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Protein

Cullin-5

Gene

cul-5

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. In association with rbx-2 seems to be involved in meiotic cell cycle progression in the germline. Required for phosphorylation of the MAP kinase MPK-1 in the germline.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

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-CEL-1227986. Signaling by ERBB2.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-5
Short name:
CUL-5
Gene namesi
Name:cul-5
ORF Names:ZK856.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiZK856.1; CE41096; WBGene00000840; cul-5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 765765Cullin-5PRO_0000119784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki709 – 709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ23639.
PaxDbiQ23639.
PRIDEiQ23639.

PTM databases

iPTMnetiQ23639.

Interactioni

Subunit structurei

Interacts with rbx-1 and rbx-2.1 Publication

Protein-protein interaction databases

BioGridi44444. 1 interaction.
DIPiDIP-25847N.
IntActiQ23639. 2 interactions.
MINTiMINT-1126406.
STRINGi6239.ZK856.1.

Structurei

3D structure databases

ProteinModelPortaliQ23639.
SMRiQ23639. Positions 1-765.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2285. Eukaryota.
COG5647. LUCA.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000007610.
InParanoidiQ23639.
KOiK10612.
OMAiNQEFAIV.
OrthoDBiEOG78D7JD.
PhylomeDBiQ23639.

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.

Q23639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFDEEWSKA DPIVHALLHQ KSVTPAAWQD LFYHVYKITS WVDDGPLKIR
60 70 80 90 100
DILTRCINDY VHEANKRIRS LQTDGSLLIG YIKEWNRFYQ QANILPLPFK
110 120 130 140 150
KIDESSRRRS VPETPEESIR TVMLEKWNEI IFMNISEQLL VEALRLVKEE
160 170 180 190 200
RDGNIIDAQN VIGIRESFVA LNDRAGEDPL LVYRQSFERQ FIEQTTEYYK
210 220 230 240 250
KICGNLLNEL GVLEYMVYAD KKLEEEQQRA KRYLEMNSPT SGKHMEKAVI
260 270 280 290 300
ALVESFEDTI LAECSKLIAS KDVERLQRLY RLIRRTRSGI DTVLKCIDTH
310 320 330 340 350
IRTEGLNDMR NNAENLSTDP ERYVQQLLLM FDKFSSLVRE GFCDDARLLT
360 370 380 390 400
ARDKAFRAVV NDSSIFKTEM MNKKGRTLSV ESKCAELLAN YCDLLLRKTQ
410 420 430 440 450
LSKKLTSEEI DEKLNQVLLV LKYVENKDVF MRFHRAHLSR RLILEMSADQ
460 470 480 490 500
EKEEMMVTKL RECGMPSDAV NKLSRMLQDI ELNKDMNSSF KKALTGTNNN
510 520 530 540 550
KSIADSINMK VLNGGAWGRG GSERIRFSLP RELEDFVPEM EAFYKKQHNG
560 570 580 590 600
RKLCWMHHWS SGTMVFGTAN GGRFDLECTT FQMAVLFCFN DRAHDKISLE
610 620 630 640 650
TLRLATELPD AELNRTLLSL VAYPKMRYQI LLCDVPSTTV TARDFTDSTK
660 670 680 690 700
FLINHDFNVV KNGKSQQRGK VNLIGRLQLS LEANAEKEHE SIVALRELRV
710 720 730 740 750
QEGIVKILKT RKTYTLAQLT MELVEILKPL FIPNRKIIKE QIDWLIENKY
760
MERRADDINT FVYIS
Length:765
Mass (Da):88,908
Last modified:January 15, 2008 - v2
Checksum:i2C264BB19B36D04D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70783 Genomic DNA. Translation: CAA94852.2.
PIRiT28043.
RefSeqiNP_505616.2. NM_073215.4.
UniGeneiCel.16970.

Genome annotation databases

EnsemblMetazoaiZK856.1; ZK856.1; WBGene00000840.
GeneIDi179413.
KEGGicel:CELE_ZK856.1.
UCSCiZK856.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70783 Genomic DNA. Translation: CAA94852.2.
PIRiT28043.
RefSeqiNP_505616.2. NM_073215.4.
UniGeneiCel.16970.

3D structure databases

ProteinModelPortaliQ23639.
SMRiQ23639. Positions 1-765.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44444. 1 interaction.
DIPiDIP-25847N.
IntActiQ23639. 2 interactions.
MINTiMINT-1126406.
STRINGi6239.ZK856.1.

PTM databases

iPTMnetiQ23639.

Proteomic databases

EPDiQ23639.
PaxDbiQ23639.
PRIDEiQ23639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiZK856.1; ZK856.1; WBGene00000840.
GeneIDi179413.
KEGGicel:CELE_ZK856.1.
UCSCiZK856.1. c. elegans.

Organism-specific databases

CTDi179413.
WormBaseiZK856.1; CE41096; WBGene00000840; cul-5.

Phylogenomic databases

eggNOGiKOG2285. Eukaryota.
COG5647. LUCA.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000007610.
InParanoidiQ23639.
KOiK10612.
OMAiNQEFAIV.
OrthoDBiEOG78D7JD.
PhylomeDBiQ23639.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-CEL-1227986. Signaling by ERBB2.

Miscellaneous databases

NextBioi905286.
PROiQ23639.

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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "C. elegans RBX-2-CUL-5- and RBX-1-CUL-2-based complexes are redundant for oogenesis and activation of the MAP kinase MPK-1."
    Sasagawa Y., Sato S., Ogura T., Higashitani A.
    FEBS Lett. 581:145-150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBX-1 AND RBX-2.

Entry informationi

Entry nameiCUL5_CAEEL
AccessioniPrimary (citable) accession number: Q23639
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 15, 2008
Last modified: May 11, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.