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Q93034

- CUL5_HUMAN

UniProt

Q93034 - CUL5_HUMAN

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Protein

Cullin-5

Gene
CUL5, VACM1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Pathwayi

GO - Molecular functioni

  1. calcium channel activity Source: ProtInc
  2. protein binding Source: UniProtKB
  3. receptor activity Source: ProtInc
  4. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. calcium ion transmembrane transport Source: GOC
  2. cell cycle arrest Source: ProtInc
  3. cell proliferation Source: ProtInc
  4. cytosolic calcium ion homeostasis Source: Ensembl
  5. G1/S transition of mitotic cell cycle Source: ProtInc
  6. intrinsic apoptotic signaling pathway Source: ProtInc
  7. negative regulation of cell proliferation Source: ProtInc
  8. protein ubiquitination Source: UniProtKB-UniPathway
  9. response to osmotic stress Source: Ensembl
  10. ubiquitin-dependent protein catabolic process Source: InterPro
  11. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_115755. Signaling by ERBB2.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9453. Vif-mediated degradation of APOBEC3G.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-5
Short name:
CUL-5
Alternative name(s):
Vasopressin-activated calcium-mobilizing receptor 1
Short name:
VACM-1
Gene namesi
Name:CUL5
Synonyms:VACM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:2556. CUL5.

Subcellular locationi

GO - Cellular componenti

  1. Cul5-RING ubiquitin ligase complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: Ensembl
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 780779Cullin-5PRO_0000119797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101Phosphothreonine1 Publication
Cross-linki724 – 724Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)1 Publication

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).

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ93034.
PaxDbiQ93034.
PRIDEiQ93034.

PTM databases

PhosphoSiteiQ93034.

Expressioni

Gene expression databases

ArrayExpressiQ93034.
BgeeiQ93034.
CleanExiHS_CUL5.
GenevestigatoriQ93034.

Organism-specific databases

HPAiCAB017787.
HPA002185.

Interactioni

Subunit structurei

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 ASB12.6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113743. 427 interactions.
DIPiDIP-43696N.
IntActiQ93034. 33 interactions.
MINTiMINT-1184052.
STRINGi9606.ENSP00000299351.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 3016
Helixi37 – 5317
Helixi57 – 8125
Helixi86 – 10318
Turni104 – 1085
Helixi109 – 1113
Helixi112 – 1154
Helixi134 – 14613
Helixi148 – 16720
Helixi175 – 18612
Helixi196 – 1994
Helixi202 – 22423
Helixi227 – 24822
Beta strandi252 – 2543
Helixi257 – 26913
Helixi271 – 2733
Helixi274 – 2774
Helixi278 – 2803
Helixi281 – 2866
Helixi290 – 30011
Turni304 – 3063
Helixi310 – 33324
Helixi337 – 35721
Turni358 – 3614
Helixi363 – 37715
Helixi405 – 41612
Beta strandi417 – 4193
Helixi420 – 4234
Helixi427 – 43812
Helixi439 – 4435
Helixi447 – 46317
Helixi470 – 48213
Helixi487 – 51327
Helixi523 – 5253
Beta strandi526 – 5327
Helixi533 – 5364
Helixi549 – 5524
Helixi555 – 5639
Beta strandi566 – 5738
Helixi575 – 5773
Beta strandi579 – 5857
Beta strandi590 – 5967
Helixi597 – 6037
Helixi604 – 6063
Helixi616 – 6238
Helixi627 – 63812
Beta strandi647 – 6526
Helixi657 – 6593
Beta strandi665 – 6684
Beta strandi674 – 68714
Turni690 – 6934
Helixi697 – 72327
Beta strandi726 – 7294
Helixi731 – 74111
Turni742 – 7454
Helixi750 – 76213
Beta strandi765 – 7695
Beta strandi772 – 7787

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ93034.
SMRiQ93034. Positions 10-387, 401-780.

Miscellaneous databases

EvolutionaryTraceiQ93034.

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.

Phylogenomic databases

eggNOGiCOG5647.
HOGENOMiHOG000007610.
HOVERGENiHBG099672.
InParanoidiQ93034.
KOiK10612.
OMAiVCLWDEK.
OrthoDBiEOG78D7JD.
PhylomeDBiQ93034.
TreeFamiTF105874.

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]
SUPFAMiSSF74788. 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.

Q93034-1 [UniParc]FASTAAdd to Basket

« Hide

MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV    50
CLWDDKGPAK IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF 100
FTQCDILPKP FCQLEITLMG KQGSNKKSNV EDSIVRKLML DTWNESIFSN 150
IKNRLQDSAM KLVHAERLGE AFDSQLVIGV RESYVNLCSN PEDKLQIYRD 200
NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE EEKRALRYLE 250
TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM 300
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR 350
FSKLVKEAFQ DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP 400
ESKCPELLAN YCDMLLRKTP LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF 450
MRYHKAHLTR RLILDISADS EIEENMVEWL REVGMPADYV NKLARMFQDI 500
KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS EKVFVSLPTE 550
LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL 600
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY 650
EPQVNSPKDF TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR 700
EEENEGIVQL RILRTQEAII QIMKMRKKIS NAQLQTELVE ILKNMFLPQK 750
KMIKEQIEWL IEHKYIRRDE SDINTFIYMA 780
Length:780
Mass (Da):90,955
Last modified:January 23, 2007 - v4
Checksum:i57463CB4ED76E303
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91N → D in AAB70253. 1 Publication
Sequence conflicti12 – 121S → F in AAB70253. 1 Publication
Sequence conflicti16 – 161E → G in AAB70253. 1 Publication
Sequence conflicti32 – 343QES → RDF in AAB70253. 1 Publication
Sequence conflicti38 – 381Q → R in AAB70253. 1 Publication
Sequence conflicti50 – 523VCL → FCF in AAB70253. 1 Publication
Sequence conflicti68 – 681D → DF in AAB70253. 1 Publication
Sequence conflicti224 – 2241Q → P in CAA57465. 1 Publication
Sequence conflicti648 – 6481L → F in CAA57465. 1 Publication
Sequence conflicti651 – 6511E → D in CAA57465. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31668.1.
RefSeqiNP_003469.2. NM_003478.3.
UniGeneiHs.440320.

Genome annotation databases

EnsembliENST00000393094; ENSP00000376808; ENSG00000166266.
ENST00000531427; ENSP00000435376; ENSG00000166266.
GeneIDi8065.
KEGGihsa:8065.
UCSCiuc001pjv.3. human.

Polymorphism databases

DMDMi14917099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31668.1.
RefSeqi NP_003469.2. NM_003478.3.
UniGenei Hs.440320.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DPL X-ray 2.60 C 401-780 [» ]
3DQV X-ray 3.00 C/D 401-780 [» ]
4JGH X-ray 3.00 D 10-386 [» ]
4N9F X-ray 3.30 3/9/C/I/O/U/V/f/l/r/w/x 12-321 [» ]
ProteinModelPortali Q93034.
SMRi Q93034. Positions 10-387, 401-780.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113743. 427 interactions.
DIPi DIP-43696N.
IntActi Q93034. 33 interactions.
MINTi MINT-1184052.
STRINGi 9606.ENSP00000299351.

PTM databases

PhosphoSitei Q93034.

Polymorphism databases

DMDMi 14917099.

Proteomic databases

MaxQBi Q93034.
PaxDbi Q93034.
PRIDEi Q93034.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393094 ; ENSP00000376808 ; ENSG00000166266 .
ENST00000531427 ; ENSP00000435376 ; ENSG00000166266 .
GeneIDi 8065.
KEGGi hsa:8065.
UCSCi uc001pjv.3. human.

Organism-specific databases

CTDi 8065.
GeneCardsi GC11P107913.
HGNCi HGNC:2556. CUL5.
HPAi CAB017787.
HPA002185.
MIMi 601741. gene.
neXtProti NX_Q93034.
PharmGKBi PA27052.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5647.
HOGENOMi HOG000007610.
HOVERGENi HBG099672.
InParanoidi Q93034.
KOi K10612.
OMAi VCLWDEK.
OrthoDBi EOG78D7JD.
PhylomeDBi Q93034.
TreeFami TF105874.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_115755. Signaling by ERBB2.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

EvolutionaryTracei Q93034.
GeneWikii CUL5.
GenomeRNAii 8065.
NextBioi 30655.
PROi Q93034.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q93034.
Bgeei Q93034.
CleanExi HS_CUL5.
Genevestigatori Q93034.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view ]
SMARTi SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view ]
SUPFAMi SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEi PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. 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.

Entry informationi

Entry nameiCUL5_HUMAN
AccessioniPrimary (citable) accession number: Q93034
Secondary accession number(s): A8K960, O14766, Q9BZC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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