; NX_Q9Y5B9; -.
OpenTargets; ENSG00000092201; -.
PharmGKB; PA36251; -.
eggNOG; KOG1189; Eukaryota.
eggNOG; COG5406; LUCA.
GeneTree; ENSGT00390000014495; -.
HOGENOM; HOG000209079; -.
HOVERGEN; HBG092544; -.
InParanoid; Q9Y5B9; -.
OMA; GLEFREN; -.
OrthoDB; EOG091G044Q; -.
PhylomeDB; Q9Y5B9; -.
TreeFam; TF300341; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-167287; HIV elongation arrest and recovery.
Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
ChiTaRS; SUPT16H; human.
GeneWiki; SUPT16H; -.
GenomeRNAi; 11198; -.
PRO; PR:Q9Y5B9; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000092201; -.
CleanEx; HS_SUPT16H; -.
ExpressionAtlas; Q9Y5B9; baseline and differential.
Genevisible; Q9Y5B9; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0035101; C:FACT complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0034724; P:DNA replication-independent nucleosome organization; IBA:GO_Central.
GO; GO:0006337; P:nucleosome disassembly; TAS:ProtInc.
GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; TAS:ProtInc.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
CDD; cd01091; CDC68-like; 1.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.40.350.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
InterPro; IPR036005; Creatinase/aminopeptidase-like.
InterPro; IPR013719; DUF1747.
InterPro; IPR029148; FACT-Spt16_Nlobe.
InterPro; IPR013953; FACT_Spt16p.
InterPro; IPR000994; Pept_M24.
InterPro; IPR033825; SPT16.
Pfam; PF14826; FACT-Spt16_Nlob; 1.
Pfam; PF00557; Peptidase_M24; 1.
Pfam; PF08512; Rtt106; 1.
Pfam; PF08644; SPT16; 1.
SMART; SM01285; FACT-Spt16_Nlob; 1.
SMART; SM01287; Rtt106; 1.
SMART; SM01286; SPT16; 1.
SUPFAM; SSF55920; SSF55920; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Chromosome; Coiled coil;
Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
CHAIN 2 1047 FACT complex subunit SPT16.
/FTId=PRO_0000245169.
COILED 432 507 {ECO:0000255}.
COMPBIAS 926 1011 Glu-rich (acidic).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
MOD_RES 139 139 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 196 196 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 223 223 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 513 513 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 658 658 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 732 732 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 786 786 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 903 903 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 904 904 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 979 979 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 982 982 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 986 986 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1015 1015 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 497 497 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 513 513 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
HELIX 7 23 {ECO:0000244|PDB:5E5B}.
HELIX 26 28 {ECO:0000244|PDB:5E5B}.
STRAND 32 38 {ECO:0000244|PDB:5E5B}.
HELIX 48 57 {ECO:0000244|PDB:5E5B}.
STRAND 62 68 {ECO:0000244|PDB:5E5B}.
STRAND 73 77 {ECO:0000244|PDB:5E5B}.
HELIX 79 89 {ECO:0000244|PDB:5E5B}.
HELIX 95 99 {ECO:0000244|PDB:5E5B}.
STRAND 103 107 {ECO:0000244|PDB:5E5B}.
STRAND 110 112 {ECO:0000244|PDB:5E5B}.
HELIX 115 127 {ECO:0000244|PDB:5E5B}.
STRAND 131 136 {ECO:0000244|PDB:5E5B}.
HELIX 145 155 {ECO:0000244|PDB:5E5B}.
STRAND 160 163 {ECO:0000244|PDB:5E5B}.
HELIX 165 173 {ECO:0000244|PDB:5E5B}.
HELIX 177 196 {ECO:0000244|PDB:5E5B}.
HELIX 198 207 {ECO:0000244|PDB:5E5B}.
HELIX 214 224 {ECO:0000244|PDB:5E5B}.
HELIX 228 230 {ECO:0000244|PDB:5E5B}.
TURN 231 233 {ECO:0000244|PDB:5E5B}.
HELIX 236 238 {ECO:0000244|PDB:5E5B}.
STRAND 239 243 {ECO:0000244|PDB:5E5B}.
STRAND 246 248 {ECO:0000244|PDB:5E5B}.
STRAND 256 259 {ECO:0000244|PDB:5E5B}.
STRAND 263 265 {ECO:0000244|PDB:5E5B}.
STRAND 268 275 {ECO:0000244|PDB:5E5B}.
STRAND 277 279 {ECO:0000244|PDB:5E5B}.
STRAND 286 293 {ECO:0000244|PDB:5E5B}.
HELIX 296 315 {ECO:0000244|PDB:5E5B}.
HELIX 322 336 {ECO:0000244|PDB:5E5B}.
HELIX 338 340 {ECO:0000244|PDB:5E5B}.
TURN 341 343 {ECO:0000244|PDB:5E5B}.
STRAND 349 351 {ECO:0000244|PDB:5E5B}.
STRAND 353 356 {ECO:0000244|PDB:5E5B}.
STRAND 358 362 {ECO:0000244|PDB:5E5B}.
STRAND 376 387 {ECO:0000244|PDB:5E5B}.
HELIX 394 397 {ECO:0000244|PDB:5E5B}.
STRAND 398 408 {ECO:0000244|PDB:5E5B}.
STRAND 411 414 {ECO:0000244|PDB:5E5B}.
HELIX 425 428 {ECO:0000244|PDB:5E5B}.
STRAND 655 657 {ECO:0000244|PDB:4Z2N}.
STRAND 661 669 {ECO:0000244|PDB:4Z2N}.
STRAND 671 674 {ECO:0000244|PDB:4Z2N}.
STRAND 677 682 {ECO:0000244|PDB:4Z2N}.
STRAND 684 691 {ECO:0000244|PDB:4Z2N}.
STRAND 696 700 {ECO:0000244|PDB:4Z2N}.
HELIX 701 703 {ECO:0000244|PDB:4Z2N}.
STRAND 704 710 {ECO:0000244|PDB:4Z2N}.
STRAND 715 730 {ECO:0000244|PDB:4Z2N}.
STRAND 733 743 {ECO:0000244|PDB:4Z2N}.
STRAND 747 749 {ECO:0000244|PDB:4Z2M}.
HELIX 759 790 {ECO:0000244|PDB:4Z2N}.
TURN 791 793 {ECO:0000244|PDB:4Z2N}.
HELIX 802 804 {ECO:0000244|PDB:4Z2N}.
STRAND 806 813 {ECO:0000244|PDB:4Z2N}.
STRAND 815 819 {ECO:0000244|PDB:4Z2N}.
STRAND 821 826 {ECO:0000244|PDB:4Z2N}.
STRAND 828 831 {ECO:0000244|PDB:4Z2N}.
STRAND 833 836 {ECO:0000244|PDB:4Z2N}.
HELIX 837 839 {ECO:0000244|PDB:4Z2N}.
STRAND 840 847 {ECO:0000244|PDB:4Z2N}.
STRAND 853 863 {ECO:0000244|PDB:4Z2N}.
STRAND 869 875 {ECO:0000244|PDB:4Z2N}.
HELIX 876 878 {ECO:0000244|PDB:4Z2N}.
HELIX 879 888 {ECO:0000244|PDB:4Z2N}.
STRAND 893 895 {ECO:0000244|PDB:4Z2N}.
HELIX 902 911 {ECO:0000244|PDB:4Z2N}.
HELIX 913 918 {ECO:0000244|PDB:4Z2N}.
HELIX 921 925 {ECO:0000244|PDB:4Z2N}.
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


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