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Protein

FACT complex subunit SPT16

Gene

SUPT16H

Organism
Homo sapiens (Human)
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).6 Publications

GO - Molecular functioni

  • histone binding Source: GO_Central
  • nucleosome binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092201-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

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
Short name:
hSPT16
Gene namesi
Name:SUPT16H
Synonyms:FACT140, FACTP140
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:11465. SUPT16H.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000092201.
PharmGKBiPA36251.

Polymorphism and mutation databases

BioMutaiSUPT16H.
DMDMi74753511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00002451692 – 1047FACT complex subunit SPT16Add BLAST1046

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei139N6-acetyllysineCombined sources1
Modified residuei188PhosphoserineCombined sources1
Modified residuei196N6-acetyllysineCombined sources1
Modified residuei223N6-acetyllysineCombined sources1
Modified residuei455PhosphoserineCombined sources1
Modified residuei508PhosphoserineCombined sources1
Modified residuei513N6-acetyllysineCombined sources1
Cross-linki647Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei650PhosphoserineCombined sources1
Modified residuei658PhosphoserineCombined sources1
Modified residuei732N6-acetyllysineCombined sources1
Modified residuei786N6-acetyllysineCombined sources1
Modified residuei903PhosphothreonineCombined sources1
Modified residuei904N6-acetyllysineCombined sources1
Modified residuei979PhosphoserineCombined sources1
Modified residuei982PhosphoserineCombined sources1
Modified residuei986PhosphoserineCombined sources1
Modified residuei1015PhosphoserineCombined sources1

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

EPDiQ9Y5B9.
MaxQBiQ9Y5B9.
PaxDbiQ9Y5B9.
PeptideAtlasiQ9Y5B9.
PRIDEiQ9Y5B9.

PTM databases

iPTMnetiQ9Y5B9.
PhosphoSitePlusiQ9Y5B9.
SwissPalmiQ9Y5B9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000092201.
CleanExiHS_SUPT16H.
ExpressionAtlasiQ9Y5B9. baseline and differential.
GenevisibleiQ9Y5B9. HS.

Organism-specific databases

HPAiCAB022551.
HPA049787.

Interactioni

Subunit structurei

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).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM4P339913EBI-1046849,EBI-374938
SSRP1Q089453EBI-1046849,EBI-353771

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116367. 149 interactors.
DIPiDIP-42757N.
IntActiQ9Y5B9. 51 interactors.
MINTiMINT-2823866.
STRINGi9606.ENSP00000216297.

Structurei

Secondary structure

11047
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 23Combined sources17
Helixi26 – 28Combined sources3
Beta strandi32 – 38Combined sources7
Helixi48 – 57Combined sources10
Beta strandi62 – 68Combined sources7
Beta strandi73 – 77Combined sources5
Helixi79 – 89Combined sources11
Helixi95 – 99Combined sources5
Beta strandi103 – 107Combined sources5
Beta strandi110 – 112Combined sources3
Helixi115 – 127Combined sources13
Beta strandi131 – 136Combined sources6
Helixi145 – 155Combined sources11
Beta strandi160 – 163Combined sources4
Helixi165 – 173Combined sources9
Helixi177 – 196Combined sources20
Helixi198 – 207Combined sources10
Helixi214 – 224Combined sources11
Helixi228 – 230Combined sources3
Turni231 – 233Combined sources3
Helixi236 – 238Combined sources3
Beta strandi239 – 243Combined sources5
Beta strandi246 – 248Combined sources3
Beta strandi256 – 259Combined sources4
Beta strandi263 – 265Combined sources3
Beta strandi268 – 275Combined sources8
Beta strandi277 – 279Combined sources3
Beta strandi286 – 293Combined sources8
Helixi296 – 315Combined sources20
Helixi322 – 336Combined sources15
Helixi338 – 340Combined sources3
Turni341 – 343Combined sources3
Beta strandi349 – 351Combined sources3
Beta strandi353 – 356Combined sources4
Beta strandi358 – 362Combined sources5
Beta strandi376 – 387Combined sources12
Helixi394 – 397Combined sources4
Beta strandi398 – 408Combined sources11
Beta strandi411 – 414Combined sources4
Helixi425 – 428Combined sources4
Beta strandi655 – 657Combined sources3
Beta strandi661 – 669Combined sources9
Beta strandi671 – 674Combined sources4
Beta strandi677 – 682Combined sources6
Beta strandi684 – 691Combined sources8
Beta strandi696 – 700Combined sources5
Helixi701 – 703Combined sources3
Beta strandi704 – 710Combined sources7
Beta strandi715 – 730Combined sources16
Beta strandi733 – 743Combined sources11
Beta strandi747 – 749Combined sources3
Helixi759 – 790Combined sources32
Turni791 – 793Combined sources3
Helixi802 – 804Combined sources3
Beta strandi806 – 813Combined sources8
Beta strandi815 – 819Combined sources5
Beta strandi821 – 826Combined sources6
Beta strandi828 – 831Combined sources4
Beta strandi833 – 836Combined sources4
Helixi837 – 839Combined sources3
Beta strandi840 – 847Combined sources8
Beta strandi853 – 863Combined sources11
Beta strandi869 – 875Combined sources7
Helixi876 – 878Combined sources3
Helixi879 – 888Combined sources10
Beta strandi893 – 895Combined sources3
Helixi902 – 911Combined sources10
Helixi913 – 918Combined sources6
Helixi921 – 925Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Z2MX-ray2.98B644-930[»]
4Z2NX-ray1.92A644-930[»]
5E5BX-ray1.84A2-432[»]
ProteinModelPortaliQ9Y5B9.
SMRiQ9Y5B9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili432 – 507Sequence analysisAdd BLAST76

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi926 – 1011Glu-rich (acidic)Add BLAST86

Domaini

The C-terminal Glu-rich acidic region is essential for FACT activity.1 Publication

Sequence similaritiesi

Belongs to the peptidase M24 family. SPT16 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1189. Eukaryota.
COG5406. LUCA.
GeneTreeiENSGT00390000014495.
HOGENOMiHOG000209079.
HOVERGENiHBG092544.
InParanoidiQ9Y5B9.
OMAiYANIDAI.
OrthoDBiEOG091G044Q.
PhylomeDBiQ9Y5B9.
TreeFamiTF300341.

Family and domain databases

CDDicd01091. CDC68-like. 1 hit.
Gene3Di3.30.70.240. 1 hit.
3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR000640. EFG_V.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24.
IPR033825. SPT16.
[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.

Q9Y5B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTLDKDAY YRRVKRLYSN WRKGEDEYAN VDAIVVSVGV DEEIVYAKST
60 70 80 90 100
ALQTWLFGYE LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA
110 120 130 140 150
PAITLLIREK NESNKSSFDK MIEAIKESKN GKKIGVFSKD KFPGEFMKSW
160 170 180 190 200
NDCLNKEGFD KIDISAVVAY TIAVKEDGEL NLMKKAASIT SEVFNKFFKE
210 220 230 240 250
RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE MCYPPIIQSG
260 270 280 290 300
GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPSQEVQE
310 320 330 340 350
NYNFLLQLQE ELLKELRHGV KICDVYNAVM DVVKKQKPEL LNKITKNLGF
360 370 380 390 400
GMGIEFREGS LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA
410 420 430 440 450
LFIGDTVLVD EDGPATVLTS VKKKVKNVGI FLKNEDEEEE 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
RASNIKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS
660 670 680 690 700
LVINLNRSNP KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL
710 720 730 740 750
YNNIKHALFQ PCDGEMIIVL HFHLKNAIMF 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 GSDAEEGDSE 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):119,914
Last modified:November 1, 1999 - v1
Checksum:i3E1B23C45BDC61C2
GO

Sequence cautioni

The sequence AAH64561 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH73849 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9569.1.
RefSeqiNP_009123.1. NM_007192.3.
UniGeneiHs.213724.

Genome annotation databases

EnsembliENST00000216297; ENSP00000216297; ENSG00000092201.
GeneIDi11198.
KEGGihsa:11198.
UCSCiuc001wao.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9569.1.
RefSeqiNP_009123.1. NM_007192.3.
UniGeneiHs.213724.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Z2MX-ray2.98B644-930[»]
4Z2NX-ray1.92A644-930[»]
5E5BX-ray1.84A2-432[»]
ProteinModelPortaliQ9Y5B9.
SMRiQ9Y5B9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116367. 149 interactors.
DIPiDIP-42757N.
IntActiQ9Y5B9. 51 interactors.
MINTiMINT-2823866.
STRINGi9606.ENSP00000216297.

Protein family/group databases

MEROPSiM24.974.

PTM databases

iPTMnetiQ9Y5B9.
PhosphoSitePlusiQ9Y5B9.
SwissPalmiQ9Y5B9.

Polymorphism and mutation databases

BioMutaiSUPT16H.
DMDMi74753511.

Proteomic databases

EPDiQ9Y5B9.
MaxQBiQ9Y5B9.
PaxDbiQ9Y5B9.
PeptideAtlasiQ9Y5B9.
PRIDEiQ9Y5B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216297; ENSP00000216297; ENSG00000092201.
GeneIDi11198.
KEGGihsa:11198.
UCSCiuc001wao.2. human.

Organism-specific databases

CTDi11198.
GeneCardsiSUPT16H.
HGNCiHGNC:11465. SUPT16H.
HPAiCAB022551.
HPA049787.
MIMi605012. gene.
neXtProtiNX_Q9Y5B9.
OpenTargetsiENSG00000092201.
PharmGKBiPA36251.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1189. Eukaryota.
COG5406. LUCA.
GeneTreeiENSGT00390000014495.
HOGENOMiHOG000209079.
HOVERGENiHBG092544.
InParanoidiQ9Y5B9.
OMAiYANIDAI.
OrthoDBiEOG091G044Q.
PhylomeDBiQ9Y5B9.
TreeFamiTF300341.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092201-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiSUPT16H. human.
GeneWikiiSUPT16H.
GenomeRNAii11198.
PROiQ9Y5B9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000092201.
CleanExiHS_SUPT16H.
ExpressionAtlasiQ9Y5B9. baseline and differential.
GenevisibleiQ9Y5B9. HS.

Family and domain databases

CDDicd01091. CDC68-like. 1 hit.
Gene3Di3.30.70.240. 1 hit.
3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR000640. EFG_V.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24.
IPR033825. SPT16.
[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...

Entry informationi

Entry nameiSP16H_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5B9
Secondary accession number(s): Q6GMT8
, Q6P2F1, Q6PJM1, Q9NRX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.