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Protein

Nuclear pore complex protein Nup98-Nup96

Gene

Nup98

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:109404. Nup98.

Subcellular locationi

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

  • 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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi831 – 8311K → A: Reduces interaction with NUP88. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 880880Nuclear pore complex protein Nup98PRO_0000421837Add
BLAST
Chaini881 – 1816936Nuclear pore complex protein Nup96PRO_0000421838Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Phosphoprotein

Proteomic databases

EPDiQ6PFD9.
MaxQBiQ6PFD9.
PaxDbiQ6PFD9.
PRIDEiQ6PFD9.

PTM databases

iPTMnetiQ6PFD9.

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. Interacts with RAE1. Does not interact with TPR (By similarity). Nup98 interacts directly with NUP88 and NUP214 (orthologs of yeast Nup82 and Nup159), subunits of the cytoplasmic filaments of the NPC.By similarity1 Publication

Protein-protein interaction databases

BioGridi234738. 61 interactions.
IntActiQ6PFD9. 59 interactions.
STRINGi10090.ENSMUSP00000068530.

Structurei

Secondary structure

1
1816
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi741 – 7455Combined sources
Helixi749 – 7524Combined sources
Beta strandi763 – 7697Combined sources
Turni770 – 7723Combined sources
Beta strandi773 – 7808Combined sources
Helixi788 – 7903Combined sources
Beta strandi792 – 7954Combined sources
Beta strandi798 – 80710Combined sources
Beta strandi813 – 8153Combined sources
Beta strandi819 – 8235Combined sources
Turni831 – 8333Combined sources
Helixi840 – 8456Combined sources
Helixi848 – 85710Combined sources
Turni858 – 8603Combined sources
Beta strandi862 – 8676Combined sources
Turni868 – 8714Combined sources
Beta strandi872 – 8787Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TKNX-ray3.40C/F/I732-880[»]
ProteinModelPortaliQ6PFD9.
SMRiQ6PFD9. Positions 158-213, 734-880.
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.
HOGENOMiHOG000044579.
HOVERGENiHBG052702.
InParanoidiQ6PFD9.
KOiK14297.
OrthoDBiEOG77WWBT.
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]

Sequencei

Sequence statusi: Complete.

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

Q6PFD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNKSFGTPF GGSTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG GGTTAGLFGS 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 VDENNQQDGE
660 670 680 690 700
DDSLVSRFYT NPIAKPIPQT PESVGNKNNS SSNVEDTIVA LNMRAALRNG
710 720 730 740 750
LEGSSEETSF HDESLQDDRE EIENNAYHIH 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 QEPVSASTHI ASSLGINPHV LQIMKASLLV
1010 1020 1030 1040 1050
DEEDVDAMDQ RFGHIPSKGE TVQEICSPRL PISASHSSKS RSIVGGLLQS
1060 1070 1080 1090 1100
KFASGTFLSP SASVQECRTP RTSSRMNIPS TSPWSVPLPL ATVFTVPSPA
1110 1120 1130 1140 1150
PEVQLKTVGI RRQPGLVPLE KSITYGKGKL LMDMALFMGR SFRVGWGPNW
1160 1170 1180 1190 1200
TLANSGEQLH GSHELENHQV ADSMEYGFLP NPVAVKSLSE SPFKVHLEKL
1210 1220 1230 1240 1250
GLRQRKLDED LQLYQTPLEL KLKHSTVHVD ELCPLIVPNP GVSVIHDYAD
1260 1270 1280 1290 1300
WVKDSPGDFL ELPIVKHWSL TWTLCEALWG HLKELDGQLD EPSEYIQTLE
1310 1320 1330 1340 1350
RRRAFSRWLS HTAAPQIEEE VSLTRRDSPV EAVFSYLTGS RISGACCLAQ
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
AFQNTPEGDK YACSPLPSYL EGCGCMVEEE KDSRRPLQDV CFHLLKLYSD
1510 1520 1530 1540 1550
RHYELNQLLE PRSITADPLD YRLSWHLWEV LRALNYTHLS EQCEGVLQAS
1560 1570 1580 1590 1600
YAGQLESEGL WEWAIFVFLH IDNSGMREKA VRELLTRHCQ LSETPESWAK
1610 1620 1630 1640 1650
EAFLTQKLCV PAEWIHEAKA VRAHMESNKH LEALYLFKAG HWNRCHKLVI
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 QHAPDATSNS TPDPQRVPLR LLAPHIGRLP MPEDYALEEL
1810
RGLTQSYLRE LTVGSQ
Length:1,816
Mass (Da):197,241
Last modified:April 3, 2013 - v2
Checksum:iCEB86B4A447E9750
GO

Sequence cautioni

The sequence AAH50911.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH57608.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI12913.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC118592 Genomic DNA. No translation available.
BC050911 mRNA. Translation: AAH50911.1. Sequence problems.
BC057608 mRNA. Translation: AAH57608.1. Sequence problems.
BC078630 mRNA. Translation: AAH78630.1.
BC112912 mRNA. Translation: AAI12913.1. Sequence problems.
RefSeqiNP_001274093.1. NM_001287164.1.
NP_001274094.1. NM_001287165.1.
NP_075355.1. NM_022979.2.
UniGeneiMm.439800.
Mm.486276.

Genome annotation databases

GeneIDi269966.
KEGGimmu:269966.
UCSCiuc009iqx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC118592 Genomic DNA. No translation available.
BC050911 mRNA. Translation: AAH50911.1. Sequence problems.
BC057608 mRNA. Translation: AAH57608.1. Sequence problems.
BC078630 mRNA. Translation: AAH78630.1.
BC112912 mRNA. Translation: AAI12913.1. Sequence problems.
RefSeqiNP_001274093.1. NM_001287164.1.
NP_001274094.1. NM_001287165.1.
NP_075355.1. NM_022979.2.
UniGeneiMm.439800.
Mm.486276.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TKNX-ray3.40C/F/I732-880[»]
ProteinModelPortaliQ6PFD9.
SMRiQ6PFD9. Positions 158-213, 734-880.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234738. 61 interactions.
IntActiQ6PFD9. 59 interactions.
STRINGi10090.ENSMUSP00000068530.

Protein family/group databases

MEROPSiS59.001.

PTM databases

iPTMnetiQ6PFD9.

Proteomic databases

EPDiQ6PFD9.
MaxQBiQ6PFD9.
PaxDbiQ6PFD9.
PRIDEiQ6PFD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi269966.
KEGGimmu:269966.
UCSCiuc009iqx.2. mouse.

Organism-specific databases

CTDi4928.
MGIiMGI:109404. Nup98.

Phylogenomic databases

eggNOGiKOG0845. Eukaryota.
ENOG410XPV4. LUCA.
HOGENOMiHOG000044579.
HOVERGENiHBG052702.
InParanoidiQ6PFD9.
KOiK14297.
OrthoDBiEOG77WWBT.
TreeFamiTF343335.

Miscellaneous databases

PROiQ6PFD9.
SOURCEiSearch...

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888 AND SER-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653; THR-670 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618; SER-623; SER-653; SER-680; SER-888; SER-1027; SER-1059; SER-1063; SER-1328 AND THR-1771, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  6. "Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex."
    Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.
    J. Mol. Biol. 419:330-346(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 732-880 IN COMPLEX WITH YEAST NUP82 AND NUP159, INTERACTION WITH NUP88, MUTAGENESIS OF LYS-831, SUBUNIT.

Entry informationi

Entry nameiNUP98_MOUSE
AccessioniPrimary (citable) accession number: Q6PFD9
Secondary accession number(s): Q68G59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: April 3, 2013
Last modified: June 8, 2016
This is version 95 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.