SP16H_MOUSE
ID SP16H_MOUSE Reviewed; 1047 AA.
AC Q920B9; Q3TZ48; Q3UFH0; Q921H4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
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;
GN Name=Supt16h; Synonyms=Fact140, Factp140, Supt16;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11471063; DOI=10.1007/s003350020036;
RA McGuire M.V., Suthipinijtham P., Gascoigne N.R.J.;
RT "The mouse Supt16h/Fact140 gene, encoding part of the FACT chromatin
RT transcription complex, maps close to Tcra and is highly expressed in
RT thymus.";
RL Mamm. Genome 12:664-667(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-637.
RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 803-1047.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND INTERACTION WITH MYOG.
RX PubMed=23364797; DOI=10.1074/jbc.m112.426718;
RA Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.;
RT "Myogenin recruits the histone chaperone facilitates chromatin
RT transcription (FACT) to promote nucleosome disassembly at muscle-specific
RT genes.";
RL J. Biol. Chem. 288:7676-7687(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196 AND LYS-513, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:0000250|UniProtKB:Q9Y5B9,
CC ECO:0000269|PubMed:23364797}.
CC -!- SUBUNIT: Interacts with MYOG (via C-terminal region) (PubMed:23364797).
CC Component of the FACT complex, a stable heterodimer of SSRP1 and
CC SUPT16H. Also a component of a CK2-SPT16-SSRP1 complex which forms
CC following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2
CC and CSNK2B. Interacts with NEK9. Binds to histone H2A-H2B. Identified
CC in a centromere complex containing histones H2A, H2B and H4, and at
CC least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and
CC RSF1. Interacts with GTF2E2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5B9, ECO:0000269|PubMed:23364797}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with RNA
CC polymerase II on chromatin. Recruited to actively transcribed loci.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, liver, heart,
CC kidneys, lungs, spleen, thymus, ovary, and testes, with highest levels
CC of expression observed in thymus. {ECO:0000269|PubMed:11471063}.
CC -!- DOMAIN: The C-terminal Glu-rich acidic region is essential for FACT
CC activity. {ECO:0000250}.
CC -!- PTM: ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic
CC stress and correlates with dissociation of FACT from chromatin.
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=AAH12433.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF323667; AAL04452.1; -; mRNA.
DR EMBL; AK148506; BAE28591.1; -; mRNA.
DR EMBL; AK158116; BAE34362.1; -; mRNA.
DR EMBL; BC012433; AAH12433.1; ALT_INIT; mRNA.
DR CCDS; CCDS27051.1; -.
DR RefSeq; NP_291096.2; NM_033618.3.
DR AlphaFoldDB; Q920B9; -.
DR SMR; Q920B9; -.
DR BioGRID; 227853; 28.
DR ComplexPortal; CPX-433; FACT complex.
DR DIP; DIP-55972N; -.
DR IntAct; Q920B9; 13.
DR MINT; Q920B9; -.
DR STRING; 10090.ENSMUSP00000042283; -.
DR MEROPS; M24.974; -.
DR iPTMnet; Q920B9; -.
DR PhosphoSitePlus; Q920B9; -.
DR EPD; Q920B9; -.
DR jPOST; Q920B9; -.
DR MaxQB; Q920B9; -.
DR PaxDb; Q920B9; -.
DR PeptideAtlas; Q920B9; -.
DR PRIDE; Q920B9; -.
DR ProteomicsDB; 257381; -.
DR DNASU; 114741; -.
DR GeneID; 114741; -.
DR KEGG; mmu:114741; -.
DR CTD; 114741; -.
DR MGI; MGI:1890948; Supt16.
DR eggNOG; KOG1189; Eukaryota.
DR InParanoid; Q920B9; -.
DR OrthoDB; 145488at2759; -.
DR PhylomeDB; Q920B9; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 114741; 25 hits in 106 CRISPR screens.
DR ChiTaRS; Supt16; mouse.
DR PRO; PR:Q920B9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q920B9; protein.
DR GO; GO:0035101; C:FACT complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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 Acetylation; ADP-ribosylation; Chromosome; Coiled coil; DNA damage;
KW DNA repair; DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT CHAIN 2..1047
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000245170"
FT REGION 491..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 465..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:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 513
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 732
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 786
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 903
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 904
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B9"
FT CONFLICT 453
FT /note="R -> G (in Ref. 1; AAL04452)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="K -> E (in Ref. 1; AAL04452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 119825 MW; 51931F5639CD221E CRC64;
MAVTLDKDAY YRRVKRLYSN WRKGEDEYAS IDAIVVSVGV DEEIVYAKST ALQTWLFGYE
LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA PAITLLVREK NESNKSSFDK
MIDAIKESKS GKKIGVFSKD KFPGEFMKSW SDCLNKEGFD KVDISAVVAY TIAVKEDGEL
NLMKKAASIT SEVFNKFFKE RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE
MCYPPIIQSG GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPTQEVQE
NYNFLLQLQE ELLKELRHGV KICDVYNSVM DVVKKQKPEL LNKITKNLGF GMGIEFREGS
LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA LFIGDTVLVD EDGPATILTS
VKKKVKNVGI FLKNEDDEEE EEEKDEAEDL LGRGSRAALL TERTRNEMTA EEKRRAHQKE
LAAQLNEEAK RRLTEQKGEQ QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM
PVFGIATPFH IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY
RASNMKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS LVINLNRSNP
KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMIIVL
HFHLKNAVMF GKKRHTDVQF YTEVGEITTD LGKHQHMHDR DDLYAEQMER EMRHKLKTAF
KNFIEKVEAL TKEELEFEVP FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV
ELIHFERVQF HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL
NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEDGDSE SEIEDETFNP SEDDYEEEEE
DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA DRESRYEEEE EQSRSMSRKR
KASVHSSGRG SNRGSRHSSA PPKKKRK
