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_MOUSE             Reviewed;         790 AA.
Q9Z2G6; Q9DBD8;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
28-FEB-2018, entry version 146.
RecName: Full=Protein sel-1 homolog 1;
AltName: Full=Suppressor of lin-12-like protein 1;
Short=Sel-1L;
Flags: Precursor;
Name=Sel1l; Synonyms=Sel1h;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=9858735; DOI=10.1016/S0925-4773(98)00146-4;
Donoviel D.B., Donoviel M.S., Fan E., Hadjantonakis A.-K.,
Bernstein A.;
"Cloning and characterization of Sel-1l, a murine homolog of the C.
elegans sel-1 gene.";
Mech. Dev. 78:203-207(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Liver;
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]
FUNCTION, DEVELOPMENTAL STAGE, AND MISCELLANEOUS.
PubMed=20170518; DOI=10.1186/1471-213X-10-19;
Li S., Francisco A.B., Munroe R.J., Schimenti J.C., Long Q.;
"SEL1L deficiency impairs growth and differentiation of pancreatic
epithelial cells.";
BMC Dev. Biol. 10:19-19(2010).
[4]
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).
[5]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
INTERACTION WITH SYVN1; LPL AND LMF1.
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).
[6]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24453213; DOI=10.1073/pnas.1318114111;
Sun S., Shi G., Han X., Francisco A.B., Ji Y., Mendonca N., Liu X.,
Locasale J.W., Simpson K.W., Duhamel G.E., Kersten S., Yates J.R. III,
Long Q., Qi L.;
"Sel1L is indispensable for mammalian endoplasmic reticulum-associated
degradation, endoplasmic reticulum homeostasis, and survival.";
Proc. Natl. Acad. Sci. U.S.A. 111:E582-E591(2014).
[7] {ECO:0000244|PDB:5B26}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 348-533, SUBUNIT,
INTERACTION WITH SYVN1, REGION, AND MUTAGENESIS OF 512-GLY-GLY-513;
515-ILE-LEU-516; TYR-519 AND LEU-521.
PubMed=27064360; DOI=10.1038/srep20261;
Jeong H., Sim H.J., Song E.K., Lee H., Ha S.C., Jun Y., Park T.J.,
Lee C.;
"Crystal structure of SEL1L: Insight into the roles of SLR motifs in
ERAD pathway.";
Sci. Rep. 6:20261-20261(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:25066055, PubMed:24453213).
Enhances SYVN1 stability (PubMed:24453213). Plays a role in LPL
maturation and secretion (PubMed:25066055). Required for normal
differentiation of the pancreas epithelium, and for normal
exocrine function and survival of pancreatic cells
(PubMed:20170518, PubMed:24453213). May play a role in Notch
signaling (PubMed:20170518). {ECO:0000269|PubMed:20170518,
ECO:0000269|PubMed:24453213, ECO:0000269|PubMed:25066055}.
-!- SUBUNIT: Homodimer and homooligomer (PubMed:27064360). Interacts
with SYVN1; the interaction is direct (PubMed:25066055,
PubMed:27064360). Part of a complex containing SEL1L, SYVN1 and
DERL2. May form a complex with ERLEC1, HSPA5, OS9, and SYVN1.
Interacts with FOXRED2 and EDEM1 (By similarity). Interacts with
LPL and LMF1; may stabilize the complex formed by LPL and LMF1 and
thereby promote the export of LPL dimers (PubMed:25066055).
{ECO:0000250|UniProtKB:Q9UBV2, ECO:0000269|PubMed:25066055,
ECO:0000269|PubMed:27064360}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9UBV2}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9UBV2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z2G6-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z2G6-2; Sequence=VSP_004384;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas, white adipose
tissue, liver and spleen (at protein level) (PubMed:25066055,
PubMed:24453213). Detected in heart, brain, spleen, lung, liver,
kidney and testis (PubMed:9858735). {ECO:0000269|PubMed:24453213,
ECO:0000269|PubMed:25066055, ECO:0000269|PubMed:9858735}.
-!- DEVELOPMENTAL STAGE: First detected at 12.5 dpc in a small number
of pancreas epithelial cells. Highly expressed in embryonic
pancreas epithelium at later stages of embryonic development.
{ECO:0000269|PubMed:20170518}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}.
-!- DISRUPTION PHENOTYPE: Taxomifen-inducible gene disruption in adult
mice leads to premature death within 3 weeks after the onset of
taxomifen treatment. Mice progressively loose weight and become
moribund despite increased food intake and normal blood glucose
levels, suggesting nutrient maladsorption. After eight days of
treatment, the pancreas was diffusely dark red and soft,
suggesting severe pancreas atrophy. Still, the endocrine parts of
the pancreas were not affected. Pancreas weight was about half of
that of wild-type, the size of secretory zymogen granules was
reduced and pancreatic lipase and alpha-amylase levels were
strongly reduced. Besides, the morphology of the endoplasmic
reticulum in pancreas acinar cells was abnormal, with swollen and
fragmented cisternae. Likewise, SYVN1 protein levels are
decreased, while those of other ERAD markers are increased
(PubMed:24453213). Adipocyte-specific gene disruption does not
give rise to any obvious phenotype when mice are kept on a low-fat
diet. Mutant mice are resistant to diet-induced obesity when kept
on a high-fat diet, in spite of normal food intake and physical
activity. Mutant mice show dramatically reduced accumulation of
fat mass relative to wild-type, while lean mass is not affected.
Intriguingly, mutant mice display enlarged livers that develop
steatosis and increased triglyceride levels. Mutant mice display
increased fasting serum triglyceride and insulin levels. Likewise,
mutant mice display hypertriglyceridemia after feeding, especially
on a high-fat diet. In spite of increased cellular LPL levels, LPL
secretion is reduced by 80 to 90% (PubMed:25066055).
{ECO:0000269|PubMed:24453213, ECO:0000269|PubMed:25066055}.
-!- MISCELLANEOUS: Gene disruption after residue 465 and replacement
of the C-terminus with a beta-galactosidase-neomycin reporter gene
construct leads to complete embryonic lethality; most die before
13.5 dpc. Only 5% of the embryos are viable at 15.5 dpc. Mutant
embryos display defects in the differentiation of the pancreas
epithelium. The defects in pancreas differentiation can be
alleviated by pharmacological inhibition of Notch signaling (in
vitro). {ECO:0000269|PubMed:20170518}.
-!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF063095; AAD05210.1; -; mRNA.
EMBL; AK005023; BAB23750.1; -; mRNA.
CCDS; CCDS26091.1; -. [Q9Z2G6-1]
CCDS; CCDS49137.1; -. [Q9Z2G6-2]
RefSeq; NP_001034178.1; NM_001039089.1. [Q9Z2G6-1]
RefSeq; NP_035474.1; NM_011344.2. [Q9Z2G6-2]
UniGene; Mm.250605; -.
PDB; 5B26; X-ray; 2.60 A; A/B/C/D=348-533.
PDBsum; 5B26; -.
ProteinModelPortal; Q9Z2G6; -.
SMR; Q9Z2G6; -.
BioGrid; 203153; 5.
DIP; DIP-61846N; -.
IntAct; Q9Z2G6; 8.
MINT; Q9Z2G6; -.
STRING; 10090.ENSMUSP00000021347; -.
iPTMnet; Q9Z2G6; -.
PhosphoSitePlus; Q9Z2G6; -.
PaxDb; Q9Z2G6; -.
PRIDE; Q9Z2G6; -.
Ensembl; ENSMUST00000021347; ENSMUSP00000021347; ENSMUSG00000020964. [Q9Z2G6-1]
Ensembl; ENSMUST00000167466; ENSMUSP00000129384; ENSMUSG00000020964. [Q9Z2G6-2]
GeneID; 20338; -.
KEGG; mmu:20338; -.
UCSC; uc007oky.1; mouse. [Q9Z2G6-1]
CTD; 6400; -.
MGI; MGI:1329016; Sel1l.
eggNOG; KOG1550; Eukaryota.
eggNOG; COG0790; LUCA.
GeneTree; ENSGT00530000063170; -.
HOVERGEN; HBG057766; -.
InParanoid; Q9Z2G6; -.
KO; K14026; -.
OMA; LAQMAMG; -.
OrthoDB; EOG091G0315; -.
TreeFam; TF315257; -.
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
Reactome; R-MMU-901032; ER Quality Control Compartment (ERQC).
ChiTaRS; Sel1l; mouse.
PRO; PR:Q9Z2G6; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020964; -.
CleanEx; MM_SEL1L; -.
ExpressionAtlas; Q9Z2G6; baseline and differential.
Genevisible; Q9Z2G6; MM.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
GO; GO:0006641; P:triglyceride metabolic process; IMP:UniProtKB.
CDD; cd00062; FN2; 1.
Gene3D; 1.25.40.10; -; 3.
Gene3D; 2.10.10.10; -; 1.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR006597; Sel1-like.
InterPro; IPR011990; TPR-like_helical_dom_sf.
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;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Membrane;
Notch signaling pathway; Phosphoprotein; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 790 Protein sel-1 homolog 1.
/FTId=PRO_0000022296.
TOPO_DOM 22 734 Lumenal. {ECO:0000255}.
TRANSMEM 735 755 Helical. {ECO:0000255}.
TOPO_DOM 756 790 Cytoplasmic. {ECO:0000255}.
DOMAIN 118 166 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 179 214 Sel1-like 1.
REPEAT 215 250 Sel1-like 2.
REPEAT 251 286 Sel1-like 3.
REPEAT 287 322 Sel1-like 4.
REPEAT 369 405 Sel1-like 5.
REPEAT 406 442 Sel1-like 6.
REPEAT 443 478 Sel1-like 7.
REPEAT 479 514 Sel1-like 8.
REPEAT 515 550 Sel1-like 9.
REPEAT 623 658 Sel1-like 10.
REPEAT 660 695 Sel1-like 11.
REGION 23 733 Interaction with ERLEC1, OS9 and SYVN1.
{ECO:0000250}.
REGION 348 533 Important for homodimerization and
oligomerization.
{ECO:0000269|PubMed:27064360}.
REGION 639 719 Interaction with SYVN1.
{ECO:0000269|PubMed:27064360}.
REGION 734 790 Mediates retention in the endoplasmic
reticulum. {ECO:0000250}.
COMPBIAS 766 789 Pro-rich.
MOD_RES 64 64 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBV2}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 604 604 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 123 149 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 137 164 {ECO:0000255|PROSITE-ProRule:PRU00479}.
VAR_SEQ 116 166 GTAHGEPCHFPFLFLDKEYDECTSDGREDGRLWCATTYDYK
TDEKWGFCET -> A (in isoform 2).
{ECO:0000303|PubMed:9858735}.
/FTId=VSP_004384.
MUTAGEN 512 513 GG->KK: Abolishes homodimerization.
{ECO:0000269|PubMed:27064360}.
MUTAGEN 515 516 IL->AA: Abolishes homodimerization; when
associated with A-519.
{ECO:0000269|PubMed:27064360}.
MUTAGEN 519 519 Y->A: Abolishes homodimerization; when
associated with 515-A-A-516.
{ECO:0000269|PubMed:27064360}.
MUTAGEN 521 521 L->A: Abolishes homodimerization.
{ECO:0000269|PubMed:27064360}.
HELIX 354 365 {ECO:0000244|PDB:5B26}.
HELIX 369 381 {ECO:0000244|PDB:5B26}.
HELIX 390 402 {ECO:0000244|PDB:5B26}.
HELIX 406 417 {ECO:0000244|PDB:5B26}.
STRAND 421 423 {ECO:0000244|PDB:5B26}.
HELIX 427 439 {ECO:0000244|PDB:5B26}.
HELIX 443 454 {ECO:0000244|PDB:5B26}.
STRAND 457 459 {ECO:0000244|PDB:5B26}.
HELIX 463 475 {ECO:0000244|PDB:5B26}.
HELIX 479 490 {ECO:0000244|PDB:5B26}.
STRAND 493 496 {ECO:0000244|PDB:5B26}.
HELIX 499 510 {ECO:0000244|PDB:5B26}.
HELIX 517 521 {ECO:0000244|PDB:5B26}.
SEQUENCE 790 AA; 88340 MW; 47869F2AFB59B936 CRC64;
MQVRVRLSLL LLCAVLLGSA AATSDDKTNQ DDSLDSKSSL PTDESVKDHT TTGKVVAGQI
FVDSEEAEVE SLLQDEEDSS KTQEEEISFL ESPNPSSKTY EELKRVRKPV LTAIEGTAHG
EPCHFPFLFL DKEYDECTSD GREDGRLWCA TTYDYKTDEK WGFCETEEDA AKRRQMQEAE
MIYQAGMKIL NGSNRKSQKR EAYRYLQKAA GMNHTKALER VSYALLFGDY LTQNIQAAKE
MFEKLTEEGS PKGQTGLGFL YASGLGVNSS QAKALVYYTF GALGGNLIAH MILGYRYWAG
IGVLQSCESA LTHYRLVANH VASDISLTGG SVVQRIRLPD EVENPGMNSG MLEEDLIQYY
QFLAEKGDVQ AQVGLGQLHL HGGRGVEQNH QRAFDYFNLA ANAGNSHAMA FLGKMYSEGS
DIVPQSNETA LHYFKKAADM GNPVGQSGLG MAYLYGRGVQ VNYDLALKYF QKAAEQGWVD
GQLQLGSMYY NGIGVKRDYK QALKYFNLAS QGGHILAFYN LAQMHASGTG VMRSCHTAVE
LFKNVCERGR WSERLMTAYN SYKDEDYNAA VVQYLLLAEQ GYEVAQSNAA FILDQREATI
VGENETYPRA LLHWNRAASQ GYTVARIKLG DYHFYGFGTD VDYETAFIHY RLASEQQHSA
QAMFNLGYMH EKGLGIKQDI HLAKRFYDMA AEASPDAQVP VFLALCKLGV VYFLQYIREA
NIRDLFTQLD MDQLLGPEWD LYLMTIIALL LGTVIAYRQR QHQDIPVPRP PGPRPAPPQQ
EGPPEQQPPQ


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