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Q9Y5B9 (SP16H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1047 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14

Subunit structure

Interacts with MYOG (via C-terminal region) By similarity. 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 C-terminal Glu-rich acidic region 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 10471046FACT complex subunit SPT16
PRO_0000245169

Regions

Coiled coil432 – 50776 Potential
Compositional bias926 – 101186Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.4 Ref.23 Ref.24
Modified residue1391N6-acetyllysine Ref.19
Modified residue1881Phosphoserine Ref.22
Modified residue1961N6-acetyllysine Ref.19
Modified residue2231N6-acetyllysine Ref.19
Modified residue5081Phosphoserine Ref.17
Modified residue5131N6-acetyllysine Ref.19
Modified residue6501Phosphoserine Ref.20 Ref.22
Modified residue6581Phosphoserine Ref.22
Modified residue7321N6-acetyllysine Ref.19
Modified residue7861N6-acetyllysine Ref.19
Modified residue9031Phosphothreonine Ref.20
Modified residue9041N6-acetyllysine Ref.19
Modified residue9791Phosphoserine Ref.15 Ref.20 Ref.22
Modified residue9821Phosphoserine Ref.15 Ref.20 Ref.22
Modified residue9861Phosphoserine Ref.22
Modified residue10151Phosphoserine Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q9Y5B9 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3E1B23C45BDC61C2

FASTA1,047119,914
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS9569.1.
RefSeqNP_009123.1. NM_007192.3.
UniGeneHs.213724.

3D structure databases

ProteinModelPortalQ9Y5B9.
SMRQ9Y5B9. Positions 5-432, 511-604, 645-926.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116367. 78 interactions.
DIPDIP-42757N.
IntActQ9Y5B9. 25 interactions.
MINTMINT-2823866.
STRING9606.ENSP00000216297.

Protein family/group databases

MEROPSM24.974.

PTM databases

PhosphoSiteQ9Y5B9.

Polymorphism databases

DMDM74753511.

Proteomic databases

MaxQBQ9Y5B9.
PaxDbQ9Y5B9.
PeptideAtlasQ9Y5B9.
PRIDEQ9Y5B9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216297; ENSP00000216297; ENSG00000092201.
GeneID11198.
KEGGhsa:11198.
UCSCuc001wao.2. human.

Organism-specific databases

CTD11198.
GeneCardsGC14M021819.
HGNCHGNC:11465. SUPT16H.
HPACAB022551.
HPA049787.
MIM605012. gene.
neXtProtNX_Q9Y5B9.
PharmGKBPA36251.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5406.
HOGENOMHOG000209079.
HOVERGENHBG092544.
InParanoidQ9Y5B9.
OMAYILTTQK.
OrthoDBEOG7VQJC8.
PhylomeDBQ9Y5B9.
TreeFamTF300341.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9Y5B9.
BgeeQ9Y5B9.
CleanExHS_SUPT16H.
GenevestigatorQ9Y5B9.

Family and domain databases

Gene3D3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamPF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]
SUPFAMSSF55920. SSF55920. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSUPT16H. human.
GeneWikiSUPT16H.
GenomeRNAi11198.
NextBio42621.
PROQ9Y5B9.
SOURCESearch...

Entry information

Entry nameSP16H_HUMAN
AccessionPrimary (citable) accession number: Q9Y5B9
Secondary accession number(s): Q6GMT8 expand/collapse secondary AC list , Q6P2F1, Q6PJM1, Q9NRX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM