Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein sel-1 homolog 1 (Suppressor of lin-12-like protein 1) (Sel-1L)

 SE1L1_HUMAN             Reviewed;         794 AA.
Q9UBV2; Q6UWT6; Q9P1T9; Q9UHK7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 3.
25-OCT-2017, entry version 154.
RecName: Full=Protein sel-1 homolog 1;
AltName: Full=Suppressor of lin-12-like protein 1;
Short=Sel-1L;
Flags: Precursor;
Name=SEL1L; Synonyms=TSA305; ORFNames=UNQ128/PRO1063;
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).
TISSUE=Pancreas;
PubMed=10496078; DOI=10.1007/s100380050171;
Harada Y., Ozaki K., Suzuki M., Fujiwara T., Takahashi E.,
Nakamura Y., Tanigami A.;
"Complete cDNA sequence and genomic organization of a human pancreas-
specific gene homologous to Caenorhabditis elegans sel-1.";
J. Hum. Genet. 44:330-336(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Pancreas;
PubMed=10746565; DOI=10.1007/s004390051032;
Biunno I., Bernard L., Dear P., Cattaneo M., Volorio S., Zannini L.,
Bankier A., Zollo M.;
"SEL1L, the human homolog of C. elegans sel-1: refined physical
mapping, gene structure and identification of polymorphic markers.";
Hum. Genet. 106:227-235(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
GLYCOSYLATION AT ASN-272.
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).
[5]
FUNCTION, INTERACTION WITH SYVN1, IDENTIFICATION IN A COMPLEX WITH
SYVN1 AND DERL2, AND SUBCELLULAR LOCATION.
PubMed=16186509; DOI=10.1073/pnas.0505014102;
Lilley B.N., Ploegh H.L.;
"Multiprotein complexes that link dislocation, ubiquitination, and
extraction of misfolded proteins from the endoplasmic reticulum
membrane.";
Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005).
[6]
GLYCOSYLATION, AND INTERACTION WITH ERLEC1; HSPA5; OS9 AND SYVN1.
PubMed=18502753; DOI=10.1074/jbc.M709336200;
Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.;
"Human XTP3-B forms an endoplasmic reticulum quality control scaffold
with the HRD1-SEL1L ubiquitin ligase complex and BiP.";
J. Biol. Chem. 283:20914-20924(2008).
[7]
INTERACTION WITH ERLEC1; OS9 AND SYVN1.
PubMed=18264092; DOI=10.1038/ncb1689;
Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
ubiquitin ligase complex for ERAD.";
Nat. Cell Biol. 10:272-282(2008).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-431 AND ASN-608.
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).
[9]
INTERACTION WITH EDEM1.
PubMed=19524542; DOI=10.1016/j.molcel.2009.05.018;
Cormier J.H., Tamura T., Sunryd J.C., Hebert D.N.;
"EDEM1 recognition and delivery of misfolded proteins to the SEL1L-
containing ERAD complex.";
Mol. Cell 34:627-633(2009).
[10]
INTERACTION WITH FOXRED2.
PubMed=19706418; DOI=10.1073/pnas.0900742106;
Riemer J., Appenzeller-Herzog C., Johansson L., Bodenmiller B.,
Hartmann-Petersen R., Ellgaard L.;
"A luminal flavoprotein in endoplasmic reticulum-associated
degradation.";
Proc. Natl. Acad. Sci. U.S.A. 106:14831-14836(2009).
[11]
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).
[12]
INTERACTION WITH LPL.
PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015;
Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L.,
Lawrence P., Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T.,
Shi H., Xue B., Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.;
"The ER-associated degradation adaptor protein Sel1L regulates LPL
secretion and lipid metabolism.";
Cell Metab. 20:458-470(2014).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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).
[14]
FUNCTION, AND INTERACTION WITH SYVN1.
PubMed=26471130; DOI=10.1111/febs.13564;
Hosokawa N., Wada I.;
"Association of the SEL1L protein transmembrane domain with HRD1
ubiquitin ligase regulates ERAD-L.";
FEBS J. 283:157-172(2016).
-!- FUNCTION: Plays a role in the endoplasmic reticulum quality
control (ERQC) system also called ER-associated degradation (ERAD)
involved in ubiquitin-dependent degradation of misfolded
endoplasmic reticulum proteins (PubMed:16186509). Enhances SYVN1
stability. Plays a role in LPL maturation and secretion. Required
for normal differentiation of the pancreas epithelium, and for
normal exocrine function and survival of pancreatic cells. May
play a role in Notch signaling. {ECO:0000250|UniProtKB:Q9Z2G6,
ECO:0000269|PubMed:16186509}.
-!- SUBUNIT: Homodimer and homooligomer (By similarity). Interacts
with SYVN1; the interaction is direct (PubMed:26471130). Part of a
complex containing SEL1L, SYVN1 and DERL2 (PubMed:16186509). May
form a complex with ERLEC1, HSPA5, OS9, and SYVN1
(PubMed:18502753, PubMed:18264092). Interacts with FOXRED2 and
EDEM1 (PubMed:19524542, PubMed:19706418). Interacts with LPL
(PubMed:25066055). Interacts with LMF1; may stabilize the complex
formed by LPL and LMF1 and thereby promote the export of LPL
dimers (By similarity). {ECO:0000250|UniProtKB:Q9Z2G6,
ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:18264092,
ECO:0000269|PubMed:18502753, ECO:0000269|PubMed:19524542,
ECO:0000269|PubMed:19706418, ECO:0000269|PubMed:25066055,
ECO:0000269|PubMed:26471130}.
-!- INTERACTION:
O75460-1:ERN1; NbExp=2; IntAct=EBI-358766, EBI-15600828;
Q8IWF2:FOXRED2; NbExp=3; IntAct=EBI-358766, EBI-10763361;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16186509}; Single-pass type I membrane protein
{ECO:0000269|PubMed:16186509}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UBV2-1; Sequence=Displayed;
Name=2;
IsoId=Q9UBV2-2; Sequence=VSP_013322, VSP_013323;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:18502753, ECO:0000269|PubMed:19159218}.
-!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SEL1LID42246ch14q24.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB024763; BAA89204.1; -; Genomic_DNA.
EMBL; AB020335; BAA87904.1; -; mRNA.
EMBL; AF052059; AAF29413.1; -; mRNA.
EMBL; AF157516; AAF24176.1; -; Genomic_DNA.
EMBL; AF198647; AAL40905.1; -; Genomic_DNA.
EMBL; AF198631; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198632; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198633; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198634; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198635; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198636; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198637; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198638; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198639; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198640; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198641; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198642; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198643; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198644; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198645; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AF198646; AAL40905.1; JOINED; Genomic_DNA.
EMBL; AY358651; AAQ89014.1; -; mRNA.
CCDS; CCDS58333.1; -. [Q9UBV2-2]
CCDS; CCDS9876.1; -. [Q9UBV2-1]
RefSeq; NP_001231913.1; NM_001244984.1. [Q9UBV2-2]
RefSeq; NP_005056.3; NM_005065.5. [Q9UBV2-1]
UniGene; Hs.181300; -.
ProteinModelPortal; Q9UBV2; -.
SMR; Q9UBV2; -.
BioGrid; 112300; 63.
CORUM; Q9UBV2; -.
DIP; DIP-46259N; -.
IntAct; Q9UBV2; 17.
MINT; MINT-1153834; -.
STRING; 9606.ENSP00000337053; -.
iPTMnet; Q9UBV2; -.
PhosphoSitePlus; Q9UBV2; -.
SwissPalm; Q9UBV2; -.
BioMuta; SEL1L; -.
DMDM; 62512184; -.
EPD; Q9UBV2; -.
PaxDb; Q9UBV2; -.
PeptideAtlas; Q9UBV2; -.
PRIDE; Q9UBV2; -.
Ensembl; ENST00000336735; ENSP00000337053; ENSG00000071537. [Q9UBV2-1]
Ensembl; ENST00000555824; ENSP00000450709; ENSG00000071537. [Q9UBV2-2]
GeneID; 6400; -.
KEGG; hsa:6400; -.
UCSC; uc001xvo.5; human. [Q9UBV2-1]
CTD; 6400; -.
DisGeNET; 6400; -.
EuPathDB; HostDB:ENSG00000071537.13; -.
GeneCards; SEL1L; -.
HGNC; HGNC:10717; SEL1L.
HPA; HPA024267; -.
MIM; 602329; gene.
neXtProt; NX_Q9UBV2; -.
OpenTargets; ENSG00000071537; -.
PharmGKB; PA35639; -.
eggNOG; KOG1550; Eukaryota.
eggNOG; COG0790; LUCA.
GeneTree; ENSGT00530000063170; -.
HOGENOM; HOG000239927; -.
HOVERGEN; HBG057766; -.
InParanoid; Q9UBV2; -.
KO; K14026; -.
OMA; LAQMAMG; -.
OrthoDB; EOG091G0315; -.
PhylomeDB; Q9UBV2; -.
TreeFam; TF315257; -.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
ChiTaRS; SEL1L; human.
GeneWiki; SEL1L; -.
GenomeRNAi; 6400; -.
PRO; PR:Q9UBV2; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000071537; -.
CleanEx; HS_SEL1L; -.
ExpressionAtlas; Q9UBV2; baseline and differential.
Genevisible; Q9UBV2; HS.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; TAS:ParkinsonsUK-UCL.
GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IMP:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; TAS:ParkinsonsUK-UCL.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; TAS:ParkinsonsUK-UCL.
CDD; cd00062; FN2; 1.
Gene3D; 2.10.10.10; -; 1.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR006597; Sel1-like.
Pfam; PF00040; fn2; 1.
Pfam; PF08238; Sel1; 12.
SMART; SM00059; FN2; 1.
SMART; SM00671; SEL1; 11.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Membrane;
Notch signaling pathway; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 794 Protein sel-1 homolog 1.
/FTId=PRO_0000022294.
TOPO_DOM 22 738 Lumenal. {ECO:0000255}.
TRANSMEM 739 759 Helical. {ECO:0000255}.
TOPO_DOM 760 794 Cytoplasmic. {ECO:0000255}.
DOMAIN 122 170 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 183 218 Sel1-like 1.
REPEAT 219 254 Sel1-like 2.
REPEAT 255 290 Sel1-like 3.
REPEAT 291 326 Sel1-like 4.
REPEAT 373 409 Sel1-like 5.
REPEAT 410 446 Sel1-like 6.
REPEAT 447 482 Sel1-like 7.
REPEAT 483 518 Sel1-like 8.
REPEAT 519 554 Sel1-like 9.
REPEAT 627 662 Sel1-like 10.
REPEAT 664 699 Sel1-like 11.
REGION 22 737 Interaction with ERLEC1, OS9 and SYVN1.
REGION 352 537 Important for homodimerization and
oligomerization.
{ECO:0000250|UniProtKB:Q9Z2G6}.
REGION 643 723 Interaction with SYVN1.
{ECO:0000250|UniProtKB:Q9Z2G6}.
REGION 738 794 Mediates retention in the endoplasmic
reticulum.
COMPBIAS 770 793 Pro-rich.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 608 608 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 127 153 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 141 168 {ECO:0000255|PROSITE-ProRule:PRU00479}.
VAR_SEQ 298 301 GYRY -> VSRL (in isoform 2).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_013322.
VAR_SEQ 302 794 Missing (in isoform 2).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_013323.
VARIANT 162 162 D -> G (in dbSNP:rs11499034).
/FTId=VAR_029303.
VARIANT 714 714 V -> I (in dbSNP:rs1051193).
/FTId=VAR_053963.
CONFLICT 186 186 M -> V (in Ref. 2; AAF29413/AAL40905).
{ECO:0000305}.
SEQUENCE 794 AA; 88755 MW; 323EB03DC7485459 CRC64;
MRVRIGLTLL LCAVLLSLAS ASSDEEGSQD ESLDSKTTLT SDESVKDHTT AGRVVAGQIF
LDSEESELES SIQEEEDSLK SQEGESVTED ISFLESPNPE NKDYEEPKKV RKPALTAIEG
TAHGEPCHFP FLFLDKEYDE CTSDGREDGR LWCATTYDYK ADEKWGFCET EEEAAKRRQM
QEAEMMYQTG MKILNGSNKK SQKREAYRYL QKAASMNHTK ALERVSYALL FGDYLPQNIQ
AAREMFEKLT EEGSPKGQTA LGFLYASGLG VNSSQAKALV YYTFGALGGN LIAHMVLGYR
YWAGIGVLQS CESALTHYRL VANHVASDIS LTGGSVVQRI RLPDEVENPG MNSGMLEEDL
IQYYQFLAEK GDVQAQVGLG QLHLHGGRGV EQNHQRAFDY FNLAANAGNS HAMAFLGKMY
SEGSDIVPQS NETALHYFKK AADMGNPVGQ SGLGMAYLYG RGVQVNYDLA LKYFQKAAEQ
GWVDGQLQLG SMYYNGIGVK RDYKQALKYF NLASQGGHIL AFYNLAQMHA SGTGVMRSCH
TAVELFKNVC ERGRWSERLM TAYNSYKDGD YNAAVIQYLL LAEQGYEVAQ SNAAFILDQR
EASIVGENET YPRALLHWNR AASQGYTVAR IKLGDYHFYG FGTDVDYETA FIHYRLASEQ
QHSAQAMFNL GYMHEKGLGI KQDIHLAKRF YDMAAEASPD AQVPVFLALC KLGVVYFLQY
IRETNIRDMF TQLDMDQLLG PEWDLYLMTI IALLLGTVIA YRQRQHQDMP APRPPGPRPA
PPQQEGPPEQ QPPQ


Related products :

Catalog number Product name Quantity
EIAAB25787 Angiotensin-II type 2 receptor-interacting protein,Atip,Microtubule-associated tumor suppressor 1 homolog,Mitochondrial tumor suppressor 1 homolog,Mtsg1,Mtus1,Rat,Rattus norvegicus
EIAAB40620 ChET 9 protein,CHET9,Chromatin precipitated E2F target 9 protein,Homo sapiens,Human,JJAZ1,Joined to JAZF1 protein,KIAA0160,Polycomb protein SUZ12,Suppressor of zeste 12 protein homolog,SUZ12
EIAAB45962 Homo sapiens,Human,SAC2 suppressor of actin mutations 2-like protein,SACM2L,Vacuolar protein sorting-associated protein 52 homolog,VPS52
EIAAB45961 Are1,Rat,Rattus norvegicus,SAC2 suppressor of actin mutations 2-like protein,Sacm2l,Vacuolar protein sorting-associated protein 52 homolog,Vps52
EIAAB38045 Mouse,Mus musculus,Sfrs8,Sfswap,Splicing factor, arginine_serine-rich 8,Splicing factor, suppressor of white-apricot homolog,Srsf8,Suppressor of white apricot protein homolog,Swap
EIAAB38047 Homo sapiens,Human,SFRS8,SFSWAP,Splicing factor, arginine_serine-rich 8,Splicing factor, suppressor of white-apricot homolog,Suppressor of white apricot protein homolog,SWAP
EIAAB38046 Rat,Rattus norvegicus,Sfrs8,Sfswap,Splicing factor, arginine_serine-rich 8,Splicing factor, suppressor of white-apricot homolog,Srsf8,Suppressor of white apricot protein homolog,Swap
EIAAB37760 Gm118,Mouse,Mus musculus,Protein sel-1 homolog 2,Sel1l2,Sel-1L2,Suppressor of lin-12-like protein 2
EIAAB37758 Mouse,Mus musculus,Protein sel-1 homolog 1,Sel1h,Sel1l,Sel-1L,Suppressor of lin-12-like protein 1
EIAAB37756 Protein sel-1 homolog 1,Rat,Rattus norvegicus,Sel1h,Sel1l,Sel-1L,Suppressor of lin-12-like protein 1
EIAAB37763 Kiaa0746,Mouse,Mus musculus,Protein sel-1 homolog 3,Sel1l3,Sel-1L3,Suppressor of lin-12-like protein 3
EIAAB37761 Protein sel-1 homolog 2,Rat,Rattus norvegicus,Sel1l2,Sel-1L2,Suppressor of lin-12-like protein 2
EIAAB37759 C20orf50,Homo sapiens,Human,Protein sel-1 homolog 2,SEL1L2,Sel-1L2,Suppressor of lin-12-like protein 2
EIAAB37762 Homo sapiens,Human,KIAA0746,Protein sel-1 homolog 3,SEL1L3,Sel-1L3,Suppressor of lin-12-like protein 3
30-622 ING1 is a tumor suppressor protein that can induce cell growth arrest and apoptosis. The protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a componen 0.1 mg
EIAAB37757 Homo sapiens,Human,Protein sel-1 homolog 1,SEL1L,Sel-1L,Suppressor of lin-12-like protein 1,TSA305,UNQ128_PRO1063
EIAAB40022 Brix domain-containing protein 3,BXDC3,Homo sapiens,Human,Peter Pan homolog,PPAN,SSF1,Ssf-1,Suppressor of SWI4 1 homolog
EIAAB34908 60S ribosomal protein L10,DXS648E,Homo sapiens,Human,Laminin receptor homolog,Protein QM,QM,RPL10,Tumor suppressor QM
EIAAB08208 CNK homolog protein 3,CNK3,Cnksr3,Connector enhancer of kinase suppressor of ras 3,Connector enhancer of KSR 3,Maguin-like protein,Parturition-related protein 4,Prp4,Rat,Rattus norvegicus
EIAAB38884 Brain-enriched WD repeat-containing protein,Bwd,Rat,Rattus norvegicus,Smu1,Smu-1 suppressor of mec-8 and unc-52 protein homolog,WD40 repeat-containing protein SMU1
EIAAB40621 D11Ertd530e,Kiaa0160,Mouse,Mus musculus,Polycomb protein Suz12,Suppressor of zeste 12 protein homolog,Suz12
EIAAB38166 ECD,Homo sapiens,hSGT1,Human,Protein ecdysoneless homolog,Protein SGT1,SGT1,Suppressor of GCR2
EIAAB14451 Cadherin family member 7,Cadherin-related tumor suppressor homolog,CDHF7,FAT,FAT1,Homo sapiens,Human,Protein fat homolog,Protocadherin Fat 1
EIAAB38888 Homo sapiens,Human,SMU1,Smu-1 suppressor of mec-8 and unc-52 protein homolog,WD40 repeat-containing protein SMU1
EIAAB38885 Mouse,Mus musculus,Smu1,Smu-1 suppressor of mec-8 and unc-52 protein homolog,WD40 repeat-containing protein SMU1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur