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Q93034

- CUL5_HUMAN

UniProt

Q93034 - CUL5_HUMAN

Protein

Cullin-5

Gene

CUL5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27052.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy 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)

    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).3 Publications

    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 ASB12.7 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93034.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91N → D in AAB70253. 1 PublicationCurated
    Sequence conflicti12 – 121S → F in AAB70253. 1 PublicationCurated
    Sequence conflicti16 – 161E → G in AAB70253. 1 PublicationCurated
    Sequence conflicti32 – 343QES → RDF in AAB70253. 1 PublicationCurated
    Sequence conflicti38 – 381Q → R in AAB70253. 1 PublicationCurated
    Sequence conflicti50 – 523VCL → FCF in AAB70253. 1 PublicationCurated
    Sequence conflicti68 – 681D → DF in AAB70253. 1 PublicationCurated
    Sequence conflicti224 – 2241Q → P in CAA57465. (PubMed:9037604)Curated
    Sequence conflicti648 – 6481L → F in CAA57465. (PubMed:9037604)Curated
    Sequence conflicti651 – 6511E → D in CAA57465. (PubMed:9037604)Curated

    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

    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: October 1, 2014
    This is version 135 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