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Protein

COMPASS component SPP1

Gene

SPP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 7251PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: SGD
  • methylated histone binding Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chromatin silencing at telomere Source: SGD
  • histone H3-K4 methylation Source: SGD
  • regulation of meiotic DNA double-strand break formation Source: SGD
  • regulation of transcription, DNA-templated Source: SGD
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34036-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
COMPASS component SPP1
Alternative name(s):
Complex proteins associated with SET1 protein SPP1
Set1C component SPP1
Suppressor of PRP protein 1
Gene namesi
Name:SPP1
Synonyms:CPS40, SAF41
Ordered Locus Names:YPL138C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL138C.
SGDiS000006059. SPP1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • cytosol Source: SGD
  • nucleus Source: SGD
  • Set1C/COMPASS complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353COMPASS component SPP1PRO_0000059338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03012.
PeptideAtlasiQ03012.

PTM databases

iPTMnetiQ03012.

Interactioni

Subunit structurei

Component of the COMPASS (Set1C) complex which consists of SET12, BRE22, SPP12, SDC11, SHG11, SWD11, SWD21, and SWD31.2 Publications

GO - Molecular functioni

  • methylated histone binding Source: SGD

Protein-protein interaction databases

BioGridi36044. 97 interactions.
DIPiDIP-2946N.
IntActiQ03012. 11 interactions.
MINTiMINT-496351.

Structurei

3D structure databases

ProteinModelPortaliQ03012.
SMRiQ03012. Positions 18-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi246 – 2516Poly-Lys

Sequence similaritiesi

Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 7251PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000000990.
InParanoidiQ03012.
KOiK14960.
OMAiEDVYCIC.
OrthoDBiEOG7PCJRV.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLPQWCPPH STLKRNPTTG EDVYCICKRP DYGELMVGCD GCDDWFHFTC
60 70 80 90 100
LHIPEQFKDL VFSFYCPYCQ AGITGKNKDA IINGEGSLPK TLWKRKCRIS
110 120 130 140 150
DCYKPCLQDS KYCSEEHGRE FVNDIWSRLK TDEDRAVVKK MVEQTGHIDK
160 170 180 190 200
FKKFGQLDFI DNNIVVKTDD EKEIFDQIVV RDMTLKTLED DLQEVQEISL
210 220 230 240 250
PLFKKKLELL EVYLGWLDNV YTEMRKLDDD AASHVECGKE DSKGTKRKKK
260 270 280 290 300
KNSSRSRARK NICGYCSTYE RIPCSVEEFV RDFGSNEEAT KIHEVCTKWK
310 320 330 340 350
CNRHLDWVST NQEQYLQQID SLESMQERLQ HLIQARKKQL NIQYYEEILR

RGL
Length:353
Mass (Da):41,468
Last modified:November 1, 1996 - v1
Checksum:iF4B8DFE0CB358CA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43703 Genomic DNA. Translation: AAB68222.1.
BK006949 Genomic DNA. Translation: DAA11296.1.
PIRiS69047.
RefSeqiNP_015187.1. NM_001183952.1.

Genome annotation databases

EnsemblFungiiYPL138C; YPL138C; YPL138C.
GeneIDi855965.
KEGGisce:YPL138C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43703 Genomic DNA. Translation: AAB68222.1.
BK006949 Genomic DNA. Translation: DAA11296.1.
PIRiS69047.
RefSeqiNP_015187.1. NM_001183952.1.

3D structure databases

ProteinModelPortaliQ03012.
SMRiQ03012. Positions 18-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36044. 97 interactions.
DIPiDIP-2946N.
IntActiQ03012. 11 interactions.
MINTiMINT-496351.

PTM databases

iPTMnetiQ03012.

Proteomic databases

MaxQBiQ03012.
PeptideAtlasiQ03012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL138C; YPL138C; YPL138C.
GeneIDi855965.
KEGGisce:YPL138C.

Organism-specific databases

EuPathDBiFungiDB:YPL138C.
SGDiS000006059. SPP1.

Phylogenomic databases

HOGENOMiHOG000000990.
InParanoidiQ03012.
KOiK14960.
OMAiEDVYCIC.
OrthoDBiEOG7PCJRV.

Enzyme and pathway databases

BioCyciYEAST:G3O-34036-MONOMER.

Miscellaneous databases

PROiQ03012.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBUNIT.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPP1_YEAST
AccessioniPrimary (citable) accession number: Q03012
Secondary accession number(s): D6W3N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1680 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.