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Protein

Cruciform DNA-recognizing protein 1

Gene

CRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cruciform DNA-binding protein which exerts an enhancing effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII from bacteriophage T4.1 Publication

GO - Molecular functioni

  • DNA binding Source: SGD
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31181-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cruciform DNA-recognizing protein 1
Cleaved into the following 2 chains:
Gene namesi
Name:CRP1
Ordered Locus Names:YHR146W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR146W.
SGDiS000001189. CRP1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Cruciform DNA-recognizing protein 1PRO_0000202923Add
BLAST
Chaini1 – 160160CRP1 short N-terminal subpeptidePRO_0000409594Add
BLAST
Chaini161 – 465305CRP1 short C-terminal subpeptidePRO_0000409595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei153 – 1531PhosphoserineCombined sources
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei182 – 1821PhosphothreonineCombined sources
Modified residuei271 – 2711PhosphoserineCombined sources
Modified residuei295 – 2951PhosphothreonineCombined sources
Modified residuei319 – 3191PhosphoserineCombined sources
Modified residuei343 – 3431PhosphoserineCombined sources
Modified residuei366 – 3661PhosphothreonineCombined sources
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei440 – 4401PhosphoserineCombined sources

Post-translational modificationi

Cleaved in the vicinity of position 160 to give an X-DNA-binding N-terminal subpeptide and a non-DNA-binding C-terminal subpeptide.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38845.
PeptideAtlasiP38845.

PTM databases

iPTMnetiP38845.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PEP4P072673EBI-24770,EBI-4040
PRC1P007292EBI-24770,EBI-4153

Protein-protein interaction databases

BioGridi36580. 31 interactions.
IntActiP38845. 20 interactions.
MINTiMINT-2734769.

Structurei

3D structure databases

ProteinModelPortaliP38845.
SMRiP38845. Positions 7-77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 1612X-DNA-binding

Sequence similaritiesi

Belongs to the CRP1/MDG1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000066262.
InParanoidiP38845.
OrthoDBiEOG73V6W7.

Family and domain databases

InterProiIPR032640. AMPK1_CBM.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF16561. AMPK1_CBM. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSELMFNYT FSWPAGPKDV ILTGTFDDWR GTLPLVKTAK GNFEITMPVK
60 70 80 90 100
LANKDDTFQF KFIVDGVWCV SDSYKKEHVS EGIENNFLQI TDLVETQEVA
110 120 130 140 150
GASRIPEAGG LLCGKPPRSA GPPSTSNRKK NKRNNKKRRS KLKKKSTKNN
160 170 180 190 200
KKSNESLDDN EEEDGVTGTT TEDVTGTSRE ETPLAEPTNV SKEAPGNFHI
210 220 230 240 250
LPIDQSADTT QSNGIIGGPG PVLVPNPGEI KEFTEIRDVD ARELNERLNK
260 270 280 290 300
KEEVPEPVAG PIVESSVTEK SPALPQADDP IVETKEVAHN VQELTPQVEA
310 320 330 340 350
VTPLINEPEP LPTPEAQISI PESSKVEPVE GSLQSKLVEK RESTEGVLDG
360 370 380 390 400
SKKVENKAKK DEEVFTLDPI VNKAPKLPLT DEQTAEGRKS PAVSEEKEKK
410 420 430 440 450
KKQEKGSKEV KRSETSKEKK PSAKEVKKQT VKAPKKQTAS PLSSSTEEPK
460
KKKTGFFGKL KKLFK
Length:465
Mass (Da):51,116
Last modified:February 1, 1995 - v1
Checksum:i30880758F37991C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10397 Genomic DNA. Translation: AAB68982.1.
BK006934 Genomic DNA. Translation: DAA06839.1.
PIRiS46759.
RefSeqiNP_012016.1. NM_001179277.1.

Genome annotation databases

EnsemblFungiiYHR146W; YHR146W; YHR146W.
GeneIDi856551.
KEGGisce:YHR146W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10397 Genomic DNA. Translation: AAB68982.1.
BK006934 Genomic DNA. Translation: DAA06839.1.
PIRiS46759.
RefSeqiNP_012016.1. NM_001179277.1.

3D structure databases

ProteinModelPortaliP38845.
SMRiP38845. Positions 7-77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36580. 31 interactions.
IntActiP38845. 20 interactions.
MINTiMINT-2734769.

PTM databases

iPTMnetiP38845.

Proteomic databases

MaxQBiP38845.
PeptideAtlasiP38845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR146W; YHR146W; YHR146W.
GeneIDi856551.
KEGGisce:YHR146W.

Organism-specific databases

EuPathDBiFungiDB:YHR146W.
SGDiS000001189. CRP1.

Phylogenomic databases

GeneTreeiENSGT00530000066262.
InParanoidiP38845.
OrthoDBiEOG73V6W7.

Enzyme and pathway databases

BioCyciYEAST:G3O-31181-MONOMER.

Miscellaneous databases

PROiP38845.

Family and domain databases

InterProiIPR032640. AMPK1_CBM.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF16561. AMPK1_CBM. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Crp1p, a new cruciform DNA-binding protein in the yeast Saccharomyces cerevisiae."
    Rass U., Kemper B.
    J. Mol. Biol. 323:685-700(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRUCIFORM DNA-BINDING, FUNCTION, DOMAIN, PROTEOLYTIC AUTOCLEAVAGE.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-156 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-295; SER-319; SER-394 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 THR-182; SER-271; THR-295; SER-343; THR-366 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCRP1_YEAST
AccessioniPrimary (citable) accession number: P38845
Secondary accession number(s): D3DL95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 109 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 2990 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.