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Cullin-1 (CUL-1)

 CUL1_MOUSE              Reviewed;         776 AA.
Q9WTX6; Q9WUI7;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
02-JUN-2021, entry version 166.
RecName: Full=Cullin-1;
Short=CUL-1;
Name=Cul1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH
PHOSPHORYLATED NFKBIA; SKP1 AND BTRC.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=10097128; DOI=10.1073/pnas.96.7.3859;
Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M.,
Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A.,
Nakayama K.;
"Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin
ligase Skp1/Cul 1/F-box protein FWD1.";
Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999).
[2]
ERRATUM OF PUBMED:10097128.
Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M.,
Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A.,
Nakayama K.;
Proc. Natl. Acad. Sci. U.S.A. 96:6571-6571(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Filippov V., Filippova M., Gill S.S.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=NIH Swiss; TISSUE=Embryo;
PubMed=10508527; DOI=10.1038/13886;
Dealy M.J., Nguyen K.V.T., Lo J., Gstaiger M., Krek W., Elson D.,
Arbeit J., Kipreos E.T., Johnson R.S.;
"Loss of Cul1 results in early embryonic lethality and dysregulation of
cyclin E.";
Nat. Genet. 23:245-248(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9663463;
Michel J.J., Xiong Y.;
"Human CUL-1, but not other cullin family members, selectively interacts
with SKP1 to form a complex with SKP2 and cyclin A.";
Cell Growth Differ. 9:435-449(1998).
[7]
IDENTIFICATION IN A COMPLEX WITH BTRC AND SKP1.
PubMed=11735228; DOI=10.1006/geno.2001.6658;
Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K.,
Nakayama K.;
"Characterization of a mouse gene (Fbxw6) that encodes a homologue of
Caenorhabditis elegans SEL-10.";
Genomics 78:214-222(2001).
[8]
INTERACTION WITH COPS2.
PubMed=11967155; DOI=10.1016/s0960-9822(02)00791-1;
Yang X., Menon S., Lykke-Andersen K., Tsuge T., Xiao D., Wang X.,
Rodriguez-Suarez R.J., Zhang H., Wei N.;
"The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase
progression via deneddylation of SCF Cul1.";
Curr. Biol. 12:667-672(2002).
[9]
FUNCTION, SUBUNIT, AND PATHWAY.
PubMed=12140560; DOI=10.1038/nature00890;
Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y.,
Matsuoka K., Yoshida M., Tanaka K., Tai T.;
"E3 ubiquitin ligase that recognizes sugar chains.";
Nature 418:438-442(2002).
[10]
INTERACTION WITH CUL7 AND FBXW8.
PubMed=16880526; DOI=10.1128/mcb.00595-06;
Tsunematsu R., Nishiyama M., Kotoshiba S., Saiga T., Kamura T.,
Nakayama K.I.;
"Fbxw8 is essential for Cul1-Cul7 complex formation and for placental
development.";
Mol. Cell. Biol. 26:6157-6169(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[12]
INTERACTION WITH MURINE CYTOMEGALOVIRUS M48 (MICROBIAL INFECTION),
DENEDDYLATION BY MURINE CYTOMEGALOVIRUS M48, AND NEDDYLATION.
PubMed=20190741; DOI=10.1038/ncb2035;
Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M.,
Di Guglielmo C., Masucci M.G.;
"A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication
by regulating the activity of cullin-RING ligases.";
Nat. Cell Biol. 12:351-361(2010).
[13]
IDENTIFICATION IN THE SCF(FBXL3) COMPLEX, AND FUNCTION.
PubMed=23452855; DOI=10.1016/j.cell.2013.01.055;
Yoo S.H., Mohawk J.A., Siepka S.M., Shan Y., Huh S.K., Hong H.K.,
Kornblum I., Kumar V., Koike N., Xu M., Nussbaum J., Liu X., Chen Z.,
Chen Z.J., Green C.B., Takahashi J.S.;
"Competing E3 ubiquitin ligases govern circadian periodicity by degradation
of CRY in nucleus and cytoplasm.";
Cell 152:1091-1105(2013).
[14]
IDENTIFICATION IN THE SCF(FBXL21) COMPLEX, AND FUNCTION.
PubMed=23452856; DOI=10.1016/j.cell.2013.01.054;
Hirano A., Yumimoto K., Tsunematsu R., Matsumoto M., Oyama M.,
Kozuka-Hata H., Nakagawa T., Lanjakornsiripan D., Nakayama K.I., Fukada Y.;
"FBXL21 regulates oscillation of the circadian clock through ubiquitination
and stabilization of cryptochromes.";
Cell 152:1106-1118(2013).
[15]
INTERACTION WITH KAT7.
PubMed=23319590; DOI=10.1074/jbc.m112.426882;
Zou C., Chen Y., Smith R.M., Snavely C., Li J., Coon T.A., Chen B.B.,
Zhao Y., Mallampalli R.K.;
"SCF(Fbxw15) mediates histone acetyltransferase binding to origin
recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate
cell proliferation.";
J. Biol. Chem. 288:6306-6316(2013).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-63, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the
ubiquitination of proteins involved in cell cycle progression, signal
transduction and transcription. SCF complexes and ARIH1 collaborate in
tandem to mediate ubiquitination of target proteins. In the SCF
complex, serves as a rigid scaffold that organizes the SKP1-F-box
protein and RBX1 subunits. May contribute to catalysis through
positioning of the substrate and the ubiquitin-conjugating enzyme. The
E3 ubiquitin-protein ligase activity of the complex is dependent on the
neddylation of the cullin subunit and exchange of the substrate
recognition component is mediated by TIP120A/CAND1. The functional
specificity of the SCF complex depends on the F-box protein as
substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct
ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11)
directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs
ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and
probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of
CEP68. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip
and is involved in regulation of G1/S transition. SCF(SKP2) directs
ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and
probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E,
NOTCH1 released notch intracellular domain (NICD), and probably PSEN1.
SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs
ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and
DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs
ubiquitination of BCL6 and DTL but does not seem to direct
ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA
at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-
RELA dimer to translocate into the nucleus and to activate
transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3)
and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9)
directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs
ubiquitination of BCL2. {ECO:0000250|UniProtKB:Q13616,
ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:23452855}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:12140560}.
-!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-
box domain-containing protein as substrate-specific subunit
(PubMed:10097128, PubMed:12140560, PubMed:16880526, PubMed:23452855,
PubMed:23452856). Component of the SCF(FBXW11) complex containing
FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it
interacts directly with SKP1, SKP2 and RBX1. Component of the
SCF(FBXW2) complex containing FBXW2. Component of the SCF(FBXO32)
complex containing FBXO32. Component of the probable SCF(FBXO7) complex
containing FBXO7. Component of the SCF(FBXO10) complex containing
FBXO10. Component of the SCF(FBXO11) complex containing FBXO11.
Component of the SCF(FBXO25) complex containing FBXO25. Component of
the SCF(FBXO33) complex containing FBXO33. Component of the probable
SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44)
complex, composed of SKP1, CUL1 and FBXO44 (By similarity). Component
of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC
(PubMed:10097128, PubMed:11735228). This complex binds phosphorylated
NFKBIA (PubMed:10097128). Part of a SCF complex consisting of CUL1,
RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing
CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex,
composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27)
complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF)
complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the
SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of
the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21.
Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9.
Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7.
Interacts with CHEK2; mediates CHEK2 ubiquitination and regulates its
function. Part of a complex with TIP120A/CAND1 and RBX1. The
unneddylated form interacts with TIP120A/CAND1 and the interaction
mediates the exchange of the F-box substrate-specific subunit. Can
self-associate (By similarity). Interacts with FBXW8 (PubMed:16880526).
Interacts with RNF7 (By similarity). Interacts with CUL7; the
interaction seems to be mediated by FBXW8 (PubMed:16880526). Interacts
with TRIM21 (By similarity). Interacts with COPS2 (PubMed:11967155).
Interacts with DCUN1D1 and UBE2M. Interacts with DCUN1D3. Interacts
with DCUN1D4 (By similarity). Identified in a complex with RBX1 and
GLMN (By similarity). Interacts with CEP68 as part of the SCF(FBXW11)
complex; the interaction is probably mediated by FBXW11 and the complex
also contains CDK5RAP2 and PCNT. Interacts (when neddylated) with
ARIH1; leading to activate the E3 ligase activity of ARIH1. Interacts
with COPS9. Interacts with UBXN1 (By similarity). Interacts with KAT7,
probably as part of an SCF complex; the interaction mediates KAT7
ubiquitination (PubMed:23319590). Interacts with NOTCH2 (By
similarity). Part of a complex that contains DCUN1D5, CUL1 and RBX1;
this interaction is bridged by CUL1 (By similarity). Interacts
(unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and
DCUN1D5; these interactions promote the cullin neddylation (By
similarity). {ECO:0000250|UniProtKB:Q13616,
ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:11735228,
ECO:0000269|PubMed:11967155, ECO:0000269|PubMed:12140560,
ECO:0000269|PubMed:16880526, ECO:0000269|PubMed:23319590,
ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}.
-!- SUBUNIT: (Microbial infection) Interacts with murine cytomegalovirus
M48. {ECO:0000269|PubMed:20190741}.
-!- INTERACTION:
Q9WTX6; O94888: UBXN7; Xeno; NbExp=3; IntAct=EBI-1551052, EBI-1993627;
Q9WTX6; P55072: VCP; Xeno; NbExp=2; IntAct=EBI-1551052, EBI-355164;
-!- TISSUE SPECIFICITY: Embryo fibroblasts and embryo preadipocytes.
{ECO:0000269|PubMed:9663463}.
-!- PTM: Neddylated; which enhances the ubiquitination activity of SCF.
Deneddylated via its interaction with the COP9 signalosome (CSN)
complex. {ECO:0000269|PubMed:20190741}.
-!- PTM: (Microbial infection) Deneddylated by murine cytomegalovirus M48
leading to a S-phase-like environment that is required for efficient
replication of the viral genome. {ECO:0000269|PubMed:20190741}.
-!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
ProRule:PRU00330}.
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EMBL; AF083216; AAD16038.1; -; mRNA.
EMBL; AF176910; AAD52657.1; -; mRNA.
EMBL; AF136441; AAD34471.1; -; mRNA.
EMBL; BC029260; AAH29260.1; -; mRNA.
CCDS; CCDS20095.1; -.
RefSeq; NP_036172.1; NM_012042.3.
RefSeq; XP_006506251.1; XM_006506188.3.
RefSeq; XP_006506252.1; XM_006506189.3.
RefSeq; XP_006506253.1; XM_006506190.3.
SMR; Q9WTX6; -.
BioGRID; 205088; 98.
CORUM; Q9WTX6; -.
DIP; DIP-39799N; -.
IntAct; Q9WTX6; 42.
MINT; Q9WTX6; -.
STRING; 10090.ENSMUSP00000031697; -.
iPTMnet; Q9WTX6; -.
PhosphoSitePlus; Q9WTX6; -.
EPD; Q9WTX6; -.
MaxQB; Q9WTX6; -.
PaxDb; Q9WTX6; -.
PeptideAtlas; Q9WTX6; -.
PRIDE; Q9WTX6; -.
ProteomicsDB; 279208; -.
Antibodypedia; 3630; 535 antibodies.
DNASU; 26965; -.
Ensembl; ENSMUST00000031697; ENSMUSP00000031697; ENSMUSG00000029686.
GeneID; 26965; -.
KEGG; mmu:26965; -.
UCSC; uc009bsz.1; mouse.
CTD; 8454; -.
MGI; MGI:1349658; Cul1.
eggNOG; KOG2166; Eukaryota.
GeneTree; ENSGT00940000154774; -.
HOGENOM; CLU_004747_6_1_1; -.
InParanoid; Q9WTX6; -.
OMA; WLWHLCK; -.
OrthoDB; 1040292at2759; -.
PhylomeDB; Q9WTX6; -.
TreeFam; TF101151; -.
Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
Reactome; R-MMU-1170546; Prolactin receptor signaling.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-MMU-68949; Orc1 removal from chromatin.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-MMU-8951664; Neddylation.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
Reactome; R-MMU-917937; Iron uptake and transport.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
BioGRID-ORCS; 26965; 13 hits in 53 CRISPR screens.
ChiTaRS; Cul1; mouse.
PRO; PR:Q9WTX6; -.
Proteomes; UP000000589; Chromosome 6.
RNAct; Q9WTX6; protein.
Bgee; ENSMUSG00000029686; Expressed in embryo and 321 other tissues.
ExpressionAtlas; Q9WTX6; baseline and differential.
Genevisible; Q9WTX6; MM.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
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; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0008283; P:cell population proliferation; IMP:MGI.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:MGI.
GO; GO:0006513; P:protein monoubiquitination; IGI:MGI.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:MGI.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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;
Host-virus interaction; Isopeptide bond; Methylation; Reference proteome;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1..776
/note="Cullin-1"
/id="PRO_0000119788"
MOD_RES 63
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
CROSSLNK 720
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in NEDD8)"
/evidence="ECO:0000250|UniProtKB:Q13616"
CONFLICT 74
/note="K -> R (in Ref. 3; AAD34471)"
/evidence="ECO:0000305"
CONFLICT 249
/note="T -> S (in Ref. 3; AAD34471)"
/evidence="ECO:0000305"
CONFLICT 308
/note="Q -> H (in Ref. 3; AAD34471)"
/evidence="ECO:0000305"
CONFLICT 334
/note="G -> R (in Ref. 3; AAD34471)"
/evidence="ECO:0000305"
CONFLICT 640..663
/note="LQILLKSKLLVLEDENANVDEVEL -> YRFTEVEIAGLRDEMPMLMRWM
(in Ref. 3; AAD34471)"
/evidence="ECO:0000305"
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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EIAAB05268 Bos taurus,Bovine,CAND1,Cullin-associated and neddylation-dissociated protein 1,Cullin-associated NEDD8-dissociated protein 1
LF-PA40298 anti-Cullin 1 (CUL1) , Rabbit polyclonal to Cullin 1 (CUL1), Isotype IgG, Host Rabbit 50 ul
LF-PA40299 anti-Cullin 2 (CUL2), Rabbit polyclonal to Cullin 2 (CUL2), Isotype IgG, Host Rabbit 50 ul
LF-PA40300 anti-Cullin 3 (CUL3) , Rabbit polyclonal to Cullin 3 (CUL3), Isotype IgG, Host Rabbit 50 ul
LF-PA40301 anti-Cullin 4A (CUL4A) , Rabbit polyclonal to Cullin 4A (CUL4A), Isotype IgG, Host Rabbit 50 ul
LF-PA40302 anti-Cullin 5 (CUL5) , Rabbit polyclonal to Cullin 5 (CUL5), Isotype IgG, Host Rabbit 50 ul
LF-PA40303 anti-Cullin 7 (CUL7) , Rabbit polyclonal to Cullin 7 (CUL7), Isotype IgG, Host Rabbit 50 ul
EIAAB05269 Cand1,Cullin-associated and neddylation-dissociated protein 1,Cullin-associated NEDD8-dissociated protein 1,D10Ertd516e,Kiaa0829,Mouse,Mus musculus,p120 CAND1
18-272-196997 Cullin 1 - Rabbit polyclonal to Cullin 1; CUL-1 Polyclonal 0.5 ml
18-272-196998 Cullin 2 - Rabbit polyclonal to Cullin 2; CUL-2 Polyclonal 0.5 ml
18-272-196999 Cullin 3 - Rabbit polyclonal to Cullin 3; CUL-3 Polyclonal 0.5 ml
18-003-42558 Cullin-associated NEDD8-dissociated protein 1 - Cullin-associated and neddylation-dissociated protein 1; p120 CAND1; TBP-interacting protein TIP120A; TBP-interacting protein of 120 kDa A Polyclonal 0.1 mg Protein A
18-272-196297 Cullin 1 prediluted - Rabbit polyclonal to Cullin 1 prediluted; CUL-1 Polyclonal 7 ml
18-272-196298 Cullin 2 prediluted - Rabbit polyclonal to Cullin 2 prediluted; CUL-2 Polyclonal 7 ml
EIAAB05272 CAND2,Cullin-associated and neddylation-dissociated protein 2,Cullin-associated NEDD8-dissociated protein 2,Homo sapiens,Human,KIAA0667,p120 CAND2,TBP-interacting protein 120B,TBP-interacting protein
EIAAB05270 CAND1,Cullin-associated and neddylation-dissociated protein 1,Cullin-associated NEDD8-dissociated protein 1,Homo sapiens,Human,KIAA0829,p120 CAND1,TBP-interacting protein 120A,TBP-interacting protein
EIAAB05274 Cand2,Cullin-associated and neddylation-dissociated protein 2,Cullin-associated NEDD8-dissociated protein 2,Kiaa0667,Mouse,Mus musculus,p120 CAND2,TBP-interacting protein 120B,TBP-interacting protein
EIAAB05273 Cand2,Cullin-associated and neddylation-dissociated protein 2,Cullin-associated NEDD8-dissociated protein 2,p120 CAND2,Rat,Rattus norvegicus,TBP-interacting protein 120B,TBP-interacting protein b,TBP-
EIAAB05271 Cand1,Cullin-associated and neddylation-dissociated protein 1,Cullin-associated NEDD8-dissociated protein 1,p120 CAND1,Rat,Rattus norvegicus,TBP-interacting protein 120A,TBP-interacting protein of 120
RP 070-05 Cullin-2; 0.5ml
RP 069-05 Cullin-1; 0.5ml
49-418 Cullin 7 Antibody 0.05 mL
49-462 Cullin 9 Antibody 0.05 mL
Pathways :
WP2359: Parkin-Ubiquitin Proteasomal System pathway

Related Genes :
[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)
[CUL1] Cullin-1 (CUL-1)
[cul-1 lin-19 D2045.6] Cullin-1 (CUL-1) (Abnormal cell lineage protein 19)
[Cul1] Cullin-1 (CUL-1)
[RTT101 CUL8 YJL047C J1166] Cullin-8 (Cullin-C) (Regulator of Ty1 transposition protein 101)
[CUL1 At4g02570 T10P11.26] Cullin-1
[CUL3A CUL3 At1g26830 T2P11.2] Cullin-3A (AtCUL3a)
[CUL3 KIAA0617] Cullin-3 (CUL-3)
[Cul3] Cullin-3 (CUL-3)
[Cul7 Kiaa0076] Cullin-7 (CUL-7) (p185) (p193)
[CUL4A] Cullin-4A (CUL-4A)
[CUL4B KIAA0695] Cullin-4B (CUL-4B)
[CUL7 KIAA0076] Cullin-7 (CUL-7)
[Cul4a] Cullin-4A (CUL-4A)
[Cul7] Cullin-7 (CUL-7)
[Cul4b mKIAA0695] Cullin-4B (CUL-4B)
[CUL2] Cullin-2 (CUL-2)
[Cul3] Cullin-3
[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)
[DCUN1D2 C13orf17 DCUN1L2] DCN1-like protein 2 (DCNL2) (DCUN1 domain-containing protein 2) (Defective in cullin neddylation protein 1-like protein 2)
[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)
[DTL CDT2 CDW1 DCAF2 L2DTL RAMP] Denticleless protein homolog (DDB1- and CUL4-associated factor 2) (Lethal(2) denticleless protein homolog) (Retinoic acid-regulated nuclear matrix-associated protein)
[KLHL12 C3IP1] Kelch-like protein 12 (CUL3-interacting protein 1) (DKIR homolog) (hDKIR)
[Cul5] Cullin-5 (CUL-5)
[DCAF15 C19orf72] DDB1- and CUL4-associated factor 15
[Cul2] Cullin-2 (CUL-2)
[CUL7] Cullin-7 (CUL-7)
[CUL3B At1g69670 T6C23.13] Cullin-3B (AtCUL3b)

Bibliography :
No related Items