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Ganglioside GM2 activator (Cerebroside sulfate activator protein) (GM2-AP) (Sphingolipid activator protein 3) (SAP-3) [Cleaved into: Ganglioside GM2 activator isoform short]
SAP3_HUMAN Reviewed; 193 AA.
P17900; B2R699; D3DQH6; Q14426; Q14428; Q6LBL5;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 4.
13-FEB-2019, entry version 187.
RecName: Full=Ganglioside GM2 activator;
AltName: Full=Cerebroside sulfate activator protein;
AltName: Full=GM2-AP;
AltName: Full=Sphingolipid activator protein 3;
Short=SAP-3;
Contains:
RecName: Full=Ganglioside GM2 activator isoform short;
Flags: Precursor;
Name=GM2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-59 AND VAL-69.
PubMed=2059210; DOI=10.1016/0006-291X(91)90671-S;
Xie B., McInnes B., Neote K., Lamhonwah A.-M., Mahuran D.;
"Isolation and expression of a full-length cDNA encoding the human G-
M2 activator protein.";
Biochem. Biophys. Res. Commun. 177:1217-1223(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
PubMed=1915857; DOI=10.1016/0014-5793(91)81084-L;
Klima H., Tanaka A., Schnabel D., Nakano T., Schroeder M., Suzuki K.,
Sandhoff K.;
"Characterization of full-length cDNAs and the gene coding for the
human GM2 activator protein.";
FEBS Lett. 289:260-264(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1554364; DOI=10.1042/bj2820807;
Nagarajan S., Chen H.C., Li S.C., Li Y.T., Lockyer J.;
"Evidence for two cDNAs encoding human GM2-activator protein.";
Biochem. J. 282:807-813(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
PubMed=1427911; DOI=10.1016/S0888-7543(05)80190-9;
Xie B., Kennedy J.L., McInnes B., Auger D., Mahuran D.J.;
"Identification of a processed pseudogene related to the functional
gene encoding the GM2 activator protein: localization of the
pseudogene to human chromosome 3 and the functional gene to human
chromosome 5.";
Genomics 14:796-798(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-19 AND
VAL-69.
TISSUE=Substantia nigra;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-19; VAL-59 AND
VAL-69.
PubMed=10364519; DOI=10.1086/302463;
Chen B., Rigat B., Curry C., Mahuran D.J.;
"Structure of the GM2A gene: identification of an exon 2 nonsense
mutation and a naturally occurring transcript with an in-frame
deletion of exon 2.";
Am. J. Hum. Genet. 65:77-87(1999).
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-59 AND
VAL-69.
TISSUE=Uterus;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-193, AND VARIANTS THR-19; VAL-59 AND
VAL-69.
PubMed=2753159; DOI=10.1016/0014-5793(89)81454-1;
Schroeder M., Klima H., Nakano T., Kwon H., Quintern L.E.,
Gaertner S., Suzuki K., Sandhoff K.;
"Isolation of a cDNA encoding the human GM2 activator protein.";
FEBS Lett. 251:197-200(1989).
[11]
PROTEIN SEQUENCE OF 32-193.
TISSUE=Kidney;
PubMed=2209618; DOI=10.1111/j.1432-1033.1990.tb19280.x;
Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.;
"The complete amino-acid sequences of human ganglioside GM2 activator
protein and cerebroside sulfate activator protein.";
Eur. J. Biochem. 192:709-714(1990).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=11090283; DOI=10.1006/jmbi.2000.4225;
Wright C.S., Li S.-C., Rastinejad F.;
"Crystal structure of human GM2-activator protein with a novel beta-
cup topology.";
J. Mol. Biol. 304:411-422(2000).
[14]
VARIANT GM2GAB ARG-138.
PubMed=1915858; DOI=10.1016/0014-5793(91)81211-P;
Schroeder M., Schnabel D., Suzuki K., Sandhoff K.;
"A mutation in the gene of a glycolipid-binding protein (GM2
activator) that causes GM2-gangliosidosis variant AB.";
FEBS Lett. 290:1-3(1991).
[15]
VARIANT GM2GAB PRO-169.
PubMed=8244332; DOI=10.1007/BF00216446;
Schroder M., Schnabel D., Hurwitz R., Young E., Suzuki K.,
Sandhoff K.;
"Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation
and expression in BHK cells.";
Hum. Genet. 92:437-440(1993).
[16]
VARIANT GM2GAB LYS-88 DEL.
PubMed=8900233;
Schepers U., Glombitza G., Lemm T., Hoffmann A., Chabas A., Ozand P.,
Sandhoff K.;
"Molecular analysis of a GM2-activator deficiency in two patients with
GM2-gangliosidosis AB variant.";
Am. J. Hum. Genet. 59:1048-1056(1996).
-!- FUNCTION: The large binding pocket can accommodate several single
chain phospholipids and fatty acids, GM2A also exhibits some
calcium-independent phospholipase activity (By similarity). Binds
gangliosides and stimulates ganglioside GM2 degradation. It
stimulates only the breakdown of ganglioside GM2 and glycolipid
GA2 by beta-hexosaminidase A. It extracts single GM2 molecules
from membranes and presents them in soluble form to beta-
hexosaminidase A for cleavage of N-acetyl-D-galactosamine and
conversion to GM3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- PTM: The serines in positions 32 and 33 are absent in 80% of the
sequenced protein.
-!- DISEASE: GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal
recessive lysosomal storage disease marked by the accumulation of
GM2 gangliosides in the neuronal cells. It is characterized by GM2
gangliosides accumulation in the presence of both normal
hexosaminidase A and B. {ECO:0000269|PubMed:1915858,
ECO:0000269|PubMed:8244332, ECO:0000269|PubMed:8900233}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SEQUENCE CAUTION:
Sequence=CAA43408.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA43994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M76477; AAA35907.1; -; mRNA.
EMBL; X62078; CAA43993.1; -; mRNA.
EMBL; X62078; CAA43994.1; ALT_INIT; mRNA.
EMBL; X61095; CAA43408.1; ALT_INIT; mRNA.
EMBL; L01439; AAA52767.1; -; mRNA.
EMBL; AF124719; AAD25741.1; -; Genomic_DNA.
EMBL; AF124717; AAD25741.1; JOINED; Genomic_DNA.
EMBL; AF124718; AAD25741.1; JOINED; Genomic_DNA.
EMBL; AK312494; BAG35396.1; -; mRNA.
EMBL; AC008385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61680.1; -; Genomic_DNA.
EMBL; CH471062; EAW61681.1; -; Genomic_DNA.
EMBL; BC009273; AAH09273.1; -; mRNA.
EMBL; X16087; CAA34215.1; -; mRNA.
CCDS; CCDS4313.1; -.
PIR; I54178; I54178.
PIR; S13195; S13195.
PIR; S22411; S22411.
RefSeq; NP_000396.2; NM_000405.4.
UniGene; Hs.483873; -.
PDB; 1G13; X-ray; 2.00 A; A/B/C=32-193.
PDB; 1PU5; X-ray; 1.90 A; A/B/C=32-193.
PDB; 1PUB; X-ray; 2.51 A; A=32-193.
PDB; 1TJJ; X-ray; 2.00 A; A/B/C=32-193.
PDB; 2AF9; X-ray; 2.00 A; A=32-193.
PDB; 2AG2; X-ray; 2.00 A; A/B/C=32-193.
PDB; 2AG4; X-ray; 1.80 A; A/B=32-193.
PDB; 2AG9; X-ray; 2.20 A; A/B=32-193.
PDBsum; 1G13; -.
PDBsum; 1PU5; -.
PDBsum; 1PUB; -.
PDBsum; 1TJJ; -.
PDBsum; 2AF9; -.
PDBsum; 2AG2; -.
PDBsum; 2AG4; -.
PDBsum; 2AG9; -.
ProteinModelPortal; P17900; -.
SMR; P17900; -.
BioGrid; 109022; 27.
IntAct; P17900; 3.
STRING; 9606.ENSP00000349687; -.
DrugBank; DB04660; Choline alfoscerate.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB03633; Lpc-Ether.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB02261; Platelet Activating Factor.
SwissLipids; SLP:000000476; -.
BioMuta; GM2A; -.
DMDM; 160331912; -.
EPD; P17900; -.
jPOST; P17900; -.
MaxQB; P17900; -.
PaxDb; P17900; -.
PeptideAtlas; P17900; -.
PRIDE; P17900; -.
ProteomicsDB; 53524; -.
DNASU; 2760; -.
Ensembl; ENST00000357164; ENSP00000349687; ENSG00000196743.
GeneID; 2760; -.
KEGG; hsa:2760; -.
UCSC; uc003ltr.5; human.
CTD; 2760; -.
DisGeNET; 2760; -.
EuPathDB; HostDB:ENSG00000196743.8; -.
GeneCards; GM2A; -.
H-InvDB; HIX0005327; -.
HGNC; HGNC:4367; GM2A.
HPA; HPA008063; -.
MalaCards; GM2A; -.
MIM; 272750; phenotype.
MIM; 613109; gene.
neXtProt; NX_P17900; -.
OpenTargets; ENSG00000196743; -.
Orphanet; 309246; GM2 gangliosidosis, AB variant.
PharmGKB; PA28752; -.
eggNOG; ENOG410IX9N; Eukaryota.
eggNOG; ENOG4111JSM; LUCA.
GeneTree; ENSGT00390000003288; -.
HOGENOM; HOG000031350; -.
HOVERGEN; HBG000260; -.
InParanoid; P17900; -.
KO; K12383; -.
OMA; WLSTGNY; -.
OrthoDB; 1548356at2759; -.
PhylomeDB; P17900; -.
TreeFam; TF353575; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; GM2A; human.
EvolutionaryTrace; P17900; -.
GeneWiki; GM2A; -.
GenomeRNAi; 2760; -.
PRO; PR:P17900; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000196743; Expressed in 239 organ(s), highest expression level in visceral pleura.
ExpressionAtlas; P17900; baseline and differential.
Genevisible; P17900; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0032428; F:beta-N-acetylgalactosaminidase activity; IEA:Ensembl.
GO; GO:0005319; F:lipid transporter activity; IEA:Ensembl.
GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
GO; GO:0030290; F:sphingolipid activator protein activity; TAS:Reactome.
GO; GO:0006689; P:ganglioside catabolic process; IEA:Ensembl.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl.
GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
Gene3D; 2.70.220.10; -; 1.
InterPro; IPR028996; GM2-AP.
InterPro; IPR036846; GM2-AP_sf.
InterPro; IPR003172; ML_dom.
PANTHER; PTHR17357; PTHR17357; 1.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF63707; SSF63707; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Gangliosidosis; Glycoprotein;
Hydrolase; Lipid metabolism; Lysosome; Polymorphism;
Reference proteome; Signal; Sphingolipid metabolism.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 31 {ECO:0000269|PubMed:2209618}.
/FTId=PRO_0000031639.
CHAIN 32 193 Ganglioside GM2 activator.
/FTId=PRO_0000031640.
CHAIN 34 193 Ganglioside GM2 activator isoform short.
/FTId=PRO_0000031641.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
DISULFID 39 183
DISULFID 99 106
DISULFID 112 138
DISULFID 125 136
VARIANT 19 19 A -> T (in dbSNP:rs1048719).
{ECO:0000269|PubMed:10364519,
ECO:0000269|PubMed:1427911,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:1915857,
ECO:0000269|PubMed:2753159}.
/FTId=VAR_013830.
VARIANT 59 59 I -> V (in dbSNP:rs153477).
{ECO:0000269|PubMed:10364519,
ECO:0000269|PubMed:1427911,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1915857,
ECO:0000269|PubMed:2059210,
ECO:0000269|PubMed:2753159}.
/FTId=VAR_036892.
VARIANT 69 69 M -> V (in dbSNP:rs153478).
{ECO:0000269|PubMed:10364519,
ECO:0000269|PubMed:1427911,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1915857,
ECO:0000269|PubMed:2059210,
ECO:0000269|PubMed:2753159}.
/FTId=VAR_036893.
VARIANT 88 88 Missing (in GM2GAB).
{ECO:0000269|PubMed:8900233}.
/FTId=VAR_011697.
VARIANT 138 138 C -> R (in GM2GAB; dbSNP:rs137852797).
{ECO:0000269|PubMed:1915858}.
/FTId=VAR_006947.
VARIANT 169 169 R -> P (in GM2GAB; dbSNP:rs104893892).
{ECO:0000269|PubMed:8244332}.
/FTId=VAR_011698.
CONFLICT 39 39 C -> R (in Ref. 5; BAG35396).
{ECO:0000305}.
STRAND 35 40 {ECO:0000244|PDB:2AG4}.
TURN 41 43 {ECO:0000244|PDB:2AG4}.
STRAND 45 74 {ECO:0000244|PDB:2AG4}.
STRAND 81 90 {ECO:0000244|PDB:2AG4}.
STRAND 93 96 {ECO:0000244|PDB:2AG4}.
STRAND 103 105 {ECO:0000244|PDB:2AG4}.
STRAND 107 109 {ECO:0000244|PDB:1PUB}.
HELIX 111 118 {ECO:0000244|PDB:2AG4}.
STRAND 121 123 {ECO:0000244|PDB:1PUB}.
HELIX 129 132 {ECO:0000244|PDB:2AG4}.
STRAND 137 140 {ECO:0000244|PDB:2AG9}.
STRAND 142 154 {ECO:0000244|PDB:2AG4}.
TURN 161 163 {ECO:0000244|PDB:2AG9}.
STRAND 164 176 {ECO:0000244|PDB:2AG4}.
STRAND 179 192 {ECO:0000244|PDB:2AG4}.
SEQUENCE 193 AA; 20838 MW; 4EB1119945365F7E CRC64;
MQSLMQAPLL IALGLLLAAP AQAHLKKPSQ LSSFSWDNCD EGKDPAVIRS LTLEPDPIIV
PGNVTLSVMG STSVPLSSPL KVDLVLEKEV AGLWIKIPCT DYIGSCTFEH FCDVLDMLIP
TGEPCPEPLR TYGLPCHCPF KEGTYSLPKS EFVVPDLELP SWLTTGNYRI ESVLSSSGKR
LGCIKIAASL KGI
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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GENTAUR Poland Sp. z o.o.
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Pathways :
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
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
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
Related Genes :
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