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Nucleoporin NUP100/NSP100 (Nuclear pore protein NUP100/NSP100)

 NU100_YEAST             Reviewed;         959 AA.
Q02629; D6VXL9;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
13-FEB-2019, entry version 178.
RecName: Full=Nucleoporin NUP100/NSP100;
AltName: Full=Nuclear pore protein NUP100/NSP100;
Name=NUP100; Synonyms=NSP100; OrderedLocusNames=YKL068W;
ORFNames=YKL336;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1385442; DOI=10.1083/jcb.119.4.705;
Wente S.R., Rout M.P., Blobel G.;
"A new family of yeast nuclear pore complex proteins.";
J. Cell Biol. 119:705-723(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091863; DOI=10.1002/yea.320100009;
Rasmussen S.W.;
"Sequence of a 20.7 kb region of yeast chromosome XI includes the
NUP100 gene, an open reading frame (ORF) possibly representing a
nucleoside diphosphate kinase gene, tRNAs for His, Val and Trp in
addition to seven ORFs with weak or no significant similarity to known
proteins.";
Yeast 10:S69-S74(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, AND MRNA-BINDING MOTIF.
PubMed=8044840; DOI=10.1016/0092-8674(94)90297-6;
Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C.;
"Nup145p is required for nuclear export of mRNA and binds
homopolymeric RNA in vitro via a novel conserved motif.";
Cell 78:275-289(1994).
[6]
FUNCTION, AND INTERACTION WITH KAP95.
PubMed=8557738; DOI=10.1083/jcb.131.6.1699;
Iovine M.K., Watkins J.L., Wente S.R.;
"The GLFG repetitive region of the nucleoporin Nup116p interacts with
Kap95p, an essential yeast nuclear import factor.";
J. Cell Biol. 131:1699-1713(1995).
[7]
CHARACTERIZATION, AND NPC SUBUNIT LOCATION.
PubMed=10684247; DOI=10.1083/jcb.148.4.635;
Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y.,
Chait B.T.;
"The yeast nuclear pore complex: composition, architecture, and
transport mechanism.";
J. Cell Biol. 148:635-651(2000).
[8]
FUNCTION, AND INTERACTION WITH MEX67.
PubMed=11104765; DOI=10.1074/jbc.M008311200;
Strawn L.A., Shen T.X., Wente S.R.;
"The GLFG regions of Nup116p and Nup100p serve as binding sites for
both Kap95p and Mex67p at the nuclear pore complex.";
J. Biol. Chem. 276:6445-6452(2001).
[9]
FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
PubMed=11387327; DOI=10.1074/jbc.M102629200;
Allen N.P., Huang L., Burlingame A., Rexach M.;
"Proteomic analysis of nucleoporin interacting proteins.";
J. Biol. Chem. 276:29268-29274(2001).
[10]
FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION, AND INTERACTION
WITH KAP95.
PubMed=12372823; DOI=10.1074/jbc.M209037200;
Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.;
"GLFG and FxFG nucleoporins bind to overlapping sites on importin-
beta.";
J. Biol. Chem. 277:50597-50606(2002).
[11]
FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
PubMed=12543930; DOI=10.1074/mcp.T200012-MCP200;
Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A.,
Lutzmann M., Hurt E.C., Rexach M.;
"Deciphering networks of protein interactions at the nuclear pore
complex.";
Mol. Cell. Proteomics 1:930-946(2002).
[12]
FUNCTION, AND AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
PubMed=12917401; DOI=10.1074/jbc.M307135200;
Pyhtila B., Rexach M.;
"A gradient of affinity for the karyopherin Kap95p along the yeast
nuclear pore complex.";
J. Biol. Chem. 278:42699-42709(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
FUNCTION, AND FG REPEAT STRUCTURE.
PubMed=12604785; DOI=10.1073/pnas.0437902100;
Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
"Disorder in the nuclear pore complex: the FG repeat regions of
nucleoporins are natively unfolded.";
Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
[15]
FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
PubMed=15039779; DOI=10.1038/ncb1097;
Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
"Minimal nuclear pore complexes define FG repeat domains essential for
transport.";
Nat. Cell Biol. 6:197-206(2004).
[16]
REVIEW.
PubMed=12791264; DOI=10.1016/S1534-5807(03)00162-X;
Suntharalingam M., Wente S.R.;
"Peering through the pore: nuclear pore complex structure, assembly,
and function.";
Dev. Cell 4:775-789(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763 AND SER-783, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Functions as a component of the nuclear pore complex
(NPC). NPC components, collectively referred to as nucleoporins
(NUPs), can play the role of both NPC structural components and of
docking or interaction partners for transiently associated nuclear
transport factors. Active directional transport is assured by
both, a Phe-Gly (FG) repeat affinity gradient for these transport
factors across the NPC and a transport cofactor concentration
gradient across the nuclear envelope (GSP1 and GSP2 GTPases
associated predominantly with GTP in the nucleus, with GDP in the
cytoplasm). NUP100 plays an important role in several nuclear
export and import pathways including poly(A)+ RNA and protein
transport. {ECO:0000269|PubMed:11104765,
ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:12372823,
ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785,
ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779,
ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8557738}.
-!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive
means of nucleocytoplasmic transport. NPCs allow the passive
diffusion of ions and small molecules and the active, nuclear
transport receptor-mediated bidirectional transport of
macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs),
and ribosomal subunits across the nuclear envelope. The 55-60 MDa
NPC is composed of at least 31 different subunits: ASM4, CDC31,
GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120,
NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42,
NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34,
SEC13 and SEH1. Due to its 8-fold rotational symmetry, all
subunits are present with 8 copies or multiples thereof. Through
its FG repeats NUP100 interacts with numerous karyopherins
including KAP95, and MEX67. {ECO:0000269|PubMed:11104765,
ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:8557738}.
-!- INTERACTION:
Q06142:KAP95; NbExp=6; IntAct=EBI-11698, EBI-9145;
Q02630:NUP116; NbExp=4; IntAct=EBI-11698, EBI-11703;
P49686:NUP42; NbExp=2; IntAct=EBI-11698, EBI-12310;
P48837:NUP57; NbExp=3; IntAct=EBI-11698, EBI-12324;
P52891:NUP84; NbExp=2; IntAct=EBI-11698, EBI-12337;
P46673:NUP85; NbExp=4; IntAct=EBI-11698, EBI-12345;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus
membrane; Peripheral membrane protein; Nucleoplasmic side.
Note=Biased towards cytoplasmic side.
-!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
karyopherins (importins, exportins) and form probably an affinity
gradient, guiding the transport proteins unidirectionally with
their cargo through the NPC. FG repeat regions are highly flexible
and lack ordered secondary structure. The overall conservation of
FG repeats regarding exact sequence, spacing, and repeat unit
length is limited. FG repeat types and their physico-chemical
environment change across the NPC from the nucleoplasmic to the
cytoplasmic side: GLFG repeats are especially abundant in NUPs in
the central region (lacking a charged environment but are enriched
in Ser, Thr, Gln, and Asn).
-!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z15035; CAA78753.1; -; Genomic_DNA.
EMBL; X75780; CAA53406.1; -; Genomic_DNA.
EMBL; Z28068; CAA81905.1; -; Genomic_DNA.
EMBL; BK006944; DAA09089.1; -; Genomic_DNA.
PIR; B44402; B44402.
RefSeq; NP_012855.1; NM_001179634.1.
DisProt; DP01076; -.
ProteinModelPortal; Q02629; -.
SMR; Q02629; -.
BioGrid; 34065; 131.
ComplexPortal; CPX-824; Nuclear pore complex.
DIP; DIP-2351N; -.
IntAct; Q02629; 31.
MINT; Q02629; -.
STRING; 4932.YKL068W; -.
MEROPS; S59.A09; -.
TCDB; 1.I.1.1.1; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q02629; -.
MaxQB; Q02629; -.
PaxDb; Q02629; -.
PRIDE; Q02629; -.
DNASU; 853796; -.
EnsemblFungi; YKL068W_mRNA; YKL068W_mRNA; YKL068W.
GeneID; 853796; -.
KEGG; sce:YKL068W; -.
EuPathDB; FungiDB:YKL068W; -.
SGD; S000001551; NUP100.
GeneTree; ENSGT00550000074799; -.
HOGENOM; HOG000093958; -.
InParanoid; Q02629; -.
KO; K14297; -.
OMA; FGQNNTQ; -.
BioCyc; YEAST:G3O-31864-MONOMER; -.
PRO; PR:Q02629; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0016021; C:integral component of membrane; ISM:SGD.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:SGD.
GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0017056; F:structural constituent of nuclear pore; IDA:SGD.
GO; GO:0006406; P:mRNA export from nucleus; IPI:SGD.
GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:SGD.
GO; GO:0000973; P:posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
GO; GO:0006606; P:protein import into nucleus; IGI:SGD.
GO; GO:0036228; P:protein localization to nuclear inner membrane; IGI:SGD.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central.
Gene3D; 3.30.1610.10; -; 1.
InterPro; IPR025574; Nucleoporin_FG_rpt.
InterPro; IPR037665; Nucleoporin_S59-like.
InterPro; IPR037637; NUP98-NUP96.
InterPro; IPR007230; Peptidase_S59.
InterPro; IPR036903; Peptidase_S59_sf.
PANTHER; PTHR23198; PTHR23198; 3.
PANTHER; PTHR23198:SF6; PTHR23198:SF6; 3.
Pfam; PF04096; Nucleoporin2; 1.
Pfam; PF13634; Nucleoporin_FG; 4.
SUPFAM; SSF82215; SSF82215; 1.
PROSITE; PS51434; NUP_C; 1.
1: Evidence at protein level;
Complete proteome; Membrane; mRNA transport; Nuclear pore complex;
Nucleus; Phosphoprotein; Protein transport; Reference proteome;
Repeat; Translocation; Transport.
CHAIN 1 959 Nucleoporin NUP100/NSP100.
/FTId=PRO_0000204830.
REPEAT 2 3 FG 1.
REPEAT 9 10 FG 2.
REPEAT 17 17 FG 3.
REPEAT 21 24 SLFG 1; approximate.
REPEAT 33 36 SLFG 2.
REPEAT 51 54 SLFG 3; approximate.
REPEAT 66 69 SLFG 4.
REPEAT 77 80 GLFG 1; approximate.
REPEAT 89 92 SLFG 5; approximate.
REPEAT 105 106 FG 4.
REPEAT 112 115 GLFG 2; approximate.
REPEAT 131 134 SLFG 6; approximate.
REPEAT 145 146 FG 5.
REPEAT 157 160 SLFG 7.
REPEAT 168 171 GLFG 3; approximate.
REPEAT 175 178 SLFG 8; approximate.
REPEAT 189 190 FG 6.
REPEAT 202 205 SLFG 9.
REPEAT 210 213 SLFG 10; approximate.
REPEAT 220 223 SLFG 11.
REPEAT 233 234 FG 7.
REPEAT 242 245 SLFG 12; approximate.
REPEAT 253 256 SLFG 13.
REPEAT 271 274 GLFG 4.
REPEAT 287 290 GLFG 5.
REPEAT 300 303 GLFG 6; approximate.
REPEAT 318 321 SLFG 14.
REPEAT 333 336 GLFG 7.
REPEAT 345 348 GLFG 8.
REPEAT 358 361 GLFG 9.
REPEAT 379 382 GLFG 10.
REPEAT 393 396 GLFG 11.
REPEAT 405 408 SLFG 15.
REPEAT 417 420 SLFG 16.
REPEAT 436 439 SLFG 17.
REPEAT 448 449 FG 8.
REPEAT 462 465 SLFG 18.
REPEAT 474 477 SLFG 19; approximate.
REPEAT 490 493 GLFG 12.
REPEAT 506 509 GLFG 13.
REPEAT 523 526 GLFG 14.
REPEAT 542 543 FG 9.
REPEAT 550 553 GLFG 15.
REPEAT 569 570 FG 10.
DOMAIN 814 956 Peptidase S59. {ECO:0000255|PROSITE-
ProRule:PRU00765}.
REGION 816 955 Nucleoporin RNA-binding motif (NRM).
COMPBIAS 32 386 Asn-rich.
COMPBIAS 37 43 Poly-Asn.
COMPBIAS 52 570 Gly-rich.
COMPBIAS 312 317 Poly-Asn.
COMPBIAS 337 390 Gln-rich.
COMPBIAS 387 390 Poly-Gln.
MOD_RES 763 763 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
SEQUENCE 959 AA; 99988 MW; D3985F9901BBAA51 CRC64;
MFGNNRPMFG GSNLSFGSNT SSFGGQQSQQ PNSLFGNSNN NNNSTSNNAQ SGFGGFTSAA
GSNSNSLFGN NNTQNNGAFG QSMGATQNSP FGSLNSSNAS NGNTFGGSSS MGSFGGNTNN
AFNNNSNSTN SPFGFNKPNT GGTLFGSQNN NSAGTSSLFG GQSTSTTGTF GNTGSSFGTG
LNGNGSNIFG AGNNSQSNTT GSLFGNQQSS AFGTNNQQGS LFGQQSQNTN NAFGNQNQLG
GSSFGSKPVG SGSLFGQSNN TLGNTTNNRN GLFGQMNSSN QGSSNSGLFG QNSMNSSTQG
VFGQNNNQMQ INGNNNNSLF GKANTFSNSA SGGLFGQNNQ QQGSGLFGQN SQTSGSSGLF
GQNNQKQPNT FTQSNTGIGL FGQNNNQQQQ STGLFGAKPA GTTGSLFGGN SSTQPNSLFG
TTNVPTSNTQ SQQGNSLFGA TKLTNMPFGG NPTANQSGSG NSLFGTKPAS TTGSLFGNNT
ASTTVPSTNG LFGNNANNST STTNTGLFGA KPDSQSKPAL GGGLFGNSNS NSSTIGQNKP
VFGGTTQNTG LFGATGTNSS AVGSTGKLFG QNNNTLNVGT QNVPPVNNTT QNALLGTTAV
PSLQQAPVTN EQLFSKISIP NSITNPVKAT TSKVNADMKR NSSLTSAYRL APKPLFAPSS
NGDAKFQKWG KTLERSDRGS STSNSITDPE SSYLNSNDLL FDPDRRYLKH LVIKNNKNLN
VINHNDDEAS KVKLVTFTTE SASKDDQASS SIAASKLTEK AHSPQTDLKD DHDESTPDPQ
SKSPNGSTSI PMIENEKISS KVPGLLSNDV TFFKNNYYIS PSIETLGNKS LIELRKINNL
VIGHRNYGKV EFLEPVDLLN TPLDTLCGDL VTFGPKSCSI YENCSIKPEK GEGINVRCRV
TLYSCFPIDK ETRKPIKNIT HPLLKRSIAK LKENPVYKFE SYDPVTGTYS YTIDHPVLT


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EIAAB28301 93 kDa nucleoporin,CBP-interacting protein 4,Cip4,Kiaa0095,Mouse,Mus musculus,Nuclear pore complex protein Nup93,Nucleoporin Nup93,Nup93
EIAAB28109 214 kDa nucleoporin,CAIN,CAN,Homo sapiens,Human,KIAA0023,Nuclear pore complex protein Nup214,Nucleoporin Nup214,NUP214,Protein CAN
EIAAB29455 Mouse,Mus musculus,Nuclear pore membrane glycoprotein 210-like,Nucleoporin 210 kDa-like,Nucleoporin Nup210-like,Nup210l
EIAAB29454 Homo sapiens,Human,Nuclear pore membrane glycoprotein 210-like,Nucleoporin 210 kDa-like,Nucleoporin Nup210-like,NUP210L
EIAAB28097 160 kDa nucleoporin,Homo sapiens,Human,KIAA0197,Nuclear pore complex protein Nup160,Nucleoporin Nup160,NUP120,NUP160
EIAAB28108 205 kDa nucleoporin,C7orf14,Homo sapiens,Human,KIAA0225,Nuclear pore complex protein Nup205,Nucleoporin Nup205,NUP205
EIAAB28292 85 kDa nucleoporin,FROUNT,Mouse,Mus musculus,Nuclear pore complex protein Nup85,Nucleoporin Nup85,Nup85,Pcnt1,Pericentrin-1
EIAAB28093 155 kDa nucleoporin,Homo sapiens,Human,KIAA0791,Nuclear pore complex protein Nup155,Nucleoporin Nup155,NUP155
EIAAB28294 85 kDa nucleoporin,Nuclear pore complex protein Nup85,Nucleoporin Nup85,Nup85,Pcnt1,Pericentrin-1,Rat,Rattus norvegicus
EIAAB28302 93 kDa nucleoporin,Homo sapiens,Human,KIAA0095,Nuclear pore complex protein Nup93,Nucleoporin Nup93,NUP93

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1502: Mitochondrial biogenesis
WP211: BMP signaling pathway
WP1049: G Protein Signaling Pathways
WP1068: Nuclear Receptors
WP1099: Nuclear receptors in lipid metabolism and toxicity
WP1165: G Protein Signaling Pathways
WP1184: Nuclear Receptors
WP1326: Nuclear receptors in lipid metabolism and toxicity
WP1371: G Protein Signaling Pathways
WP1385: Nuclear Receptors
WP139: Nuclear receptors in lipid metabolism and toxicity
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism

Related Genes :
[NUP100 NSP100 YKL068W YKL336] Nucleoporin NUP100/NSP100 (Nuclear pore protein NUP100/NSP100)
[NUP116 NSP116 YMR047C YM9532.12C] Nucleoporin NUP116/NSP116 (Nuclear pore protein NUP116/NSP116)
[NUP84 YDL116W] Nucleoporin NUP84 (Nuclear pore protein NUP84)
[NUP57 YGR119C G6320] Nucleoporin NUP57 (Nuclear pore protein NUP57)
[NUP85 RAT9 YJR042W J1624] Nucleoporin NUP85 (Nuclear pore protein NUP85)
[NUP42 RIP1 UIP1 YDR192C YD9346.04C] Nucleoporin NUP42 (Nuclear pore protein NUP42)
[GLE2 RAE1 YER107C] Nucleoporin GLE2 (Nuclear pore protein GLE2) (poly(A) RNA export protein RAE1)
[NUP145 RAT10 YGL092W] Nucleoporin NUP145 (EC 3.4.21.-) (Nuclear pore protein NUP145) [Cleaved into: Nucleoporin NUP145N (N-NUP145); Nucleoporin NUP145C (C-NUP145)]
[NIC96 YFR002W] Nucleoporin NIC96 (96 kDa nucleoporin-interacting component) (Nuclear pore protein NIC96)
[npp-5 F07A11.3] Nuclear pore complex protein 5 (Nuclear pore complex protein Nup107) (Nucleoporin npp-5)
[NUP107] Nuclear pore complex protein Nup107 (107 kDa nucleoporin) (Nucleoporin Nup107)
[POM152 YMR129W YM9553.05] Nucleoporin POM152 (Nuclear pore protein POM152) (P150) (Pore membrane protein POM152)
[NDC1 YML031W] Nucleoporin NDC1 (Nuclear division cycle protein 1) (Nuclear pore protein NDC1)
[NSP1 YJL041W J1207] Nucleoporin NSP1 (Nuclear pore protein NSP1) (Nucleoskeletal-like protein) (p110)
[NUP49 NSP49 YGL172W G1648] Nucleoporin NUP49/NSP49 (Nuclear pore protein NUP49/NSP49)
[NUP170 NLE3 YBL079W YBL0725] Nucleoporin NUP170 (Nuclear pore protein NUP170)
[NUP159 NUP158 RAT7 YIL115C] Nucleoporin NUP159 (Nuclear pore protein NUP159)
[NUP157 YER105C] Nucleoporin NUP157 (Nuclear pore protein NUP157)
[NUP133 RAT3 YKR082W YKR402] Nucleoporin NUP133 (Nuclear pore protein NUP133)
[NUP2 YLR335W L8300.9] Nucleoporin NUP2 (Nuclear pore protein NUP2) (p95)
[NUP1 YOR098C YOR3182C] Nucleoporin NUP1 (Nuclear pore protein NUP1)
[NUP82 YJL061W HRB187 J1135] Nucleoporin NUP82 (Nuclear pore protein NUP82)
[NUP60 FUN17 YAR002W] Nucleoporin NUP60 (Nuclear pore protein NUP60)
[NUP120 RAT2 YKL057C YKL313 YKL314] Nucleoporin NUP120 (Nuclear pore protein NUP120)
[SEH1 YGL100W] Nucleoporin SEH1 (Nuclear pore protein SEH1) (SEC13 homolog 1)
[GLE1 BRR3 RSS1 YDL207W D1049] Nucleoporin GLE1 (Nuclear pore protein GLE1) (RNA export factor GLE1)
[NUP53 YMR153W YM8520.02] Nucleoporin NUP53 (Nuclear pore protein NUP53)
[ASM4 NUP59 YDL088C D2420] Nucleoporin ASM4 (Nuclear pore protein NUP59)
[NUP188 YML103C] Nucleoporin NUP188 (Nuclear pore protein NUP188)
[CDC31 DSK1 YOR257W] Cell division control protein 31 (Nuclear pore protein CDC31) (Nucleoporin CDC31)

Bibliography :
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