Reviewed, UniProtKB/Swiss-Prot Q03012 (SPP1_YEAST)

Names and origin

Protein names

Recommended name:
    COMPASS component SPP1
Alternative name(s):
    Complex proteins associated with SET1 protein SPP1
    Set1C component SPP1
    Suppressor of PRP protein 1

Gene names

Name:	SPP1
Synonyms:	CPS40, SAF41
Ordered Locus Names:	YPL138C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Ref.2 Ref.3
Subunit structure	Component of the COMPASS (Set1C) complex which consists of SET12, BRE22, SPP12, SDC11, SHG11, SWD11, SWD21, and SWD31. Ref.2 Ref.4
Subcellular location	Nucleus Probable.
Miscellaneous	Present with 1680 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Contains 1 PHD-type zinc finger.

Ontologies

Keywords
Cellular component	Chromosomal protein Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin silencing at telomere Ref.3 Ref.4 Inferred from mutant phenotype. Source: SGD histone H3-K4 methylation Ref.2 Ref.3 Inferred from direct assay. Source: SGD
Cellular component	Set1C/COMPASS complex Ref.2 Ref.4 Inferred from physical interaction. Source: SGD chromosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chromatin binding Inferred from direct assay. Source: SGD methylated histone residue binding Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MTR2	P34232	1	EBI-32540,EBI-11585

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 353	353	COMPASS component SPP1		PRO_0000059338
Regions
	Zinc finger	22 – 72	51	PHD-type
	Compositional bias	246 – 251	6	Poly-Lys
Amino acid modifications
	Modified residue	87	1	Phosphoserine Ref.6 Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q03012-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F4B8DFE0CB358CA4	FASTA	353	41,468
	10 20 30 40 50 60 MSLPQWCPPH STLKRNPTTG EDVYCICKRP DYGELMVGCD GCDDWFHFTC LHIPEQFKDL 70 80 90 100 110 120 VFSFYCPYCQ AGITGKNKDA IINGEGSLPK TLWKRKCRIS DCYKPCLQDS KYCSEEHGRE 130 140 150 160 170 180 FVNDIWSRLK TDEDRAVVKK MVEQTGHIDK FKKFGQLDFI DNNIVVKTDD EKEIFDQIVV 190 200 210 220 230 240 RDMTLKTLED DLQEVQEISL PLFKKKLELL EVYLGWLDNV YTEMRKLDDD AASHVECGKE 250 260 270 280 290 300 DSKGTKRKKK KNSSRSRARK NICGYCSTYE RIPCSVEEFV RDFGSNEEAT KIHEVCTKWK 310 320 330 340 350 CNRHLDWVST NQEQYLQQID SLESMQERLQ HLIQARKKQL NIQYYEEILR RGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4." Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M., Aasland R., Stewart A.F. EMBO J. 20:7137-7148(2001) [PubMed: 11742990] [Abstract] Cited for: FUNCTION, SUBUNIT.
[3]	"COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression." Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J., Johnston M., Shilatifard A. J. Biol. Chem. 277:10753-10755(2002) [PubMed: 11805083] [Abstract] Cited for: FUNCTION.
[4]	"COMPASS: a complex of proteins associated with a trithorax-related SET domain protein." Miller T., Krogan N.J., Dover J., Erdjument-Bromage H., Tempst P., Johnston M., Greenblatt J.F., Shilatifard A. Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001) [PubMed: 11687631] [Abstract] Cited for: SUBUNIT.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U43703 Genomic DNA. Translation: AAB68222.1.
PIR	S69047.
RefSeq	NP_015187.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2946N.
IntAct	Q03012. 11 interactions.
STRING	Q03012.
Proteomic databases
PeptideAtlas	Q03012.
Genome annotation databases
Ensembl	YPL138C; YPL138C; YPL138C; Saccharomyces cerevisiae. [Genome view]
GeneID	855965.
KEGG	sce:YPL138C.
NMPDR	fig|4932.3.peg.6317.
Organism-specific databases
CYGD	YPL138c.
SGD	S000006059. SPP1.
Phylogenomic databases
HOGENOM	Q03012.
OMA	EDVYCIC
OrthoDB	EOG9Z37X4
Gene expression databases
ArrayExpress	Q03012.
Genevestigator	Q03012.
GermOnline	YPL138C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. [Graphical view]
Pfam	PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00249. PHD. 1 hit. [Graphical view]
PROSITE	PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	980771.

Entry information

Entry name

SPP1_YEAST

Accession

Primary (citable) accession number: Q03012

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	November 1, 1996
Last modified:	November 24, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)