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P32558 (SPT16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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):
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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1035 AA.
Sequence statusComplete.
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. 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 processDNA damage
DNA repair
DNA replication
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   DomainCoiled coil
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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_componentFACT 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

transcription elongation factor complex

Inferred from physical interaction Ref.16. Source: SGD

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11805826Ref.16PubMed 16429126PubMed 21179020. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

POB3Q046369EBI-4334,EBI-27863

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10351035FACT complex subunit SPT16
PRO_0000089448

Regions

Coiled coil208 – 23427 Potential
Coiled coil636 – 66631 Potential
Coiled coil959 – 98325 Potential
Compositional bias958 – 102164Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue5261Phosphoserine Ref.26
Modified residue7651Phosphoserine Ref.26

Experimental info

Mutagenesis5651P → S in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with L-570. Ref.12
Mutagenesis5701P → L in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with S-565. Ref.12
Mutagenesis8361G → D in cdc68-1; induces a spt phenotype characterized by depletion of many mRNAs. Ref.8
Mutagenesis848 – 8503TTD → IIY in spt16-7; induces a spt phenotype characterized by depletion of many mRNAs. Ref.12
Mutagenesis9201P → L in spt16-6; induces a spt phenotype characterized by depletion of many mRNAs. Ref.12

Secondary structure

..................................................................................................................... 1035
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32558 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 4F01C772E299E2E6

FASTA1,035118,630
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"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-526 AND SER-765, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS18512.
RefSeqNP_011308.1. NM_001181072.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BIPX-ray1.94A/B1-465[»]
3BIQX-ray1.73A1-465[»]
3BITX-ray1.90A/B1-451[»]
4IOYX-ray1.94X675-958[»]
ProteinModelPortalP32558.
SMRP32558. Positions 1-447, 533-652, 677-941.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33049. 169 interactions.
DIPDIP-2546N.
IntActP32558. 57 interactions.
MINTMINT-427889.
STRING4932.YGL207W.

Proteomic databases

MaxQBP32558.
PaxDbP32558.
PeptideAtlasP32558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL207W; YGL207W; YGL207W.
GeneID852665.
KEGGsce:YGL207W.

Organism-specific databases

CYGDYGL207w.
SGDS000003175. SPT16.

Phylogenomic databases

eggNOGCOG5406.
GeneTreeENSGT00390000014495.
HOGENOMHOG000209079.
OMANDEVASY.
OrthoDBEOG7SFJ58.

Enzyme and pathway databases

BioCycYEAST:G3O-30684-MONOMER.

Gene expression databases

GenevestigatorP32558.

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

EvolutionaryTraceP32558.
NextBio971957.
PROP32558.

Entry information

Entry nameSPT16_YEAST
AccessionPrimary (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: June 11, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references