SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P38845

- CRP1_YEAST

UniProt

P38845 - CRP1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Cruciform DNA-recognizing protein 1
Gene
CRP1, YHR146W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 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

  1. 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
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR146w.
SGDiS000001189. CRP1.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Cruciform DNA-recognizing protein 1
PRO_0000202923Add
BLAST
Chaini1 – 160160CRP1 short N-terminal subpeptide
PRO_0000409594Add
BLAST
Chaini161 – 465305CRP1 short C-terminal subpeptide
PRO_0000409595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei153 – 1531Phosphoserine1 Publication
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei182 – 1821Phosphothreonine1 Publication
Modified residuei271 – 2711Phosphoserine2 Publications
Modified residuei295 – 2951Phosphothreonine2 Publications
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei343 – 3431Phosphoserine1 Publication
Modified residuei366 – 3661Phosphothreonine1 Publication
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei440 – 4401Phosphoserine3 Publications

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.
PaxDbiP38845.
PeptideAtlasiP38845.

Expressioni

Gene expression databases

GenevestigatoriP38845.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
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

Protein-protein interaction databases

BioGridi36580. 32 interactions.
IntActiP38845. 20 interactions.
MINTiMINT-2734769.
STRINGi4932.YHR146W.

Structurei

3D structure databases

ProteinModelPortaliP38845.
SMRiP38845. Positions 9-93.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the CRP1/MDG1 family.

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00530000066262.
OMAiVEIISAV.
OrthoDBiEOG73V6W7.

Family and domain databases

InterProiIPR014756. Ig_E-set.
[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

MSSELMFNYT FSWPAGPKDV ILTGTFDDWR GTLPLVKTAK GNFEITMPVK    50
LANKDDTFQF KFIVDGVWCV SDSYKKEHVS EGIENNFLQI TDLVETQEVA 100
GASRIPEAGG LLCGKPPRSA GPPSTSNRKK NKRNNKKRRS KLKKKSTKNN 150
KKSNESLDDN EEEDGVTGTT TEDVTGTSRE ETPLAEPTNV SKEAPGNFHI 200
LPIDQSADTT QSNGIIGGPG PVLVPNPGEI KEFTEIRDVD ARELNERLNK 250
KEEVPEPVAG PIVESSVTEK SPALPQADDP IVETKEVAHN VQELTPQVEA 300
VTPLINEPEP LPTPEAQISI PESSKVEPVE GSLQSKLVEK RESTEGVLDG 350
SKKVENKAKK DEEVFTLDPI VNKAPKLPLT DEQTAEGRKS PAVSEEKEKK 400
KKQEKGSKEV KRSETSKEKK PSAKEVKKQT VKAPKKQTAS PLSSSTEEPK 450
KKKTGFFGKL KKLFK 465
Length:465
Mass (Da):51,116
Last modified:February 1, 1995 - v1
Checksum:i30880758F37991C7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U10397 Genomic DNA. Translation: AAB68982.1 .
BK006934 Genomic DNA. Translation: DAA06839.1 .
PIRi S46759.
RefSeqi NP_012016.1. NM_001179277.1.

3D structure databases

ProteinModelPortali P38845.
SMRi P38845. Positions 9-93.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36580. 32 interactions.
IntActi P38845. 20 interactions.
MINTi MINT-2734769.
STRINGi 4932.YHR146W.

Proteomic databases

MaxQBi P38845.
PaxDbi P38845.
PeptideAtlasi P38845.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHR146W ; YHR146W ; YHR146W .
GeneIDi 856551.
KEGGi sce:YHR146W.

Organism-specific databases

CYGDi YHR146w.
SGDi S000001189. CRP1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00530000066262.
OMAi VEIISAV.
OrthoDBi EOG73V6W7.

Enzyme and pathway databases

BioCyci YEAST:G3O-31181-MONOMER.

Miscellaneous databases

NextBioi 982357.

Gene expression databases

Genevestigatori P38845.

Family and domain databases

InterProi IPR014756. Ig_E-set.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

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 11, 2014
This is version 96 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.

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

External Data

Dasty 3

Similar proteinsi