UniProt Accession

 SP16H_HUMAN; Q9Y5B9; Q6GMT8; Q6P2F1; Q6PJM1; Q9NRX0 

Genbank Protein ID

 AF152961; BC000565; BC014046; BC064561; BC073849; AF164924 

Genbank Nucleotide ID

 AAD43978.1; AAH00565.1; AAH14046.1; AAH64561.1; AAH73849.1; AAF28231.1 

Protein Name

 FACT complex subunit SPT16 

Protein Synonyms/Alias

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

Gene Name

 SUPT16H 

Gene Synonyms/Alias

 FACT140; FACTP140 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MAVTLDKDAYYRRV	ubiquitination	[1]
80	IIFMASKKKVEFLKQ	ubiquitination	[1]
86	KKKVEFLKQIANTKG	ubiquitination	[2, 3]
92	LKQIANTKGNENANG	ubiquitination	[1]
120	SNKSSFDKMIEAIKE	acetylation	[4]
120	SNKSSFDKMIEAIKE	ubiquitination	[1, 2, 3, 4]
126	DKMIEAIKESKNGKK	ubiquitination	[1]
139	KKIGVFSKDKFPGEF	acetylation	[4, 5, 6]
141	IGVFSKDKFPGEFMK	acetylation	[4]
156	SWNDCLNKEGFDKID	ubiquitination	[4, 7]
196	ITSEVFNKFFKERVM	acetylation	[4, 5]
196	ITSEVFNKFFKERVM	ubiquitination	[1, 2, 3, 4, 7]
199	EVFNKFFKERVMEIV	ubiquitination	[8]
211	EIVDADEKVRHSKLA	acetylation	[4]
211	EIVDADEKVRHSKLA	ubiquitination	[1, 8]
216	DEKVRHSKLAESVEK	acetylation	[4, 6]
223	KLAESVEKAIEEKKY	acetylation	[4, 5]
263	KFSVVSDKNHMHFGA	ubiquitination	[1]
280	CAMGIRFKSYCSNLV	ubiquitination	[1]
335	AVMDVVKKQKPELLN	acetylation	[5]
337	MDVVKKQKPELLNKI	acetylation	[5]
366	GSLVINSKNQYKLKK	ubiquitination	[1, 4, 7]
370	INSKNQYKLKKGMVF	ubiquitination	[4]
426	TSVKKKVKNVGIFLK	ubiquitination	[2, 3]
479	EKRRAHQKELAAQLN	ubiquitination	[1, 4, 7]
490	AQLNEEAKRRLTEQK	ubiquitination	[1]
497	KRRLTEQKGEQQIQK	ubiquitination	[1, 4, 8, 9]
504	KGEQQIQKARKSNVS	ubiquitination	[1, 10]
513	RKSNVSYKNPSLMPK	acetylation	[5, 6, 11]
513	RKSNVSYKNPSLMPK	ubiquitination	[1, 2, 3, 7, 8]
596	NPEATFVKEITYRAS	acetylation	[4, 11]
596	NPEATFVKEITYRAS	ubiquitination	[1, 2, 3, 4, 8, 10, 12]
606	TYRASNIKAPGEQTV	ubiquitination	[1, 4]
626	QNAFRIIKEVQKRYK	acetylation	[6]
647	KEKEGIVKQDSLVIN	ubiquitination	[1, 2, 3, 4, 8]
663	NRSNPKLKDLYIRPN	acetylation	[4]
663	NRSNPKLKDLYIRPN	ubiquitination	[1, 2, 3, 4]
674	IRPNIAQKRMQGSLE	acetylation	[4, 6, 11]
674	IRPNIAQKRMQGSLE	ubiquitination	[1, 2, 3]
696	FTSVRGDKVDILYNN	ubiquitination	[1, 2, 3, 4, 7]
732	KNAIMFGKKRHTDVQ	acetylation	[5]
733	NAIMFGKKRHTDVQF	ubiquitination	[1]
753	EITTDLGKHQHMHDR	ubiquitination	[1]
777	REMRHKLKTAFKNFI	ubiquitination	[1]
781	HKLKTAFKNFIEKVE	acetylation	[4]
781	HKLKTAFKNFIEKVE	ubiquitination	[1, 2, 3]
786	AFKNFIEKVEALTKE	acetylation	[4, 5, 6]
786	AFKNFIEKVEALTKE	ubiquitination	[2, 3]
792	EKVEALTKEELEFEV	ubiquitination	[8]
904	VQSLNWTKIMKTIVD	acetylation	[5, 6]
904	VQSLNWTKIMKTIVD	ubiquitination	[1, 2, 3, 4, 10]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [11] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [12] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 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). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 139 139 N6-acetyllysine.
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 196 196 N6-acetyllysine.
 MOD_RES 223 223 N6-acetyllysine.
 MOD_RES 508 508 Phosphoserine.
 MOD_RES 513 513 N6-acetyllysine.
 MOD_RES 650 650 Phosphoserine.
 MOD_RES 658 658 Phosphoserine.
 MOD_RES 732 732 N6-acetyllysine.
 MOD_RES 786 786 N6-acetyllysine.
 MOD_RES 903 903 Phosphothreonine.
 MOD_RES 904 904 N6-acetyllysine.
 MOD_RES 979 979 Phosphoserine.
 MOD_RES 982 982 Phosphoserine.
 MOD_RES 986 986 Phosphoserine.
 MOD_RES 1015 1015 Phosphoserine.  

Keyword

 Acetylation; ADP-ribosylation; Chromosome; Coiled coil; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1047 AA 

Protein Sequence

Gene Ontology

 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0006337; P:nucleosome disassembly; TAS:ProtInc.
 GO:0032786; P:positive regulation of DNA-dependent transcription, elongation; TAS:ProtInc.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 

Interpro

 IPR013719; DUF1747.
 IPR013953; FACT_Spt16p.
 IPR000994; Pept_M24_structural-domain. 

Pfam

 PF00557; Peptidase_M24
 PF08512; Rtt106
 PF08644; SPT16 

SMART

  

PROSITE

  

PRINTS