Q9Y5B9 (SP16H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FACT complex subunit SPT16

Alternative name(s):
Chromatin-specific transcription elongation factor 140 kDa subunit
FACT 140 kDa subunit
FACTp140
Facilitates chromatin transcription complex subunit SPT16
Short name=hSPT16

Gene names

Name:	SUPT16H
Synonyms:	FACT140, FACTP140

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1047 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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). Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14
Subunit structure	Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with NEK9. Binds to histone H2A-H2B. Interacts with GTF2E2. Ref.1 Ref.5 Ref.9 Ref.10 Ref.11 Ref.13
Subcellular location	Nucleus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.1
Tissue specificity	Ubiquitous. Ref.5
Domain	The Glu-rich acidic region in C-terminus is essential for FACT activity. Ref.12
Post-translational modification	ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic stress and correlates with dissociation of FACT from chromatin.
Sequence similarities	Belongs to the peptidase M24 family. SPT16 subfamily.
Caution	Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.
Sequence caution	The sequence AAH64561.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH73849.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Domain	Coiled coil
PTM	ADP-ribosylation Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW nucleosome disassembly Traceable author statement Ref.1. Source: ProtInc positive regulation of DNA-dependent transcription, elongation Traceable author statement Ref.1. Source: ProtInc positive regulation of viral transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3 Ref.4
	Chain	2 – 1047	1046	FACT complex subunit SPT16		PRO_0000245169
Regions
	Coiled coil	432 – 507	76	Potential
	Compositional bias	926 – 1011	86	Glu-rich (acidic)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3 Ref.4
	Modified residue	139	1	N6-acetyllysine Ref.18
	Modified residue	188	1	Phosphoserine Ref.21
	Modified residue	196	1	N6-acetyllysine Ref.18
	Modified residue	223	1	N6-acetyllysine Ref.18
	Modified residue	508	1	Phosphoserine Ref.17
	Modified residue	513	1	N6-acetyllysine Ref.18
	Modified residue	650	1	Phosphoserine Ref.19 Ref.21
	Modified residue	658	1	Phosphoserine Ref.21
	Modified residue	732	1	N6-acetyllysine Ref.18
	Modified residue	786	1	N6-acetyllysine Ref.18
	Modified residue	903	1	Phosphothreonine Ref.19
	Modified residue	904	1	N6-acetyllysine Ref.18
	Modified residue	979	1	Phosphoserine Ref.15 Ref.19 Ref.21
	Modified residue	982	1	Phosphoserine Ref.15 Ref.19 Ref.21
	Modified residue	986	1	Phosphoserine Ref.21
	Modified residue	1015	1	Phosphoserine Ref.17

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5B9 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 3E1B23C45BDC61C2	FASTA	1,047	119,914
	10 20 30 40 50 60 MAVTLDKDAY YRRVKRLYSN WRKGEDEYAN VDAIVVSVGV DEEIVYAKST ALQTWLFGYE 70 80 90 100 110 120 LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA PAITLLIREK NESNKSSFDK 130 140 150 160 170 180 MIEAIKESKN GKKIGVFSKD KFPGEFMKSW NDCLNKEGFD KIDISAVVAY TIAVKEDGEL 190 200 210 220 230 240 NLMKKAASIT SEVFNKFFKE RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE 250 260 270 280 290 300 MCYPPIIQSG GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPSQEVQE 310 320 330 340 350 360 NYNFLLQLQE ELLKELRHGV KICDVYNAVM DVVKKQKPEL LNKITKNLGF GMGIEFREGS 370 380 390 400 410 420 LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA LFIGDTVLVD EDGPATVLTS 430 440 450 460 470 480 VKKKVKNVGI FLKNEDEEEE EEEKDEAEDL LGRGSRAALL TERTRNEMTA EEKRRAHQKE 490 500 510 520 530 540 LAAQLNEEAK RRLTEQKGEQ QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM 550 560 570 580 590 600 PVFGIATPFH IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY 610 620 630 640 650 660 RASNIKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS LVINLNRSNP 670 680 690 700 710 720 KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMIIVL 730 740 750 760 770 780 HFHLKNAIMF GKKRHTDVQF YTEVGEITTD LGKHQHMHDR DDLYAEQMER EMRHKLKTAF 790 800 810 820 830 840 KNFIEKVEAL TKEELEFEVP FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV 850 860 870 880 890 900 ELIHFERVQF HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL 910 920 930 940 950 960 NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEEGDSE SEIEDETFNP SEDDYEEEEE 970 980 990 1000 1010 1020 DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA DRESRYEEEE EQSRSMSRKR 1030 1040 KASVHSSGRG SNRGSRHSSA PPKKKRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins." Orphanides G., Wu W.-H., Lane W.S., Hampsey M., Reinberg D. Nature 400:284-288(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH SSRP1; H2A AND H2B.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-638. Tissue: Brain, Eye and Testis.
[3]	Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12 AND 480-490, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Hepatoma.
[4]	Bienvenut W.V., Vousden K.H., Lukashchuk N. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12; 93-108 AND 582-596, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[5]	"Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68." Kang S.-W., Kuzuhara T., Horikoshi M. Genes Cells 5:251-263(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1047, TISSUE SPECIFICITY, INTERACTION WITH GTF2E2.
[6]	"FACT, a factor that facilitates transcript elongation through nucleosomes." Orphanides G., LeRoy G., Chang C.-H., Luse D.S., Reinberg D. Cell 92:105-116(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Requirement of RSF and FACT for transcription of chromatin templates in vitro." LeRoy G., Orphanides G., Lane W.S., Reinberg D. Science 282:1900-1904(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH." Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H. Mol. Cell 5:1067-1072(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1." Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H. Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
[10]	"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex." Keller D.M., Lu H. J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SSRP1; CSNK2A1; CSNK2A2 AND CSNK2B.
[11]	"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome." Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S. Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[12]	"FACT facilitates transcription-dependent nucleosome alteration." Belotserkovskaya R., Oh S., Bondarenko V.A., Orphanides G., Studitsky V.M., Reinberg D. Science 301:1090-1093(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN.
[13]	"Nek9, a novel FACT-associated protein, modulates interphase progression." Tan B.C.-M., Lee S.-C. J. Biol. Chem. 279:9321-9330(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEK9.
[14]	"Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II." Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 AND SER-982, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation." Huang J.-Y., Chen W.-H., Chang Y.-L., Wang H.-T., Chuang W.-T., Lee S.-C. Nucleic Acids Res. 34:2398-2407(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ADP-RIBOSYLATION.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 AND SER-1015, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-196; LYS-223; LYS-513; LYS-732; LYS-786 AND LYS-904, MASS SPECTROMETRY.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650; THR-903; SER-979 AND SER-982, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-650; SER-658; SER-979; SER-982 AND SER-986, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF152961 mRNA. Translation: AAD43978.1. BC000565 mRNA. Translation: AAH00565.1. BC014046 mRNA. Translation: AAH14046.1. BC064561 mRNA. Translation: AAH64561.1. Sequence problems. BC073849 mRNA. Translation: AAH73849.1. Sequence problems. AF164924 mRNA. Translation: AAF28231.1.
IPI	IPI00026970.
RefSeq	NP_009123.1. NM_007192.3.
UniGene	Hs.213724.
3D structure databases
ProteinModelPortal	Q9Y5B9.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42757N.
IntAct	Q9Y5B9. 13 interactions.
MINT	MINT-2823866.
STRING	9606.ENSP00000216297.
Protein family/group databases
MEROPS	M24.974.
PTM databases
PhosphoSite	Q9Y5B9.
Polymorphism databases
DMDM	74753511.
Proteomic databases
PaxDb	Q9Y5B9.
PeptideAtlas	Q9Y5B9.
PRIDE	Q9Y5B9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216297; ENSP00000216297; ENSG00000092201.
GeneID	11198.
KEGG	hsa:11198.
UCSC	uc001wao.2. human.
Organism-specific databases
CTD	11198.
GeneCards	GC14M021819.
HGNC	HGNC:11465. SUPT16H.
HPA	CAB022551.
MIM	605012. gene.
neXtProt	NX_Q9Y5B9.
PharmGKB	PA36251.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5406.
HOGENOM	HOG000209079.
HOVERGEN	HBG092544.
InParanoid	Q9Y5B9.
OMA	MEIIDAD.
OrthoDB	EOG40K7Z3.
PhylomeDB	Q9Y5B9.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_1788. Transcription. REACT_1892. Elongation arrest and recovery. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9Y5B9.
Bgee	Q9Y5B9.
CleanEx	HS_SUPT16H.
Genevestigator	Q9Y5B9.
GermOnline	ENSG00000092201. Homo sapiens.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR013719. DUF1747. IPR013953. FACT_Spt16p. IPR000994. Pept_M24_structural-domain. [Graphical view]
Pfam	PF00557. Peptidase_M24. 1 hit. PF08512. Rtt106. 1 hit. PF08644. SPT16. 1 hit. [Graphical view]
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SUPT16H. human.
GenomeRNAi	11198.
NextBio	42621.
SOURCE	Search...

Entry information

Entry name

SP16H_HUMAN

Accession

Primary (citable) accession number: Q9Y5B9
Secondary accession number(s): Q6GMT8 , Q6P2F1, Q6PJM1, Q9NRX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.