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P38845 (CRP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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:
Cruciform DNA-recognizing protein 1

Cleaved into the following 2 chains:

  1. CRP1 short N-terminal subpeptide
  2. CRP1 short C-terminal subpeptide
Gene names
Name:CRP1
Ordered Locus Names:YHR146W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cruciform DNA-binding protein which exerts an enhancing effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII from bacteriophage T4. Ref.3

Post-translational modification

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

Miscellaneous

Present with 2990 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the CRP1/MDG1 family.

Ontologies

Keywords
   LigandDNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleus

Inferred by curator Ref.3. Source: SGD

   Molecular_functionDNA binding

Inferred from direct assay Ref.3. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-24770,EBI-24770
AGP1P253761EBI-24770,EBI-2357
ALO1P547831EBI-24770,EBI-2519
ARF1P110761EBI-24770,EBI-2816
ARF3P409941EBI-24770,EBI-2824
ATG21Q028871EBI-24770,EBI-2045775
BAP2P380841EBI-24770,EBI-3414
CAB5Q039411EBI-24770,EBI-22174
CAN1P048171EBI-24770,EBI-3993
CHO1P084561EBI-24770,EBI-14055
COT1P327981EBI-24770,EBI-5006
DFG5Q050311EBI-24770,EBI-27512
DIP5P533881EBI-24770,EBI-5904
EMP47P435551EBI-24770,EBI-6439
ENA2Q018961EBI-24770,EBI-2055692
ERG1P324761EBI-24770,EBI-6545
ERG25P530451EBI-24770,EBI-6506
ERP1Q053591EBI-24770,EBI-6581
ERV25P548371EBI-24770,EBI-6642
FAA3P390021EBI-24770,EBI-10089
FMP42Q049911EBI-24770,EBI-27478
FMP45Q076511EBI-24770,EBI-2051056
FTH1P383101EBI-24770,EBI-20959
FTR1P400881EBI-24770,EBI-7138
GAP1P191451EBI-24770,EBI-7314
GPX2P381431EBI-24770,EBI-7863
GTT1P405821EBI-24770,EBI-7941
HNM1P198071EBI-24770,EBI-8409
HSP30P256191EBI-24770,EBI-8563
HXT1P324651EBI-24770,EBI-8759
HXT3P324661EBI-24770,EBI-8770
HXT5P386951EBI-24770,EBI-8778
HXT7P390041EBI-24770,EBI-8790
ITR1P306051EBI-24770,EBI-2050956
MCD4P360511EBI-24770,EBI-2070979
MSC3Q058121EBI-24770,EBI-33150
MUP1P502761EBI-24770,EBI-11624
ORM2Q061441EBI-24770,EBI-34916
PDR12Q027851EBI-24770,EBI-13065
PDR5P333021EBI-24770,EBI-13038
PEX11Q124621EBI-24770,EBI-13198
PIS1P061971EBI-24770,EBI-13458
PLM2Q043831EBI-24770,EBI-2079237
PMC1P389291EBI-24770,EBI-3097
PMP2P409751EBI-24770,EBI-2043041
PMP3P872841EBI-24770,EBI-13555
QDR2P404741EBI-24770,EBI-25203
QDR3P382271EBI-24770,EBI-21433
RIM1P324451EBI-24770,EBI-15206
SAC1P323681EBI-24770,EBI-16210
SCS7Q035291EBI-24770,EBI-16747
SDS23P531721EBI-24770,EBI-23782
SEC4P075601EBI-24770,EBI-16858
SFK1P357351EBI-24770,EBI-26678
SNA3P143591EBI-24770,EBI-26122
SNA4Q075491EBI-24770,EBI-22078
SNQ2P325681EBI-24770,EBI-17590
SPC1P469651EBI-24770,EBI-17823
SPF1P399861EBI-24770,EBI-3128
SWP1Q027951EBI-24770,EBI-12666
TMS1Q121161EBI-24770,EBI-19306
TPO1Q078241EBI-24770,EBI-38106
TPO2P532831EBI-24770,EBI-2044753
TPO3Q064511EBI-24770,EBI-34275
VHS3Q084381EBI-24770,EBI-30482
VHT1P532411EBI-24770,EBI-20297
VMA21P418061EBI-24770,EBI-20323
VMA6P323661EBI-24770,EBI-20201
VPH1P325631EBI-24770,EBI-20455
YBL039W-BP0C2681EBI-24770,EBI-2044092
YCK3P399621EBI-24770,EBI-4740
YDR034W-BQ6Q5X21EBI-24770,EBI-2043695
YOP1Q124021EBI-24770,EBI-37092
YPT1P011231EBI-24770,EBI-29496
YVH1Q022561EBI-24770,EBI-14322

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Cruciform DNA-recognizing protein 1
PRO_0000202923
Chain1 – 160160CRP1 short N-terminal subpeptide
PRO_0000409594
Chain161 – 465305CRP1 short C-terminal subpeptide
PRO_0000409595

Regions

Region160 – 1612X-DNA-binding

Amino acid modifications

Modified residue1241Phosphoserine Ref.9
Modified residue1251Phosphothreonine Ref.9
Modified residue1531Phosphoserine Ref.6 Ref.8
Modified residue1561Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue1781Phosphoserine Ref.9
Modified residue1821Phosphothreonine Ref.9
Modified residue1911Phosphoserine Ref.9
Modified residue2711Phosphoserine Ref.5 Ref.8 Ref.9
Modified residue2951Phosphothreonine Ref.9
Modified residue3191Phosphoserine Ref.9
Modified residue3231Phosphoserine Ref.9
Modified residue3241Phosphoserine Ref.9
Modified residue3321Phosphoserine Ref.9
Modified residue3431Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue3441Phosphothreonine Ref.8 Ref.9
Modified residue3901Phosphoserine Ref.8 Ref.9
Modified residue3941Phosphoserine Ref.8 Ref.9
Modified residue4401Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue4431Phosphoserine Ref.9
Modified residue4441Phosphoserine Ref.9

Sequences

Sequence LengthMass (Da)Tools
P38845 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 30880758F37991C7

FASTA46551,116
        10         20         30         40         50         60 
MSSELMFNYT FSWPAGPKDV ILTGTFDDWR GTLPLVKTAK GNFEITMPVK LANKDDTFQF 

        70         80         90        100        110        120 
KFIVDGVWCV SDSYKKEHVS EGIENNFLQI TDLVETQEVA GASRIPEAGG LLCGKPPRSA 

       130        140        150        160        170        180 
GPPSTSNRKK NKRNNKKRRS KLKKKSTKNN KKSNESLDDN EEEDGVTGTT TEDVTGTSRE 

       190        200        210        220        230        240 
ETPLAEPTNV SKEAPGNFHI LPIDQSADTT QSNGIIGGPG PVLVPNPGEI KEFTEIRDVD 

       250        260        270        280        290        300 
ARELNERLNK KEEVPEPVAG PIVESSVTEK SPALPQADDP IVETKEVAHN VQELTPQVEA 

       310        320        330        340        350        360 
VTPLINEPEP LPTPEAQISI PESSKVEPVE GSLQSKLVEK RESTEGVLDG SKKVENKAKK 

       370        380        390        400        410        420 
DEEVFTLDPI VNKAPKLPLT DEQTAEGRKS PAVSEEKEKK KKQEKGSKEV KRSETSKEKK 

       430        440        450        460 
PSAKEVKKQT VKAPKKQTAS PLSSSTEEPK KKKTGFFGKL KKLFK

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"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].
[5]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, MASS SPECTROMETRY.
Strain: YAL6B.
[6]"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, MASS SPECTROMETRY.
Strain: ADR376.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, MASS SPECTROMETRY.
[8]"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-153; SER-156; SER-271; SER-343; THR-344; SER-390; SER-394 AND SER-440, MASS SPECTROMETRY.
[9]"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-124; THR-125; SER-156; SER-178; THR-182; SER-191; SER-271; THR-295; SER-319; SER-323; SER-324; SER-332; SER-343; THR-344; SER-390; SER-394; SER-440; SER-443 AND SER-444, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U10397 Genomic DNA. Translation: AAB68982.1.
BK006934 Genomic DNA. Translation: DAA06839.1.
PIRS46759.
RefSeqNP_012016.1. NM_001179277.1.

3D structure databases

ProteinModelPortalP38845.
ModBaseSearch...

Protein-protein interaction databases

IntActP38845. 20 interactions.
MINTMINT-2734769.
STRING4932.YHR146W.

Proteomic databases

PaxDbP38845.
PeptideAtlasP38845.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR146W; YHR146W; YHR146W.
GeneID856551.
KEGGsce:YHR146W.

Organism-specific databases

CYGDYHR146w.
SGDS000001189. CRP1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00530000066262.
OMANTHIESQ.
OrthoDBEOG4TTKTV.

Enzyme and pathway databases

BioCycYEAST:G3O-31181-MONOMER.

Gene expression databases

GenevestigatorP38845.
GermOnlineYHR146W. Saccharomyces cerevisiae.

Family and domain databases

ProtoNetSearch...

Other

NextBio982357.

Entry information

Entry nameCRP1_YEAST
AccessionPrimary (citable) accession number: P38845
Secondary accession number(s): D3DL95
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VIII

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents