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Melanocortin-2 receptor accessory protein 2 (MC2R accessory protein 2)

 MRAP2_HUMAN             Reviewed;         205 AA.
Q96G30; A8K9M1; Q8IXM9; Q8N2D1;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
13-FEB-2019, entry version 124.
RecName: Full=Melanocortin-2 receptor accessory protein 2;
Short=MC2R accessory protein 2;
Name=MRAP2; Synonyms=C6orf117;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala, and Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Colon;
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-9,
INTERACTION WITH MC1R; MC2R; MC3R; MC4R; MC5R AND MRAP, TISSUE
SPECIFICITY, AND MUTAGENESIS OF ASN-9.
PubMed=19329486; DOI=10.1073/pnas.0809918106;
Chan L.F., Webb T.R., Chung T.T., Meimaridou E., Cooray S.N.,
Guasti L., Chapple J.P., Egertova M., Elphick M.R., Cheetham M.E.,
Metherell L.A., Clark A.J.;
"MRAP and MRAP2 are bidirectional regulators of the melanocortin
receptor family.";
Proc. Natl. Acad. Sci. U.S.A. 106:6146-6151(2009).
[6]
FUNCTION, SUBUNIT, TOPOLOGY, AND INTERACTION WITH MRAP.
PubMed=20371771; DOI=10.1126/scisignal.2000593;
Sebag J.A., Hinkle P.M.;
"Regulation of G protein-coupled receptor signaling: specific
dominant-negative effects of melanocortin 2 receptor accessory protein
2.";
Sci. Signal. 3:RA28-RA28(2010).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
POLYMORPHISM, INVOLVEMENT IN OBESITY, AND VARIANTS TYR-88; VAL-115 AND
CYS-125.
PubMed=23869016; DOI=10.1126/science.1233000;
Asai M., Ramachandrappa S., Joachim M., Shen Y., Zhang R.,
Nuthalapati N., Ramanathan V., Strochlic D.E., Ferket P., Linhart K.,
Ho C., Novoselova T.V., Garg S., Ridderstrale M., Marcus C.,
Hirschhorn J.N., Keogh J.M., O'Rahilly S., Chan L.F., Clark A.J.,
Farooqi I.S., Majzoub J.A.;
"Loss of function of the melanocortin 2 receptor accessory protein 2
is associated with mammalian obesity.";
Science 341:275-278(2013).
-!- FUNCTION: Modulator of melanocortin receptor 4 (MC4R), a receptor
involved in energy homeostasis. Plays a central role in the
control of energy homeostasis and body weight regulation by
increasing ligand-sensitivity of MC4R and MC4R-mediated generation
of cAMP (By similarity). May also act as a negative regulator of
MC2R: competes with MRAP for binding to MC2R and impairs the
binding of corticotropin (ACTH) to MC2R. May also regulate
activity of other melanocortin receptors (MC1R, MC3R and MC5R);
however, additional evidences are required in vivo. {ECO:0000250,
ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.
-!- SUBUNIT: Homodimer and heterodimer. Forms antiparallel homodimers
and heterodimers with MRAP. Interacts with MC1R, MC2R, MC3R, MC4R
and MC5R. {ECO:0000269|PubMed:19329486,
ECO:0000269|PubMed:20371771}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-9537218, EBI-9537218;
Q01718:MC2R; NbExp=2; IntAct=EBI-9537218, EBI-9537171;
Q8TCY5:MRAP; NbExp=3; IntAct=EBI-9537218, EBI-9538727;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19329486};
Single-pass membrane protein {ECO:0000269|PubMed:19329486}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:19329486};
Single-pass membrane protein {ECO:0000269|PubMed:19329486}.
Note=The formation of antiparallel homo- and heterodimers suggest
that N- and C-terminus can both localize in the cytoplasmic and
extracellular parts, depending on the context.
{ECO:0000269|PubMed:20371771}.
-!- TISSUE SPECIFICITY: Expressed in the adrenal gland and brain. Not
expressed in other tissues. {ECO:0000269|PubMed:19329486}.
-!- POLYMORPHISM: Genetic variations in MRAP2 define the body mass
index quantitative trait locus 18 (BMIQ18) [MIM:615457]. Variance
in body mass index is a susceptibility factor for obesity.
{ECO:0000269|PubMed:23869016}.
-!- DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized
by an increase of body weight beyond the limitation of skeletal
and physical requirements, as the result of excessive accumulation
of body fat. {ECO:0000269|PubMed:23869016}. Note=Disease
susceptibility may be associated with variations affecting the
gene represented in this entry.
-!- SIMILARITY: Belongs to the MRAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK090775; BAC03517.1; -; mRNA.
EMBL; AK292736; BAF85425.1; -; mRNA.
EMBL; AL161621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48646.1; -; Genomic_DNA.
EMBL; BC010003; AAH10003.2; -; mRNA.
EMBL; BC039855; AAH39855.1; -; mRNA.
CCDS; CCDS5001.1; -.
RefSeq; NP_001333470.1; NM_001346541.1.
RefSeq; NP_001333471.1; NM_001346542.1.
RefSeq; NP_001333473.1; NM_001346544.1.
RefSeq; NP_612418.2; NM_138409.3.
RefSeq; XP_016865709.1; XM_017010220.1.
UniGene; Hs.370055; -.
ProteinModelPortal; Q96G30; -.
BioGrid; 125195; 62.
DIP; DIP-48793N; -.
IntAct; Q96G30; 10.
MINT; Q96G30; -.
STRING; 9606.ENSP00000257776; -.
iPTMnet; Q96G30; -.
PhosphoSitePlus; Q96G30; -.
BioMuta; MRAP2; -.
DMDM; 68565259; -.
PaxDb; Q96G30; -.
PeptideAtlas; Q96G30; -.
PRIDE; Q96G30; -.
ProteomicsDB; 76591; -.
DNASU; 112609; -.
Ensembl; ENST00000257776; ENSP00000257776; ENSG00000135324.
GeneID; 112609; -.
KEGG; hsa:112609; -.
UCSC; uc003pkg.5; human.
CTD; 112609; -.
DisGeNET; 112609; -.
EuPathDB; HostDB:ENSG00000135324.5; -.
GeneCards; MRAP2; -.
HGNC; HGNC:21232; MRAP2.
MalaCards; MRAP2; -.
MIM; 601665; phenotype.
MIM; 615410; gene.
MIM; 615457; phenotype.
neXtProt; NX_Q96G30; -.
OpenTargets; ENSG00000135324; -.
PharmGKB; PA162396161; -.
eggNOG; ENOG410IHNK; Eukaryota.
eggNOG; ENOG4111S4H; LUCA.
GeneTree; ENSGT00650000093438; -.
HOGENOM; HOG000290703; -.
HOVERGEN; HBG095178; -.
InParanoid; Q96G30; -.
OMA; TGAPHQE; -.
OrthoDB; 1318662at2759; -.
PhylomeDB; Q96G30; -.
TreeFam; TF338691; -.
SIGNOR; Q96G30; -.
GenomeRNAi; 112609; -.
PRO; PR:Q96G30; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000135324; Expressed in 167 organ(s), highest expression level in thoracic aorta.
Genevisible; Q96G30; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0031780; F:corticotropin hormone receptor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030545; F:receptor regulator activity; IEA:Ensembl.
GO; GO:0070996; F:type 1 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031781; F:type 3 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031782; F:type 4 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031783; F:type 5 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; ISS:UniProtKB.
GO; GO:0007631; P:feeding behavior; ISS:UniProtKB.
GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
InterPro; IPR028111; MRAP.
PANTHER; PTHR28675; PTHR28675; 1.
Pfam; PF15183; MRAP; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Endoplasmic reticulum; Glycoprotein;
Membrane; Obesity; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 205 Melanocortin-2 receptor accessory protein
2.
/FTId=PRO_0000089522.
TRANSMEM 45 65 Helical. {ECO:0000255}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 9 9 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19329486}.
VARIANT 88 88 N -> Y (found in a patient with obesity;
unknown pathological significance;
dbSNP:rs761868293).
{ECO:0000269|PubMed:23869016}.
/FTId=VAR_069986.
VARIANT 115 115 L -> V (found in a patient with obesity;
unknown pathological significance;
dbSNP:rs368589399).
{ECO:0000269|PubMed:23869016}.
/FTId=VAR_069987.
VARIANT 125 125 R -> C (found in a patient with obesity;
unknown pathological significance;
dbSNP:rs148904867).
{ECO:0000269|PubMed:23869016}.
/FTId=VAR_069988.
MUTAGEN 9 9 N->Q: Abolishes N-glycosylation.
{ECO:0000269|PubMed:19329486}.
CONFLICT 62 62 F -> I (in Ref. 1; BAC03517).
{ECO:0000305}.
SEQUENCE 205 AA; 23548 MW; 3B18B493AE75260B CRC64;
MSAQRLISNR TSQQSASNSD YTWEYEYYEI GPVSFEGLKA HKYSIVIGFW VGLAVFVIFM
FFVLTLLTKT GAPHQDNAES SEKRFRMNSF VSDFGRPLEP DKVFSRQGNE ESRSLFHCYI
NEVERLDRAK ACHQTTALDS DVQLQEAIRS SGQPEEELNR LMKFDIPNFV NTDQNYFGED
DLLISEPPIV LETKPLSQTS HKDLD


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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism

Related Genes :
[MC2R ACTHR] Adrenocorticotropic hormone receptor (ACTH receptor) (ACTH-R) (Adrenocorticotropin receptor) (Melanocortin receptor 2) (MC2-R)
[MRAP C21orf61 FALP] Melanocortin-2 receptor accessory protein (B27) (Fat cell-specific low molecular weight protein) (Fat tissue-specific low MW protein)
[Mrap Falp] Melanocortin-2 receptor accessory protein (Fat cell-specific low molecular weight protein) (Fat tissue-specific low MW protein)
[IL1RAPL1 OPHN4] Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (Oligophrenin-4) (Three immunoglobulin domain-containing IL-1 receptor-related 2) (TIGIRR-2) (X-linked interleukin-1 receptor accessory protein-like 1)
[IL1RAP C3orf13 IL1R3] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-33 receptot beta chain)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[SP Acp70A PAPB CG17673] Accessory gland-specific peptide 70A (Paragonial peptide B) (Sex peptide) (SP)
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[3a] Protein 3a (Accessory protein 3a) (Protein U274) (Protein X1)
[POLG2 MTPOLB] DNA polymerase subunit gamma-2, mitochondrial (EC 2.7.7.7) (DNA polymerase gamma accessory 55 kDa subunit) (p55) (Mitochondrial DNA polymerase accessory subunit) (MtPolB) (PolG-beta)
[HCFC1 HCF1 HFC1] Host cell factor 1 (HCF) (HCF-1) (C1 factor) (CFF) (VCAF) (VP16 accessory protein) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6]
[daf-2 Y55D5A.5] Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]
[ATP6AP2 ATP6IP2 CAPER ELDF10 HT028 MSTP009 PSEC0072] Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (ER-localized type I transmembrane adaptor) (Embryonic liver differentiation factor 10) (N14F) (Renin/prorenin receptor) (Vacuolar ATP synthase membrane sector-associated protein M8-9) (ATP6M8-9) (V-ATPase M8.9 subunit)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[Med1 Crsp210 Drip205 Pbp Pparbp Trap220 Trip2] Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2)
[Fcgr2 Fcgr2b Ly-17] Low affinity immunoglobulin gamma Fc region receptor II (Fc gamma receptor IIB) (Fc-gamma RII) (Fc-gamma-RIIB) (FcRII) (IgG Fc receptor II beta) (Lymphocyte antigen 17) (Ly-17) (CD antigen CD32)
[OR1D2 OLFR1] Olfactory receptor 1D2 (Olfactory receptor 17-4) (OR17-4) (Olfactory receptor OR17-6) (Olfactory receptor-like protein HGMP07E)
[Rack1 Gnb2-rs1 Gnb2l1] Receptor of activated protein C kinase 1 (12-3) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) (p205) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[Acp36DE CG7157] Accessory gland protein Acp36DE
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[MC1R MSHR] Melanocyte-stimulating hormone receptor (MSH-R) (Melanocortin receptor 1) (MC1-R)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[BRI1 At4g39400 F23K16.30] Protein BRASSINOSTEROID INSENSITIVE 1 (AtBRI1) (EC 2.7.10.1) (EC 2.7.11.1) (Brassinosteroid LRR receptor kinase)

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