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Nucleoporin NIC96 (96 kDa nucleoporin-interacting component) (Nuclear pore protein NIC96)

 NIC96_YEAST             Reviewed;         839 AA.
P34077; D6VTN2;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
25-OCT-2017, entry version 164.
RecName: Full=Nucleoporin NIC96;
AltName: Full=96 kDa nucleoporin-interacting component;
AltName: Full=Nuclear pore protein NIC96;
Name=NIC96; OrderedLocusNames=YFR002W;
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], AND PARTIAL PROTEIN SEQUENCE.
PubMed=7688296;
Grandi P., Doye V., Hurt E.C.;
"Purification of NSP1 reveals complex formation with 'GLFG'
nucleoporins and a novel nuclear pore protein NIC96.";
EMBO J. 12:3061-3071(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7670463; DOI=10.1038/ng0795-261;
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
Yamazaki M., Tashiro H., Eki T.;
"Analysis of the nucleotide sequence of chromosome VI from
Saccharomyces cerevisiae.";
Nat. Genet. 10:261-268(1995).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-591.
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8789262;
DOI=10.1002/(SICI)1097-0061(199601)12:1<77::AID-YEA887>3.0.CO;2-5;
Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H.,
Shibata T., Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
Eki T., Murakami Y.;
"Sequencing of a 23 kb fragment from Saccharomyces cerevisiae
chromosome VI.";
Yeast 12:77-84(1996).
[5]
PROTEIN SEQUENCE OF 104-116 AND 277-291.
PubMed=8522578; DOI=10.1083/jcb.131.5.1133;
Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W.;
"Two novel related yeast nucleoporins Nup170p and Nup157p:
complementation with the vertebrate homologue Nup155p and functional
interactions with the yeast nuclear pore-membrane protein Pom152p.";
J. Cell Biol. 131:1133-1148(1995).
[6]
FUNCTION, AND HEPTAD REPEAT DEPENDENT INTERACTION WITH NSP1.
PubMed=7828598;
Grandi P., Schlaich N.L., Tekotte H., Hurt E.C.;
"Functional interaction of Nic96p with a core nucleoporin complex
consisting of Nsp1p, Nup49p and a novel protein Nup57p.";
EMBO J. 14:76-87(1995).
[7]
INTERACTION WITH NUP188.
PubMed=8682854; DOI=10.1083/jcb.133.6.1141;
Zabel U., Doye V., Tekotte H., Wepf R., Grandi P., Hurt E.C.;
"Nic96p is required for nuclear pore formation and functionally
interacts with a novel nucleoporin, Nup188p.";
J. Cell Biol. 133:1141-1152(1996).
[8]
FUNCTION, AND INTERACTION WITH NUP188.
PubMed=8682855; DOI=10.1083/jcb.133.6.1153;
Nehrbass U., Rout M.P., Maguire S., Blobel G., Wozniak R.W.;
"The yeast nucleoporin Nup188p interacts genetically and physically
with the core structures of the nuclear pore complex.";
J. Cell Biol. 133:1153-1162(1996).
[9]
FUNCTION, AND INTERACTION WITH NUP57 SUBCOMPLEX.
PubMed=9017593; DOI=10.1091/mbc.8.1.33;
Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.;
"In vitro reconstitution of a heterotrimeric nucleoporin complex
consisting of recombinant Nsp1p, Nup49p, and Nup57p.";
Mol. Biol. Cell 8:33-46(1997).
[10]
FUNCTION, AND INTERACTION WITH NUP192.
PubMed=10428845; DOI=10.1074/jbc.274.32.22646;
Kosova B., Pante N., Rollenhagen C., Hurt E.C.;
"Nup192p is a conserved nucleoporin with a preferential location at
the inner site of the nuclear membrane.";
J. Biol. Chem. 274:22646-22651(1999).
[11]
FUNCTION, AND INTERACTION WITH MLP2.
PubMed=10617624; DOI=10.1074/jbc.275.1.343;
Kosova B., Pante N., Rollenhagen C., Podtelejnikov A., Mann M.,
Aebi U., Hurt E.C.;
"Mlp2p, a component of nuclear pore attached intranuclear filaments,
associates with nic96p.";
J. Biol. Chem. 275:343-350(2000).
[12]
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).
[13]
FUNCTION, AND NPC DE NOVO ASSEMBLY.
PubMed=11121302; DOI=10.1006/jsbi.2000.4305;
Gomez-Ospina N., Morgan G., Giddings T.H. Jr., Kosova B., Hurt E.C.,
Winey M.;
"Yeast nuclear pore complex assembly defects determined by nuclear
envelope reconstruction.";
J. Struct. Biol. 132:1-5(2000).
[14]
FUNCTION, AND LOCATION WITHIN THE NPC.
PubMed=10806080; DOI=10.1006/jsbi.2000.4223;
Fahrenkrog B., Aris J.P., Hurt E.C., Pante N., Aebi U.;
"Comparative spatial localization of protein-A-tagged and authentic
yeast nuclear pore complex proteins by immunogold electron
microscopy.";
J. Struct. Biol. 129:295-305(2000).
[15]
FUNCTION, AND INTERACTION WITH NSP1 COILED-COIL DOMAIN.
PubMed=11689687; DOI=10.1128/MCB.21.23.7944-7955.2001;
Bailer S.M., Balduf C., Hurt E.C.;
"The Nsp1p carboxy-terminal domain is organized into functionally
distinct coiled-coil regions required for assembly of nucleoporin
subcomplexes and nucleocytoplasmic transport.";
Mol. Cell. Biol. 21:7944-7955(2001).
[16]
FUNCTION, AND INTERACTION WITH NUP53.
PubMed=12403813; DOI=10.1083/jcb.200203079;
Lusk C.P., Makhnevych T., Marelli M., Aitchison J.D., Wozniak R.W.;
"Karyopherins in nuclear pore biogenesis: a role for Kap121p in the
assembly of Nup53p into nuclear pore complexes.";
J. Cell Biol. 159:267-278(2002).
[17]
FUNCTION, AND INTERACTION WITH NUP53 AND NUP120.
PubMed=12496130; DOI=10.1016/S0006-3495(02)75363-0;
Damelin M., Silver P.A.;
"In situ analysis of spatial relationships between proteins of the
nuclear pore complex.";
Biophys. J. 83:3626-3636(2002).
[18]
FUNCTION, AND NUCLEAR GSP1 IMPORT.
PubMed=12730220; DOI=10.1074/jbc.M301607200;
Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
"Nuclear accumulation of the small GTPase Gsp1p depends on
nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-
CoA carboxylase Acc1p.";
J. Biol. Chem. 278:25331-25340(2003).
[19]
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).
[20]
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).
[21]
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).
-!- 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. NIC96, which is localized to the core of the
NPC and the distal ring of the nuclear basket, is required for de
novo assembly of NPCs. It is involved in nuclear GSP1 import.
{ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10617624,
ECO:0000269|PubMed:10806080, ECO:0000269|PubMed:11121302,
ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12403813,
ECO:0000269|PubMed:12496130, ECO:0000269|PubMed:12730220,
ECO:0000269|PubMed:7828598, ECO:0000269|PubMed:8682855,
ECO:0000269|PubMed:9017593}.
-!- 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,
SEH1 and SEC1. Due to its 8-fold rotational symmetry, all subunits
are present with 8 copies or multiples thereof. NIC96 is part of
three NPC subcomplexes, interacting with NSP1 of the NUP57
subcomplex (NIC96, NSP1, NUP49, NUP57), with NUP120 of the NUP84
subcomplex (SEH1,NUP85, NUP120, NUP145C, SEC13, NUP84, NUP133),
and with NUP53 of the NUP53-NUP59-NUP170 subcomplex. The
interaction with NUP53 is cell cycle dependent. NIC96 is also
associated with the distal ring of the nuclear basket and
interacts here with MLP2, which forms together with MLP1 nuclear
pore-attached intranuclear filaments.
{ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10617624,
ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12403813,
ECO:0000269|PubMed:12496130, ECO:0000269|PubMed:8682854,
ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9017593}.
-!- INTERACTION:
P47054:NUP192; NbExp=3; IntAct=EBI-12056, EBI-25846;
Q02199:NUP49; NbExp=3; IntAct=EBI-12056, EBI-12315;
Q03790:NUP53; NbExp=3; IntAct=EBI-12056, EBI-27321;
P48837:NUP57; NbExp=5; IntAct=EBI-12056, EBI-12324;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus
membrane; Peripheral membrane protein; Nucleoplasmic side.
Note=Symmetric distribution.
-!- MISCELLANEOUS: Present with 15500 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
family. {ECO:0000305}.
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EMBL; X72923; CAA51427.1; -; Genomic_DNA.
EMBL; D50617; BAA09241.1; -; Genomic_DNA.
EMBL; BK006940; DAA12442.1; -; Genomic_DNA.
PIR; S35319; S35319.
RefSeq; NP_116657.1; NM_001179967.1.
PDB; 2QX5; X-ray; 2.50 A; A/B=186-839.
PDB; 2RFO; X-ray; 2.60 A; A/B=189-839.
PDBsum; 2QX5; -.
PDBsum; 2RFO; -.
ProteinModelPortal; P34077; -.
SMR; P34077; -.
BioGrid; 31150; 83.
DIP; DIP-745N; -.
IntAct; P34077; 31.
MINT; MINT-398487; -.
STRING; 4932.YFR002W; -.
TCDB; 1.I.1.1.1; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P34077; -.
MaxQB; P34077; -.
PRIDE; P34077; -.
EnsemblFungi; BAA09241; BAA09241; BAA09241.
EnsemblFungi; YFR002W; YFR002W; YFR002W.
GeneID; 850552; -.
KEGG; sce:YFR002W; -.
EuPathDB; FungiDB:YFR002W; -.
SGD; S000001898; NIC96.
GeneTree; ENSGT00390000016353; -.
HOGENOM; HOG000093574; -.
InParanoid; P34077; -.
KO; K14309; -.
OMA; IAFLFRM; -.
OrthoDB; EOG092C0JRR; -.
BioCyc; YEAST:G3O-30455-MONOMER; -.
EvolutionaryTrace; P34077; -.
PRO; PR:P34077; -.
Proteomes; UP000002311; Chromosome VI.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:SGD.
GO; GO:0044612; C:nuclear pore linkers; IDA:SGD.
GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
GO; GO:0051292; P:nuclear pore complex assembly; IBA:GO_Central.
GO; GO:0006999; P:nuclear pore organization; IMP:SGD.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
PANTHER; PTHR11225; PTHR11225; 1.
Pfam; PF04097; Nic96; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Membrane;
mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
Reference proteome; Translocation; Transport.
CHAIN 1 839 Nucleoporin NIC96.
/FTId=PRO_0000124787.
REGION 25 60 Leucine zipper-like heptad repeat,
required for interaction with NSP1.
COMPBIAS 187 236 Asn-rich.
CONFLICT 59 59 Missing (in Ref. 1; CAA51427).
{ECO:0000305}.
HELIX 206 227 {ECO:0000244|PDB:2QX5}.
HELIX 234 243 {ECO:0000244|PDB:2QX5}.
HELIX 248 261 {ECO:0000244|PDB:2QX5}.
TURN 262 265 {ECO:0000244|PDB:2QX5}.
HELIX 270 293 {ECO:0000244|PDB:2QX5}.
HELIX 301 311 {ECO:0000244|PDB:2QX5}.
STRAND 312 314 {ECO:0000244|PDB:2QX5}.
STRAND 316 318 {ECO:0000244|PDB:2QX5}.
STRAND 320 322 {ECO:0000244|PDB:2QX5}.
HELIX 333 341 {ECO:0000244|PDB:2QX5}.
TURN 342 344 {ECO:0000244|PDB:2QX5}.
HELIX 346 355 {ECO:0000244|PDB:2QX5}.
HELIX 357 359 {ECO:0000244|PDB:2QX5}.
HELIX 367 373 {ECO:0000244|PDB:2QX5}.
TURN 375 378 {ECO:0000244|PDB:2RFO}.
STRAND 384 387 {ECO:0000244|PDB:2RFO}.
HELIX 388 397 {ECO:0000244|PDB:2RFO}.
TURN 398 400 {ECO:0000244|PDB:2RFO}.
STRAND 402 404 {ECO:0000244|PDB:2RFO}.
HELIX 406 416 {ECO:0000244|PDB:2QX5}.
HELIX 420 422 {ECO:0000244|PDB:2QX5}.
HELIX 426 428 {ECO:0000244|PDB:2QX5}.
HELIX 432 441 {ECO:0000244|PDB:2QX5}.
STRAND 449 452 {ECO:0000244|PDB:2RFO}.
HELIX 459 469 {ECO:0000244|PDB:2QX5}.
HELIX 471 474 {ECO:0000244|PDB:2QX5}.
HELIX 478 484 {ECO:0000244|PDB:2QX5}.
HELIX 488 496 {ECO:0000244|PDB:2QX5}.
HELIX 500 512 {ECO:0000244|PDB:2QX5}.
HELIX 534 542 {ECO:0000244|PDB:2QX5}.
TURN 543 548 {ECO:0000244|PDB:2QX5}.
HELIX 550 558 {ECO:0000244|PDB:2QX5}.
HELIX 559 562 {ECO:0000244|PDB:2QX5}.
HELIX 566 583 {ECO:0000244|PDB:2QX5}.
HELIX 586 590 {ECO:0000244|PDB:2QX5}.
STRAND 595 597 {ECO:0000244|PDB:2RFO}.
HELIX 603 606 {ECO:0000244|PDB:2QX5}.
HELIX 609 611 {ECO:0000244|PDB:2QX5}.
HELIX 616 633 {ECO:0000244|PDB:2QX5}.
HELIX 637 646 {ECO:0000244|PDB:2QX5}.
HELIX 650 667 {ECO:0000244|PDB:2QX5}.
STRAND 675 679 {ECO:0000244|PDB:2RFO}.
TURN 681 683 {ECO:0000244|PDB:2QX5}.
HELIX 685 696 {ECO:0000244|PDB:2QX5}.
HELIX 700 703 {ECO:0000244|PDB:2QX5}.
HELIX 708 728 {ECO:0000244|PDB:2QX5}.
HELIX 732 741 {ECO:0000244|PDB:2QX5}.
HELIX 750 753 {ECO:0000244|PDB:2RFO}.
HELIX 754 759 {ECO:0000244|PDB:2QX5}.
HELIX 760 762 {ECO:0000244|PDB:2QX5}.
HELIX 765 768 {ECO:0000244|PDB:2QX5}.
HELIX 771 790 {ECO:0000244|PDB:2QX5}.
HELIX 799 819 {ECO:0000244|PDB:2QX5}.
HELIX 820 823 {ECO:0000244|PDB:2QX5}.
HELIX 826 833 {ECO:0000244|PDB:2QX5}.
SEQUENCE 839 AA; 96174 MW; 48EC3BC71281CB44 CRC64;
MLETLRGNKL HSGTSKGANK KLNELLESSD NLPSASSELG SIQVSINELR RRVFQLRSKN
KASKDYTKAH YLLANSGLSF EDVDAFIKDL QTNQFLEPNP PKIIESEELE FYIRTKKEEN
ILMSIEQLLN GATKDFDNFI NHNLNLDWAQ HKNEVMKNFG ILIQDKKTVD HKKSISSLDP
KLPSWGNKGN NILNSNESRL NVNENNILRE KFENYARIVF QFNNSRQANG NFDIANEFIS
ILSSANGTRN AQLLESWKIL ESMKSKDINI VEVGKQYLEQ QFLQYTDNLY KKNMNEGLAT
NVNKIKSFID TKLKKADKSW KISNLTVING VPIWALIFYL LRAGLIKEAL QVLVENKANI
KKVEQSFLTY FKAYASSKDH GLPVEYSTKL HTEYNQHIKS SLDGDPYRLA VYKLIGRCDL
SRKNIPAVTL SIEDWLWMHL MLIKEKDAEN DPVYERYSLE DFQNIIISYG PSRFSNYYLQ
TLLLSGLYGL AIDYTYTFSE MDAVHLAIGL ASLKLFKIDS STRLTKKPKR DIRFANILAN
YTKSFRYSDP RVAVEYLVLI TLNEGPTDVE LCHEALRELV LETKEFTVLL GKIGRDGARI
PGVIEERQPL LHVRDEKEFL HTITEQAARR ADEDGRIYDS ILLYQLAEEY DIVITLVNSL
LSDTLSASDL DQPLVGPDDN SETNPVLLAR RMASIYFDNA GISRQIHVKN KEICMLLLNI
SSIRELYFNK QWQETLSQME LLDLLPFSDE LSARKKAQDF SNLDDNIVKN IPNLLIITLS
CISNMIHILN ESKYQSSTKG QQIDSLKNVA RQCMIYAGMI QYRMPRETYS TLINIDVSL


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EIAAB28096 160 kDa nucleoporin,Gene trap locus 1-13 protein,Gtl1-13,GTL-13,Kiaa0197,Mouse,Mus musculus,Nuclear pore complex protein Nup160,Nucleoporin Nup160,Nup160


 

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