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Protein translocation protein SEC63 (Protein NPL1) (Sec62/63 complex 73 kDa subunit)

 SEC63_YEAST             Reviewed;         663 AA.
P14906; D6W2V5; Q08690;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
03-JUL-2019, entry version 192.
RecName: Full=Protein translocation protein SEC63;
AltName: Full=Protein NPL1;
AltName: Full=Sec62/63 complex 73 kDa subunit;
Name=SEC63; Synonyms=NPL1, PTL1; OrderedLocusNames=YOR254C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2556404; DOI=10.1083/jcb.109.6.2665;
Sadler I., Chiang A., Kurihara T., Rothblatt J.A., Way J.,
Silver P.A.;
"A yeast gene important for protein assembly into the endoplasmic
reticulum and the nucleus has homology to DnaJ, an Escherichia coli
heat shock protein.";
J. Cell Biol. 109:2665-2675(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9153759;
DOI=10.1002/(SICI)1097-0061(199704)13:5<483::AID-YEA105>3.0.CO;2-U;
Poirey R., Jauniaux J.-C.;
"Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV
reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1,
RBL2, PNT1, PAC1 and VPH1.";
Yeast 13:483-487(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
IDENTIFICATION IN THE SEC62/63 COMPLEX.
PubMed=2000150; DOI=10.1038/349806a0;
Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.;
"Assembly of yeast Sec proteins involved in translocation into the
endoplasmic reticulum into a membrane-bound multisubunit complex.";
Nature 349:806-808(1991).
[6]
IDENTIFICATION IN THE SEC62/63 COMPLEX.
PubMed=1620130; DOI=10.1128/MCB.12.7.3288;
Feldheim D., Rothblatt J., Schekman R.;
"Topology and functional domains of Sec63p, an endoplasmic reticulum
membrane protein required for secretory protein translocation.";
Mol. Cell. Biol. 12:3288-3296(1992).
[7]
MUTAGENESIS.
PubMed=8514125;
Nelson M.K., Kurihara T., Silver P.A.;
"Extragenic suppressors of mutations in the cytoplasmic C-terminus of
SEC63 define five genes in Saccharomyces cerevisiae.";
Genetics 134:159-173(1993).
[8]
IDENTIFICATION IN A COMPLEX WITH KAR2; SEC66 AND SEC72.
PubMed=8253836; DOI=10.1083/jcb.123.6.1355;
Brodsky J.L., Schekman R.;
"A Sec63p-BiP complex from yeast is required for protein translocation
in a reconstituted proteoliposome.";
J. Cell Biol. 123:1355-1363(1993).
[9]
ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
PubMed=7758110; DOI=10.1016/0092-8674(95)90077-2;
Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.;
"Posttranslational protein transport in yeast reconstituted with a
purified complex of Sec proteins and Kar2p.";
Cell 81:561-570(1995).
[10]
FUNCTION.
PubMed=11226176; DOI=10.1093/emboj/20.1.262;
Young B.P., Craven R.A., Reid P.J., Willer M., Stirling C.J.;
"Sec63p and Kar2p are required for the translocation of SRP-dependent
precursors into the yeast endoplasmic reticulum in vivo.";
EMBO J. 20:262-271(2001).
[11]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14690591; DOI=10.1016/S1097-2765(03)00476-3;
Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
Yates J.R. III, Davis T.N.;
"Assigning function to yeast proteins by integration of
technologies.";
Mol. Cell 12:1353-1365(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
INTERACTION WITH SEC63.
PubMed=12518317; DOI=10.1002/yea.954;
Willer M., Jermy A.J., Young B.P., Stirling C.J.;
"Identification of novel protein-protein interactions at the cytosolic
surface of the Sec63 complex in the yeast ER membrane.";
Yeast 20:133-148(2003).
[14]
PHOSPHORYLATION BY CASEIN KINASE II, INTERACTION WITH SEC63, AND
MUTAGENESIS OF THR-652 AND THR-654.
PubMed=15671059; DOI=10.1242/jcs.01671;
Wang X., Johnsson N.;
"Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of
the endoplasmic reticulum protein translocation apparatus.";
J. Cell Sci. 118:723-732(2005).
[15]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Acts as component of the Sec62/63 complex which is
involved in SRP-independent post-translational translocation
across the endoplasmic reticulum (ER) and functions together with
the Sec61 complex and KAR2 in a channel-forming translocon
complex. A cycle of assembly and disassembly of Sec62/63 complex
from SEC61 may govern the activity of the translocon. SEC63 may
affect SEC1-polypeptide interactions by increasing the affinity of
targeting pathways for SEC61 and/or by modifying SEC61 to allow
more efficient polypeptide interaction. May also be involved in
SRP-dependent cotranslational translocation. Is essential for cell
growth and for germination. {ECO:0000269|PubMed:11226176}.
-!- SUBUNIT: Component of the heterotetrameric Sec62/63complex
composed of SEC62, SEC63, SEC66 and SEC72. The Sec62/63 complex
associates with the Sec61 complex to form the Sec complex. SEC63
interacts in its phosphorylated form with SEC62. May physically
associate with KAR2 in the endoplasmic reticulum and this
interaction may be regulated by ATP hydrolysis. Part of a complex
consisting of KAR2, SEC63, SEC66 and SEC72.
{ECO:0000269|PubMed:12518317, ECO:0000269|PubMed:15671059,
ECO:0000269|PubMed:1620130, ECO:0000269|PubMed:2000150,
ECO:0000269|PubMed:8253836}.
-!- INTERACTION:
P21825:SEC62; NbExp=7; IntAct=EBI-16636, EBI-16632;
P33754:SEC66; NbExp=4; IntAct=EBI-16636, EBI-16647;
P39742:SEC72; NbExp=4; IntAct=EBI-16636, EBI-16651;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Nucleus membrane; Multi-pass membrane protein.
Nucleus inner membrane; Multi-pass membrane protein.
-!- PTM: Phosphotylated by casein kinase II.
-!- MISCELLANEOUS: Present with 17700 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
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EMBL; X16388; CAA34424.1; -; Genomic_DNA.
EMBL; Z75162; CAA99476.1; -; Genomic_DNA.
EMBL; BK006948; DAA11021.1; -; Genomic_DNA.
PIR; A33618; A33618.
RefSeq; NP_014897.1; NM_001183673.1.
PDB; 6N3Q; EM; 3.68 A; D=1-663.
PDB; 6ND1; EM; 4.10 A; A=1-663.
PDBsum; 6N3Q; -.
PDBsum; 6ND1; -.
SMR; P14906; -.
BioGrid; 34644; 650.
ComplexPortal; CPX-3055; Translocon complex.
ComplexPortal; CPX-3056; SEC62-SEC63 complex.
DIP; DIP-2396N; -.
IntAct; P14906; 18.
MINT; P14906; -.
STRING; 4932.YOR254C; -.
TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
iPTMnet; P14906; -.
MaxQB; P14906; -.
PaxDb; P14906; -.
PRIDE; P14906; -.
EnsemblFungi; YOR254C_mRNA; YOR254C_mRNA; YOR254C.
GeneID; 854428; -.
KEGG; sce:YOR254C; -.
EuPathDB; FungiDB:YOR254C; -.
SGD; S000005780; SEC63.
GeneTree; ENSGT00390000001965; -.
HOGENOM; HOG000248842; -.
InParanoid; P14906; -.
KO; K09540; -.
OMA; ANSNDVW; -.
BioCyc; YEAST:G3O-33745-MONOMER; -.
PRO; PR:P14906; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; HDA:SGD.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0031207; C:Sec62/Sec63 complex; IPI:SGD.
GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; IMP:SGD.
GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; IMP:SGD.
GO; GO:0031204; P:posttranslational protein targeting to membrane, translocation; IDA:SGD.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:SGD.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR036869; J_dom_sf.
InterPro; IPR027137; Sec63.
InterPro; IPR004179; Sec63-dom.
PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
Pfam; PF00226; DnaJ; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SMART; SM00973; Sec63; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Endoplasmic reticulum;
Membrane; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 663 Protein translocation protein SEC63.
/FTId=PRO_0000071095.
TOPO_DOM 1 13 Lumenal. {ECO:0000255}.
TRANSMEM 14 41 Helical. {ECO:0000255}.
TOPO_DOM 42 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 108 Helical. {ECO:0000255}.
TOPO_DOM 109 220 Lumenal. {ECO:0000255}.
TRANSMEM 221 239 Helical. {ECO:0000255}.
TOPO_DOM 240 663 Cytoplasmic. {ECO:0000255}.
DOMAIN 123 198 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
DOMAIN 228 532 SEC63.
REPEAT 461 471 1.
REPEAT 493 503 2.
REGION 461 503 2 X 11 AA repeats.
COMPBIAS 612 663 Asp/Glu-rich (highly acidic).
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 179 179 A->T: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 426 426 P->L: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 431 431 I->N: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 503 503 P->A: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 511 511 G->R: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 652 652 T->A: Abolishes interaction with SEC62;
defect in protein translocation.
{ECO:0000269|PubMed:15671059}.
MUTAGEN 654 654 T->A: Abolishes interaction with SEC62;
defect in protein translocation.
{ECO:0000269|PubMed:15671059}.
CONFLICT 263 263 V -> I (in Ref. 1; CAA34424).
{ECO:0000305}.
CONFLICT 293 293 F -> L (in Ref. 1; CAA34424).
{ECO:0000305}.
SEQUENCE 663 AA; 75345 MW; 7D6757144C8A301F CRC64;
MPTNYEYDEA SETWPSFILT GLLMVVGPMT LLQIYQIFFG ANAEDGNSGK SKEFNEEVFK
NLNEEYTSDE IKQFRRKFDK NSNKKSKIWS RRNIIIIVGW ILVAILLQRI NSNDAIKDAA
TKLFDPYEIL GISTSASDRD IKSAYRKLSV KFHPDKLAKG LTPDEKSVME ETYVQITKAY
ESLTDELVRQ NYLKYGHPDG PQSTSHGIAL PRFLVDGSAS PLLVVCYVAL LGLILPYFVS
RWWARTQSYT KKGIHNVTAS NFVSNLVNYK PSEIVTTDLI LHWLSFAHEF KQFFPDLQPT
DFEKLLQDHI NRRDSGKLNN AKFRIVAKCH SLLHGLLDIA CGFRNLDIAL GAINTFKCIV
QAVPLTPNCQ ILQLPNVDKE HFITKTGDIH TLGKLFTLED AKIGEVLGIK DQAKLNETLR
VASHIPNLKI IKADFLVPGE NQVTPSSTPY ISLKVLVRSA KQPLIPTSLI PEENLTEPQD
FESQRDPFAM MSKQPLVPYS FAPFFPTKRR GSWCCLVSSQ KDGKILQTPI IIEKLSYKNL
NDDKDFFDKR IKMDLTKHEK FDINDWEIGT IKIPLGQPAP ETVGDFFFRV IVKSTDYFTT
DLDITMNMKV RDSPAVEQVE VYSEEDDEYS TDDDETESDD ESDASDYTDI DTDTEAEDDE
SPE


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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP1663: Homologous recombination
WP2292: Chemokine signaling pathway
WP1672: Mismatch repair
WP1644: DNA replication
WP1700: Selenoamino acid metabolism
WP731: Sterol regulatory element binding protein related
WP1661: Glyoxylate and dicarboxylate metabolism
WP2324: AGE/RAGE pathway
WP1613: 1,4-Dichlorobenzene degradation
WP1714: Tyrosine metabolism
WP813: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP1624: Bacterial secretion system
WP1892: Protein folding
WP2032: TSH signaling pathway
WP1438: Influenza A virus infection
WP1690: Propanoate metabolism
WP35: G Protein Signaling Pathways
WP1654: gamma-Hexachlorocyclohexane degradation
WP211: BMP signaling pathway

Related Genes :
[SEC63 NPL1 PTL1 YOR254C] Protein translocation protein SEC63 (Protein NPL1) (Sec62/63 complex 73 kDa subunit)
[SEC66 HSS1 SEC71 YBR171W YBR1232] Translocation protein SEC66 (Protein HSS1) (Sec62/63 complex 31.5 kDa subunit)
[SEC63 SEC63L] Translocation protein SEC63 homolog
[SEC62 YPL094C LPG14C] Translocation protein SEC62 (Sec62/63 complex 30 kDa subunit)
[Sec63 Sec63l] Translocation protein SEC63 homolog
[SEC72 SEC67 SIM2 YLR292C L8003.18] Translocation protein SEC72 (Sec62/63 complex 23 kDa subunit) (p23)
[PHOT2 CAV1 KIN7 NPL1 At5g58140 K21L19.6] Phototropin-2 (EC 2.7.11.1) (Defective in chloroplast avoidance protein 1) (Non-phototropic hypocotyl 1-like protein 1) (AtKin7) (NPH1-like protein 1)
[sec63 SPBC36B7.03] Translocation protein sec63
[SNRNP200 ASCC3L1 HELIC2 KIAA0788] U5 small nuclear ribonucleoprotein 200 kDa helicase (EC 3.6.4.13) (Activating signal cointegrator 1 complex subunit 3-like 1) (BRR2 homolog) (U5 snRNP-specific 200 kDa protein) (U5-200KD)
[HFM1 SEC3D1] Probable ATP-dependent DNA helicase HFM1 (EC 3.6.4.12) (SEC63 domain-containing protein 1)
[VPH1 YOR270C] V-type proton ATPase subunit a, vacuolar isoform (V-ATPase a 1 subunit) (V-ATPase 95 kDa subunit) (Vacuolar pH protein 1) (Vacuolar proton pump a subunit) (Vacuolar proton translocating ATPase subunit a 1)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[NUDT21 CFIM25 CPSF25 CPSF5] Cleavage and polyadenylation specificity factor subunit 5 (Cleavage and polyadenylation specificity factor 25 kDa subunit) (CPSF 25 kDa subunit) (Cleavage factor Im complex 25 kDa subunit) (CFIm25) (Nucleoside diphosphate-linked moiety X motif 21) (Nudix motif 21) (Nudix hydrolase 21) (Pre-mRNA cleavage factor Im 68 kDa subunit)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Steroidogenesis-activator polypeptide)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[ileS NPL1_01610] Isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS)
[atpE NPL1_01060] ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein)
[TP63 KET P63 P73H P73L TP73L] Tumor protein 63 (p63) (Chronic ulcerative stomatitis protein) (CUSP) (Keratinocyte transcription factor KET) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L) (p40) (p51)
[atpF NPL1_01065] ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b)
[plsY NPL1_00590] Glycerol-3-phosphate acyltransferase (Acyl-PO4 G3P acyltransferase) (Acyl-phosphate--glycerol-3-phosphate acyltransferase) (G3P acyltransferase) (GPAT) (EC 2.3.1.275) (Lysophosphatidic acid synthase) (LPA synthase)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78 I79_019946] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[sec62 SPAC17G6.09] Translocation protein sec62
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Fragment)
[Hspa8 Hsc70 Hsc73] Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)
[SSRP1 FACT80] FACT complex subunit SSRP1 (Chromatin-specific transcription elongation factor 80 kDa subunit) (Facilitates chromatin transcription complex 80 kDa subunit) (FACT 80 kDa subunit) (FACTp80) (Facilitates chromatin transcription complex subunit SSRP1) (Recombination signal sequence recognition protein 1) (Structure-specific recognition protein 1) (hSSRP1) (T160)
[deoB NPL1_03540 NPL2_02370 NPL4_01035] Phosphopentomutase (EC 5.4.2.7) (Phosphodeoxyribomutase)
[PRKAA1 AMPK1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (AMPK 63 kDa subunit) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26) (Fragments)

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