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Translocon-associated protein subunit alpha (TRAP-alpha) (Signal sequence receptor subunit alpha) (SSR-alpha)

 SSRA_HUMAN              Reviewed;         286 AA.
P43307; A8K685; Q53GX2; Q53H19; Q5TAM3; Q6IB43; Q8NBH9; Q96IA2;
Q9TNQ8; Q9UN49;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 3.
25-APR-2018, entry version 163.
RecName: Full=Translocon-associated protein subunit alpha;
Short=TRAP-alpha;
AltName: Full=Signal sequence receptor subunit alpha;
Short=SSR-alpha;
Flags: Precursor;
Name=SSR1; Synonyms=TRAPA; ORFNames=PSEC0262;
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), AND VARIANT SER-28.
PubMed=8050590; DOI=10.1016/0014-5793(94)00693-8;
Hartmann E., Prehn S.;
"The N-terminal region of the alpha-subunit of the TRAP complex has a
conserved cluster of negative charges.";
FEBS Lett. 349:324-326(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10437777; DOI=10.1016/S0014-5793(99)00885-6;
Hirama T., Miller C.W., Koeffler H.P.;
"Translocon-associated protein alpha transcripts are induced by
granulocyte-macrophage colony-stimulating factor and exhibit complex
alternative polyadenylation.";
FEBS Lett. 455:223-227(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-28.
TISSUE=Liver;
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Teratocarcinoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
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]
PROTEIN SEQUENCE OF 19-31.
PubMed=1557127; DOI=10.1038/356443a0;
Wei M.L., Cresswell P.;
"HLA-A2 molecules in an antigen-processing mutant cell contain signal
sequence-derived peptides.";
Nature 356:443-446(1992).
[11]
GLYCOSYLATION AT ASN-136.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-268, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-191.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260 AND SER-268, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH CALNEXIN.
PubMed=22314232; DOI=10.1038/emboj.2012.15;
Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B.,
Kihara A., Dal Peraro M., van der Goot F.G.;
"Palmitoylated calnexin is a key component of the ribosome-translocon
complex.";
EMBO J. 31:1823-1835(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND 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).
[23]
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).
-!- FUNCTION: TRAP proteins are part of a complex whose function is to
bind calcium to the ER membrane and thereby regulate the retention
of ER resident proteins. May be involved in the recycling of the
translocation apparatus after completion of the translocation
process or may function as a membrane-bound chaperone facilitating
folding of translocated proteins.
-!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the
interaction is required for efficient folding of glycosylated
proteins. {ECO:0000269|PubMed:22314232}.
-!- INTERACTION:
P27824:CANX; NbExp=5; IntAct=EBI-714168, EBI-355947;
P01009:SERPINA1; NbExp=4; IntAct=EBI-714168, EBI-986224;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P43307-1; Sequence=Displayed;
Name=2;
IsoId=P43307-2; Sequence=VSP_013621;
Note=No experimental confirmation available.;
-!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
being highly negatively charged, and the cytoplasmic C-terminus
positively charged.
-!- MISCELLANEOUS: Seems to bind calcium.
-!- SIMILARITY: Belongs to the TRAP-alpha family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI16444.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; Z12830; CAA78290.1; -; mRNA.
EMBL; AF156965; AAD48778.1; -; mRNA.
EMBL; BT007387; AAP36051.1; -; mRNA.
EMBL; AK291550; BAF84239.1; -; mRNA.
EMBL; CR456961; CAG33242.1; -; mRNA.
EMBL; AK222762; BAD96482.1; -; mRNA.
EMBL; AK222809; BAD96529.1; -; mRNA.
EMBL; AK075562; BAC11701.1; -; mRNA.
EMBL; AL139095; CAI16444.1; ALT_SEQ; Genomic_DNA.
EMBL; BC007710; AAH07710.1; -; mRNA.
CCDS; CCDS4499.1; -. [P43307-1]
PIR; I38246; I38246.
RefSeq; NP_001278937.1; NM_001292008.1.
RefSeq; NP_003135.2; NM_003144.4. [P43307-1]
UniGene; Hs.114033; -.
ProteinModelPortal; P43307; -.
BioGrid; 112623; 72.
IntAct; P43307; 47.
MINT; P43307; -.
STRING; 9606.ENSP00000244763; -.
iPTMnet; P43307; -.
PhosphoSitePlus; P43307; -.
BioMuta; SSR1; -.
DMDM; 22261821; -.
EPD; P43307; -.
MaxQB; P43307; -.
PaxDb; P43307; -.
PeptideAtlas; P43307; -.
PRIDE; P43307; -.
TopDownProteomics; P43307-1; -. [P43307-1]
TopDownProteomics; P43307-2; -. [P43307-2]
DNASU; 6745; -.
Ensembl; ENST00000244763; ENSP00000244763; ENSG00000124783. [P43307-1]
GeneID; 6745; -.
KEGG; hsa:6745; -.
UCSC; uc003mxf.6; human. [P43307-1]
CTD; 6745; -.
DisGeNET; 6745; -.
EuPathDB; HostDB:ENSG00000124783.12; -.
GeneCards; SSR1; -.
HGNC; HGNC:11323; SSR1.
HPA; HPA011276; -.
HPA; HPA017062; -.
MIM; 600868; gene.
neXtProt; NX_P43307; -.
OpenTargets; ENSG00000124783; -.
PharmGKB; PA36147; -.
eggNOG; KOG1631; Eukaryota.
eggNOG; ENOG410XNTM; LUCA.
GeneTree; ENSGT00400000022103; -.
HOVERGEN; HBG009736; -.
InParanoid; P43307; -.
KO; K13249; -.
PhylomeDB; P43307; -.
TreeFam; TF321074; -.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
ChiTaRS; SSR1; human.
GeneWiki; SSR1; -.
GenomeRNAi; 6745; -.
PRO; PR:P43307; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124783; -.
ExpressionAtlas; P43307; baseline and differential.
Genevisible; P43307; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
InterPro; IPR005595; TRAP_alpha.
Pfam; PF03896; TRAP_alpha; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000269|PubMed:1557127}.
CHAIN 19 286 Translocon-associated protein subunit
alpha.
/FTId=PRO_0000033281.
TOPO_DOM 19 207 Lumenal. {ECO:0000255}.
TRANSMEM 208 228 Helical. {ECO:0000255}.
TOPO_DOM 229 286 Cytoplasmic. {ECO:0000255}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 260 260 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 68 94 Missing (in isoform 2).
{ECO:0000303|PubMed:16303743}.
/FTId=VSP_013621.
VARIANT 28 28 L -> S (in dbSNP:rs10004).
{ECO:0000269|PubMed:8050590,
ECO:0000269|Ref.6}.
/FTId=VAR_022427.
CONFLICT 6 6 R -> G (in Ref. 7; BAC11701).
{ECO:0000305}.
CONFLICT 37 37 E -> A (in Ref. 6; BAD96529).
{ECO:0000305}.
CONFLICT 130 130 Y -> H (in Ref. 1; CAA78290).
{ECO:0000305}.
CONFLICT 190 190 F -> Y (in Ref. 4; BAF84239).
{ECO:0000305}.
CONFLICT 220 220 L -> P (in Ref. 6; BAD96529).
{ECO:0000305}.
CONFLICT 263 263 Q -> R (in Ref. 4; BAF84239).
{ECO:0000305}.
CONFLICT 286 286 E -> D (in Ref. 5; CAG33242).
{ECO:0000305}.
SEQUENCE 286 AA; 32235 MW; 2C631DC0CC3EB489 CRC64;
MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE
PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK
VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE


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EIAAB40058 Mouse,Mus musculus,Signal sequence receptor subunit alpha,Ssr1,SSR-alpha,Translocon-associated protein subunit alpha,TRAP-alpha
EIAAB40063 Bos taurus,Bovine,Signal sequence receptor subunit alpha,SSR1,SSR-alpha,Translocon-associated protein subunit alpha,TRAP-alpha
EIAAB40059 Ac2-238,Liver regeneration-related protein LRRG137,Rat,Rattus norvegicus,Signal sequence receptor subunit alpha,Ssr1,SSR-alpha,Translocon-associated protein subunit alpha,TRAP-alpha
EIAAB40062 Canis familiaris,Canis lupus familiaris,Dog,PGP35,Signal sequence receptor subunit alpha,SSR1,SSR-alpha,Translocon-associated protein subunit alpha,TRAP-alpha
EIAAB39922 Bos taurus,Bovine,Docking protein alpha,DP-alpha,Signal recognition particle receptor subunit alpha,SR-alpha,SRPR
EIAAB39924 Docking protein alpha,DP-alpha,Mouse,Mus musculus,Signal recognition particle receptor subunit alpha,SR-alpha,Srpr
EIAAB39921 Docking protein alpha,DP-alpha,Homo sapiens,Human,Signal recognition particle receptor subunit alpha,SR-alpha,SRPR
E1345m ELISA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA kit Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
U1345m CLIA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
EIAAB08300 Chicken,Ciliary neurotrophic factor receptor subunit alpha,CNTF receptor subunit alpha,CNTFR,CNTFR-alpha,Gallus gallus,GPA receptor subunit alpha,GPAR-alpha,Growth-promoting activity receptor subunit
U1815h CLIA gp80,Homo sapiens,Human,IL-6 receptor subunit alpha,IL6R,IL-6R 1,IL-6R subunit alpha,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Membrane glycoprotein 80 96T
U1815h CLIA kit gp80,Homo sapiens,Human,IL-6 receptor subunit alpha,IL6R,IL-6R 1,IL-6R subunit alpha,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Membrane glycoprotein 80 96T
E1815h ELISA gp80,Homo sapiens,Human,IL-6 receptor subunit alpha,IL6R,IL-6R 1,IL-6R subunit alpha,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Membrane glycoprotein 80 96T
E1815h ELISA kit gp80,Homo sapiens,Human,IL-6 receptor subunit alpha,IL6R,IL-6R 1,IL-6R subunit alpha,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Membrane glycoprotein 80 96T
E2031h ELISA 582J2.1,Homo sapiens,Human,IL-4 receptor subunit alpha,IL4R,IL-4R subunit alpha,IL4RA,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha 96T
U2031h CLIA kit 582J2.1,Homo sapiens,Human,IL-4 receptor subunit alpha,IL4R,IL-4R subunit alpha,IL4RA,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha 96T
E2031h ELISA kit 582J2.1,Homo sapiens,Human,IL-4 receptor subunit alpha,IL4R,IL-4R subunit alpha,IL4RA,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha 96T
U2031h CLIA 582J2.1,Homo sapiens,Human,IL-4 receptor subunit alpha,IL4R,IL-4R subunit alpha,IL4RA,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha 96T
U1815m CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Mouse,Mus musculus 96T
U1815r CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
E2031m ELISA IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Mouse,Mus musculus 96T
E2031r ELISA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Rat,Rattus norvegicus 96T


 

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