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Protein

FACT complex subunit SPT16

Gene

Supt16h

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Protein family/group databases

MEROPSiM24.974.

Names & Taxonomyi

Protein namesi
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
Gene namesi
Name:Supt16h
Synonyms:Fact140, Factp140, Supt16
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1890948. Supt16.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10471046FACT complex subunit SPT16PRO_0000245170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei196 – 1961N6-acetyllysineCombined sources
Modified residuei223 – 2231N6-acetyllysineBy similarity
Modified residuei508 – 5081PhosphoserineBy similarity
Modified residuei513 – 5131N6-acetyllysineCombined sources
Cross-linki647 – 647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei650 – 6501PhosphoserineBy similarity
Modified residuei732 – 7321N6-acetyllysineBy similarity
Modified residuei786 – 7861N6-acetyllysineBy similarity
Modified residuei903 – 9031PhosphothreonineBy similarity
Modified residuei904 – 9041N6-acetyllysineBy similarity
Modified residuei979 – 9791PhosphoserineBy similarity
Modified residuei982 – 9821PhosphoserineBy similarity
Modified residuei986 – 9861PhosphoserineBy similarity
Modified residuei1015 – 10151PhosphoserineBy similarity

Post-translational modificationi

ADP-ribosylated. ADP-ribosylation by PARP1 is induced by genotoxic stress and correlates with dissociation of FACT from chromatin.

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ920B9.
MaxQBiQ920B9.
PaxDbiQ920B9.
PRIDEiQ920B9.

PTM databases

iPTMnetiQ920B9.
PhosphoSiteiQ920B9.

Expressioni

Tissue specificityi

Widely expressed. Expressed in brain, liver, heart, kidneys, lungs, spleen, thymus, ovary, and testes, with highest levels of expression observed in thymus.1 Publication

Gene expression databases

CleanExiMM_SUPT16H.

Interactioni

Subunit structurei

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. Interacts with NEK9. Binds to histone H2A-H2B. Interacts with GTF2E2 (By similarity). Interacts with MYOG (via C-terminal region).By similarity1 Publication

Protein-protein interaction databases

BioGridi227853. 6 interactions.
DIPiDIP-55972N.
IntActiQ920B9. 9 interactions.
MINTiMINT-4122296.
STRINGi10090.ENSMUSP00000042283.

Structurei

3D structure databases

ProteinModelPortaliQ920B9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili465 – 50743Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi438 – 4436Poly-Glu
Compositional biasi926 – 101186Glu-rich (acidic)Add
BLAST

Domaini

The C-terminal Glu-rich acidic region is essential for FACT activity.By similarity

Sequence similaritiesi

Belongs to the peptidase M24 family. SPT16 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1189. Eukaryota.
COG5406. LUCA.
HOGENOMiHOG000209079.
HOVERGENiHBG092544.
InParanoidiQ920B9.
PhylomeDBiQ920B9.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]
SMARTiSM01285. FACT-Spt16_Nlob. 1 hit.
SM01287. Rtt106. 1 hit.
SM01286. SPT16. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q920B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTLDKDAY YRRVKRLYSN WRKGEDEYAS IDAIVVSVGV DEEIVYAKST
60 70 80 90 100
ALQTWLFGYE LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA
110 120 130 140 150
PAITLLVREK NESNKSSFDK MIDAIKESKS GKKIGVFSKD KFPGEFMKSW
160 170 180 190 200
SDCLNKEGFD KVDISAVVAY TIAVKEDGEL NLMKKAASIT SEVFNKFFKE
210 220 230 240 250
RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE MCYPPIIQSG
260 270 280 290 300
GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPTQEVQE
310 320 330 340 350
NYNFLLQLQE ELLKELRHGV KICDVYNSVM DVVKKQKPEL LNKITKNLGF
360 370 380 390 400
GMGIEFREGS LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA
410 420 430 440 450
LFIGDTVLVD EDGPATILTS VKKKVKNVGI FLKNEDDEEE EEEKDEAEDL
460 470 480 490 500
LGRGSRAALL TERTRNEMTA EEKRRAHQKE LAAQLNEEAK RRLTEQKGEQ
510 520 530 540 550
QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM PVFGIATPFH
560 570 580 590 600
IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY
610 620 630 640 650
RASNMKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS
660 670 680 690 700
LVINLNRSNP KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL
710 720 730 740 750
YNNIKHALFQ PCDGEMIIVL HFHLKNAVMF GKKRHTDVQF YTEVGEITTD
760 770 780 790 800
LGKHQHMHDR DDLYAEQMER EMRHKLKTAF KNFIEKVEAL TKEELEFEVP
810 820 830 840 850
FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV ELIHFERVQF
860 870 880 890 900
HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL
910 920 930 940 950
NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEDGDSE SEIEDETFNP
960 970 980 990 1000
SEDDYEEEEE DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA
1010 1020 1030 1040
DRESRYEEEE EQSRSMSRKR KASVHSSGRG SNRGSRHSSA PPKKKRK
Length:1,047
Mass (Da):119,825
Last modified:July 11, 2006 - v2
Checksum:i51931F5639CD221E
GO

Sequence cautioni

The sequence AAH12433.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti453 – 4531R → G in AAL04452 (PubMed:11471063).Curated
Sequence conflicti862 – 8621K → E in AAL04452 (PubMed:11471063).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323667 mRNA. Translation: AAL04452.1.
AK148506 mRNA. Translation: BAE28591.1.
AK158116 mRNA. Translation: BAE34362.1.
BC012433 mRNA. Translation: AAH12433.1. Different initiation.
CCDSiCCDS27051.1.
RefSeqiNP_291096.2. NM_033618.3.
UniGeneiMm.21662.
Mm.489682.

Genome annotation databases

GeneIDi114741.
KEGGimmu:114741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323667 mRNA. Translation: AAL04452.1.
AK148506 mRNA. Translation: BAE28591.1.
AK158116 mRNA. Translation: BAE34362.1.
BC012433 mRNA. Translation: AAH12433.1. Different initiation.
CCDSiCCDS27051.1.
RefSeqiNP_291096.2. NM_033618.3.
UniGeneiMm.21662.
Mm.489682.

3D structure databases

ProteinModelPortaliQ920B9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi227853. 6 interactions.
DIPiDIP-55972N.
IntActiQ920B9. 9 interactions.
MINTiMINT-4122296.
STRINGi10090.ENSMUSP00000042283.

Protein family/group databases

MEROPSiM24.974.

PTM databases

iPTMnetiQ920B9.
PhosphoSiteiQ920B9.

Proteomic databases

EPDiQ920B9.
MaxQBiQ920B9.
PaxDbiQ920B9.
PRIDEiQ920B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114741.
KEGGimmu:114741.

Organism-specific databases

CTDi114741.
MGIiMGI:1890948. Supt16.

Phylogenomic databases

eggNOGiKOG1189. Eukaryota.
COG5406. LUCA.
HOGENOMiHOG000209079.
HOVERGENiHBG092544.
InParanoidiQ920B9.
PhylomeDBiQ920B9.

Miscellaneous databases

NextBioi368789.
PROiQ920B9.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SUPT16H.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]
SMARTiSM01285. FACT-Spt16_Nlob. 1 hit.
SM01287. Rtt106. 1 hit.
SM01286. SPT16. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse Supt16h/Fact140 gene, encoding part of the FACT chromatin transcription complex, maps close to Tcra and is highly expressed in thymus."
    McGuire M.V., Suthipinijtham P., Gascoigne N.R.J.
    Mamm. Genome 12:664-667(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-637.
    Strain: C57BL/6J.
    Tissue: Inner ear and Pancreas.
  3. "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 803-1047.
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver and Spleen.
  5. "Myogenin recruits the histone chaperone facilitates chromatin transcription (FACT) to promote nucleosome disassembly at muscle-specific genes."
    Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.
    J. Biol. Chem. 288:7676-7687(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYOG.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196 AND LYS-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSP16H_MOUSE
AccessioniPrimary (citable) accession number: Q920B9
Secondary accession number(s): Q3TZ48, Q3UFH0, Q921H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: May 11, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.