Skip Header

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

Cullin-1

Gene

cul1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(pop1-pop2) is required for the maintenance of ploidy and directs ubiquitination of cig2.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiR-SPO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-1
Short name:
Cul-1
Alternative name(s):
Cell division control 53 homolog
Gene namesi
Name:cul1
Synonyms:pcu1
ORF Names:SPAC17G6.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17G6.12.
PomBaseiSPAC17G6.12. cul1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nuclear SCF ubiquitin ligase complex Source: PomBase
  • SCF ubiquitin ligase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi713 – 7131K → R: Loss of neddylation; results in impaired cell proliferation and marked stabilization of the cyclin-dependent kinase inhibitor rum1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Cullin-1PRO_0000119808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki713 – 713Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO13790.

Interactioni

Subunit structurei

Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of cul1, skp1, pip1 and a variable F-box domain-containing protein as substrate-specific subunit (By similarity). Binds to the pop1 homodimer, the pop2 homodimer and the pop1/pop2 heterodimer forming the SCF(pop1-pop2) complex. Interacts with pof3, pof14 and skp1.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
pof3O749912EBI-1154807,EBI-1153554
pop2O141703EBI-1154807,EBI-1185414
skp1Q9Y7092EBI-1154807,EBI-1172248

Protein-protein interaction databases

BioGridi278857. 30 interactions.
IntActiO13790. 7 interactions.
MINTiMINT-3377010.

Structurei

3D structure databases

ProteinModelPortaliO13790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi263 – 2664Poly-Glu
Compositional biasi444 – 4474Poly-Ile

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000176713.
InParanoidiO13790.
KOiK03347.
OMAiVTMEIDF.
OrthoDBiEOG7FJH80.
PhylomeDBiO13790.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLNTNDKD LPIVKKYDSL NGTWDFLKTG VSQIFERLDE GMTITKYMEL
60 70 80 90 100
YTAIHNYCAD ASKTITVDNF NDQTANVLGE ALYNNLVLYL EEYLARLRKE
110 120 130 140 150
CISQTNHEEQ LAAYAKYWTR FTTSARFINH LFGYLNRYWV KLKNRFTETL
160 170 180 190 200
VYDIYTLCLV SWHHHVFSHI RDSLLQNLLY MFTKKRLYEP TDMKYVEVCV
210 220 230 240 250
DSITSLSFDK TDMTKPNLSS YKTFFETNFI ENTKNFYAKE SSEYLASHSI
260 270 280 290 300
TDYLKKAEIR LAEEEELVRL YLHESTLKPL LEATEDVLIA QHEEVLHNDF
310 320 330 340 350
ARMLDQNCSE DIIRMYRLMS RTPNGLQPLR QTFEEFVKRS GFAAVAKIVP
360 370 380 390 400
QVGGEADVDP KEYMEMLLST YKASKELVNT AFHGDTDFTK SLDTAFRELV
410 420 430 440 450
NRNVVCQRSS SRSPELLAKY ADSILRKSNK NVDIDDVEDC LSSIIIIFRY
460 470 480 490 500
VEDKDVFQNF YTKLLAKRLV NGTSNSQDAE SSMLSKLKEV CGFEYTSKLQ
510 520 530 540 550
RMFQDISLSQ EITEAFWQLP QSRAGNIDFS ALVLGTSFWP LSPNNVNFHL
560 570 580 590 600
PEELVPLYEG FQNYYYSCHN GRKLSWLFHL SKGEIKARIN PQTNVTYVFQ
610 620 630 640 650
VSTYQMGVLL LYNHRDSYTY EELAKITGLS TDFLTGILNI FLKAKVLLLG
660 670 680 690 700
DNDKLGDPNS TYKINENFRM KKIRVQLNLP IRSEQKQESL ETHKTIEEDR
710 720 730 740 750
KLLLQSAIVR IMKARRTLKH VVLVKETIDQ IKSRFTPKVS DIKQCIDMLI
760
EKEYLERQGR DEYIYLA
Length:767
Mass (Da):89,426
Last modified:January 1, 1998 - v1
Checksum:i458CA31B5D97FAA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231Missing in BAA32428 (PubMed:9990507).Curated
Sequence conflicti52 – 521T → TR in BAA32428 (PubMed:9990507).Curated
Sequence conflicti74 – 741T → A in BAA32428 (PubMed:9990507).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016896 Genomic DNA. Translation: BAA32428.2.
CU329670 Genomic DNA. Translation: CAB16223.1.
AB027897 Genomic DNA. Translation: BAA87201.1.
PIRiT37844.
T43398.
RefSeqiNP_594259.1. NM_001019682.2.

Genome annotation databases

EnsemblFungiiSPAC17G6.12.1; SPAC17G6.12.1:pep; SPAC17G6.12.
GeneIDi2542393.
KEGGispo:SPAC17G6.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016896 Genomic DNA. Translation: BAA32428.2.
CU329670 Genomic DNA. Translation: CAB16223.1.
AB027897 Genomic DNA. Translation: BAA87201.1.
PIRiT37844.
T43398.
RefSeqiNP_594259.1. NM_001019682.2.

3D structure databases

ProteinModelPortaliO13790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278857. 30 interactions.
IntActiO13790. 7 interactions.
MINTiMINT-3377010.

Proteomic databases

MaxQBiO13790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17G6.12.1; SPAC17G6.12.1:pep; SPAC17G6.12.
GeneIDi2542393.
KEGGispo:SPAC17G6.12.

Organism-specific databases

EuPathDBiFungiDB:SPAC17G6.12.
PomBaseiSPAC17G6.12. cul1.

Phylogenomic databases

HOGENOMiHOG000176713.
InParanoidiO13790.
KOiK03347.
OMAiVTMEIDF.
OrthoDBiEOG7FJH80.
PhylomeDBiO13790.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-SPO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiO13790.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in fission yeast SCF (Skip-cullin-1-F-box) ubiquitin ligase."
    Kominami K., Ochotorena I., Toda T.
    Genes Cells 3:721-735(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 197-359.
    Strain: ATCC 38364 / 968.
  4. "Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast."
    Osaka F., Saeki M., Katayama S., Aida N., Toh-e A., Kominami K., Toda T., Suzuki T., Chiba T., Tanaka K., Kato S.
    EMBO J. 19:3475-3484(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION AT LYS-713, MUTAGENESIS OF LYS-713.
  5. "Fission yeast F-box protein Pof3 is required for genome integrity and telomere function."
    Katayama S., Kitamura K., Lehmann A., Nikaido O., Toda T.
    Mol. Biol. Cell 13:211-224(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POF3.
  6. "Molecular interactions of fission yeast Skp1 and its role in the DNA damage checkpoint."
    Lehmann A., Katayama S., Harrison C., Dhut S., Kitamura K., McDonald N., Toda T.
    Genes Cells 9:367-382(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP1.
  7. "Repression of ergosterol level during oxidative stress by fission yeast F-box protein Pof14 independently of SCF."
    Tafforeau L., Le Blastier S., Bamps S., Dewez M., Vandenhaute J., Hermand D.
    EMBO J. 25:4547-4556(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POF14.
  8. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCUL1_SCHPO
AccessioniPrimary (citable) accession number: O13790
Secondary accession number(s): Q9USB3, Q9UUL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.