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Protein

Nucleoporin NIC96

Gene

NIC96

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.11 Publications

GO - Molecular functioni

  • structural constituent of nuclear pore Source: SGD

GO - Biological processi

  • mRNA transport Source: UniProtKB-KW
  • nuclear pore organization Source: SGD
  • protein import into nucleus Source: SGD
  • ribosomal large subunit export from nucleus Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30455-MONOMER.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NIC96
Alternative name(s):
96 kDa nucleoporin-interacting component
Nuclear pore protein NIC96
Gene namesi
Name:NIC96
Ordered Locus Names:YFR002W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFR002W.
SGDiS000001898. NIC96.

Subcellular locationi

GO - Cellular componenti

  • nuclear membrane Source: UniProtKB-SubCell
  • nuclear pore Source: SGD
  • nuclear pore linkers Source: SGD
  • nuclear pore nuclear basket Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 839839Nucleoporin NIC96PRO_0000124787Add
BLAST

Proteomic databases

MaxQBiP34077.
PeptideAtlasiP34077.

PTM databases

iPTMnetiP34077.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUP192P470543EBI-12056,EBI-25846
NUP49Q021993EBI-12056,EBI-12315
NUP57P488374EBI-12056,EBI-12324

Protein-protein interaction databases

BioGridi31150. 80 interactions.
DIPiDIP-745N.
IntActiP34077. 29 interactions.
MINTiMINT-398487.

Structurei

Secondary structure

1
839
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi206 – 22722Combined sources
Helixi234 – 24310Combined sources
Helixi248 – 26114Combined sources
Turni262 – 2654Combined sources
Helixi270 – 29324Combined sources
Helixi301 – 31111Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi320 – 3223Combined sources
Helixi333 – 3419Combined sources
Turni342 – 3443Combined sources
Helixi346 – 35510Combined sources
Helixi357 – 3593Combined sources
Helixi367 – 3737Combined sources
Turni375 – 3784Combined sources
Beta strandi384 – 3874Combined sources
Helixi388 – 39710Combined sources
Turni398 – 4003Combined sources
Beta strandi402 – 4043Combined sources
Helixi406 – 41611Combined sources
Helixi420 – 4223Combined sources
Helixi426 – 4283Combined sources
Helixi432 – 44110Combined sources
Beta strandi449 – 4524Combined sources
Helixi459 – 46911Combined sources
Helixi471 – 4744Combined sources
Helixi478 – 4847Combined sources
Helixi488 – 4969Combined sources
Helixi500 – 51213Combined sources
Helixi534 – 5429Combined sources
Turni543 – 5486Combined sources
Helixi550 – 5589Combined sources
Helixi559 – 5624Combined sources
Helixi566 – 58318Combined sources
Helixi586 – 5905Combined sources
Beta strandi595 – 5973Combined sources
Helixi603 – 6064Combined sources
Helixi609 – 6113Combined sources
Helixi616 – 63318Combined sources
Helixi637 – 64610Combined sources
Helixi650 – 66718Combined sources
Beta strandi675 – 6795Combined sources
Turni681 – 6833Combined sources
Helixi685 – 69612Combined sources
Helixi700 – 7034Combined sources
Helixi708 – 72821Combined sources
Helixi732 – 74110Combined sources
Helixi750 – 7534Combined sources
Helixi754 – 7596Combined sources
Helixi760 – 7623Combined sources
Helixi765 – 7684Combined sources
Helixi771 – 79020Combined sources
Helixi799 – 81921Combined sources
Helixi820 – 8234Combined sources
Helixi826 – 8338Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QX5X-ray2.50A/B186-839[»]
2RFOX-ray2.60A/B189-839[»]
ProteinModelPortaliP34077.
SMRiP34077. Positions 204-835.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34077.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 6036Leucine zipper-like heptad repeat, required for interaction with NSP1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi187 – 23650Asn-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000016353.
HOGENOMiHOG000093574.
InParanoidiP34077.
KOiK14309.
OMAiHTEYNQH.
OrthoDBiEOG7380D3.

Family and domain databases

InterProiIPR007231. Nucleoporin_int_Nup93/Nic96.
[Graphical view]
PANTHERiPTHR11225. PTHR11225. 1 hit.
PfamiPF04097. Nic96. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLETLRGNKL HSGTSKGANK KLNELLESSD NLPSASSELG SIQVSINELR
60 70 80 90 100
RRVFQLRSKN KASKDYTKAH YLLANSGLSF EDVDAFIKDL QTNQFLEPNP
110 120 130 140 150
PKIIESEELE FYIRTKKEEN ILMSIEQLLN GATKDFDNFI NHNLNLDWAQ
160 170 180 190 200
HKNEVMKNFG ILIQDKKTVD HKKSISSLDP KLPSWGNKGN NILNSNESRL
210 220 230 240 250
NVNENNILRE KFENYARIVF QFNNSRQANG NFDIANEFIS ILSSANGTRN
260 270 280 290 300
AQLLESWKIL ESMKSKDINI VEVGKQYLEQ QFLQYTDNLY KKNMNEGLAT
310 320 330 340 350
NVNKIKSFID TKLKKADKSW KISNLTVING VPIWALIFYL LRAGLIKEAL
360 370 380 390 400
QVLVENKANI KKVEQSFLTY FKAYASSKDH GLPVEYSTKL HTEYNQHIKS
410 420 430 440 450
SLDGDPYRLA VYKLIGRCDL SRKNIPAVTL SIEDWLWMHL MLIKEKDAEN
460 470 480 490 500
DPVYERYSLE DFQNIIISYG PSRFSNYYLQ TLLLSGLYGL AIDYTYTFSE
510 520 530 540 550
MDAVHLAIGL ASLKLFKIDS STRLTKKPKR DIRFANILAN YTKSFRYSDP
560 570 580 590 600
RVAVEYLVLI TLNEGPTDVE LCHEALRELV LETKEFTVLL GKIGRDGARI
610 620 630 640 650
PGVIEERQPL LHVRDEKEFL HTITEQAARR ADEDGRIYDS ILLYQLAEEY
660 670 680 690 700
DIVITLVNSL LSDTLSASDL DQPLVGPDDN SETNPVLLAR RMASIYFDNA
710 720 730 740 750
GISRQIHVKN KEICMLLLNI SSIRELYFNK QWQETLSQME LLDLLPFSDE
760 770 780 790 800
LSARKKAQDF SNLDDNIVKN IPNLLIITLS CISNMIHILN ESKYQSSTKG
810 820 830
QQIDSLKNVA RQCMIYAGMI QYRMPRETYS TLINIDVSL
Length:839
Mass (Da):96,174
Last modified:November 1, 1995 - v2
Checksum:i48EC3BC71281CB44
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591Missing in CAA51427 (PubMed:7688296).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72923 Genomic DNA. Translation: CAA51427.1.
D50617 Genomic DNA. Translation: BAA09241.1.
BK006940 Genomic DNA. Translation: DAA12442.1.
PIRiS35319.
RefSeqiNP_116657.1. NM_001179967.1.

Genome annotation databases

EnsemblFungiiBAA09241; BAA09241; BAA09241.
YFR002W; YFR002W; YFR002W.
GeneIDi850552.
KEGGisce:YFR002W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72923 Genomic DNA. Translation: CAA51427.1.
D50617 Genomic DNA. Translation: BAA09241.1.
BK006940 Genomic DNA. Translation: DAA12442.1.
PIRiS35319.
RefSeqiNP_116657.1. NM_001179967.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QX5X-ray2.50A/B186-839[»]
2RFOX-ray2.60A/B189-839[»]
ProteinModelPortaliP34077.
SMRiP34077. Positions 204-835.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31150. 80 interactions.
DIPiDIP-745N.
IntActiP34077. 29 interactions.
MINTiMINT-398487.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP34077.

Proteomic databases

MaxQBiP34077.
PeptideAtlasiP34077.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09241; BAA09241; BAA09241.
YFR002W; YFR002W; YFR002W.
GeneIDi850552.
KEGGisce:YFR002W.

Organism-specific databases

EuPathDBiFungiDB:YFR002W.
SGDiS000001898. NIC96.

Phylogenomic databases

GeneTreeiENSGT00390000016353.
HOGENOMiHOG000093574.
InParanoidiP34077.
KOiK14309.
OMAiHTEYNQH.
OrthoDBiEOG7380D3.

Enzyme and pathway databases

BioCyciYEAST:G3O-30455-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP34077.
PROiP34077.

Family and domain databases

InterProiIPR007231. Nucleoporin_int_Nup93/Nic96.
[Graphical view]
PANTHERiPTHR11225. PTHR11225. 1 hit.
PfamiPF04097. Nic96. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96."
    Grandi P., Doye V., Hurt E.C.
    EMBO J. 12:3061-3071(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-591.
    Strain: ATCC 204511 / S288c / AB972.
  5. "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."
    Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W.
    J. Cell Biol. 131:1133-1148(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 104-116 AND 277-291.
  6. "Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p."
    Grandi P., Schlaich N.L., Tekotte H., Hurt E.C.
    EMBO J. 14:76-87(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HEPTAD REPEAT DEPENDENT INTERACTION WITH NSP1.
  7. "Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p."
    Zabel U., Doye V., Tekotte H., Wepf R., Grandi P., Hurt E.C.
    J. Cell Biol. 133:1141-1152(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUP188.
  8. "The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex."
    Nehrbass U., Rout M.P., Maguire S., Blobel G., Wozniak R.W.
    J. Cell Biol. 133:1153-1162(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP188.
  9. "In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p."
    Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.
    Mol. Biol. Cell 8:33-46(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP57 SUBCOMPLEX.
  10. "Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane."
    Kosova B., Pante N., Rollenhagen C., Hurt E.C.
    J. Biol. Chem. 274:22646-22651(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP192.
  11. "Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p."
    Kosova B., Pante N., Rollenhagen C., Podtelejnikov A., Mann M., Aebi U., Hurt E.C.
    J. Biol. Chem. 275:343-350(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLP2.
  12. "The yeast nuclear pore complex: composition, architecture, and transport mechanism."
    Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.
    J. Cell Biol. 148:635-651(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
  13. "Yeast nuclear pore complex assembly defects determined by nuclear envelope reconstruction."
    Gomez-Ospina N., Morgan G., Giddings T.H. Jr., Kosova B., Hurt E.C., Winey M.
    J. Struct. Biol. 132:1-5(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NPC DE NOVO ASSEMBLY.
  14. "Comparative spatial localization of protein-A-tagged and authentic yeast nuclear pore complex proteins by immunogold electron microscopy."
    Fahrenkrog B., Aris J.P., Hurt E.C., Pante N., Aebi U.
    J. Struct. Biol. 129:295-305(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LOCATION WITHIN THE NPC.
  15. "The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport."
    Bailer S.M., Balduf C., Hurt E.C.
    Mol. Cell. Biol. 21:7944-7955(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NSP1 COILED-COIL DOMAIN.
  16. "Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes."
    Lusk C.P., Makhnevych T., Marelli M., Aitchison J.D., Wozniak R.W.
    J. Cell Biol. 159:267-278(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP53.
  17. "In situ analysis of spatial relationships between proteins of the nuclear pore complex."
    Damelin M., Silver P.A.
    Biophys. J. 83:3626-3636(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUP53 AND NUP120.
  18. "Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p."
    Gao H., Sumanaweera N., Bailer S.M., Stochaj U.
    J. Biol. Chem. 278:25331-25340(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEAR GSP1 IMPORT.
  19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  20. "Peering through the pore: nuclear pore complex structure, assembly, and function."
    Suntharalingam M., Wente S.R.
    Dev. Cell 4:775-789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  21. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNIC96_YEAST
AccessioniPrimary (citable) accession number: P34077
Secondary accession number(s): D6VTN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 15500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.