UniProtKB - Q9Y5B9 (SP16H_HUMAN)
FACT complex subunit SPT16
SUPT16H
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 PublicationsCaution
GO - Molecular functioni
- nucleosome binding Source: GO_Central
- RNA binding Source: UniProtKB
GO - Biological processi
- DNA repair Source: UniProtKB-KW
- DNA replication Source: UniProtKB-KW
- DNA replication-independent chromatin organization Source: GO_Central
- nucleosome assembly Source: ComplexPortal
- nucleosome disassembly Source: ComplexPortal
- positive regulation of DNA-templated transcription, elongation Source: ProtInc
- positive regulation of transcription elongation from RNA polymerase II promoter Source: GO_Central
- transcription by RNA polymerase II Source: ProtInc
- transcription elongation from RNA polymerase II promoter Source: GO_Central
Keywordsi
Biological process | DNA damage, DNA repair, DNA replication, Host-virus interaction, Transcription, Transcription regulation |
Enzyme and pathway databases
PathwayCommonsi | Q9Y5B9 |
Reactomei | R-HSA-112382, Formation of RNA Pol II elongation complex 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 |
SignaLinki | Q9Y5B9 |
Protein family/group databases
MEROPSi | M24.974 |
Names & Taxonomyi
Protein namesi | Recommended name: FACT complex subunit SPT16Alternative 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:11465, SUPT16H |
MIMi | 605012, gene |
neXtProti | NX_Q9Y5B9 |
VEuPathDBi | HostDB:ENSG00000092201 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Other locations
- Chromosome 1 Publication
Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Nucleus
- FACT complex Source: ComplexPortal
- nucleoplasm Source: HPA
- nucleus Source: ComplexPortal
Keywords - Cellular componenti
Chromosome, NucleusPathology & Biotechi
Organism-specific databases
DisGeNETi | 11198 |
OpenTargetsi | ENSG00000092201 |
PharmGKBi | PA36251 |
Miscellaneous databases
Pharosi | Q9Y5B9, Tbio |
Genetic variation databases
BioMutai | SUPT16H |
DMDMi | 74753511 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources2 Publications | |||
ChainiPRO_0000245169 | 2 – 1047 | FACT complex subunit SPT16Add BLAST | 1046 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources2 Publications | 1 | |
Modified residuei | 139 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 188 | PhosphoserineCombined sources | 1 | |
Modified residuei | 196 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 223 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 455 | PhosphoserineCombined sources | 1 | |
Cross-linki | 497 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 508 | PhosphoserineCombined sources | 1 | |
Modified residuei | 513 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 513 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 647 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 650 | PhosphoserineCombined sources | 1 | |
Modified residuei | 658 | PhosphoserineCombined sources | 1 | |
Modified residuei | 732 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 786 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 903 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 904 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 979 | PhosphoserineCombined sources | 1 | |
Modified residuei | 982 | PhosphoserineCombined sources | 1 | |
Modified residuei | 986 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1015 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q9Y5B9 |
jPOSTi | Q9Y5B9 |
MassIVEi | Q9Y5B9 |
MaxQBi | Q9Y5B9 |
PaxDbi | Q9Y5B9 |
PeptideAtlasi | Q9Y5B9 |
PRIDEi | Q9Y5B9 |
ProteomicsDBi | 86338 |
PTM databases
GlyGeni | Q9Y5B9, 1 site, 2 O-linked glycans (1 site) |
iPTMneti | Q9Y5B9 |
MetOSitei | Q9Y5B9 |
PhosphoSitePlusi | Q9Y5B9 |
SwissPalmi | Q9Y5B9 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000092201, Expressed in ventricular zone and 173 other tissues |
ExpressionAtlasi | Q9Y5B9, baseline and differential |
Genevisiblei | Q9Y5B9, HS |
Organism-specific databases
HPAi | ENSG00000092201, Low tissue specificity |
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(Microbial infection) Interacts with Herpes simplex virus 1 (HHV-1) protein ICP22; this interaction relocalizes the FACT complex to viral genomes in infected cells.
1 PublicationBinary interactionsi
Q9Y5B9
With | #Exp. | IntAct |
---|---|---|
APP [P05067] | 3 | EBI-1046849,EBI-77613 |
MCM4 [P33991] | 3 | EBI-1046849,EBI-374938 |
SSRP1 [Q08945] | 6 | EBI-1046849,EBI-353771 |
Protein-protein interaction databases
BioGRIDi | 116367, 331 interactors |
ComplexPortali | CPX-419, FACT complex |
CORUMi | Q9Y5B9 |
DIPi | DIP-42757N |
IntActi | Q9Y5B9, 111 interactors |
MINTi | Q9Y5B9 |
STRINGi | 9606.ENSP00000216297 |
Miscellaneous databases
RNActi | Q9Y5B9, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q9Y5B9 |
SMRi | Q9Y5B9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 492 – 518 | DisorderedSequence analysisAdd BLAST | 27 | |
Regioni | 918 – 1047 | DisorderedSequence analysisAdd BLAST | 130 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 432 – 507 | Sequence analysisAdd BLAST | 76 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 929 – 971 | Acidic residuesSequence analysisAdd BLAST | 43 | |
Compositional biasi | 972 – 1018 | Basic and acidic residuesSequence analysisAdd BLAST | 47 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | KOG1189, Eukaryota |
GeneTreei | ENSGT00390000014495 |
HOGENOMi | CLU_004627_0_0_1 |
InParanoidi | Q9Y5B9 |
OMAi | HQFFLDG |
OrthoDBi | 145488at2759 |
PhylomeDBi | Q9Y5B9 |
TreeFami | TF300341 |
Family and domain databases
CDDi | cd01091, CDC68-like, 1 hit |
Gene3Di | 2.30.29.30, 1 hit 3.40.350.10, 1 hit 3.90.230.10, 1 hit |
InterProi | View protein in InterPro IPR029149, Creatin/AminoP/Spt16_NTD IPR036005, Creatinase/aminopeptidase-like IPR013719, DUF1747 IPR029148, FACT-Spt16_Nlobe IPR013953, FACT_Spt16 IPR000994, Pept_M24 IPR011993, PH-like_dom_sf IPR040258, Spt16 IPR033825, Spt16_M24 |
PANTHERi | PTHR13980, PTHR13980, 1 hit |
Pfami | View protein in Pfam PF14826, FACT-Spt16_Nlob, 1 hit PF00557, Peptidase_M24, 1 hit PF08512, Rtt106, 1 hit PF08644, SPT16, 1 hit |
SMARTi | View protein in SMART SM01285, FACT-Spt16_Nlob, 1 hit SM01287, Rtt106, 1 hit SM01286, SPT16, 1 hit |
SUPFAMi | SSF55920, SSF55920, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketG3V5A4 | G3V5A4_HUMAN | FACT complex subunit | SUPT16H | 66 | Annotation score: | ||
G3V401 | G3V401_HUMAN | FACT complex subunit | SUPT16H | 81 | Annotation score: | ||
G3V2X0 | G3V2X0_HUMAN | FACT complex subunit SPT16 | SUPT16H | 83 | Annotation score: |
Sequence cautioni
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 |
CCDSi | CCDS9569.1 |
RefSeqi | NP_009123.1, NM_007192.3 |
Genome annotation databases
Ensembli | ENST00000216297.7; ENSP00000216297.2; ENSG00000092201.10 |
GeneIDi | 11198 |
KEGGi | hsa:11198 |
MANE-Selecti | ENST00000216297.7; ENSP00000216297.2; NM_007192.4; NP_009123.1 |
UCSCi | uc001wao.2, human |
Similar proteinsi
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 |
CCDSi | CCDS9569.1 |
RefSeqi | NP_009123.1, NM_007192.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4Z2M | X-ray | 2.98 | B | 644-930 | [»] | |
4Z2N | X-ray | 1.92 | A | 644-930 | [»] | |
5E5B | X-ray | 1.84 | A | 2-432 | [»] | |
5UMT | X-ray | 2.09 | A | 1-434 | [»] | |
5UMU | X-ray | 1.90 | A/B | 649-926 | [»] | |
5XM2 | X-ray | 2.19 | A/B | 1-437 | [»] | |
6UPK | electron microscopy | 4.90 | G | 2-925 | [»] | |
6UPL | electron microscopy | 7.40 | G | 2-925 | [»] | |
AlphaFoldDBi | Q9Y5B9 | |||||
SMRi | Q9Y5B9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 116367, 331 interactors |
ComplexPortali | CPX-419, FACT complex |
CORUMi | Q9Y5B9 |
DIPi | DIP-42757N |
IntActi | Q9Y5B9, 111 interactors |
MINTi | Q9Y5B9 |
STRINGi | 9606.ENSP00000216297 |
Protein family/group databases
MEROPSi | M24.974 |
PTM databases
GlyGeni | Q9Y5B9, 1 site, 2 O-linked glycans (1 site) |
iPTMneti | Q9Y5B9 |
MetOSitei | Q9Y5B9 |
PhosphoSitePlusi | Q9Y5B9 |
SwissPalmi | Q9Y5B9 |
Genetic variation databases
BioMutai | SUPT16H |
DMDMi | 74753511 |
Proteomic databases
EPDi | Q9Y5B9 |
jPOSTi | Q9Y5B9 |
MassIVEi | Q9Y5B9 |
MaxQBi | Q9Y5B9 |
PaxDbi | Q9Y5B9 |
PeptideAtlasi | Q9Y5B9 |
PRIDEi | Q9Y5B9 |
ProteomicsDBi | 86338 |
Protocols and materials databases
Antibodypediai | 22129, 427 antibodies from 40 providers |
DNASUi | 11198 |
Genome annotation databases
Ensembli | ENST00000216297.7; ENSP00000216297.2; ENSG00000092201.10 |
GeneIDi | 11198 |
KEGGi | hsa:11198 |
MANE-Selecti | ENST00000216297.7; ENSP00000216297.2; NM_007192.4; NP_009123.1 |
UCSCi | uc001wao.2, human |
Organism-specific databases
CTDi | 11198 |
DisGeNETi | 11198 |
GeneCardsi | SUPT16H |
HGNCi | HGNC:11465, SUPT16H |
HPAi | ENSG00000092201, Low tissue specificity |
MIMi | 605012, gene |
neXtProti | NX_Q9Y5B9 |
OpenTargetsi | ENSG00000092201 |
PharmGKBi | PA36251 |
VEuPathDBi | HostDB:ENSG00000092201 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1189, Eukaryota |
GeneTreei | ENSGT00390000014495 |
HOGENOMi | CLU_004627_0_0_1 |
InParanoidi | Q9Y5B9 |
OMAi | HQFFLDG |
OrthoDBi | 145488at2759 |
PhylomeDBi | Q9Y5B9 |
TreeFami | TF300341 |
Enzyme and pathway databases
PathwayCommonsi | Q9Y5B9 |
Reactomei | R-HSA-112382, Formation of RNA Pol II elongation complex 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 |
SignaLinki | Q9Y5B9 |
Miscellaneous databases
BioGRID-ORCSi | 11198, 766 hits in 1063 CRISPR screens |
ChiTaRSi | SUPT16H, human |
GeneWikii | SUPT16H |
GenomeRNAii | 11198 |
Pharosi | Q9Y5B9, Tbio |
PROi | PR:Q9Y5B9 |
RNActi | Q9Y5B9, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000092201, Expressed in ventricular zone and 173 other tissues |
ExpressionAtlasi | Q9Y5B9, baseline and differential |
Genevisiblei | Q9Y5B9, HS |
Family and domain databases
CDDi | cd01091, CDC68-like, 1 hit |
Gene3Di | 2.30.29.30, 1 hit 3.40.350.10, 1 hit 3.90.230.10, 1 hit |
InterProi | View protein in InterPro IPR029149, Creatin/AminoP/Spt16_NTD IPR036005, Creatinase/aminopeptidase-like IPR013719, DUF1747 IPR029148, FACT-Spt16_Nlobe IPR013953, FACT_Spt16 IPR000994, Pept_M24 IPR011993, PH-like_dom_sf IPR040258, Spt16 IPR033825, Spt16_M24 |
PANTHERi | PTHR13980, PTHR13980, 1 hit |
Pfami | View protein in Pfam PF14826, FACT-Spt16_Nlob, 1 hit PF00557, Peptidase_M24, 1 hit PF08512, Rtt106, 1 hit PF08644, SPT16, 1 hit |
SMARTi | View protein in SMART SM01285, FACT-Spt16_Nlob, 1 hit SM01287, Rtt106, 1 hit SM01286, SPT16, 1 hit |
SUPFAMi | SSF55920, SSF55920, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SP16H_HUMAN | |
Accessioni | Q9Y5B9Primary (citable) accession number: Q9Y5B9 Secondary accession number(s): Q6GMT8 Q9NRX0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 11, 2006 |
Last sequence update: | November 1, 1999 | |
Last modified: | May 25, 2022 | |
This is version 182 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families