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Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)

 CACO2_HUMAN             Reviewed;         446 AA.
Q13137; B2RBT0; B4DDC4; B4DDT4; B4DP36; B4E0C0; E7ENK0; E7ETP5;
E9PBE5; Q53FQ5; Q53HB5; Q6IBN9; Q9BTF7;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
13-FEB-2019, entry version 155.
RecName: Full=Calcium-binding and coiled-coil domain-containing protein 2;
AltName: Full=Antigen nuclear dot 52 kDa protein;
AltName: Full=Nuclear domain 10 protein NDP52 {ECO:0000305};
Short=Nuclear domain 10 protein 52 {ECO:0000303|PubMed:7540613};
AltName: Full=Nuclear dot protein 52 {ECO:0000303|PubMed:9230084};
Name=CALCOCO2; Synonyms=NDP52 {ECO:0000303|PubMed:7540613};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=7540613; DOI=10.1083/jcb.130.1.1;
Korioth F., Gieffers C., Maul G.G., Frey J.;
"Molecular characterization of NDP52, a novel protein of the nuclear
domain 10, which is redistributed upon virus infection and interferon
treatment.";
J. Cell Biol. 130:1-13(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5),
AND VARIANTS GLU-140; ALA-248 AND ALA-389.
TISSUE=Mammary gland, Neuroblastoma, Teratocarcinoma, and Thymus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-248.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-389.
TISSUE=Brain, and Gastric mucosa;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-389.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-273.
TISSUE=Kidney, and Skin;
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).
[8]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=9230084; DOI=10.1083/jcb.138.2.435;
Sternsdorf T., Jensen K., Zuchner D., Will H.;
"Cellular localization, expression, and structure of the nuclear dot
protein 52.";
J. Cell Biol. 138:435-448(1997).
[9]
INTERACTION WITH GEMIN4, AND SUBCELLULAR LOCATION.
PubMed=12869526; DOI=10.1093/jb/mvg091;
Di Y., Li J., Zhang Y., He X., Lu H., Xu D., Ling J., Huo K., Wan D.,
Li Y.Y., Gu J.;
"HCC-associated protein HCAP1, a variant of GEMIN4, interacts with
zinc-finger proteins.";
J. Biochem. 133:713-718(2003).
[10]
FUNCTION, INTERACTION WITH TAX1BP1 AND MYO6, MUTAGENESIS OF CYS-400
AND CYS-425, AND SUBCELLULAR LOCATION.
PubMed=17635994; DOI=10.1242/jcs.007005;
Morriswood B., Ryzhakov G., Puri C., Arden S.D., Roberts R.,
Dendrou C., Kendrick-Jones J., Buss F.;
"T6BP and NDP52 are myosin VI binding partners with potential roles in
cytokine signalling and cell adhesion.";
J. Cell Sci. 120:2574-2585(2007).
[11]
FUNCTION, AND INTERACTION WITH LGALS8.
PubMed=22246324; DOI=10.1038/nature10744;
Thurston T.L., Wandel M.P., von Muhlinen N., Foeglein A., Randow F.;
"Galectin 8 targets damaged vesicles for autophagy to defend cells
against bacterial invasion.";
Nature 482:414-418(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, 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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
FUNCTION, DOMAIN, MUTAGENESIS OF CYS-425, INTERACTION WITH MAP1LC3A;
MAP1LC3C; MAP1LC3B; GABARAP; GABARAPL1; GABARAPL2 AND LGALS8, AND
SUBCELLULAR LOCATION.
PubMed=25771791; DOI=10.1016/j.chom.2015.02.008;
Verlhac P., Gregoire I.P., Azocar O., Petkova D.S., Baguet J.,
Viret C., Faure M.;
"Autophagy receptor NDP52 regulates pathogen-containing autophagosome
maturation.";
Cell Host Microbe 17:515-525(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 21-141 IN COMPLEX WITH
MAP1LC3C, FUNCTION, DOMAIN, INTERACTION WITH MAP1LC3C, AND MUTAGENESIS
OF VAL-136.
PubMed=23022382; DOI=10.1016/j.molcel.2012.08.024;
von Muhlinen N., Akutsu M., Ravenhill B.J., Foeglein A., Bloor S.,
Rutherford T.J., Freund S.M., Komander D., Randow F.;
"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is
required for antibacterial autophagy.";
Mol. Cell 48:329-342(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 372-385 IN COMPLEX WITH
LGALS8, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-374 AND TYR-380.
PubMed=23511477; DOI=10.1038/ncomms2606;
Kim B.W., Hong S.B., Kim J.H., Kwon do H., Song H.K.;
"Structural basis for recognition of autophagic receptor NDP52 by the
sugar receptor galectin-8.";
Nat. Commun. 4:1613-1613(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 368-381 IN COMPLEX WITH
LGALS8, DOMAIN, MUTAGENESIS OF LEU-374; TYR-376; ASN-378 AND TYR-380,
INTERACTION WITH LGALS8, AND FUNCTION.
PubMed=23386746; DOI=10.1126/scisignal.2003730;
Li S., Wandel M.P., Li F., Liu Z., He C., Wu J., Shi Y., Randow F.;
"Sterical hindrance promotes selectivity of the autophagy cargo
receptor NDP52 for the danger receptor galectin-8 in antibacterial
autophagy.";
Sci. Signal. 6:RA9-RA9(2013).
-!- FUNCTION: Xenophagy-specific receptor required for autophagy-
mediated intracellular bacteria degradation. Acts as an effector
protein of galectin-sensed membrane damage that restricts the
proliferation of infecting pathogens such as Salmonella
typhimurium upon entry into the cytosol by targeting LGALS8-
associated bacteria for autophagy (PubMed:22246324). Initially
orchestrates bacteria targeting to autophagosomes and subsequently
ensures pathogen degradation by regulating pathogen-containing
autophagosome maturation (PubMed:23022382, PubMed:25771791).
Bacteria targeting to autophagosomes relies on its interaction
with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of
pathogen-containing autophagosome maturation requires the
interaction with MAP3LC3C (PubMed:23022382, PubMed:25771791). May
play a role in ruffle formation and actin cytoskeleton
organization and seems to negatively regulate constitutive
secretion (PubMed:17635994). {ECO:0000269|PubMed:17635994,
ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:23022382,
ECO:0000269|PubMed:23386746, ECO:0000269|PubMed:25771791}.
-!- SUBUNIT: Dimer (PubMed:23511477). Part of a complex consisting of
CALCOCO2, TAX1BP1 and MYO6 (PubMed:17635994). Interacts with
GEMIN4 (PubMed:12869526). Interacts with ATG8 family members
MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2
(PubMed:25771791). Interacts with ATG8 family member MAP1LC3C
(PubMed:23022382). Interacts with LGALS8 (PubMed:22246324,
PubMed:25771791, PubMed:23511477, PubMed:23386746).
{ECO:0000269|PubMed:12869526, ECO:0000269|PubMed:17635994,
ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:23022382,
ECO:0000269|PubMed:23386746, ECO:0000269|PubMed:23511477,
ECO:0000269|PubMed:25771791}.
-!- INTERACTION:
B2R9Y1:-; NbExp=3; IntAct=EBI-739580, EBI-10175746;
Q8WU02:-; NbExp=3; IntAct=EBI-739580, EBI-747182;
Q9WMX2:- (xeno); NbExp=3; IntAct=EBI-739580, EBI-6863741;
Q08117:AES; NbExp=3; IntAct=EBI-739580, EBI-717810;
Q02040-3:AKAP17A; NbExp=3; IntAct=EBI-739580, EBI-10222656;
Q9Y4X0:AMMECR1; NbExp=3; IntAct=EBI-739580, EBI-8583355;
Q6P4J0:ARD1A; NbExp=3; IntAct=EBI-739580, EBI-10252815;
Q8N4T4:ARHGEF39; NbExp=3; IntAct=EBI-739580, EBI-745468;
Q12774:ARHGEF5; NbExp=3; IntAct=EBI-739580, EBI-602199;
A0A0S2Z4M1:AXIN1; NbExp=3; IntAct=EBI-739580, EBI-16429430;
O15169:AXIN1; NbExp=3; IntAct=EBI-739580, EBI-710484;
Q8TBE0:BAHD1; NbExp=3; IntAct=EBI-739580, EBI-742750;
A8KA13:BCL6B; NbExp=3; IntAct=EBI-739580, EBI-10174813;
Q9BXY8:BEX2; NbExp=3; IntAct=EBI-739580, EBI-745073;
Q9HC52:CBX8; NbExp=5; IntAct=EBI-739580, EBI-712912;
P51946:CCNH; NbExp=3; IntAct=EBI-739580, EBI-741406;
Q8IYX8:CEP57L1; NbExp=3; IntAct=EBI-739580, EBI-1104570;
Q9NX63:CHCHD3; NbExp=3; IntAct=EBI-739580, EBI-743375;
Q2TBE0:CWF19L2; NbExp=3; IntAct=EBI-739580, EBI-5453285;
Q15038:DAZAP2; NbExp=4; IntAct=EBI-739580, EBI-724310;
Q9UJW0:DCTN4; NbExp=3; IntAct=EBI-739580, EBI-2134033;
O43602:DCX; NbExp=3; IntAct=EBI-739580, EBI-8646694;
Q96D03:DDIT4L; NbExp=3; IntAct=EBI-739580, EBI-742054;
P26196:DDX6; NbExp=5; IntAct=EBI-739580, EBI-351257;
Q92608:DOCK2; NbExp=3; IntAct=EBI-739580, EBI-448771;
Q9UNI6:DUSP12; NbExp=4; IntAct=EBI-739580, EBI-715161;
Q9BV47:DUSP26; NbExp=3; IntAct=EBI-739580, EBI-2924519;
O43324:EEF1E1; NbExp=3; IntAct=EBI-739580, EBI-1048486;
Q9H0I2:ENKD1; NbExp=3; IntAct=EBI-739580, EBI-744099;
Q9NQT4:EXOSC5; NbExp=3; IntAct=EBI-739580, EBI-371876;
Q3B820:FAM161A; NbExp=5; IntAct=EBI-739580, EBI-719941;
Q92567:FAM168A; NbExp=3; IntAct=EBI-739580, EBI-7957930;
Q86YD7:FAM90A1; NbExp=6; IntAct=EBI-739580, EBI-6658203;
O95363:FARS2; NbExp=5; IntAct=EBI-739580, EBI-2513774;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-739580, EBI-10244131;
Q96D16:FBXL18; NbExp=4; IntAct=EBI-739580, EBI-744419;
Q9UIM3:FKBPL; NbExp=3; IntAct=EBI-739580, EBI-719882;
Q9BVV2:FNDC11; NbExp=4; IntAct=EBI-739580, EBI-744935;
Q9H0R8:GABARAPL1; NbExp=6; IntAct=EBI-739580, EBI-746969;
P60520:GABARAPL2; NbExp=6; IntAct=EBI-739580, EBI-720116;
Q8WXI9:GATAD2B; NbExp=3; IntAct=EBI-739580, EBI-923440;
Q8IVS8:GLYCTK; NbExp=3; IntAct=EBI-739580, EBI-748515;
Q8WUI4-5:HDAC7; NbExp=3; IntAct=EBI-739580, EBI-10276431;
P17482:HOXB9; NbExp=3; IntAct=EBI-739580, EBI-745290;
Q7Z3B3:KANSL1; NbExp=4; IntAct=EBI-739580, EBI-740244;
Q9P2K6:KLHL42; NbExp=3; IntAct=EBI-739580, EBI-739890;
Q96BZ8:LENG1; NbExp=3; IntAct=EBI-739580, EBI-726510;
O00214:LGALS8; NbExp=4; IntAct=EBI-739580, EBI-740058;
Q7Z4I7-5:LIMS2; NbExp=3; IntAct=EBI-739580, EBI-10257651;
Q99732:LITAF; NbExp=7; IntAct=EBI-739580, EBI-725647;
Q9BU23:LMF2; NbExp=3; IntAct=EBI-739580, EBI-10298556;
P25791:LMO2; NbExp=3; IntAct=EBI-739580, EBI-739696;
P61968:LMO4; NbExp=3; IntAct=EBI-739580, EBI-2798728;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-739580, EBI-2341787;
Q9Y4Z0:LSM4; NbExp=6; IntAct=EBI-739580, EBI-372521;
Q96A72:MAGOHB; NbExp=5; IntAct=EBI-739580, EBI-746778;
Q7Z434:MAVS; NbExp=3; IntAct=EBI-739580, EBI-995373;
Q9H7H0:METTL17; NbExp=6; IntAct=EBI-739580, EBI-749353;
Q9H7H0-2:METTL17; NbExp=3; IntAct=EBI-739580, EBI-11098807;
Q9UJV3-2:MID2; NbExp=3; IntAct=EBI-739580, EBI-10172526;
P00540:MOS; NbExp=5; IntAct=EBI-739580, EBI-1757866;
Q9NVV4:MTPAP; NbExp=2; IntAct=EBI-739580, EBI-2556166;
P50539:MXI1; NbExp=3; IntAct=EBI-739580, EBI-752241;
P50539-3:MXI1; NbExp=5; IntAct=EBI-739580, EBI-10211940;
P41227:NAA10; NbExp=5; IntAct=EBI-739580, EBI-747693;
Q9UMS0:NFU1; NbExp=3; IntAct=EBI-739580, EBI-725252;
Q9UBV8:PEF1; NbExp=4; IntAct=EBI-739580, EBI-724639;
Q86TG7:PEG10; NbExp=3; IntAct=EBI-739580, EBI-2858265;
Q99471:PFDN5; NbExp=4; IntAct=EBI-739580, EBI-357275;
O43189:PHF1; NbExp=3; IntAct=EBI-739580, EBI-530034;
Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-739580, EBI-2557469;
Q8WWY3:PRPF31; NbExp=6; IntAct=EBI-739580, EBI-1567797;
P25786:PSMA1; NbExp=3; IntAct=EBI-739580, EBI-359352;
Q14997:PSME4; NbExp=3; IntAct=EBI-739580, EBI-1236916;
Q96T37:RBM15; NbExp=3; IntAct=EBI-739580, EBI-2514922;
Q13671:RIN1; NbExp=4; IntAct=EBI-739580, EBI-366017;
P32969:RPL9P9; NbExp=3; IntAct=EBI-739580, EBI-358122;
P62979:RPS27A; NbExp=3; IntAct=EBI-739580, EBI-357375;
Q14D33:RTP5; NbExp=5; IntAct=EBI-739580, EBI-10217913;
P28702-3:RXRB; NbExp=3; IntAct=EBI-739580, EBI-16429492;
O00560:SDCBP; NbExp=3; IntAct=EBI-739580, EBI-727004;
Q05CH4:SLC15A3; NbExp=3; IntAct=EBI-739580, EBI-10223741;
P49901:SMCP; NbExp=3; IntAct=EBI-739580, EBI-750494;
P14678-2:SNRPB; NbExp=3; IntAct=EBI-739580, EBI-372475;
Q86W54:SPATA24; NbExp=3; IntAct=EBI-739580, EBI-3916986;
P30626:SRI; NbExp=5; IntAct=EBI-739580, EBI-750459;
O75716:STK16; NbExp=3; IntAct=EBI-739580, EBI-749295;
Q9NU19:TBC1D22B; NbExp=3; IntAct=EBI-739580, EBI-8787464;
Q9UHD2:TBK1; NbExp=5; IntAct=EBI-739580, EBI-356402;
Q969Z0:TBRG4; NbExp=3; IntAct=EBI-739580, EBI-702328;
P56279:TCL1A; NbExp=7; IntAct=EBI-739580, EBI-749995;
Q9BXF9:TEKT3; NbExp=3; IntAct=EBI-739580, EBI-8644516;
Q6PIY7:TENT2; NbExp=3; IntAct=EBI-739580, EBI-2802204;
Q96S44:TP53RK; NbExp=4; IntAct=EBI-739580, EBI-739588;
Q8NBM4:UBAC2; NbExp=3; IntAct=EBI-739580, EBI-724045;
Q5U5U6:UBB; NbExp=3; IntAct=EBI-739580, EBI-1642104;
Q96C32:UBC; NbExp=3; IntAct=EBI-739580, EBI-745483;
P26640:VARS; NbExp=3; IntAct=EBI-739580, EBI-355765;
Q9Y3M9:ZNF337; NbExp=3; IntAct=EBI-739580, EBI-714987;
Q9H9D4:ZNF408; NbExp=3; IntAct=EBI-739580, EBI-347633;
Q8TBZ8:ZNF564; NbExp=3; IntAct=EBI-739580, EBI-10273713;
Q9P0T4:ZNF581; NbExp=3; IntAct=EBI-739580, EBI-745520;
A0A0S2Z5X4:ZNF688; NbExp=3; IntAct=EBI-739580, EBI-16429014;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:12869526, ECO:0000269|PubMed:17635994,
ECO:0000269|PubMed:9230084}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:17635994}. Cytoplasmic vesicle, autophagosome
membrane {ECO:0000269|PubMed:25771791}; Peripheral membrane
protein {ECO:0000305}. Note=According to PubMed:7540613, localizes
to nuclear dots. According to PubMed:9230084 and PubMed:12869526,
it is not a nuclear dot-associated protein but localizes
predominantly in the cytoplasm with a coarse-grained distribution
preferentially close to the nucleus. {ECO:0000269|PubMed:12869526,
ECO:0000269|PubMed:7540613, ECO:0000269|PubMed:9230084}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q13137-1; Sequence=Displayed;
Name=2;
IsoId=Q13137-2; Sequence=VSP_044728;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q13137-3; Sequence=VSP_046766;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q13137-4; Sequence=VSP_046767;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q13137-5; Sequence=VSP_047414;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested with highest
expression in skeletal muscle and lowest in brain.
{ECO:0000269|PubMed:7540613}.
-!- INDUCTION: Treatment with IFNB1/IFN-beta and IFNG/IFN-gamma show
an increase in number and size of CALCOCO2-specific dots and
partial redistribution to the cytoplasm (PubMed:7540613).
IFNG/IFN-gamma increases gene expression only slightly and IFNB
does not increase expression (PubMed:9230084).
{ECO:0000269|PubMed:7540613, ECO:0000269|PubMed:9230084}.
-!- DOMAIN: The MYO6-binding domain is required for autophagy-mediated
degradation of infecting bacteria such as Salmonella typhimurium,
but not for bacteria targeting to autophagosomes.
{ECO:0000269|PubMed:25771791}.
-!- DOMAIN: The CLIR (LC3C-interacting region) motif is required for
interaction with MAP1LC3C, but dispensable for CALCOCO2-mediated
autophagosome maturation. {ECO:0000269|PubMed:23022382,
ECO:0000269|PubMed:25771791}.
-!- DOMAIN: The LIR-like motif is required for interaction with
MAP1LC3A, MAP1LC3B and GABARAPL2, as well as for CALCOCO2-mediated
autophagosome maturation. {ECO:0000269|PubMed:25771791}.
-!- DOMAIN: The LGALS8-binding domain is essential for the recruitment
to cytosol-exposed infecting bacteria.
{ECO:0000269|PubMed:23386746}.
-!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U22897; AAA75297.1; -; mRNA.
EMBL; AK293137; BAG56685.1; -; mRNA.
EMBL; AK293329; BAG56845.1; -; mRNA.
EMBL; AK298177; BAG60448.1; -; mRNA.
EMBL; AK303313; BAG64382.1; -; mRNA.
EMBL; AK314796; BAG37327.1; -; mRNA.
EMBL; CR456763; CAG33044.1; -; mRNA.
EMBL; AK222666; BAD96386.1; -; mRNA.
EMBL; AK223227; BAD96947.1; -; mRNA.
EMBL; AC068531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94707.1; -; Genomic_DNA.
EMBL; BC004130; AAH04130.1; -; mRNA.
EMBL; BC015893; AAH15893.1; -; mRNA.
CCDS; CCDS11538.1; -. [Q13137-1]
CCDS; CCDS58558.1; -. [Q13137-3]
CCDS; CCDS58559.1; -. [Q13137-4]
CCDS; CCDS58560.1; -. [Q13137-2]
CCDS; CCDS58561.1; -. [Q13137-5]
PIR; A56733; A56733.
RefSeq; NP_001248319.1; NM_001261390.1. [Q13137-4]
RefSeq; NP_001248320.1; NM_001261391.1. [Q13137-3]
RefSeq; NP_001248322.1; NM_001261393.1. [Q13137-2]
RefSeq; NP_001248324.1; NM_001261395.1. [Q13137-5]
RefSeq; NP_005822.1; NM_005831.4. [Q13137-1]
UniGene; Hs.514920; -.
PDB; 2MXP; NMR; -; A=414-446.
PDB; 3VVV; X-ray; 1.35 A; A=21-141.
PDB; 3VVW; X-ray; 2.50 A; A=21-141.
PDB; 4GXL; X-ray; 2.02 A; B=368-381.
PDB; 4HAN; X-ray; 2.55 A; C/D=372-385.
PDB; 4XKL; X-ray; 2.10 A; B/D=414-446.
PDB; 5AAQ; NMR; -; A=388-446.
PDB; 5Z7A; X-ray; 2.38 A; A/B=1-126.
PDB; 5Z7L; X-ray; 2.02 A; A/B=10-126.
PDBsum; 2MXP; -.
PDBsum; 3VVV; -.
PDBsum; 3VVW; -.
PDBsum; 4GXL; -.
PDBsum; 4HAN; -.
PDBsum; 4XKL; -.
PDBsum; 5AAQ; -.
PDBsum; 5Z7A; -.
PDBsum; 5Z7L; -.
ProteinModelPortal; Q13137; -.
SMR; Q13137; -.
BioGrid; 115535; 223.
DIP; DIP-57534N; -.
IntAct; Q13137; 189.
MINT; Q13137; -.
STRING; 9606.ENSP00000258947; -.
iPTMnet; Q13137; -.
PhosphoSitePlus; Q13137; -.
BioMuta; CALCOCO2; -.
DMDM; 74735623; -.
EPD; Q13137; -.
jPOST; Q13137; -.
MaxQB; Q13137; -.
PaxDb; Q13137; -.
PeptideAtlas; Q13137; -.
PRIDE; Q13137; -.
ProteomicsDB; 59186; -.
DNASU; 10241; -.
Ensembl; ENST00000258947; ENSP00000258947; ENSG00000136436. [Q13137-1]
Ensembl; ENST00000416445; ENSP00000406974; ENSG00000136436. [Q13137-2]
Ensembl; ENST00000448105; ENSP00000398523; ENSG00000136436. [Q13137-4]
Ensembl; ENST00000508679; ENSP00000423437; ENSG00000136436. [Q13137-5]
Ensembl; ENST00000509507; ENSP00000424352; ENSG00000136436. [Q13137-3]
GeneID; 10241; -.
KEGG; hsa:10241; -.
UCSC; uc002iof.4; human. [Q13137-1]
CTD; 10241; -.
DisGeNET; 10241; -.
EuPathDB; HostDB:ENSG00000136436.14; -.
GeneCards; CALCOCO2; -.
H-InvDB; HIX0013950; -.
HGNC; HGNC:29912; CALCOCO2.
HPA; HPA022989; -.
HPA; HPA023019; -.
HPA; HPA023195; -.
MIM; 604587; gene.
neXtProt; NX_Q13137; -.
OpenTargets; ENSG00000136436; -.
PharmGKB; PA143485407; -.
eggNOG; ENOG410IKI3; Eukaryota.
eggNOG; ENOG4112B0R; LUCA.
GeneTree; ENSGT00530000063216; -.
HOGENOM; HOG000050230; -.
HOVERGEN; HBG104102; -.
InParanoid; Q13137; -.
KO; K21348; -.
OMA; TCYYTLT; -.
OrthoDB; 179838at2759; -.
PhylomeDB; Q13137; -.
TreeFam; TF329501; -.
ChiTaRS; CALCOCO2; human.
GeneWiki; CALCOCO2; -.
GenomeRNAi; 10241; -.
PRO; PR:Q13137; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000136436; Expressed in 234 organ(s), highest expression level in testis.
ExpressionAtlas; Q13137; baseline and differential.
Genevisible; Q13137; HS.
GO; GO:0005776; C:autophagosome; IDA:GO_Central.
GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:GO_Central.
GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL.
GO; GO:0016032; P:viral process; TAS:ProtInc.
GO; GO:0098792; P:xenophagy; IMP:GO_Central.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autophagy; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Membrane; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 446 Calcium-binding and coiled-coil domain-
containing protein 2.
/FTId=PRO_0000312337.
REGION 371 381 Interaction with LGALS8.
{ECO:0000269|PubMed:23386746,
ECO:0000269|PubMed:23511477}.
REGION 395 446 Interaction with MYO6.
{ECO:0000269|PubMed:17635994}.
COILED 137 349 {ECO:0000255}.
MOTIF 133 136 CLIR. {ECO:0000305|PubMed:23022382,
ECO:0000305|PubMed:25771791}.
MOTIF 203 206 LIR-like. {ECO:0000305|PubMed:25771791}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 72 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047414.
VAR_SEQ 60 60 R -> RCSLNQTIQLLITPDTGSIWHQ (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_046766.
VAR_SEQ 60 60 R -> RAFKCFQDKLEQELLKWRSQGQKLQ (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046767.
VAR_SEQ 139 180 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044728.
VARIANT 140 140 G -> E (in dbSNP:rs550510).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_037489.
VARIANT 227 227 G -> R (in dbSNP:rs2303016).
/FTId=VAR_037490.
VARIANT 248 248 V -> A (in dbSNP:rs2303015).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.3}.
/FTId=VAR_037491.
VARIANT 273 273 T -> A (in dbSNP:rs17849804).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037492.
VARIANT 389 389 P -> A (in dbSNP:rs10278).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.4, ECO:0000269|Ref.6}.
/FTId=VAR_037493.
MUTAGEN 136 136 V->S: Abrogates the interaction with
MAP1LC3C. {ECO:0000269|PubMed:23022382}.
MUTAGEN 203 206 DYWE->AAAA: Abrogates interaction with
MAPLC3A, MAPLC3B and GABARAPL2.
{ECO:0000269|PubMed:25771791}.
MUTAGEN 374 374 L->A: Severely reduces affinity for
LGALS8. {ECO:0000269|PubMed:23386746,
ECO:0000269|PubMed:23511477}.
MUTAGEN 376 376 Y->A: Severely reduces affinity for
LGALS8. {ECO:0000269|PubMed:23386746}.
MUTAGEN 378 378 N->A: Prevents interaction with LGALS8.
{ECO:0000269|PubMed:23386746}.
MUTAGEN 380 380 Y->A,F: Severely reduced affinity for
LGALS8. {ECO:0000269|PubMed:23386746,
ECO:0000269|PubMed:23511477}.
MUTAGEN 400 400 C->A: Does not affect interaction with
MYO6. {ECO:0000269|PubMed:17635994}.
MUTAGEN 425 425 C->A: Fails interact with MYO6 and to
promote maturation of autophagosomes.
{ECO:0000269|PubMed:17635994,
ECO:0000269|PubMed:25771791}.
CONFLICT 102 102 D -> Y (in Ref. 2; BAG64382).
{ECO:0000305}.
CONFLICT 313 313 R -> G (in Ref. 2; BAG56685).
{ECO:0000305}.
STRAND 22 27 {ECO:0000244|PDB:3VVV}.
STRAND 30 32 {ECO:0000244|PDB:3VVV}.
STRAND 38 44 {ECO:0000244|PDB:3VVV}.
STRAND 55 60 {ECO:0000244|PDB:3VVV}.
HELIX 66 68 {ECO:0000244|PDB:3VVV}.
STRAND 70 74 {ECO:0000244|PDB:3VVV}.
STRAND 89 93 {ECO:0000244|PDB:3VVV}.
HELIX 95 97 {ECO:0000244|PDB:3VVV}.
STRAND 105 110 {ECO:0000244|PDB:3VVV}.
STRAND 116 119 {ECO:0000244|PDB:3VVV}.
STRAND 123 126 {ECO:0000244|PDB:3VVV}.
STRAND 133 135 {ECO:0000244|PDB:3VVW}.
TURN 401 403 {ECO:0000244|PDB:5AAQ}.
STRAND 404 406 {ECO:0000244|PDB:5AAQ}.
HELIX 410 413 {ECO:0000244|PDB:5AAQ}.
STRAND 419 421 {ECO:0000244|PDB:4XKL}.
TURN 423 425 {ECO:0000244|PDB:4XKL}.
STRAND 428 430 {ECO:0000244|PDB:4XKL}.
HELIX 431 433 {ECO:0000244|PDB:2MXP}.
HELIX 434 443 {ECO:0000244|PDB:4XKL}.
SEQUENCE 446 AA; 52254 MW; 609B121DA1A9DCB8 CRC64;
MEETIKDPPT SAVLLDHCHF SQVIFNSVEK FYIPGGDVTC HYTFTQHFIP RRKDWIGIFR
VGWKTTREYY TFMWVTLPID LNNKSAKQQE VQFKAYYLPK DDEYYQFCYV DEDGVVRGAS
IPFQFRPENE EDILVVTTQG EVEEIEQHNK ELCKENQELK DSCISLQKQN SDMQAELQKK
QEELETLQSI NKKLELKVKE QKDYWETELL QLKEQNQKMS SENEKMGIRV DQLQAQLSTQ
EKEMEKLVQG DQDKTEQLEQ LKKENDHLFL SLTEQRKDQK KLEQTVEQMK QNETTAMKKQ
QELMDENFDL SKRLSENEII CNALQRQKER LEGENDLLKR ENSRLLSYMG LDFNSLPYQV
PTSDEGGARQ NPGLAYGNPY SGIQESSSPS PLSIKKCPIC KADDICDHTL EQQQMQPLCF
NCPICDKIFP ATEKQIFEDH VFCHSL


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1502: Mitochondrial biogenesis
WP1689: Porphyrin and chlorophyll metabolism
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
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
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
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

Related Genes :
[CALCOCO2 NDP52] Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)
[CALCOCO2 NDP52] Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)
[Calcoco2 Ndp52 Ndp52l1] Calcium-binding and coiled-coil domain-containing protein 2 (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52)
[CALCOCO2 NDP52] Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)
[CALCOCO2 NDP52 QtsA-10956] Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)
[NFKB2 LYT10] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[SP100] Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa)
[Nfkb2] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[SYNE1 C6orf98 KIAA0796 KIAA1262 KIAA1756 MYNE1] Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)
[RUVBL1 INO80H NMP238 TIP49 TIP49A] RuvB-like 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein) (49 kDa TBP-interacting protein) (54 kDa erythrocyte cytosolic protein) (ECP-54) (INO80 complex subunit H) (Nuclear matrix protein 238) (NMP 238) (Pontin 52) (TIP49a) (TIP60-associated protein 54-alpha) (TAP54-alpha)
[npp-10 ZK328.5] Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (CeNup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (CeNup96)]
[NUMA1 NMP22 NUMA] Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)
[SYNE2 KIAA1011 NUA] Nesprin-2 (KASH domain-containing protein 2) (KASH2) (Nuclear envelope spectrin repeat protein 2) (Nucleus and actin connecting element protein) (Protein NUANCE) (Synaptic nuclear envelope protein 2) (Syne-2)
[Syne1] Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)
[Syne2] Nesprin-2 (KASH domain-containing protein 2) (KASH2) (Nuclear envelope spectrin repeat protein 2) (Nucleus and actin connecting element protein) (Protein NUANCE) (Synaptic nuclear envelope protein 2) (Syne-2)
[U2AF1L4 U2AF1-RS3 U2AF1L3] Splicing factor U2AF 26 kDa subunit (U2 auxiliary factor 26) (U2 small nuclear RNA auxiliary factor 1-like protein 4) (U2AF1-like 4) (U2(RNU2) small nuclear RNA auxiliary factor 1-like protein 3) (U2 small nuclear RNA auxiliary factor 1-like protein 3) (U2AF1-like protein 3)
[PABPN1 PAB2 PABP2] Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (Nuclear poly(A)-binding protein 1) (Poly(A)-binding protein II) (PABII) (Polyadenylate-binding nuclear protein 1)
[PQBP1 NPW38 JM26] Polyglutamine-binding protein 1 (PQBP-1) (38 kDa nuclear protein containing a WW domain) (Npw38) (Polyglutamine tract-binding protein 1)
[SRRM2 KIAA0324 SRL300 SRM300 HSPC075] Serine/arginine repetitive matrix protein 2 (300 kDa nuclear matrix antigen) (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803)
[TRIM21 RNF81 RO52 SSA1] E3 ubiquitin-protein ligase TRIM21 (EC 2.3.2.27) (52 kDa Ro protein) (52 kDa ribonucleoprotein autoantigen Ro/SS-A) (RING finger protein 81) (RING-type E3 ubiquitin transferase TRIM21) (Ro(SS-A)) (Sjoegren syndrome type A antigen) (SS-A) (Tripartite motif-containing protein 21)
[NUP98 ADAR2] Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)]
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[MORC3 KIAA0136 NXP2 ZCWCC3] MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)
[RIOX2 MDIG MINA MINA53 NO52] Ribosomal oxygenase 2 (60S ribosomal protein L27a histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.-) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Mineral dust-induced gene protein) (Nucleolar protein 52) (Ribosomal oxygenase MINA) (ROX)
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
[] Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]

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