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Q93034 (CUL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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

Names and origin

Protein namesRecommended name:
Cullin-5

Short name=CUL-5
Alternative name(s):
Vasopressin-activated calcium-mobilizing receptor 1
Short name=VACM-1
Gene names
Name:CUL5
Synonyms:VACM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of multiple SCF-like ECS (Elongin-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.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes formed of CUL5, 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 complex (TCEB1 and TCEB2), RBX1 and TCEB3. May also form complexes containing CUL5, Elongin BC (TCEB1 and TCEB2), RBX1 and VHL. The substrate recognition component can also be a viral protein such as HIV Vif, or human adenovirus 5 E1B large T-antigen and E4-orf6. Interacts with RNF7/RBX2, LRRC41, SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2, ASB6, ASB7 and ASB12. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Post-translational modification

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

Sequence similarities

Belongs to the cullin family.

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Molecular functionReceptor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement PubMed 8681378. Source: ProtInc

calcium ion transmembrane transport

Traceable author statement PubMed 9581826. Source: GOC

cell cycle arrest

Traceable author statement PubMed 8681378. Source: ProtInc

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cytosolic calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement PubMed 9581826. Source: ProtInc

negative regulation of cell proliferation

Traceable author statement PubMed 8681378. Source: ProtInc

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

viral process

Traceable author statement. Source: Reactome

   Cellular_componentCul5-RING ubiquitin ligase complex

Inferred from direct assay PubMed 17636018. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium channel activity

Traceable author statement PubMed 9581826. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 12504025PubMed 18826954. Source: UniProtKB

receptor activity

Traceable author statement PubMed 9581826. Source: ProtInc

ubiquitin protein ligase binding

Inferred from direct assay PubMed 17636018. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ASB2Q96Q274EBI-1057139,EBI-2880677
GAMMAHV.ORF73O419742EBI-1057139,EBI-6933128From a different organism.
RBX1P628773EBI-1057139,EBI-398523
vifP125045EBI-1057139,EBI-779991From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 780779Cullin-5
PRO_0000119797

Amino acid modifications

Modified residue2101Phosphothreonine Ref.14
Cross-link724Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Ref.16

Experimental info

Sequence conflict91N → D in AAB70253. Ref.2
Sequence conflict121S → F in AAB70253. Ref.2
Sequence conflict161E → G in AAB70253. Ref.2
Sequence conflict32 – 343QES → RDF in AAB70253. Ref.2
Sequence conflict381Q → R in AAB70253. Ref.2
Sequence conflict50 – 523VCL → FCF in AAB70253. Ref.2
Sequence conflict681D → DF in AAB70253. Ref.2
Sequence conflict2241Q → P in CAA57465. Ref.1
Sequence conflict6481L → F in CAA57465. Ref.1
Sequence conflict6511E → D in CAA57465. Ref.1

Secondary structure

...................................................................................................... 780
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q93034 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 57463CB4ED76E303

FASTA78090,955
        10         20         30         40         50         60 
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK 

        70         80         90        100        110        120 
IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEITLMG 

       130        140        150        160        170        180 
KQGSNKKSNV EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV 

       190        200        210        220        230        240 
RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE 

       250        260        270        280        290        300 
EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM 

       310        320        330        340        350        360 
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ 

       370        380        390        400        410        420 
DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAN YCDMLLRKTP 

       430        440        450        460        470        480 
LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL 

       490        500        510        520        530        540 
REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS 

       550        560        570        580        590        600 
EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL 

       610        620        630        640        650        660 
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY EPQVNSPKDF 

       670        680        690        700        710        720 
TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII 

       730        740        750        760        770        780 
QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQIEWL IEHKYIRRDE SDINTFIYMA 

« Hide

References

« Hide 'large scale' references
[1]"Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23."
Byrd P.J., Stankovic T., McConville C.M., Smith A.D., Cooper P.R., Taylor A.M.R.
Genome Res. 7:71-75(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Longo K.A., North W.G., Du J., Fay M.J.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Kanaya K., Kamitani T.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Placenta.
[7]"ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBX1 AND RNF7.
[8]"Covalent modification of all members of human cullin family proteins by NEDD8."
Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NEDDYLATION.
[9]"Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."
Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.
J. Biol. Chem. 276:29748-29753(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH LRRC41, IDENTIFICATION IN A COMPLEX WITH TCEB3, IDENTIFICATION IN A COMPLEX WITH SOCS1, IDENTIFICATION IN A COMPLEX WITH WSB1.
[10]"Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery."
Harada J.N., Shevchenko A., Shevchenko A., Pallas D.C., Berk A.J.
J. Virol. 76:9194-9206(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH HUMAN ADENOVIRUS 5 PROTEINS, NEDDYLATION.
[11]"Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation."
Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.
Genes Dev. 18:2861-2866(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV VIF.
[12]"VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE ECS(LRRC41) COMPLEX, IDENTIFICATION IN THE ECS(SOCS3) COMPLEX, IDENTIFICATION IN THE ECS(SPSB1) COMPLEX, IDENTIFICATION IN THE ECS(SPSB2) COMPLEX, IDENTIFICATION IN THE ECS(SPSB4) COMPLEX, IDENTIFICATION IN THE ECS(RAB40C) COMPLEX, IDENTIFICATION IN THE ECS(WSB1) COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH LRRC41; SOCS3; SPSB1; SPSB2; SPSB4; WSB1 AND RAB40C.
[13]"ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase complexes."
Kohroki J., Nishiyama T., Nakamura T., Masuho Y.
FEBS Lett. 579:6796-6802(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASB1; ASB2; ASB6; ASB7 AND ASB12.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation."
Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.
Cell 134:995-1006(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 401-780 IN COMPLEX WITH NEDD8 AND RBX1, NEDDYLATION AT LYS-724.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81882 mRNA. Translation: CAA57465.1.
AF017061 mRNA. Translation: AAB70253.1.
AF327710 mRNA. Translation: AAK07472.1.
AK292575 mRNA. Translation: BAF85264.1.
CH471065 Genomic DNA. Translation: EAW67102.1.
BC063306 mRNA. Translation: AAH63306.1.
CCDSCCDS31668.1.
RefSeqNP_003469.2. NM_003478.3.
UniGeneHs.440320.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DPLX-ray2.60C401-780[»]
3DQVX-ray3.00C/D401-780[»]
4JGHX-ray3.00D10-386[»]
4N9FX-ray3.303/9/C/I/O/U/V/f/l/r/w/x12-321[»]
ProteinModelPortalQ93034.
SMRQ93034. Positions 10-387, 401-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113743. 425 interactions.
DIPDIP-43696N.
IntActQ93034. 33 interactions.
MINTMINT-1184052.
STRING9606.ENSP00000299351.

PTM databases

PhosphoSiteQ93034.

Polymorphism databases

DMDM14917099.

Proteomic databases

MaxQBQ93034.
PaxDbQ93034.
PRIDEQ93034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393094; ENSP00000376808; ENSG00000166266.
ENST00000531427; ENSP00000435376; ENSG00000166266.
GeneID8065.
KEGGhsa:8065.
UCSCuc001pjv.3. human.

Organism-specific databases

CTD8065.
GeneCardsGC11P107913.
HGNCHGNC:2556. CUL5.
HPACAB017787.
HPA002185.
MIM601741. gene.
neXtProtNX_Q93034.
PharmGKBPA27052.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5647.
HOGENOMHOG000007610.
HOVERGENHBG099672.
InParanoidQ93034.
KOK10612.
OMAVCLWDEK.
OrthoDBEOG78D7JD.
PhylomeDBQ93034.
TreeFamTF105874.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ93034.
BgeeQ93034.
CleanExHS_CUL5.
GenevestigatorQ93034.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ93034.
GeneWikiCUL5.
GenomeRNAi8065.
NextBio30655.
PROQ93034.
SOURCESearch...

Entry information

Entry nameCUL5_HUMAN
AccessionPrimary (citable) accession number: Q93034
Secondary accession number(s): A8K960, O14766, Q9BZC6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM