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Protein transport protein Sec31A (SEC31-like protein 1) (SEC31-related protein A)

 SC31A_MOUSE             Reviewed;        1230 AA.
Q3UPL0; Q3UYH3; Q6IQZ3; Q7TQJ7; Q811J4;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 2.
07-APR-2021, entry version 129.
RecName: Full=Protein transport protein Sec31A;
AltName: Full=SEC31-like protein 1;
AltName: Full=SEC31-related protein A;
Name=Sec31a; Synonyms=Sec31l1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 286-1230 (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Salivary gland;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-612 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-531, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion affinity
chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of electron
capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-531, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[7]
SUBCELLULAR LOCATION.
PubMed=25201882; DOI=10.15252/embj.201487807;
Cho H.J., Yu J., Xie C., Rudrabhatla P., Chen X., Wu J., Parisiadou L.,
Liu G., Sun L., Ma B., Ding J., Liu Z., Cai H.;
"Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow
ER-Golgi export.";
EMBO J. 33:2314-2331(2014).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-423, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER) (By similarity). The coat has two main functions, the
physical deformation of the endoplasmic reticulum membrane into
vesicles and the selection of cargo molecules (By similarity).
{ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}.
-!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
tetramer that forms the edge element of the COPII outer coat. The
tetramer self-assembles in multiple copies to form the complete
polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity).
Interacts with PDCD6; interaction takes place in response to cytosolic
calcium increase and leads to bridge together the BCR(KLHL12) complex
and SEC31A, leading to monoubiquitination. Interacts with KLHL12 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:O94979}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O94979};
Peripheral membrane protein {ECO:0000250|UniProtKB:O94979}; Cytoplasmic
side {ECO:0000250|UniProtKB:O94979}. Endoplasmic reticulum membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Note=Associates with membranes in a GTP-dependent manner (By
similarity). Localizes to endoplasmic reticulum exit sites (ERES), also
known as transitional endoplasmic reticulum (tER) (PubMed:25201882).
{ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:25201882}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q3UPL0-1; Sequence=Displayed;
Name=2;
IsoId=Q3UPL0-2; Sequence=VSP_026753;
Name=3;
IsoId=Q3UPL0-3; Sequence=VSP_026752;
-!- DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF
sequence that binds hydrophobic pocket 3 of PDCD6.
{ECO:0000250|UniProtKB:O94979}.
-!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
leading to regulate the size of COPII coats.
{ECO:0000250|UniProtKB:O94979}.
-!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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EMBL; BC043942; AAH43942.1; -; mRNA.
EMBL; BC054358; AAH54358.1; -; mRNA.
EMBL; BC071249; AAH71249.1; -; mRNA.
EMBL; AK134681; BAE22239.1; -; mRNA.
EMBL; AK143455; BAE25385.1; -; mRNA.
CCDS; CCDS51573.1; -. [Q3UPL0-1]
RefSeq; NP_081245.1; NM_026969.1. [Q3UPL0-1]
RefSeq; XP_011247860.1; XM_011249558.2. [Q3UPL0-2]
BioGRID; 213263; 16.
IntAct; Q3UPL0; 2.
MINT; Q3UPL0; -.
STRING; 10090.ENSMUSP00000092157; -.
iPTMnet; Q3UPL0; -.
PhosphoSitePlus; Q3UPL0; -.
SwissPalm; Q3UPL0; -.
EPD; Q3UPL0; -.
jPOST; Q3UPL0; -.
MaxQB; Q3UPL0; -.
PaxDb; Q3UPL0; -.
PeptideAtlas; Q3UPL0; -.
PRIDE; Q3UPL0; -.
ProteomicsDB; 256601; -. [Q3UPL0-1]
ProteomicsDB; 256602; -. [Q3UPL0-2]
ProteomicsDB; 256603; -. [Q3UPL0-3]
Antibodypedia; 1692; 139 antibodies.
Ensembl; ENSMUST00000094578; ENSMUSP00000092157; ENSMUSG00000035325. [Q3UPL0-1]
Ensembl; ENSMUST00000182886; ENSMUSP00000138213; ENSMUSG00000035325. [Q3UPL0-2]
GeneID; 69162; -.
KEGG; mmu:69162; -.
UCSC; uc008yhi.1; mouse. [Q3UPL0-2]
UCSC; uc008yhk.2; mouse. [Q3UPL0-1]
CTD; 22872; -.
MGI; MGI:1916412; Sec31a.
eggNOG; KOG0307; Eukaryota.
GeneTree; ENSGT00390000003175; -.
HOGENOM; CLU_003033_1_0_1; -.
InParanoid; Q3UPL0; -.
OMA; FMIAICG; -.
OrthoDB; 100998at2759; -.
PhylomeDB; Q3UPL0; -.
TreeFam; TF313842; -.
Reactome; R-MMU-204005; COPII-mediated vesicle transport.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
BioGRID-ORCS; 69162; 11 hits in 53 CRISPR screens.
ChiTaRS; Sec31a; mouse.
PRO; PR:Q3UPL0; -.
Proteomes; UP000000589; Chromosome 5.
RNAct; Q3UPL0; protein.
Bgee; ENSMUSG00000035325; Expressed in secondary oocyte and 310 other tissues.
Genevisible; Q3UPL0; MM.
GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0030120; C:vesicle coat; ISO:MGI.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:MGI.
GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0051592; P:response to calcium ion; ISO:MGI.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR024298; ACE1_Sec16_Sec31.
InterPro; IPR040251; SEC31-like.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR13923; PTHR13923; 1.
Pfam; PF12931; Sec16_C; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; ER-Golgi transport; Isopeptide bond; Membrane;
Methylation; Phosphoprotein; Protein transport; Reference proteome; Repeat;
Transport; Ubl conjugation; WD repeat.
CHAIN 1..1230
/note="Protein transport protein Sec31A"
/id="PRO_0000295148"
REPEAT 4..47
/note="WD 1"
REPEAT 64..111
/note="WD 2"
REPEAT 120..160
/note="WD 3"
REPEAT 166..206
/note="WD 4"
REPEAT 209..254
/note="WD 5"
REPEAT 258..298
/note="WD 6"
REPEAT 301..342
/note="WD 7"
REPEAT 397..429
/note="WD 8; interaction with SEC13"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
REGION 161..470
/note="Interaction with SEC13"
/evidence="ECO:0000250|UniProtKB:O94979"
REGION 799..1123
/note="Interaction with PDCD6"
/evidence="ECO:0000250|UniProtKB:O94979"
MOTIF 841..847
/note="ALG-2-binding site motif-2 (ABS-2),"
/evidence="ECO:0000250|UniProtKB:O94979"
COMPBIAS 832..1101
/note="Pro-rich"
MOD_RES 423
/note="Asymmetric dimethylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 526
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17242355,
ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
ECO:0007744|PubMed:21183079"
MOD_RES 531
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18630941,
ECO:0007744|PubMed:21183079"
MOD_RES 798
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O94979"
MOD_RES 1171
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:O94979"
MOD_RES 1173
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O94979"
CROSSLNK 646
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O94979"
CROSSLNK 1227
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O94979"
VAR_SEQ 1..923
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_026752"
VAR_SEQ 503..541
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_026753"
CONFLICT 820
/note="S -> P (in Ref. 1; AAH54358)"
/evidence="ECO:0000305"
SEQUENCE 1230 AA; 133569 MW; B6119EFDEF121A76 CRC64;
MKLKEIDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPHKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQKDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFAS SPLRVLENHA RGILAVAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSIDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQSAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFESV AVPLQQGAEQ
QRRQPVFISQ VVTEKDFLNR SAQLQHAVQS QGFIGYCQKK IEASQTEFEK NVWSFLKVNF
EEDSRGKYLE LLGYRKEDLG QKIALALNKV DGPDVALKDS DQVAQSDGEE SPAAEEQLLG
ERIKEEKQEC DFLPSAGGTF NISVSGDIDG LITRALLTGN FESAVDLCLH DNRMADAIIL
AIAGGQELLA QTQKKYFAKS QSKITRLITA VVMKNWREIV ESCDLKNWRE ALAAVLTYAK
PDEFSALCDL LGTRLEREGD SLLRTQACLC YICAGNVERL VACWTKAQDG SSPLSLQDLI
EKVVILRKAV QLTQALDTNT VGALLAEKMS QYASLLAAQG SIAAALAFLP DNTNQPNIVQ
LRDRLCKAQG KPVSGQESSQ SPYERQPLSK GRPGPVAGHS QMPRVQTQQY YPHGENPPPP
GFIMQGNVIP NPAAPLPTAP GHMPSQLPPY PQPQPYQPAQ QYSFGTGGAA AYRPQQPVAP
PASNAYPNTP YISPVASYSG QPQMYTAQQA SSPTSSSAAS FPPPSSGASF QHGGPGAPPS
SSAYALPPGT TGTPPAASEL PASQRTENQS FQDQASILEG PQNGWNDPPA LNRVPKKKKM
PENFMPPVPI TSPIMNPSGD PQSQGLQQQP STPGPLSSHA SFPQQHLAGG QPFHGVQQPL
AQTGMPPSFS KPNTEGAPGA PIGNTIQHVQ ALPTEKITKK PIPEEHLILK TTFEDLIQRC
LSSATDPQTK RKLDDASKRL EFLYDKLREQ TLSPTIINGL HSIARSIETR NYSEGLSVHT
HIVSTSNFSE TSAFMPVLKV VLSQASKLGV


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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1616: ABC transporters
WP1689: Porphyrin and chlorophyll metabolism
WP1713: Two-component system
WP1502: Mitochondrial biogenesis
WP731: Sterol regulatory element binding protein related
WP2199: Seed Development
WP1685: Peptidoglycan biosynthesis
WP1624: Bacterial secretion system
WP1909: Signal regulatory protein (SIRP) family interactions
WP1650: Fluorobenzoate degradation
WP1692: Protein export
WP2324: AGE/RAGE pathway
WP1371: G Protein Signaling Pathways
WP1700: Selenoamino acid metabolism
WP346: Protein Modifications
WP1659: Glycine, serine and threonine metabolism
WP1939: Unfolded Protein Response
WP1665: Limonene and pinene degradation
WP2032: TSH signaling pathway
WP73: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP211: BMP signaling pathway
WP2218: sGC
WP813: G Protein Signaling Pathways

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[PDCD6 ALG2] Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2)
[Pdcd6 Alg2] Programmed cell death protein 6 (ALG-257) (Apoptosis-linked gene 2 protein) (ALG-2) (PMP41)
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[ALK] ALK tyrosine kinase receptor (EC 2.7.10.1) (Anaplastic lymphoma kinase) (CD antigen CD246)
[sec31 B24N11.230 NCU06738] Protein transport protein sec31
[CUL3 KIAA0617] Cullin-3 (CUL-3)
[Cul3] Cullin-3 (CUL-3)
[Cul3] Cullin-3
[Lrrk2] Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (EC 3.6.5.-)
[Pef1] Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1)
[sec31 DDB_G0270992] Protein transport protein SEC31
[SEC13 ANU3 YLR208W L8167.4] Protein transport protein SEC13
[Pef1] Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1)
[PF3D7_0214100] Protein transport protein SEC31
[SEC24 ANU1 YIL109C] Protein transport protein SEC24 (Abnormal nuclear morphology 1)
[REL] Proto-oncogene c-Rel
[Klhl12 C3ip1] Kelch-like protein 12 (CUL3-interacting protein 1)
[npp-20 CeSec13R sec-13 Y77E11A.13] Protein SEC13 homolog (CeSEH13R) (GATOR complex protein SEC13) (Nuclear pore complex protein 20)
[Klhl12 C3ip1] Kelch-like protein 12 (CUL3-interacting protein 1)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Processing enhancing protein) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase complex 50 kDa protein)
[fes-1 NCU06606] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Complex III subunit V) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (Ubiquinol-cytochrome c reductase complex 25 kDa protein)
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[] 3C-like proteinase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.6.4.12) (EC 3.6.4.13) (Exoribonuclease) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 1) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (Peptide HD2) (Putative 2'-O-methyl transferase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p195)
[Or22a AN11 DOR22A.1 dor53 Or22A.1 CG12193] Odorant receptor 22a
[Lrp1 A2mr] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[] 3C-like proteinase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.6.4.12) (EC 3.6.4.13) (Exoribonuclease) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 1) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (Peptide HD2) (Putative 2'-O-methyl transferase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p12) (p195) (p23) (p34) (p5) (p87) (p9)
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[SLC27A5 ACSB ACSVL6 FACVL3 FATP5] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Fatty-acid-coenzyme A ligase, very long-chain 3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase homolog 2) (VLCS-H2) (VLCSH2) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)

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