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Nucleoporin SEH1 (GATOR complex protein SEH1) (Nup107-160 subcomplex subunit SEH1) (SEC13-like protein)

 SEH1_HUMAN              Reviewed;         360 AA.
Q96EE3; A8K5B1; Q8NFU6; Q96MH3; Q9C069;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 3.
20-JUN-2018, entry version 158.
RecName: Full=Nucleoporin SEH1 {ECO:0000305};
AltName: Full=GATOR complex protein SEH1 {ECO:0000305};
AltName: Full=Nup107-160 subcomplex subunit SEH1;
AltName: Full=SEC13-like protein;
Name=SEH1L; Synonyms=SEC13L, SEH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Liver;
Pan H., Yu Y., Shen L., Huo K.-K., Li Y.-Y.;
"cDNA cloning of a human homolog of yeast SEH1 gene.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=12196509; DOI=10.1083/jcb.200206106;
Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.;
"Proteomic analysis of the mammalian nuclear pore complex.";
J. Cell Biol. 158:915-927(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT ASN-342.
TISSUE=Adrenal gland;
Li Y., Gu Y., Peng Y., Fu S., Gu J., Zhang L., Jiang C., Yu Y.,
Han Z., Wang Y., Chen Z., Fu G.;
"A novel gene expressed in human adrenal gland.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT
ASN-342.
TISSUE=Skeletal muscle;
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 A).
TISSUE=Eye;
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).
[6]
FUNCTION, ASSOCIATION WITH THE NUP107-160 COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=15146057; DOI=10.1091/mbc.E03-12-0878;
Loieodice I., Alves A., Rabut G., Van Overbeek M., Ellenberg J.,
Sibarita J.-B., Doye V.;
"The entire Nup107-160 complex, including three new members, is
targeted as one entity to kinetochores in mitosis.";
Mol. Biol. Cell 15:3333-3344(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17363900; DOI=10.1038/sj.emboj.7601642;
Zuccolo M., Alves A., Galy V., Bolhy S., Formstecher E., Racine V.,
Sibarita J.-B., Fukagawa T., Shiekhattar R., Yen T., Doye V.;
"The human Nup107-160 nuclear pore subcomplex contributes to proper
kinetochore functions.";
EMBO J. 26:1853-1864(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
NUP107-160 COMPLEX.
PubMed=17360435; DOI=10.1073/pnas.0700058104;
Glavy J.S., Krutchinsky A.N., Cristea I.M., Berke I.C., Boehmer T.,
Blobel G., Chait B.T.;
"Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160
subcomplex.";
Proc. Natl. Acad. Sci. U.S.A. 104:3811-3816(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 (ISOFORM B), 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-190, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[11]
INTERACTION WITH SESN1; SESN2 AND SESN3.
PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
"The Sestrins interact with GATOR2 to negatively regulate the amino-
acid-sensing pathway upstream of mTORC1.";
Cell Rep. 9:1-8(2014).
[12]
FUNCTION, AND INTERACTION WITH SESN2.
PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C.,
Akopiants K., Guan K.L., Karin M., Budanov A.V.;
"Sestrins inhibit mTORC1 kinase activation through the GATOR
complex.";
Cell Rep. 9:1281-1291(2014).
[13]
INTERACTION WITH CASTOR2 AND CASTOR1.
PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K.,
Wyant G.A., Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
"The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
Cell 165:153-164(2016).
[14]
FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG
PROTEINS.
PubMed=23723238; DOI=10.1126/science.1232044;
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
Sabatini D.M.;
"A Tumor suppressor complex with GAP activity for the Rag GTPases that
signal amino acid sufficiency to mTORC1.";
Science 340:1100-1106(2013).
[15]
FUNCTION.
PubMed=27487210; DOI=10.1038/nature19079;
Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
Sabatini D.M.;
"Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
Nature 536:229-233(2016).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
SUBCELLULAR LOCATION.
PubMed=28199306; DOI=10.1038/nature21423;
Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M.,
Shen K., Condon K.J., Petri S., Kedir J., Scaria S.M.,
Abu-Remaileh M., Frankel W.N., Sabatini D.M.;
"KICSTOR recruits GATOR1 to the lysosome and is necessary for
nutrients to regulate mTORC1.";
Nature 543:438-442(2017).
-!- FUNCTION: Component of the Nup107-160 subcomplex of the nuclear
pore complex (NPC). The Nup107-160 subcomplex is required for the
assembly of a functional NPC. The Nup107-160 subcomplex is also
required for normal kinetochore microtubule attachment, mitotic
progression and chromosome segregation. This subunit plays a role
in recruitment of the Nup107-160 subcomplex to the kinetochore.
{ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}.
-!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
within the amino acid-sensing branch of the TORC1 signaling
pathway. Indirectly activates mTORC1 and the TORC1 signaling
pathway through the inhibition of the GATOR1 subcomplex
(PubMed:23723238). It is negatively regulated by the upstream
amino acid sensors SESN2 and CASTOR1 (PubMed:25457612,
PubMed:27487210). {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
-!- SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear
pore complex (NPC). The Nup107-160 subcomplex includes NUP160,
NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. The
SEH1 subunit appears to be only weakly associated with the Nup107-
160 subcomplex. Within the GATOR complex, component of the GATOR2
subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR
complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC
heterodimers (PubMed:17360435, PubMed:23723238). The GATOR2
complex interacts with CASTOR2 and CASTOR1; the interaction is
negatively regulated by arginine (PubMed:26972053). The GATOR2
complex interacts with SESN1, SESN2 and SESN3; the interaction is
negatively regulated by amino acids (PubMed:25263562,
PubMed:25457612). {ECO:0000269|PubMed:17360435,
ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25263562,
ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053}.
-!- INTERACTION:
Q9BW27:NUP85; NbExp=3; IntAct=EBI-922818, EBI-716392;
P55735:SEC13; NbExp=3; IntAct=EBI-922818, EBI-1046596;
-!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}.
Nucleus, nuclear pore complex {ECO:0000269|PubMed:15146057,
ECO:0000269|PubMed:17363900}. Lysosome membrane
{ECO:0000269|PubMed:28199306}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=SEH1A;
IsoId=Q96EE3-2; Sequence=Displayed;
Name=B; Synonyms=SEH1B;
IsoId=Q96EE3-1; Sequence=VSP_037954;
Note=Contains a phosphoserine at position 365.
{ECO:0000244|PubMed:18669648};
-!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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EMBL; AF255625; AAM21169.1; -; mRNA.
EMBL; AF431970; AAM44214.1; -; mRNA.
EMBL; AF514996; AAM76707.1; -; mRNA.
EMBL; AF136976; AAG49437.1; -; mRNA.
EMBL; AK056940; BAB71317.1; -; mRNA.
EMBL; AK291226; BAF83915.1; -; mRNA.
EMBL; BC012430; AAH12430.1; -; mRNA.
CCDS; CCDS32791.1; -. [Q96EE3-1]
CCDS; CCDS45832.1; -. [Q96EE3-2]
RefSeq; NP_001013455.1; NM_001013437.1. [Q96EE3-1]
RefSeq; NP_112493.2; NM_031216.3. [Q96EE3-2]
UniGene; Hs.301048; -.
PDB; 5A9Q; EM; 23.00 A; 7/G/P/Y=1-360.
PDBsum; 5A9Q; -.
ProteinModelPortal; Q96EE3; -.
BioGrid; 123629; 81.
CORUM; Q96EE3; -.
IntAct; Q96EE3; 64.
MINT; Q96EE3; -.
STRING; 9606.ENSP00000382779; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q96EE3; -.
PhosphoSitePlus; Q96EE3; -.
SwissPalm; Q96EE3; -.
BioMuta; SEH1L; -.
DMDM; 257051064; -.
EPD; Q96EE3; -.
PaxDb; Q96EE3; -.
PeptideAtlas; Q96EE3; -.
PRIDE; Q96EE3; -.
ProteomicsDB; 76398; -.
ProteomicsDB; 76399; -. [Q96EE3-1]
DNASU; 81929; -.
Ensembl; ENST00000262124; ENSP00000262124; ENSG00000085415. [Q96EE3-2]
Ensembl; ENST00000399892; ENSP00000382779; ENSG00000085415. [Q96EE3-1]
GeneID; 81929; -.
KEGG; hsa:81929; -.
UCSC; uc002krq.5; human. [Q96EE3-2]
CTD; 81929; -.
EuPathDB; HostDB:ENSG00000085415.15; -.
GeneCards; SEH1L; -.
HGNC; HGNC:30379; SEH1L.
HPA; HPA039964; -.
MIM; 609263; gene.
neXtProt; NX_Q96EE3; -.
OpenTargets; ENSG00000085415; -.
PharmGKB; PA134912135; -.
eggNOG; KOG2445; Eukaryota.
eggNOG; ENOG410XRNW; LUCA.
GeneTree; ENSGT00550000074999; -.
HOGENOM; HOG000216896; -.
InParanoid; Q96EE3; -.
KO; K14299; -.
OMA; IYEAPDI; -.
OrthoDB; EOG091G09MA; -.
PhylomeDB; Q96EE3; -.
TreeFam; TF105924; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; Q96EE3; -.
SIGNOR; Q96EE3; -.
ChiTaRS; SEH1L; human.
GenomeRNAi; 81929; -.
PRO; PR:Q96EE3; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000085415; -.
CleanEx; HS_SEH1L; -.
ExpressionAtlas; Q96EE3; baseline and differential.
Genevisible; Q96EE3; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0034629; P:cellular protein-containing complex localization; IMP:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0002534; P:cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0006999; P:nuclear pore organization; IMP:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
GO; GO:0016032; P:viral process; TAS:Reactome.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR037597; Nucleoporin_Seh1.
InterPro; IPR037363; Sec13/Seh1_fam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR11024; PTHR11024; 1.
PANTHER; PTHR11024:SF3; PTHR11024:SF3; 1.
Pfam; PF00400; WD40; 2.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Centromere; Chromosome; Chromosome partition; Complete proteome;
Isopeptide bond; Kinetochore; Lysosome; Membrane; Mitosis;
mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
Translocation; Transport; Ubl conjugation; WD repeat.
CHAIN 1 360 Nucleoporin SEH1.
/FTId=PRO_0000051213.
REPEAT 10 49 WD 1.
REPEAT 55 96 WD 2.
REPEAT 111 152 WD 3.
REPEAT 160 210 WD 4.
REPEAT 217 258 WD 5.
REPEAT 276 315 WD 6.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 12 12 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 358 360 KHS -> YFFTPLDSPRAGSRWSSYAQLLPPPPPPLVEHSC
DADTANLQYPHPRRRYLSRPLNPLPENEGI (in
isoform B). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_037954.
VARIANT 342 342 T -> N (in dbSNP:rs6505776).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.3}.
/FTId=VAR_053417.
CONFLICT 78 78 S -> P (in Ref. 4; BAB71317).
{ECO:0000305}.
SEQUENCE 360 AA; 39649 MW; FB9ED2440C4EC9AB CRC64;
MFVARSIAAD HKDLIHDVSF DFHGRRMATC SSDQSVKVWD KSESGDWHCT ASWKTHSGSV
WRVTWAHPEF GQVLASCSFD RTAAVWEEIV GESNDKLRGQ SHWVKRTTLV DSRTSVTDVK
FAPKHMGLML ATCSADGIVR IYEAPDVMNL SQWSLQHEIS CKLSCSCISW NPSSSRAHSP
MIAVGSDDSS PNAMAKVQIF EYNENTRKYA KAETLMTVTD PVHDIAFAPN LGRSFHILAI
ATKDVRIFTL KPVRKELTSS GGPTKFEIHI VAQFDNHNSQ VWRVSWNITG TVLASSGDDG
CVRLWKANYM DNWKCTGILK GNGSPVNGSS QQGTSNPSLG STIPSLQNSL NGSSAGRKHS


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EIAAB28088 107 kDa nucleoporin,Homo sapiens,Human,Nuclear pore complex protein Nup107,Nucleoporin Nup107,NUP107
EIAAB28087 107 kDa nucleoporin,Nuclear pore complex protein Nup107,Nucleoporin Nup107,Nup107,p105,Rat,Rattus norvegicus
EIAAB28086 107 kDa nucleoporin,Mouse,Mus musculus,Nuclear pore complex protein Nup107,Nucleoporin Nup107,Nup107
CSB-EL020972MO Mouse SEH1-like (S. cerevisiae) (SEH1L) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL020972HU Human SEH1-like (S. cerevisiae) (SEH1L) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL020972BO Bovine SEH1-like (S. cerevisiae) (SEH1L) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
SEH1L SEH1L Gene SEH1-like (S. cerevisiae)
EIAAB28277 Homo sapiens,Human,Nucleoporin Nup37,Nup107-160 subcomplex subunit Nup37,NUP37,p37
EIAAB28278 Homo sapiens,Human,Nucleoporin Nup43,Nup107-160 subcomplex subunit Nup43,NUP43,p42
EIAAB28276 Mouse,Mus musculus,Nucleoporin Nup37,Nup107-160 subcomplex subunit Nup37,Nup37
EIAAB28279 Mouse,Mus musculus,Nucleoporin Nup43,Nup107-160 subcomplex subunit Nup43,Nup43
EIAAB37775 D3S1231E,Homo sapiens,Human,Protein SEC13 homolog,SEC13,SEC13L1,SEC13-like protein 1,SEC13R,SEC13-related protein
EIAAB37778 Mouse,Mus musculus,Protein SEC13 homolog,Sec13,Sec13l1,SEC13-like protein 1,SEC13-related protein


 

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