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Protein

Nuclear pore complex protein Nup98-Nup96

Gene

Nup98

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC.

GO - Molecular functioni

  • nuclear localization sequence binding Source: RGD
  • peptide binding Source: RGD
  • structural constituent of nuclear pore Source: UniProtKB

GO - Biological processi

  • DNA replication Source: Ensembl
  • mRNA transport Source: UniProtKB-KW
  • nuclear pore complex assembly Source: UniProtKB
  • protein import into nucleus, docking Source: RGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-RNO-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-RNO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5578749. Transcriptional regulation by small RNAs.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.

Protein family/group databases

MEROPSiS59.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup98-Nup96
Cleaved into the following 2 chains:
Alternative name(s):
98 kDa nucleoporin
Nucleoporin Nup98
Short name:
Nup98
Alternative name(s):
96 kDa nucleoporin
Nucleoporin Nup96
Short name:
Nup96
Gene namesi
Name:Nup98
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi71033. Nup98.

Subcellular locationi

  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Nucleoplasmic side By similarity
  • Nucleusnuclear pore complex 1 Publication

  • Note: NUP98 is localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket. Dissociates from the dissasembled NPC structure early during prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear basket of NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection.By similarity

GO - Cellular componenti

  • kinetochore Source: Ensembl
  • nuclear inclusion body Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nuclear periphery Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nuclear pore nuclear basket Source: UniProtKB
  • nuclear pore outer ring Source: UniProtKB
  • nucleoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 880880Nuclear pore complex protein Nup98PRO_0000204890Add
BLAST
Chaini881 – 1816936Nuclear pore complex protein Nup96PRO_0000405578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241PhosphoserineBy similarity
Modified residuei603 – 6031N6-acetyllysineBy similarity
Modified residuei608 – 6081PhosphoserineBy similarity
Modified residuei612 – 6121PhosphoserineBy similarity
Modified residuei618 – 6181PhosphoserineBy similarity
Modified residuei623 – 6231PhosphoserineCombined sources
Modified residuei625 – 6251PhosphoserineBy similarity
Modified residuei653 – 6531PhosphoserineCombined sources
Modified residuei670 – 6701PhosphothreonineBy similarity
Modified residuei673 – 6731PhosphoserineBy similarity
Modified residuei680 – 6801PhosphoserineBy similarity
Modified residuei681 – 6811PhosphoserineBy similarity
Modified residuei839 – 8391PhosphoserineBy similarity
Modified residuei888 – 8881PhosphoserineCombined sources
Modified residuei934 – 9341PhosphoserineCombined sources
Modified residuei1027 – 10271PhosphoserineBy similarity
Modified residuei1042 – 10421PhosphoserineBy similarity
Modified residuei1059 – 10591PhosphoserineBy similarity
Modified residuei1063 – 10631PhosphoserineBy similarity
Modified residuei1069 – 10691PhosphothreonineBy similarity
Modified residuei1328 – 13281PhosphoserineBy similarity
Modified residuei1771 – 17711PhosphothreonineBy similarity

Post-translational modificationi

The N-terminus is blocked.
Isoform 1 is autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively. Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96.

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Phosphoprotein

Proteomic databases

PaxDbiP49793.
PRIDEiP49793.

PTM databases

iPTMnetiP49793.
PhosphoSiteiP49793.

Expressioni

Gene expression databases

ExpressionAtlasiP49793. baseline and differential.
GenevisibleiP49793. RN.

Interactioni

Subunit structurei

Part of the nuclear pore complex (NPC). Nup98 interacts directly with Nup96. Nup96 is part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus. Nup98 interacts directly with NUP88 and NUP214, subunits of the cytoplasmic filaments of the NPC. Interacts with RAE1. Does not interact with TPR (By similarity).By similarity

Protein-protein interaction databases

BioGridi249610. 1 interaction.
STRINGi10116.ENSRNOP00000027575.

Structurei

3D structure databases

ProteinModelPortaliP49793.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini738 – 880143Peptidase S59PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156FG repeats 1Add
BLAST
Regioni157 – 21357GLEBS; interaction with RAE1By similarityAdd
BLAST
Regioni214 – 480267FG repeats 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 481475Gly/Thr-richAdd
BLAST
Compositional biasi890 – 8945Poly-Glu

Domaini

Contains G-L-F-G repeats. The FG repeat domains have a direct role in the transport (By similarity).By similarity

Sequence similaritiesi

Belongs to the nucleoporin GLFG family.Curated
Contains 1 peptidase S59 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0845. Eukaryota.
ENOG410XPV4. LUCA.
GeneTreeiENSGT00550000074799.
HOGENOMiHOG000044579.
HOVERGENiHBG052702.
InParanoidiP49793.
KOiK14297.
OMAiKQHCITA.
OrthoDBiEOG77WWBT.
PhylomeDBiP49793.
TreeFamiTF343335.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49793-1) [UniParc]FASTAAdd to basket

Also known as: Nup98-Nup96 precursor

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTANTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GNTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSAF
260 270 280 290 300
SYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTPNTGF
310 320 330 340 350
SFGNTSTLGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQPNTGFGAV GSTLFGNNKL TTFGTSTTSA PSFGTTSGGL FGNKPTLTLG
410 420 430 440 450
TNTNTSNFGF GTNNSGSSIF GSKPAAGTLG TGLGTGFGTA LGAGQASLFG
460 470 480 490 500
NNQPKIGGPL GTGAFGAPGF NTSTAILGFG APQAPVALTD PNASAAQQAV
510 520 530 540 550
LQQHLNSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY
560 570 580 590 600
KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
610 620 630 640 650
VLKNLNNSNL FSPVNHDSED LASPSEYPEN GERFSFLSKP VDENHQQDGD
660 670 680 690 700
DDSLVSRFYT NPIAKPIPQT PESAGNKNNS SSNVEDTFIA LNMRAALRNG
710 720 730 740 750
LEGSSEETSF HDESLQDDRD EIENSAFQIH PAGIVLTKVG YYTIPSMDDL
760 770 780 790 800
AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVI
810 820 830 840 850
VYVDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG
860 870 880 890 900
RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPPKTT
910 920 930 940 950
SKKLKTAPLP PAGQATTFQM TLNGKPAPPP QSQSPEVEQL GRVVELDSDM
960 970 980 990 1000
VDITQEPVPD SVLEESVPED QEPVSASTQI ASSLGINPHV LQIMKASLLV
1010 1020 1030 1040 1050
DEEDVDAMEQ RFGHFPSRGD TAQEICSPRL PISASHSSKS RSIVGGLLQS
1060 1070 1080 1090 1100
KFASGTFLSP SASVQECRTP RTSSLMNVPS TSPWSVPLPL ATVFTVPSPA
1110 1120 1130 1140 1150
PEVPLKTVGI RRQPGLVPLE KSITYGKGKL LMDMALFMGR SFRVGWGPNW
1160 1170 1180 1190 1200
TLANSGEQLH GSHELENHQV AESMEYGFLP NPVAVKSLSE SPFKVHLEKL
1210 1220 1230 1240 1250
GLRQRKLDED LQLYQTPLEL KLKHSTVHVD ELCPLIVPNP GVSVIHGYAD
1260 1270 1280 1290 1300
WVKKSPRDLL ELPIVKHWSL TWTLCEALWG HLKELDSQLD EPSEYIQTLE
1310 1320 1330 1340 1350
RRRAFSRWLS HTAAPQIEEE VSLTRRDSPI EAVFSYLTGS RISEACCLAQ
1360 1370 1380 1390 1400
QSGDHRLALL LSQLVGSQSV RELLTMQLAD WHQLQADSFI HDERLRIFAL
1410 1420 1430 1440 1450
LAGKPVWQLS EQKQINVCSQ LDWKRTLAIH LWYLLPPTAS ISRALSMYEE
1460 1470 1480 1490 1500
AFQNTCEGDK YACPPLPSYL EGSGCVVEEE KDPQRPLQDV CFHLLKLYSD
1510 1520 1530 1540 1550
RHYGLNQLLE PRSITADPLD YRLSWHLWEV LRALNYTHLS EQCEGVLQAS
1560 1570 1580 1590 1600
YAGQLESEGL WEWAIFVFLH IDNSGMREKA VRELLTRHCQ LSETPESWAK
1610 1620 1630 1640 1650
ETFLTQKLCV PAEWIHEAKA VRAHMESNKH LEALYLFKAG HWNRCHKLVV
1660 1670 1680 1690 1700
RHLASDAIIN ENYDYLKGFL EDLAPPERSS LIQDWETSGL VYLDYIRVIE
1710 1720 1730 1740 1750
MLHRIQQVDC SGYELEHLHT KVTSLCNRIE QIPCYNAKDR LAQSDMAKRV
1760 1770 1780 1790 1800
ANLLRVVLSL QHTPDATSNS TPDPQRVPLR LLAPHIGRLP MPEDYALEEL
1810
RGLTQSYLRE LTVGSQ
Length:1,816
Mass (Da):197,283
Last modified:March 8, 2011 - v2
Checksum:i70A7D8E23D542B42
GO
Isoform 2 (identifier: P49793-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     930-938: PQSQSPEVE → TSGREGQRM
     939-1816: Missing.

Show »
Length:938
Mass (Da):97,928
Checksum:i541463D374531C1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111Missing in AAC42054 (PubMed:7736573).Curated
Sequence conflicti46 – 461N → S in AAC42054 (PubMed:7736573).Curated
Sequence conflicti68 – 681F → L in AAC42054 (PubMed:7736573).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei930 – 9389PQSQSPEVE → TSGREGQRM in isoform 2. 1 PublicationVSP_040702
Alternative sequencei939 – 1816878Missing in isoform 2. 1 PublicationVSP_040703Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473956 Genomic DNA. Translation: EDM18207.1.
L39991 mRNA. Translation: AAC42054.1.
PIRiA56517.
RefSeqiNP_112336.2. NM_031074.2. [P49793-1]
XP_006229954.1. XM_006229892.2. [P49793-1]
UniGeneiRn.11324.

Genome annotation databases

EnsembliENSRNOT00000027575; ENSRNOP00000027575; ENSRNOG00000020347. [P49793-1]
GeneIDi81738.
KEGGirno:81738.
UCSCiRGD:71033. rat. [P49793-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473956 Genomic DNA. Translation: EDM18207.1.
L39991 mRNA. Translation: AAC42054.1.
PIRiA56517.
RefSeqiNP_112336.2. NM_031074.2. [P49793-1]
XP_006229954.1. XM_006229892.2. [P49793-1]
UniGeneiRn.11324.

3D structure databases

ProteinModelPortaliP49793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249610. 1 interaction.
STRINGi10116.ENSRNOP00000027575.

Protein family/group databases

MEROPSiS59.001.

PTM databases

iPTMnetiP49793.
PhosphoSiteiP49793.

Proteomic databases

PaxDbiP49793.
PRIDEiP49793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027575; ENSRNOP00000027575; ENSRNOG00000020347. [P49793-1]
GeneIDi81738.
KEGGirno:81738.
UCSCiRGD:71033. rat. [P49793-1]

Organism-specific databases

CTDi4928.
RGDi71033. Nup98.

Phylogenomic databases

eggNOGiKOG0845. Eukaryota.
ENOG410XPV4. LUCA.
GeneTreeiENSGT00550000074799.
HOGENOMiHOG000044579.
HOVERGENiHBG052702.
InParanoidiP49793.
KOiK14297.
OMAiKQHCITA.
OrthoDBiEOG77WWBT.
PhylomeDBiP49793.
TreeFamiTF343335.

Enzyme and pathway databases

ReactomeiR-RNO-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-RNO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5578749. Transcriptional regulation by small RNAs.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.

Miscellaneous databases

PROiP49793.

Gene expression databases

ExpressionAtlasiP49793. baseline and differential.
GenevisibleiP49793. RN.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex."
    Radu A., Moore M.S., Blobel G.
    Cell 81:215-222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    Strain: Brown Norway.
  3. "A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96."
    Fontoura B.M.A., Blobel G., Matunis M.J.
    J. Cell Biol. 144:1097-1112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPROTEOLYTIC CLEAVAGE.
  4. "Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
    Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
    J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-653; SER-888 AND SER-934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUP98_RAT
AccessioniPrimary (citable) accession number: P49793
Secondary accession number(s): D3ZMW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 8, 2011
Last modified: June 8, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.