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Clusterin (Dimeric acid glycoprotein) (DAG) (Sulfated glycoprotein 2) (SGP-2) (Testosterone repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]

 CLUS_RAT                Reviewed;         447 AA.
P05371;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
13-FEB-2019, entry version 140.
RecName: Full=Clusterin;
AltName: Full=Dimeric acid glycoprotein;
Short=DAG;
AltName: Full=Sulfated glycoprotein 2;
Short=SGP-2;
AltName: Full=Testosterone repressed prostate message 2;
Short=TRPM-2;
Contains:
RecName: Full=Clusterin beta chain;
Contains:
RecName: Full=Clusterin alpha chain;
Flags: Precursor;
Name=Clu;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-45 AND 227-241,
PROTEOLYTIC PROCESSING, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=3651384; DOI=10.1021/bi00386a008;
Collard M.W., Griswold M.D.;
"Biosynthesis and molecular cloning of sulfated glycoprotein 2
secreted by rat Sertoli cells.";
Biochemistry 26:3297-3303(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=2920020; DOI=10.1042/bj2570293;
Bettuzzi S., Hiipakka R.A., Gilna P., Liao S.;
"Identification of an androgen-repressed mRNA in rat ventral prostate
as coding for sulphated glycoprotein 2 by cDNA cloning and sequence
analysis.";
Biochem. J. 257:293-296(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Sprague-Dawley;
PubMed=7680346;
Wong P., Pineault J.M., Lakins J., Taillefer D., Leger J., Wang C.,
Tenniswood M.;
"Genomic organization and expression of the rat TRPM-2 (clusterin)
gene, a gene implicated in apoptosis.";
J. Biol. Chem. 268:5021-5031(1993).
[4]
PROTEIN SEQUENCE OF 22-51 AND 227-256, SUBCELLULAR LOCATION, SUBUNIT,
AND PROTEOLYTIC PROCESSING.
PubMed=3415696; DOI=10.1016/S0006-291X(88)81051-9;
Cheng C.Y., Chen C.C., Feng Z., Marshall A., Bardin C.W.;
"Rat clusterin isolated from primary Sertoli cell-enriched culture
medium is sulfated glycoprotein-2 (SGP-2).";
Biochem. Biophys. Res. Commun. 155:398-404(1988).
[5]
CHARACTERIZATION OF TRPM-2.
PubMed=2299741;
Bandyk M.G., Sawczuk I.S., Olsson C.A., Katz A.E., Buttyan R.;
"Characterization of the products of a gene expressed during androgen-
programmed cell death and their potential use as a marker of
urogenital injury.";
J. Urol. 143:407-413(1990).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Functions as extracellular chaperone that prevents
aggregation of nonnative proteins. Prevents stress-induced
aggregation of blood plasma proteins. Inhibits formation of
amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and
aggregation-prone LYZ variants (in vitro). Does not require ATP.
Maintains partially unfolded proteins in a state appropriate for
subsequent refolding by other chaperones, such as HSPA8/HSC70.
Does not refold proteins by itself. Binding to cell surface
receptors triggers internalization of the chaperone-client complex
and subsequent lysosomal or proteasomal degradation. When
secreted, protects cells against apoptosis and against cytolysis
by complement. Intracellular forms interact with ubiquitin and SCF
(SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes
and promote the ubiquitination and subsequent proteasomal
degradation of target proteins. Promotes proteasomal degradation
of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional
activity. Promotes apoptosis when in the nucleus. Inhibits
apoptosis when associated with the mitochondrial membrane by
interference with BAX-dependent release of cytochrome c into the
cytoplasm. Plays a role in the regulation of cell proliferation
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha
chain and a beta chain. Self-associates and forms higher
oligomers. Interacts with a broad range of misfolded proteins,
including APP, APOC2 and LYZ. Slightly acidic pH promotes
interaction with misfolded proteins. Forms high-molecular weight
oligomers upon interaction with misfolded proteins. Interacts with
APOA1, LRP2, CLUAP1 AND PON1. Interacts with the complement
complex. Interacts with SYVN1, COMMD1, BTRC, CUL1 and with
ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
ligase complexes. Interacts (via alpha chain) with BAX in stressed
cells, where BAX undergoes a conformation change leading to
association with the mitochondrial membrane. Does not interact
with BAX in unstressed cells. Interacts (via alpha chain) with
XRCC6 (By similarity). Found in a complex with LTF, CLU, EPPIN and
SEMG1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3415696,
ECO:0000269|PubMed:3651384}. Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Cytoplasm, cytosol {ECO:0000250}. Microsome {ECO:0000250}.
Endoplasmic reticulum {ECO:0000250}. Cytoplasmic vesicle,
secretory vesicle, chromaffin granule {ECO:0000250}. Note=Can
retrotranslocate from the secretory compartments to the cytosol
upon cellular stress. Detected in perinuclear foci that may be
aggresomes containing misfolded, ubiquitinated proteins. Detected
at the mitochondrion membrane upon induction of apoptosis (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in Sertoli cells (at protein level).
Detected in cultured Sertoli cells, testis, epididymis, liver and
brain. {ECO:0000269|PubMed:3651384}.
-!- DEVELOPMENTAL STAGE: Expressed by cells undergoing programmed
death as a result of the hormonal stimuli or a traumatic insult.
-!- PTM: Extensively glycosylated with sulfated N-linked
carbohydrates. {ECO:0000269|PubMed:3651384}.
-!- PTM: Proteolytically cleaved on its way through the secretory
system, probably within the Golgi lumen. {ECO:0000250}.
-!- PTM: Polyubiquitinated, leading to proteasomal degradation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the clusterin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M16975; AAA41273.1; -; mRNA.
EMBL; X13231; CAA31618.1; -; mRNA.
EMBL; M64723; AAA42298.1; -; mRNA.
EMBL; M64733; AAA42299.1; -; Genomic_DNA.
PIR; A45890; A27205.
RefSeq; NP_444180.2; NM_053021.2.
UniGene; Rn.1780; -.
DisProt; DP00014; -.
SMR; P05371; -.
IntAct; P05371; 1.
MINT; P05371; -.
STRING; 10116.ENSRNOP00000022095; -.
CarbonylDB; P05371; -.
iPTMnet; P05371; -.
PhosphoSitePlus; P05371; -.
jPOST; P05371; -.
PaxDb; P05371; -.
PRIDE; P05371; -.
GeneID; 24854; -.
KEGG; rno:24854; -.
UCSC; RGD:3907; rat.
CTD; 1191; -.
RGD; 3907; Clu.
eggNOG; ENOG410IHRB; Eukaryota.
eggNOG; ENOG410YYKB; LUCA.
HOGENOM; HOG000111799; -.
HOVERGEN; HBG006908; -.
InParanoid; P05371; -.
KO; K17252; -.
OrthoDB; 973835at2759; -.
PhylomeDB; P05371; -.
PRO; PR:P05371; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016235; C:aggresome; IDA:RGD.
GO; GO:0097440; C:apical dendrite; ISS:Alzheimers_University_of_Toronto.
GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0097418; C:neurofibrillary tangle; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0034366; C:spherical high-density lipoprotein particle; ISS:UniProtKB.
GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0000902; P:cell morphogenesis; ISS:Alzheimers_University_of_Toronto.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0032286; P:central nervous system myelin maintenance; ISS:Alzheimers_University_of_Toronto.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:Alzheimers_University_of_Toronto.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0031018; P:endocrine pancreas development; IMP:RGD.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0001774; P:microglial cell activation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0061518; P:microglial cell proliferation; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISS:BHF-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; ISS:Alzheimers_University_of_Toronto.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0017038; P:protein import; ISS:Alzheimers_University_of_Toronto.
GO; GO:0050821; P:protein stabilization; IDA:CAFA.
GO; GO:1900221; P:regulation of amyloid-beta clearance; ISS:Alzheimers_University_of_Toronto.
GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902847; P:regulation of neuronal signal transduction; ISS:Alzheimers_University_of_Toronto.
GO; GO:0009416; P:response to light stimulus; IEP:RGD.
GO; GO:0051788; P:response to misfolded protein; ISS:UniProtKB.
GO; GO:0035864; P:response to potassium ion; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
InterPro; IPR016016; Clusterin.
InterPro; IPR000753; Clusterin-like.
InterPro; IPR016015; Clusterin_C.
InterPro; IPR033986; Clusterin_CS.
InterPro; IPR016014; Clusterin_N.
PANTHER; PTHR10970; PTHR10970; 1.
PANTHER; PTHR10970:SF1; PTHR10970:SF1; 1.
Pfam; PF01093; Clusterin; 1.
PIRSF; PIRSF002368; Clusterin; 1.
SMART; SM00035; CLa; 1.
SMART; SM00030; CLb; 1.
PROSITE; PS00492; CLUSTERIN_1; 1.
PROSITE; PS00493; CLUSTERIN_2; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
Microsome; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
Secreted; Signal; Spermatogenesis; Ubl conjugation.
SIGNAL 1 21 {ECO:0000269|PubMed:3415696,
ECO:0000269|PubMed:3651384}.
CHAIN 22 447 Clusterin.
/FTId=PRO_0000005544.
CHAIN 22 226 Clusterin beta chain.
/FTId=PRO_0000005545.
CHAIN 227 447 Clusterin alpha chain.
/FTId=PRO_0000005546.
MOTIF 77 80 Nuclear localization signal.
{ECO:0000250}.
MOTIF 441 445 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P10909}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:P10909}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
DISULFID 101 312 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 112 304 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 115 301 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 120 294 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 128 284 Interchain (between beta and alpha
chains). {ECO:0000250}.
CONFLICT 187 187 D -> H (in Ref. 1; AAA41273).
{ECO:0000305}.
SEQUENCE 447 AA; 51375 MW; 9E2FA33E5E0C146E CRC64;
MKILLLCVAL LLTWDNGMVL GEQEFSDNEL QELSTQGSRY VNKEIQNAVQ GVKHIKTLIE
KTNAERKSLL NSLEEAKKKK EGALDDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC
MKFYARVCRS GSGLVGRQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFT
RASGIIDTLF QDRFFTHEPQ DIHHFSPMGF PHKRPHFLYP KSRLVRSLMP LSHYGPLSFH
NMFQPFFDMI HQAQQAMDVQ LHSPALQFPD VDFLKEGEDD PTVCKEIRHN STGCLKMKGQ
CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTQQY NELLHSLQSK MLNTSSLLEQ
LNDQFTWVSQ LANLTQGDDQ YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE
VSKDNPKFMD TVAEKALQEY RRKSRME


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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1996: Linoleate Biosynthesis
WP2434: very-long-chain-fatty-acid-biosynthesis
WP542: Electron Transport Chain
WP1002: Electron Transport Chain
WP105: Fatty Acid Beta Oxidation 2
WP1061: Fatty Acid Beta Oxidation
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1237: Fatty Acid Beta Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1307: Fatty Acid Beta Oxidation
WP1339: Electron Transport Chain
WP143: Fatty Acid Beta Oxidation
WP1434: Osteopontin Signaling
WP148: Fatty Acid Beta Oxidation 2

Related Genes :
[Clu] Clusterin (Dimeric acid glycoprotein) (DAG) (Sulfated glycoprotein 2) (SGP-2) (Testosterone repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU APOJ CLI KUB1 AAG4] Clusterin (Aging-associated gene 4 protein) (Apolipoprotein J) (Apo-J) (Complement cytolysis inhibitor) (CLI) (Complement-associated protein SP-40,40) (Ku70-binding protein 1) (NA1/NA2) (Testosterone-repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain (ApoJalpha) (Complement cytolysis inhibitor a chain); Clusterin alpha chain (ApoJbeta) (Complement cytolysis inhibitor b chain)]
[Clu Apoj Msgp-2] Clusterin (Apolipoprotein J) (Apo-J) (Clustrin) (Sulfated glycoprotein 2) (SGP-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU] Clusterin (Glycoprotein III) (GpIII) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU] Clusterin (Glycoprotein 80) (Gp80) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU] Clusterin (Sulfated glycoprotein 2) (SGP-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain] (Fragment)
[CLU] Clusterin [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU] Clusterin (CP40) (Complement cytolysis inhibitor) (CLI) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU] Clusterin (Apolipoprotein J) (Apo-J) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[CLU] Clusterin (Sulfated glycoprotein 2) (SGP-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain] (Fragments)
[CLU T64] Clusterin (51.5 kDa protein) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]
[AKR1C3 DDH1 HSD17B5 KIAA0119 PGFS] Aldo-keto reductase family 1 member C3 (EC 1.-.-.-) (17-beta-hydroxysteroid dehydrogenase type 5) (17-beta-HSD 5) (3-alpha-HSD type II, brain) (3-alpha-hydroxysteroid dehydrogenase type 2) (3-alpha-HSD type 2) (EC 1.1.1.357) (Chlordecone reductase homolog HAKRb) (Dihydrodiol dehydrogenase 3) (DD-3) (DD3) (Dihydrodiol dehydrogenase type I) (HA1753) (Indanol dehydrogenase) (EC 1.1.1.112) (Prostaglandin F synthase) (PGFS) (EC 1.1.1.188) (Testosterone 17-beta-dehydrogenase 5) (EC 1.1.1.239) (EC 1.1.1.64) (Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase) (EC 1.3.1.20)
[Hsd17b8 H2-Ke6 Hke6] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[ITGA2B GP2B ITGAB] Integrin alpha-IIb (GPalpha IIb) (GPIIb) (Platelet membrane glycoprotein IIb) (CD antigen CD41) [Cleaved into: Integrin alpha-IIb heavy chain; Integrin alpha-IIb light chain, form 1; Integrin alpha-IIb light chain, form 2]
[GP] Envelope glycoprotein (GP1,2) (GP) [Cleaved into: GP1; GP2; GP2-delta]
[HSD17B8 FABGL HKE6 RING2 SDR30C1] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Really interesting new gene 2 protein) (Short chain dehydrogenase/reductase family 30C member 1) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[AHSG FETUA PRO2743] Alpha-2-HS-glycoprotein (Alpha-2-Z-globulin) (Ba-alpha-2-glycoprotein) (Fetuin-A) [Cleaved into: Alpha-2-HS-glycoprotein chain A; Alpha-2-HS-glycoprotein chain B]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[AKR1C3] Aldo-keto reductase family 1 member C3 homolog (EC 1.-.-.-) (17-beta-hydroxysteroid dehydrogenase type 5) (17-beta-HSD 5) (3-alpha-hydroxysteroid dehydrogenase type 2) (3-alpha-HSD type 2) (EC 1.1.1.357) (Indanol dehydrogenase) (EC 1.1.1.112) (Prostaglandin F synthase) (PGFS) (EC 1.1.1.188) (Testosterone 17-beta-dehydrogenase 5) (EC 1.1.1.239) (EC 1.1.1.64) (Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase) (EC 1.3.1.20)
[ABO] Histo-blood group ABO system transferase (Fucosylglycoprotein 3-alpha-galactosyltransferase) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase) (EC 2.4.1.40) (Glycoprotein-fucosylgalactoside alpha-galactosyltransferase) (EC 2.4.1.37) (Histo-blood group A transferase) (A transferase) (Histo-blood group B transferase) (B transferase) (NAGAT) [Cleaved into: Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form]
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[Abo] Histo-blood group ABO system transferase (Cis-AB transferase) (Fucosylglycoprotein 3-alpha-galactosyltransferase) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase) (EC 2.4.1.40) (Glycoprotein-fucosylgalactoside alpha-galactosyltransferase) (EC 2.4.1.37) (Histo-blood group A transferase) (A transferase) (Histo-blood group B transferase) (B transferase) (NAGAT)
[Abo2] Histo-blood group ABO system transferase 2 (B blood group galactosyltransferase) (Blood group A glycosyltransferase 2) (Cis-AB transferase 2) (Fucosylglycoprotein 3-alpha-galactosyltransferase) (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase) (Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase) (EC 2.4.1.40) (Glycoprotein-fucosylgalactoside alpha-galactosyltransferase) (EC 2.4.1.37) (Histo-blood group A transferase) (A transferase) (Histo-blood group B transferase) (B transferase) (NAGAT 2) (Putative blood group A transferase T2)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

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