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Cul1 protein (Cullin 1) (Cullin 1 (Predicted), isoform CRA_a)

 B1WBY1_RAT              Unreviewed;       776 AA.
B1WBY1;
20-MAY-2008, integrated into UniProtKB/TrEMBL.
20-MAY-2008, sequence version 1.
02-JUN-2021, entry version 110.
SubName: Full=Cul1 protein {ECO:0000313|EMBL:AAI61932.1};
SubName: Full=Cullin 1 {ECO:0000313|Ensembl:ENSRNOP00000007620};
SubName: Full=Cullin 1 (Predicted), isoform CRA_a {ECO:0000313|EMBL:EDM15554.1};
Name=Cul1 {ECO:0000313|EMBL:AAI61932.1,
ECO:0000313|Ensembl:ENSRNOP00000007620, ECO:0000313|RGD:1308157};
Synonyms=Cul1_predicted {ECO:0000313|EMBL:EDM15554.1};
ORFNames=rCG_28370 {ECO:0000313|EMBL:EDM15554.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|EMBL:AAI61932.1};
[1] {ECO:0000313|EMBL:AAI61932.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney {ECO:0000313|EMBL:AAI61932.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2] {ECO:0000313|Ensembl:ENSRNOP00000007620, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007620,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
Mockrin S., Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into mammalian
evolution.";
Nature 428:493-521(2004).
[3] {ECO:0000313|EMBL:EDM15554.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM15554.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[4] {ECO:0000313|EMBL:EDM15554.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM15554.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|Ensembl:ENSRNOP00000007620}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007620};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
[6] {ECO:0000313|Ensembl:ENSRNOP00000074678}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000074678};
Ensembl;
Submitted (JUN-2015) to UniProtKB.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000256|ARBA:ARBA00004906}.
-!- SIMILARITY: Belongs to the cullin family.
{ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
ECO:0000256|RuleBase:RU003829}.
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EMBL; AABR07060512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC161932; AAI61932.1; -; mRNA.
EMBL; CH473959; EDM15554.1; -; Genomic_DNA.
EMBL; CH473959; EDM15555.1; -; Genomic_DNA.
RefSeq; NP_001102097.1; NM_001108627.2.
RefSeq; XP_006236473.1; XM_006236411.2.
SMR; B1WBY1; -.
IntAct; B1WBY1; 2.
STRING; 10116.ENSRNOP00000007620; -.
PeptideAtlas; B1WBY1; -.
PRIDE; B1WBY1; -.
Ensembl; ENSRNOT00000007620; ENSRNOP00000007620; ENSRNOG00000005310.
Ensembl; ENSRNOT00000085805; ENSRNOP00000074678; ENSRNOG00000005310.
GeneID; 362356; -.
KEGG; rno:362356; -.
UCSC; RGD:1308157; rat.
CTD; 8454; -.
RGD; 1308157; Cul1.
eggNOG; KOG2166; Eukaryota.
GeneTree; ENSGT00940000154774; -.
HOGENOM; CLU_004747_6_1_1; -.
OMA; WLWHLCK; -.
OrthoDB; 1040292at2759; -.
TreeFam; TF101151; -.
Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
Reactome; R-RNO-1170546; Prolactin receptor signaling.
Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-RNO-202424; Downstream TCR signaling.
Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-RNO-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-RNO-68949; Orc1 removal from chromatin.
Reactome; R-RNO-69231; Cyclin D associated events in G1.
Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-RNO-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-RNO-8951664; Neddylation.
Reactome; R-RNO-9020702; Interleukin-1 signaling.
Reactome; R-RNO-917937; Iron uptake and transport.
Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000005310; Expressed in cerebellum and 20 other tissues.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISO:RGD.
GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
GO; GO:0006915; P:apoptotic process; ISO:RGD.
GO; GO:0008283; P:cell population proliferation; ISO:RGD.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:RGD.
GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
Gene3D; 1.10.10.10; -; 2.
InterPro; IPR016157; Cullin_CS.
InterPro; IPR016158; Cullin_homology.
InterPro; IPR036317; Cullin_homology_sf.
InterPro; IPR001373; Cullin_N.
InterPro; IPR019559; Cullin_neddylation_domain.
InterPro; IPR016159; Cullin_repeat-like_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00888; Cullin; 1.
Pfam; PF10557; Cullin_Nedd8; 1.
SMART; SM00182; CULLIN; 1.
SMART; SM00884; Cullin_Nedd8; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF74788; SSF74788; 1.
SUPFAM; SSF75632; SSF75632; 1.
PROSITE; PS01256; CULLIN_1; 1.
PROSITE; PS50069; CULLIN_2; 1.
1: Evidence at protein level;
Coiled coil {ECO:0000256|SAM:Coils};
Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
Proteomics identification {ECO:0007829|PeptideAtlas:B1WBY1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
DOMAIN 417..644
/note="CULLIN_2"
/evidence="ECO:0000259|PROSITE:PS50069"
COILED 261..281
/evidence="ECO:0000256|SAM:Coils"
SEQUENCE 776 AA; 89692 MW; 3E1F8B63C6E498F4 CRC64;
MSSNRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA


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Pathways :
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1685: Peptidoglycan biosynthesis
WP375: Wnt Signaling Pathway NetPath
WP1616: ABC transporters
WP211: BMP signaling pathway
WP980: Wnt Signaling Pathway NetPath
WP1644: DNA replication
WP2218: sGC
WP1064: Delta-Notch Signaling Pathway
WP1692: Protein export
WP539: Wnt Signaling Pathway NetPath
WP1163: TNF-alpha NF-kB Signaling Pathway
WP1700: Selenoamino acid metabolism
WP754: Wnt Signaling Pathway NetPath
WP1657: Glycerolipid metabolism
WP232: G Protein Signaling Pathways
WP1663: Homologous recombination
WP2371: Parkinsons Disease Pathway
WP1371: G Protein Signaling Pathways
WP1888: Post-translational protein modification
WP813: G Protein Signaling Pathways
WP1939: Unfolded Protein Response
WP926: TGF-beta Receptor Signaling Pathway
WP1673: Naphthalene and anthracene degradation

Related Genes :
[CUL1] Cullin-1 (CUL-1)
[Cul1] Cullin-1 (CUL-1)
[cul-1 lin-19 D2045.6] Cullin-1 (CUL-1) (Abnormal cell lineage protein 19)
[CUL1 At4g02570 T10P11.26] Cullin-1
[DCUN1D2 C13orf17 DCUN1L2] DCN1-like protein 2 (DCNL2) (DCUN1 domain-containing protein 2) (Defective in cullin neddylation protein 1-like protein 2)
[CUL4A] Cullin-4A (CUL-4A)
[DCUN1D1 DCN1 DCUN1L1 RP42 SCCRO] DCN1-like protein 1 (DCNL1) (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Squamous cell carcinoma-related oncogene)
[CUL3 KIAA0617] Cullin-3 (CUL-3)
[DCUN1D5 SCCRO5] DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5)
[DCUN1D3 SCCRO3] DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3) (Squamous cell carcinoma-related oncogene 3)
[Cul7 Kiaa0076] Cullin-7 (CUL-7) (p185) (p193)
[CUL4B KIAA0695] Cullin-4B (CUL-4B)
[CUL7 KIAA0076] Cullin-7 (CUL-7)
[CUL2] Cullin-2 (CUL-2)
[Dcun1d5] DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5)
[Cul7] Cullin-7 (CUL-7)
[Dcun1d1 Dcun1l1 Rp42 Tes3] DCN1-like protein 1 (DCNL1) (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Testis-specific protein 3)
[DCUN1D3] DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3)
[CUL1] Cullin-1 (CUL-1)
[CSN5A AJH1 CSN5B At1g22920 F19G10.12] COP9 signalosome complex subunit 5a (Signalosome subunit 5a) (EC 3.4.-.-) (Jun activation domain-binding homolog 1)
[RTT101 CUL8 YJL047C J1166] Cullin-8 (Cullin-C) (Regulator of Ty1 transposition protein 101)
[Dcun1d3] DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3)
[BTRC BTRCP FBW1A FBXW1A] F-box/WD repeat-containing protein 1A (E3RSIkappaB) (Epididymis tissue protein Li 2a) (F-box and WD repeats protein beta-TrCP) (pIkappaBalpha-E3 receptor subunit)
[Cul4b mKIAA0695] Cullin-4B (CUL-4B)
[Dcun1d3] DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3)
[TRIM21 RNF81 RO52 SSA1] E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27) (52 kDa Ro protein) (52 kDa ribonucleoprotein autoantigen Ro/SS-A) (RING finger protein 81) (RING-type E3 ubiquitin transferase TRIM21) (Ro(SS-A)) (Sjoegren syndrome type A antigen) (SS-A) (Tripartite motif-containing protein 21)
[CUL3A CUL3 At1g26830 T2P11.2] Cullin-3A (AtCUL3a)
[CUL5 VACM1] Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1)
[Cul5 Vacm1] Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1)
[Cul4a] Cullin-4A (CUL-4A)

Bibliography :
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