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Cullin homolog 1 (Lin-19 homolog protein)

 CUL1_DROME              Reviewed;         774 AA.
Q24311; A4UZ78; Q0E9G0; Q9V312;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
02-JUN-2021, entry version 163.
RecName: Full=Cullin homolog 1;
AltName: Full=Lin-19 homolog protein;
Name=Cul1; Synonyms=cul-1, lin19; ORFNames=CG1877;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Oregon-R; TISSUE=Larval brain;
Filippov V.A., Filippova M.A., Sehnal F.;
"Homolog of C.elegans lin-19 gene.";
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Dealy M.J., Heriche J.K., Nguyen K.V.T., Lo J., Gstaiger M., Krek W.,
Ang D., Bier E., Elson D., Arbeit J., Kipreos E.T., O'Farrell P.H.,
Johnson R.S.;
"Cul-1 limits cyclin E level in mouse and cyclin E function in
Drosophila.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic
review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH ROC1A AND SLMB.
PubMed=11500045; DOI=10.1006/bbrc.2001.5394;
Bocca S.N., Muzzopappa M., Silberstein S., Wappner P.;
"Occurrence of a putative SCF ubiquitin ligase complex in Drosophila.";
Biochem. Biophys. Res. Commun. 286:357-364(2001).
[7]
NEDDYLATION, AND DENEDDYLATION BY THE CSN COMPLEX.
PubMed=12183637; DOI=10.1126/science.1075901;
Cope G.A., Suh G.S.B., Aravind L., Schwarz S.E., Zipursky S.L.,
Koonin E.V., Deshaies R.J.;
"Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8
from Cul1.";
Science 298:608-611(2002).
[8]
NEDDYLATION.
PubMed=18493598; DOI=10.1371/journal.pone.0002239;
Rencus-Lazar S., Amir Y., Wu J., Chien C.T., Chamovitz D.A., Segal D.;
"The proto-oncogene Int6 is essential for neddylation of Cul1 and Cul3 in
Drosophila.";
PLoS ONE 3:E2239-E2239(2008).
[9]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH SKPA AND NTC, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=20392747; DOI=10.1242/dev.050088;
Bader M., Arama E., Steller H.;
"A novel F-box protein is required for caspase activation during cellular
remodeling in Drosophila.";
Development 137:1679-1688(2010).
[10]
INTERACTION WITH FSN.
PubMed=20123973; DOI=10.1128/mcb.01100-09;
Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
"Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3
ligase specificity receptors.";
Mol. Cell. Biol. 30:1769-1782(2010).
[11]
FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN
SCF COMPLEX.
PubMed=24068890; DOI=10.1371/journal.pbio.1001657;
Wong J.J., Li S., Lim E.K., Wang Y., Wang C., Zhang H., Kirilly D., Wu C.,
Liou Y.C., Wang H., Yu F.;
"A Cullin1-based SCF E3 ubiquitin ligase targets the InR/PI3K/TOR pathway
to regulate neuronal pruning.";
PLoS Biol. 11:E1001657-E1001657(2013).
[12]
FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
PubMed=24413555; DOI=10.1002/embr.201337966;
Li S., Wang C., Sandanaraj E., Aw S.S., Koe C.T., Wong J.J., Yu F.,
Ang B.T., Tang C., Wang H.;
"The SCFSlimb E3 ligase complex regulates asymmetric division to inhibit
neuroblast overgrowth.";
EMBO Rep. 15:165-174(2014).
[13]
FUNCTION, AND INTERACTION WITH CAD99C AND SANS.
PubMed=27331610; DOI=10.7554/elife.15258;
Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
Groves A.K., Bellen H.J.;
"The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
the auditory organs of Drosophila and mammals.";
Elife 5:E15258-E15258(2016).
[14]
INTERACTION WITH DLISH.
PubMed=27692068; DOI=10.7554/elife.16624;
Zhang Y., Wang X., Matakatsu H., Fehon R., Blair S.S.;
"The novel SH3 domain protein Dlish/CG10933 mediates fat signaling in
Drosophila by binding and regulating Dachs.";
Elife 5:E16624-E16624(2016).
[15]
ERRATUM OF PUBMED:27692068.
PubMed=27824307; DOI=10.7554/elife.22672;
Zhang Y., Wang X., Matakatsu H., Fehon R., Blair S.S.;
Elife 5:E22672-E22672(2016).
-!- FUNCTION: Core component of multiple 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. 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. During early metamorphosis, part of the SCF-slmb
complex that negatively regulates the InR/PI3K/TOR pathway to activate
the pruning of unnecessary larval ddaC dendrites and mushroom body
axons (PubMed:24068890). The SCF-slmb complex also regulates
asymmetrical division of neuroblasts and inhibits ectopic neuroblast
formation partly through SAK and Akt1 (PubMed:24413555). Also part of
an SCF complex required for caspase activation during sperm
differentiation (PubMed:20392747). Necessary for auditory transduction:
plays a role in Johnston's organ organization by acting in the
regulation of zip and ck function in scolopidial apical attachment
(PubMed:27331610). May function by acting in a Ubr3-mediated pathway
that negatively regulates the ubiquitination of zip, consequently
affecting its interaction with ck (PubMed:27331610).
{ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:24068890,
ECO:0000269|PubMed:24413555, ECO:0000269|PubMed:27331610}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of SCF E3 ubiquitin-protein ligase complexes
consisting of Skpa, Cul1, Roc1a and an F-box protein. In larval
neuroblast self renewal and asymmetric division, as well as ddaC
dendrite and mushroom body axon pruning, the complex contains the F-box
protein slmb (SCF-slmb) (PubMed:24068890, PubMed:24413555). In caspase
activation during sperm differentiation, the complex contains the F-box
protein ntc (PubMed:20392747). Interacts directly with Roc1a
(PubMed:11500045). Interacts with Fsn (PubMed:20123973). Interacts with
Dlish (PubMed:27692068). Interacts with Cad99C (via the cytoplasmic
domain) (PubMed:27331610). Interacts with Sans (PubMed:27331610).
{ECO:0000269|PubMed:11500045, ECO:0000269|PubMed:20123973,
ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:24068890,
ECO:0000269|PubMed:24413555, ECO:0000269|PubMed:27331610,
ECO:0000269|PubMed:27692068}.
-!- INTERACTION:
Q24311; P91666: Rca1; NbExp=2; IntAct=EBI-136038, EBI-7085629;
Q24311; O77430: SkpA; NbExp=2; IntAct=EBI-136038, EBI-180180;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20392747}. Note=In
the spermatid, colocalizes with ntc at the actin-based
individualization complex and the cystic bulge.
-!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:20392747}.
-!- PTM: Neddylated (PubMed:12183637, PubMed:18493598). Deneddylated via
its interaction with the COP9 signalosome (CSN) complex
(PubMed:12183637). {ECO:0000269|PubMed:12183637,
ECO:0000269|PubMed:18493598}.
-!- DISRUPTION PHENOTYPE: Severe dendrite pruning defects in ddaC neurons
at 16 hours after puparium formation (APF) and axon pruning defects in
mushroom body gamma neurons at 24 hours APF. RNAi-mediated knockdown
results in a significant increase in Akt1 protein levels and activity
in ddaC somas (PubMed:24068890). In the larval brain there is a large
increase in the number of neuroblasts, 40% of which show a spindle
misorientation at metaphase (PubMed:24413555). RNAi-mediated knockdown
results in apical detachment of scolopidial cells in Johnston's organ
(PubMed:27331610). {ECO:0000269|PubMed:24068890,
ECO:0000269|PubMed:24413555, ECO:0000269|PubMed:27331610}.
-!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
ProRule:PRU00330}.
---------------------------------------------------------------------------
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EMBL; L41642; AAA85085.1; -; mRNA.
EMBL; AF136343; AAD33676.1; -; mRNA.
EMBL; AE013599; AAF59174.1; -; Genomic_DNA.
EMBL; AE013599; AAM68871.1; -; Genomic_DNA.
EMBL; AE013599; AAM68872.1; -; Genomic_DNA.
EMBL; BT010290; AAQ23608.1; -; mRNA.
RefSeq; NP_523655.1; NM_078931.4.
RefSeq; NP_724621.1; NM_165569.2.
RefSeq; NP_724622.1; NM_165570.3.
RefSeq; NP_724623.1; NM_165571.2.
SMR; Q24311; -.
BioGRID; 61606; 40.
DIP; DIP-19461N; -.
IntAct; Q24311; 8.
MINT; Q24311; -.
STRING; 7227.FBpp0087921; -.
PaxDb; Q24311; -.
PRIDE; Q24311; -.
DNASU; 35742; -.
EnsemblMetazoa; FBtr0088845; FBpp0087921; FBgn0015509.
EnsemblMetazoa; FBtr0088846; FBpp0087922; FBgn0015509.
EnsemblMetazoa; FBtr0088847; FBpp0087923; FBgn0015509.
EnsemblMetazoa; FBtr0088848; FBpp0087924; FBgn0015509.
GeneID; 35742; -.
KEGG; dme:Dmel_CG1877; -.
UCSC; CG1877-RA; d. melanogaster.
CTD; 8454; -.
FlyBase; FBgn0015509; Cul1.
eggNOG; KOG2166; Eukaryota.
GeneTree; ENSGT00940000154774; -.
HOGENOM; CLU_004747_6_1_1; -.
InParanoid; Q24311; -.
OMA; WLWHLCK; -.
OrthoDB; 1040292at2759; -.
PhylomeDB; Q24311; -.
Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-DME-202424; Downstream TCR signaling.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
Reactome; R-DME-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-DME-68949; Orc1 removal from chromatin.
Reactome; R-DME-69231; Cyclin D associated events in G1.
Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-DME-8951664; Neddylation.
Reactome; R-DME-9020702; Interleukin-1 signaling.
Reactome; R-DME-917937; Iron uptake and transport.
Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q24311; -.
UniPathway; UPA00143; -.
BioGRID-ORCS; 35742; 1 hit in 1 CRISPR screen.
GenomeRNAi; 35742; -.
PRO; PR:Q24311; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0015509; Expressed in egg chamber and 34 other tissues.
ExpressionAtlas; Q24311; baseline and differential.
Genevisible; Q24311; DM.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:FlyBase.
GO; GO:0060090; F:molecular adaptor activity; IPI:FlyBase.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IMP:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IGI:FlyBase.
GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IGI:FlyBase.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IGI:FlyBase.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase.
GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:FlyBase.
GO; GO:0030163; P:protein catabolic process; IMP:FlyBase.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:FlyBase.
GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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;
Cytoplasm; Isopeptide bond; Reference proteome; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1..774
/note="Cullin homolog 1"
/id="PRO_0000119786"
CROSSLNK 718
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in NEDD8)"
/evidence="ECO:0000250|UniProtKB:Q13616"
CONFLICT 266
/note="Missing (in Ref. 1; AAA85085)"
/evidence="ECO:0000305"
SEQUENCE 774 AA; 89511 MW; 1AF0D035DE85363C CRC64;
MNRSGNSQTT QKLVNLDDIW SELVEGIMQV FEHEKSLTRS QYMRFYTHVY DYCTSVSAAP
SGRSSGKTGG AQLVGKKLYD RLEQFLKSYL SELLTKFKAI SGEEVLLSRY TKQWKSYQFS
STVLDGICNY LNRNWVKREC EEGQKGIYKI YRLALVAWKG HLFQVLNEPV TKAVLKSIEE
ERQGKLINRS LVRDVIECYV ELSFNEEDTD AEQQKLSVYK QNFENKFIAD TSAFYEKESD
AFLSTNTVTE YLKHVENRLE EETQRVRGFN SKNGLSYLHE TTADVLKSTC EEVLIEKHLK
IFHTEFQNLL NADRNDDLKR MYSLVALSSK NLTDLKSILE NHILHQGTEA IAKCCTTDAA
NDPKTYVQTI LDVHKKYNAL VLTAFNNDNG FVAALDKACG KFINSNVVTI ANSASKSPEL
LAKYCDLLLK KSSKNPEDKE LEDNLNQVMV VFKYIEDKDV FQKYYSKMLA KRLVNHTSAS
DDAEAMMISK LKQTCGYEYT VKLQRMFQDI GVSKDLNSYF KQYLAEKNLT MEIDFGIEVL
SSGSWPFQLS NNFLLPSELE RSVRQFNEFY AARHSGRKLN WLYQMCKGEL IMNVNRNNSS
TYTLQASTFQ MSVLLQFNDQ LSFTVQQLQD NTQTQQENLI QVLQILLKAK VLTSSDNENS
LTPESTVELF LDYKNKKRRI NINQPLKTEL KVEQETVHKH IEEDRKLLIQ AAIVRIMKMR
KRLNHTNLIS EVLNQLSTRF KPKVPVIKKC IDILIEKEYL ERMEGHKDTY SYLA


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EIAAB05358 Btz,Cancer susceptibility candidate gene 3 protein homolog,Casc3,mBtz,Metastatic lymph node gene 51 protein homolog,MLN 51 homolog,Mln51,Mouse,Mus musculus,Protein barentsz,Protein CASC3
EIAAB30152 Chicken,Gallus gallus,Pachytene checkpoint protein 2 homolog,PCH2,Thyroid hormone receptor interactor 13 homolog,Thyroid receptor-interacting protein 13 homolog,TR-interacting protein 13 homolog,TRIP1
EIAAB34392 Fox-1 homolog B,Fox-1 homolog Fxh,Fox2,Fxh,Hexaribonucleotide-binding protein 2,Hrnbp2,Mouse,Mus musculus,Rbfox2,Rbm9,RNA binding protein fox-1 homolog 2,RNA-binding motif protein 9,RNA-binding protei
EIAAB06889 Ceramide synthase 5,CerS5,Cers5,LAG1 longevity assurance homolog 5,Lass5,Mouse,Mus musculus,TRAM homolog 4,Translocating chain-associating membrane protein homolog 4,Trh4
EIAAB06888 Ceramide synthase 4,CerS4,Cers4,LAG1 longevity assurance homolog 4,Lass4,Mouse,Mus musculus,TRAM homolog 1,Translocating chain-associating membrane protein homolog 1,Trh1
EIAAB06884 Ceramide synthase 2,CerS2,Cers2,LAG1 longevity assurance homolog 2,Lass2,Mouse,Mus musculus,TRAM homolog 3,Translocating chain-associating membrane protein homolog 3,Trh3
E0648h ELISA Homo sapiens,hSMAD7,Human,MAD homolog 7,MAD homolog 8,MADH7,MADH8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers agains 96T
E1313m ELISA HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
U1313m CLIA HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
U1313b CLIA Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
E1313m ELISA kit HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
E1313b ELISA kit Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
E1313b ELISA Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
EIAAB08651 Coenzyme Q biosynthesis protein 7 homolog,COQ7,Homo sapiens,Human,Timing protein clk-1 homolog,Ubiquinone biosynthesis protein COQ7 homolog
U0648h CLIA Homo sapiens,hSMAD7,Human,MAD homolog 7,MAD homolog 8,MADH7,MADH8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against 96T
E0648h ELISA kit Homo sapiens,hSMAD7,Human,MAD homolog 7,MAD homolog 8,MADH7,MADH8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers a 96T
E0648m ELISA MAD homolog 7,MAD homolog 8,Madh7,Madh8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against DPP homolog 8,Mouse,Mus 96T
E0648m ELISA kit MAD homolog 7,MAD homolog 8,Madh7,Madh8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against DPP homolog 8,Mouse 96T
U0648m CLIA MAD homolog 7,MAD homolog 8,Madh7,Madh8,Mothers against decapentaplegic homolog 7,Mothers against decapentaplegic homolog 8,Mothers against DPP homolog 7,Mothers against DPP homolog 8,Mouse,Mus m 96T
Pathways :
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP32: Translation Factors
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP1659: Glycine, serine and threonine metabolism
WP1665: Limonene and pinene degradation
WP2371: Parkinsons Disease Pathway
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1675: Nitrogen metabolism
WP35: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP731: Sterol regulatory element binding protein related
WP1616: ABC transporters
WP2199: Seed Development
WP1644: DNA replication
WP2272: Pathogenic Escherichia coli infection
WP1692: Protein export
WP1700: Selenoamino acid metabolism
WP1657: Glycerolipid metabolism
WP2324: AGE/RAGE pathway
WP1663: Homologous recombination

Related Genes :
[LIN7A MALS1 VELI1] Protein lin-7 homolog A (Lin-7A) (hLin-7) (Mammalian lin-seven protein 1) (MALS-1) (Tax interaction protein 33) (TIP-33) (Vertebrate lin-7 homolog 1) (Veli-1)
[Lin7a Mals1 Veli1] Protein lin-7 homolog A (Lin-7A) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1)
[Lin7a Mals1 Veli1] Protein lin-7 homolog A (Lin-7A) (mLin-7) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1)
[Lin7b Mals2 Veli1a Veli2] Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2)
[Lin7c Mals3 Veli3] Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[Lin7c Mals3 Veli3] Protein lin-7 homolog C (Lin-7C) (mLin7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[Lin7b Mals2 Veli2] Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2)
[LIN28A CSDD1 LIN28 ZCCHC1] Protein lin-28 homolog A (Lin-28A) (Zinc finger CCHC domain-containing protein 1)
[LIN7B MALS2 VELI2 UNQ3116/PRO10200] Protein lin-7 homolog B (Lin-7B) (hLin7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2) (hVeli2)
[LIN7C MALS3 VELI3] Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[lin-42 F47F6.1] Period protein homolog lin-42 (Abnormal cell lineage protein 42)
[CASK LIN2] Peripheral plasma membrane protein CASK (hCASK) (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase) (Protein lin-2 homolog)
[orf1ab ORF1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[lag-1 K08B4.1] Suppressor of hairless protein homolog (CSL transcription factor lag-1) (Lin-12 and glp-1 phenotype protein)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[lin-35 C32F10.2] Retinoblastoma-like protein homolog lin-35 (Abnormal cell lineage protein 35) (Synthetic multivulva protein lin-35)
[LIN54 CXCDC1 KIAA2037] Protein lin-54 homolog (CXC domain-containing protein 1)
[CSN5A AJH1 CSN5B At1g22920 F19G10.12] COP9 signalosome complex subunit 5a (Signalosome subunit 5a) (EC 3.4.-.-) (Jun activation domain-binding homolog 1)
[Lin28a Lin28 Tex17] Protein lin-28 homolog A (Lin-28A) (Testis-expressed protein 17)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[sel-2 F10F2.1] Putative neurobeachin homolog (Suppressor enhancer of lin-12)
[ORF1ab ORF1a orf1ab] 3C-like proteinase (EC 3.4.19.12) (EC 3.4.22.69) (Growth factor-like peptide) (Leader protein) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (Papain-like proteinase) (p65 homolog)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (Non-structural protein 16) (nsp16)]
[] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Trim71 Gm1127 Lin41] E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (mLin41) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)
[RPT5B TBP1 At1g09100 F7G19.2] 26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)
[lin28a lin28 si:ch211-232d9.4 zgc:55584] Protein lin-28 homolog A (Lin-28A)
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.354) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[mip120 CG6061] Protein lin-54 homolog (Myb complex protein of 120 kDa)
[cul-1 lin-19 D2045.6] Cullin-1 (CUL-1) (Abnormal cell lineage protein 19)

Bibliography :