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-5

Gene

Cul5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Core component of multiple SCF-like ECS (Elongin BC-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. Seems to be involved in proteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a cell surface vasopressin receptor.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 - Molecular functioni

  • protein heterodimerization activity Source: MGI
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  • cerebral cortex radially oriented cell migration Source: MGI
  • protein ubiquitination Source: MGI
  • radial glia guided migration of Purkinje cell Source: MGI
  • ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 3474.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-5
Short name:
CUL-5
Gene namesi
Name:Cul5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1922967. Cul5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 780779Cullin-5PRO_0000119798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101PhosphothreonineBy similarity
Cross-linki724 – 724Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

Post-translational modificationi

Neddylated; which enhances the ubiquitination activity of SCF and prevents binding of the inhibitor CAND1. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D5V5.
MaxQBiQ9D5V5.
PaxDbiQ9D5V5.
PRIDEiQ9D5V5.

PTM databases

iPTMnetiQ9D5V5.
PhosphoSiteiQ9D5V5.

Expressioni

Gene expression databases

BgeeiQ9D5V5.
CleanExiMM_CUL5.

Interactioni

Subunit structurei

Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes formed of CUL5, the Elongin BC (TCEB1 and TCEB2), RBX2 and a variable SOCS box domain-containing protein as substrate-specific recognition component. Component of the probable ECS(LRRC41) complex with the substrate recognition component LRRC41. Component of the probable ECS(SOCS1) complex with the substrate recognition component SOCS1. Component of the probable ECS(WSB1) complex with the substrate recognition subunit WSB1. Component of the probable ECS(SOCS3) complex with the substrate recognition component SOCS3. Component of the probable ECS(SPSB1) complex with the substrate recognition component SPSB1. Component of the probable ECS(SPSB2) complex with the substrate recognition component SPSB2. Component of the probable ECS(SPSB4) complex with the substrate recognition component SPSB4. Component of the probable ECS(RAB40C) complex with the substrate recognition subunit RAB40C. May also form complexes containing CUL5, Elongin BC (TCEB1 and TCEB2), RBX1 and TCEB3. May also form complexes containing CUL5, elongin BC complex (TCEB1 and TCEB2), RBX1 and VHL. Interacts with RNF7/RBX2, LRRC41, SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2, ASB6, ASB7 and ASB12 (By similarity).By similarity

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI
  • ubiquitin protein ligase binding Source: MGI

Protein-protein interaction databases

BioGridi217689. 16 interactions.
IntActiQ9D5V5. 2 interactions.
STRINGi10090.ENSMUSP00000034529.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 3117Combined sources
Helixi37 – 5317Combined sources
Helixi57 – 8125Combined sources
Helixi86 – 10318Combined sources
Turni104 – 1085Combined sources
Helixi109 – 1113Combined sources
Helixi112 – 1154Combined sources
Helixi134 – 14613Combined sources
Helixi148 – 16720Combined sources
Helixi175 – 18612Combined sources
Helixi196 – 2005Combined sources
Helixi202 – 24847Combined sources
Helixi257 – 26913Combined sources
Helixi271 – 2733Combined sources
Helixi274 – 2785Combined sources
Helixi281 – 2866Combined sources
Helixi290 – 30011Combined sources
Helixi308 – 32922Combined sources
Helixi330 – 3323Combined sources
Turni333 – 3353Combined sources
Helixi337 – 35923Combined sources
Helixi363 – 38220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WZKX-ray2.05A1-384[»]
ProteinModelPortaliQ9D5V5.
SMRiQ9D5V5. Positions 12-386, 401-780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D5V5.

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2285. Eukaryota.
COG5647. LUCA.
HOGENOMiHOG000007610.
HOVERGENiHBG099672.
InParanoidiQ9D5V5.
KOiK10612.
PhylomeDBiQ9D5V5.

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.

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

Q9D5V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSNLLKNK GSLQFEDKWD FMHPIVLKLL RQESVTKQQW FDLFSDVHAV
60 70 80 90 100
CLWDDKGSSK IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF
110 120 130 140 150
FTQCDILPKP FCQLEVTLLG KQSSNKKSNM EDSIVRKLML DTWNESIFSN
160 170 180 190 200
IKNRLQDSAM KLVHAERLGE AFDSQLVIGV RESYVNLCSN PEDKLQIYRD
210 220 230 240 250
NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE EEKRALRYLE
260 270 280 290 300
TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM
310 320 330 340 350
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR
360 370 380 390 400
FSKLVKEAFQ DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP
410 420 430 440 450
ESKCPELLAN YCDMLLRKTP LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF
460 470 480 490 500
MRYHKAHLTR RLILDISADS EIEENMVEWL REVGMPADYV NKLARMFQDI
510 520 530 540 550
KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS EKVFVSLPTE
560 570 580 590 600
LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL
610 620 630 640 650
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY
660 670 680 690 700
DPQVNSPKDF TEGTLFSVNQ DFSLIKNAKV QKRGKINLIG RLQLTTERMR
710 720 730 740 750
EEENEGIVQL RILRTQEAII QIMKMRKKIS NAQLQTELVE ILKNMFLPQK
760 770 780
KMIKEQMEWL IEHRYIRRDE ADINTFIYMA
Length:780
Mass (Da):90,974
Last modified:January 23, 2007 - v3
Checksum:iC6EE7A1AF1038C0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti573 – 5731W → C in BAC27621 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014894 mRNA. Translation: BAB29609.1.
AK030306 mRNA. Translation: BAC26889.1.
AK031955 mRNA. Translation: BAC27621.1.
AK046030 mRNA. Translation: BAC32575.1.
AK080305 mRNA. Translation: BAC37872.1.
BC075710 mRNA. Translation: AAH75710.1.
RefSeqiNP_001155090.1. NM_001161618.1.
NP_082083.2. NM_027807.3.
UniGeneiMm.218910.
Mm.491606.

Genome annotation databases

GeneIDi75717.
KEGGimmu:75717.
UCSCiuc009pmj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014894 mRNA. Translation: BAB29609.1.
AK030306 mRNA. Translation: BAC26889.1.
AK031955 mRNA. Translation: BAC27621.1.
AK046030 mRNA. Translation: BAC32575.1.
AK080305 mRNA. Translation: BAC37872.1.
BC075710 mRNA. Translation: AAH75710.1.
RefSeqiNP_001155090.1. NM_001161618.1.
NP_082083.2. NM_027807.3.
UniGeneiMm.218910.
Mm.491606.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WZKX-ray2.05A1-384[»]
ProteinModelPortaliQ9D5V5.
SMRiQ9D5V5. Positions 12-386, 401-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217689. 16 interactions.
IntActiQ9D5V5. 2 interactions.
STRINGi10090.ENSMUSP00000034529.

PTM databases

iPTMnetiQ9D5V5.
PhosphoSiteiQ9D5V5.

Proteomic databases

EPDiQ9D5V5.
MaxQBiQ9D5V5.
PaxDbiQ9D5V5.
PRIDEiQ9D5V5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi75717.
KEGGimmu:75717.
UCSCiuc009pmj.1. mouse.

Organism-specific databases

CTDi8065.
MGIiMGI:1922967. Cul5.

Phylogenomic databases

eggNOGiKOG2285. Eukaryota.
COG5647. LUCA.
HOGENOMiHOG000007610.
HOVERGENiHBG099672.
InParanoidiQ9D5V5.
KOiK10612.
PhylomeDBiQ9D5V5.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9D5V5.
PROiQ9D5V5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D5V5.
CleanExiMM_CUL5.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain, Medulla oblongata, Ovary, Testis and Uterus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "Molecular architecture of the ankyrin SOCS box family of Cul5-dependent E3 ubiquitin ligases."
    Muniz J.R., Guo K., Kershaw N.J., Ayinampudi V., von Delft F., Babon J.J., Bullock A.N.
    J. Mol. Biol. 425:3166-3177(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-384, FUNCTION.

Entry informationi

Entry nameiCUL5_MOUSE
AccessioniPrimary (citable) accession number: Q9D5V5
Secondary accession number(s): Q8BMQ6, Q8BV53, Q8C098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.