P32558 (SPT16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FACT complex subunit SPT16

Alternative name(s):
Cell division control protein 68
Facilitates chromatin transcription complex subunit SPT16
Suppressor of Ty protein 16

Gene names

Name:	SPT16
Synonyms:	CDC68, SSF1
Ordered Locus Names:	YGL207W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1035 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication. Ref.10 Ref.12 Ref.15 Ref.19 Ref.22 Ref.24 Ref.25
Subunit structure	Forms a stable heterodimer with POB3. The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the FACT (yFACT or SNP) complex. The FACT complex interacts with the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the components of the transcription machinery CHD1, CTR9, PAF1 and CDC73. The FACT complex interacts with the PAF1 complex. SPT16 interacts with SAS3 and POL1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17
Subcellular location	Nucleus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.10 Ref.19 Ref.23
Miscellaneous	Present with 18500 molecules/cell in log phase SD medium.
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.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Domain	Coiled coil
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication-independent nucleosome organization Inferred from direct assay PubMed 19683499. Source: SGD DNA-dependent DNA replication Inferred from physical interaction Ref.7. Source: SGD nucleosome assembly Inferred from direct assay Ref.18Ref.24. Source: SGD positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from direct assay Ref.25. Source: SGD positive regulation of transcription initiation from RNA polymerase II promoter Inferred from mutant phenotype PubMed 19574230. Source: SGD regulation of transcription by chromatin organization Inferred from mutant phenotype PubMed 19683500. Source: SGD transcription elongation from RNA polymerase II promoter Inferred from physical interaction Ref.16. Source: SGD
Cellular_component	FACT complex Inferred from genetic interaction Ref.12. Source: SGD nuclear chromatin Inferred from direct assay Ref.10. Source: SGD replication fork protection complex Inferred from direct assay PubMed 16531994. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POB3	Q04636	9	EBI-4334,EBI-27863

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1035

1035

FACT complex subunit SPT16

PRO_0000089448

Regions

Coiled coil

208 – 234

27

Potential

Coiled coil

636 – 666

31

Potential

Coiled coil

959 – 983

25

Potential

Compositional bias

958 – 1021

64

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

235

1

Phosphoserine Ref.27

Modified residue

460

1

Phosphoserine Ref.26 Ref.27

Modified residue

526

1

Phosphoserine Ref.27

Modified residue

542

1

Phosphoserine Ref.27

Modified residue

598

1

Phosphoserine Ref.27

Modified residue

601

1

Phosphoserine Ref.27

Modified residue

602

1

Phosphoserine Ref.27

Modified residue

765

1

Phosphoserine Ref.27

Modified residue

1011

1

Phosphoserine Ref.27

Experimental info

Mutagenesis

565

1

P → S in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with L-570. Ref.12

Mutagenesis

570

1

P → L in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with S-565. Ref.12

Mutagenesis

836

1

G → D in cdc68-1; induces a spt phenotype characterized by depletion of many mRNAs. Ref.8

Mutagenesis

848 – 850

3

TTD → IIY in spt16-7; induces a spt phenotype characterized by depletion of many mRNAs. Ref.12

Mutagenesis

920

1

P → L in spt16-6; induces a spt phenotype characterized by depletion of many mRNAs. Ref.12

Secondary structure

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1035

Helix Strand Turn

Details...

Helix

8 – 21

14

Helix

22 – 24

3

Beta strand

30 – 36

7

Helix

47 – 56

10

Beta strand

61 – 68

8

Beta strand

71 – 77

7

Helix

78 – 84

7

Helix

85 – 91

7

Beta strand

92 – 95

4

Beta strand

99 – 105

7

Helix

110 – 127

18

Beta strand

129 – 133

5

Helix

142 – 158

17

Beta strand

161 – 164

4

Helix

166 – 172

7

Helix

178 – 207

30

Helix

214 – 223

10

Helix

224 – 226

3

Helix

228 – 239

12

Helix

250 – 252

3

Beta strand

253 – 257

5

Beta strand

260 – 262

3

Beta strand

277 – 279

3

Beta strand

283 – 290

8

Beta strand

292 – 294

3

Beta strand

301 – 308

8

Helix

311 – 330

20

Helix

338 – 352

15

Helix

354 – 359

6

Beta strand

365 – 367

3

Beta strand

369 – 372

4

Helix

375 – 377

3

Beta strand

378 – 380

3

Beta strand

393 – 403

11

Turn

406 – 408

3

Beta strand

412 – 421

10

Beta strand

431 – 433

3

Helix

440 – 443

4

Beta strand

679 – 686

8

Beta strand

689 – 691

3

Beta strand

696 – 700

5

Beta strand

702 – 707

6

Helix

712 – 714

3

Beta strand

717 – 720

4

Helix

721 – 723

3

Beta strand

724 – 730

7

Beta strand

735 – 750

16

Beta strand

753 – 763

11

Helix

790 – 818

29

Turn

819 – 821

3

Beta strand

825 – 827

3

Helix

830 – 832

3

Beta strand

834 – 841

8

Beta strand

843 – 847

5

Beta strand

849 – 854

6

Beta strand

856 – 859

4

Beta strand

861 – 864

4

Helix

865 – 867

3

Beta strand

868 – 874

7

Beta strand

881 – 891

11

Beta strand

897 – 903

7

Helix

904 – 906

3

Helix

907 – 916

10

Beta strand

921 – 923

3

Helix

931 – 939

9

Sequences

	Sequence		Length	Mass (Da)
	P32558 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 4F01C772E299E2E6	FASTA	1,035	118,630
	10 20 30 40 50 60 MEELNIDFDV FKKRIELLYS KYNEFEGSPN SLLFVLGSSN AENPYQKTTI LHNWLLSYEF 70 80 90 100 110 120 PATLIALVPG KVIIITSSAK AKHLQKAIDL FKDPESKITL ELWQRNNKEP ELNKKLFDDV 130 140 150 160 170 180 IALINSAGKT VGIPEKDSYQ GKFMTEWNPV WEAAVKENEF NVIDISLGLS KVWEVKDVNE 190 200 210 220 230 240 QAFLSVSSKG SDKFMDLLSN EMVRAVDEEL KITNAKLSDK IENKIDDVKF LKQLSPDLSA 250 260 270 280 290 300 LCPPNYKFNF DLLDWTYSPI IQSGKKFDLR VSARSTNDQL YGNGCILASC GIRYNNYCSN 310 320 330 340 350 360 ITRTFLIDPS EEMANNYDFL LTLQKEIVTN ILKPGRTPKE VYESVIEYIE KTKPELVPNF 370 380 390 400 410 420 TKNIGSLIGL EFRDSNFILN VKNDYRKIQR GDCFNISFGF NNLKDSQSAN NYALQLADTV 430 440 450 460 470 480 QIPLDETEPP RFLTNYTKAK SQISFYFNNE EEDNNKKKSS PATKVPSKPD RNSKILRTKL 490 500 510 520 530 540 RGEARGGAED AQKEQIRKEN QKKLHEKLEK NGLLRFSAAD ANGPDSEPRQ YFKKYESYVR 550 560 570 580 590 600 DSQLPTNIRD LRIHVDWKSQ TIILPIYGRP VPFHINSYKN GSKNEEGEYT YLRLNFNSPG 610 620 630 640 650 660 SSGGISKKVE ELPYEESADN QFVRSITLRS KDGDRMSETF KQIADLKKEA TKREQERKAL 670 680 690 700 710 720 ADVVQQDKLI ENKTGRTKRL DQIFVRPNPD TKRVPSTVFI HENGIRFQSP LRTDSRIDIL 730 740 750 760 770 780 FSNIKNLIFQ SCKGELIVVI HIHLKNPILM GKKKIQDVQF YREASDMSVD ETGGGRRGQS 790 800 810 820 830 840 RFRRYGDEDE LEQEQEERRK RAALDKEFKY FADAIAEASN GLLTVENTFR DLGFQGVPNR 850 860 870 880 890 900 SAVFCMPTTD CLVQLIEPPF LVINLEEVEI CILERVQFGL KNFDMVFVYK DFNKPVTHIN 910 920 930 940 950 960 TVPIESLDFL KQWLTDMDIP YTVSTINLNW ATIMKSLQDD PYQFFLDGGW NFLATGSDDE 970 980 990 1000 1010 1020 ASDESEEEVS EYEASEDDVS DESAFSEDEE GSEVDDDISG DESEDYTGDE SEEGEDWDEL 1030 EKKAARADRG ANFRD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CDC68, a yeast gene that affects regulation of cell proliferation and transcription, encodes a protein with a highly acidic carboxyl terminus." Rowley A., Singer R.A., Johnston G.C. Mol. Cell. Biol. 11:5718-5726(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Mutations in SPT16/CDC68 suppress cis- and trans-acting mutations that affect promoter function in Saccharomyces cerevisiae." Malone E.A., Clark C.D., Chiang A., Winston F. Mol. Cell. Biol. 11:5710-5717(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII reveals 11 open reading frames: two correspond to new genes." Feuermann M., Simeonava L., Souciet J.-L., Potier S. Yeast 13:475-477(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex." Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S. Gene 79:59-70(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158. Strain: ATCC 28383 / FL100 / VTT C-80102.
[7]	"The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein." Wittmeyer J., Formosa T. Mol. Cell. Biol. 17:4178-4190(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POL1.
[8]	"The yeast protein complex containing cdc68 and pob3 mediates core-promoter repression through the cdc68 N-terminal domain." Evans D.R.H., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C., Singer R.A. Genetics 150:1393-1405(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POB3, MUTAGENESIS OF GLY-836.
[9]	"Characterization of the CP complex, an abundant dimer of Cdc68 and Pob3 proteins that regulates yeast transcriptional activation and chromatin repression." Brewster N.K., Johnston G.C., Singer R.A. J. Biol. Chem. 273:21972-21979(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POB3.
[10]	"Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha." Wittmeyer J., Joss L., Formosa T. Biochemistry 38:8961-8971(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH POB3, SUBCELLULAR LOCATION.
[11]	"The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex." John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L. Genes Dev. 14:1196-1208(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SAS3.
[12]	"Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN." Formosa T., Eriksson P., Wittmeyer J., Ginn J., Yu Y., Stillman D.J. EMBO J. 20:3506-3517(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B AND NUCLEOSOMES, FUNCTION OF THE FACT COMPLEX, MUTAGENESIS OF PRO-565; PRO-570; 848-THR--ASP-850 AND PRO-920.
[13]	"A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription." Brewster N.K., Johnston G.C., Singer R.A. Mol. Cell. Biol. 21:3491-3502(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
[14]	"The Paf1 complex physically and functionally associates with transcription elongation factors in vivo." Squazzo S.L., Costa P.J., Lindstrom D.L., Kumer K.E., Simic R., Jennings J.L., Link A.J., Arndt K.M., Hartzog G.A. EMBO J. 21:1764-1774(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAF1 COMPLEX.
[15]	"Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure." Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., Rhoades A.R., Kaufman P.D., Stillman D.J. Genetics 162:1557-1571(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[16]	"RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach." Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F. Mol. Cell. Biol. 22:6979-6992(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHD1; CTR9; PAF1; CDC73; CKA1; CKA2; CKB1; CKB2 AND HISTONES.
[17]	"Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes." Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J., Johnson A.D., Hartzog G.A., Arndt K.M. EMBO J. 22:1846-1856(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHD1.
[18]	"Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes." Ruone S., Rhoades A.R., Formosa T. J. Biol. Chem. 278:45288-45295(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
[19]	"The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo." Mason P.B., Struhl K. Mol. Cell. Biol. 23:8323-8333(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX, SUBCELLULAR LOCATION.
[20]	Erratum Mason P.B., Struhl K. Mol. Cell. Biol. 24:6536-6536(2004)
[21]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[22]	"Transcription elongation factors repress transcription initiation from cryptic sites." Kaplan C.D., Laprade L., Winston F. Science 301:1096-1099(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[23]	"Transitions in RNA polymerase II elongation complexes at the 3' ends of genes." Kim M., Ahn S.-H., Krogan N.J., Greenblatt J.F., Buratowski S. EMBO J. 23:354-364(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[24]	"Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6." Rhoades A.R., Ruone S., Formosa T. Mol. Cell. Biol. 24:3907-3917(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[25]	"The yeast FACT complex has a role in transcriptional initiation." Biswas D., Yu Y., Prall M., Formosa T., Stillman D.J. Mol. Cell. Biol. 25:5812-5822(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[26]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, MASS SPECTROMETRY.
[27]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-460; SER-526; SER-542; SER-598; SER-601; SER-602; SER-765 AND SER-1011, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M73533 Genomic DNA. No translation available.
Z72729 Genomic DNA. Translation: CAA96920.1.
M27174 Genomic DNA. No translation available.
BK006941 Genomic DNA. Translation: DAA07909.1.

PIR

S18512.

RefSeq

NP_011308.1. NM_001181072.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BIP	X-ray	1.94	A/B	1-465	[»]
3BIQ	X-ray	1.73	A	1-465	[»]
3BIT	X-ray	1.90	A/B	1-451	[»]
4IOY	X-ray	1.94	X	675-958	[»]

ProteinModelPortal

P32558.

SMR

P32558. Positions 1-447.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2546N.

IntAct

P32558. 57 interactions.

MINT

MINT-427889.

STRING

4932.YGL207W.

Proteomic databases

PaxDb

P32558.

PeptideAtlas

P32558.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL207W; YGL207W; YGL207W.

GeneID

852665.

KEGG

sce:YGL207W.

Organism-specific databases

CYGD

YGL207w.

SGD

S000003175. SPT16.

Phylogenomic databases

eggNOG

COG5406.

GeneTree

ENSGT00390000014495.

HOGENOM

HOG000209079.

OMA

THEAVIS.

OrthoDB

EOG4QC4DF.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30684-MONOMER.

Gene expression databases

Genevestigator

P32558.

GermOnline

YGL207W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.90.230.10. 1 hit.

InterPro

IPR013719. DUF1747.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]

Pfam

PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P32558.

NextBio

971957.

Entry information

Entry name

SPT16_YEAST

Accession

Primary (citable) accession number: P32558
Secondary accession number(s): D6VTU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 29, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program