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Protein

Nuclear pore complex protein Nup98-Nup96

Gene

NUP98

Organism
Homo sapiens (Human)
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. Nup98 and Nup96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC.1 Publication

GO - Molecular functioni

  • nuclear localization sequence binding Source: GO_Central
  • nucleocytoplasmic transporter activity Source: GO_Central
  • RNA binding Source: GO_Central
  • structural constituent of nuclear pore Source: UniProtKB
  • transporter activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110713-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiP52948.

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
Synonyms:ADAR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8068. NUP98.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nuclear envelope Source: UniProtKB
  • nuclear inclusion body Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nuclear periphery Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nuclear pore cytoplasmic filaments Source: GO_Central
  • nuclear pore nuclear basket Source: UniProtKB
  • nuclear pore outer ring Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23.

A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1.

A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1.

A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1.

A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4.

A chromosomal aberration involving NUP98 has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse promotes the proliferative capacity and self-renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro-megakaryocytic lineage.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei531 – 532Breakpoint for translocation to form NUP98-CCDC28A2
Sitei531 – 532Breakpoint for translocation to form NUP98-PHF23 oncogene2

Organism-specific databases

DisGeNETi4928.
OpenTargetsiENSG00000110713.
PharmGKBiPA31856.

Polymorphism and mutation databases

BioMutaiNUP98.
DMDMi308153660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000199291 – 880Nuclear pore complex protein Nup98Add BLAST880
ChainiPRO_0000019930881 – 1817Nuclear pore complex protein Nup96Add BLAST937

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei524PhosphoserineCombined sources1
Modified residuei603N6-acetyllysineCombined sources1
Modified residuei608PhosphoserineCombined sources1
Modified residuei612PhosphoserineCombined sources1
Modified residuei618PhosphoserineCombined sources1
Modified residuei623PhosphoserineCombined sources1
Modified residuei625PhosphoserineCombined sources1
Modified residuei653PhosphoserineBy similarity1
Modified residuei670PhosphothreonineCombined sources1
Modified residuei673PhosphoserineCombined sources1
Modified residuei681PhosphoserineCombined sources1
Modified residuei683PhosphoserineCombined sources1
Modified residuei839PhosphoserineCombined sources1
Modified residuei888PhosphoserineCombined sources1
Modified residuei897PhosphoserineCombined sources1
Modified residuei934PhosphoserineCombined sources1
Modified residuei1000PhosphothreonineCombined sources1
Modified residuei1023PhosphoserineCombined sources1
Modified residuei1028PhosphoserineCombined sources1
Modified residuei1043PhosphoserineCombined sources1
Modified residuei1060PhosphoserineCombined sources1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1070PhosphothreonineCombined sources1
Modified residuei1329PhosphoserineBy similarity1
Modified residuei1772PhosphothreonineBy similarity1

Post-translational modificationi

Isoform 1 to isoform 4 are 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 Nup96.1 Publication
Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Phosphoprotein

Proteomic databases

EPDiP52948.
MaxQBiP52948.
PaxDbiP52948.
PeptideAtlasiP52948.
PRIDEiP52948.

PTM databases

iPTMnetiP52948.
PhosphoSitePlusiP52948.

Miscellaneous databases

PMAP-CutDBP52948.

Expressioni

Gene expression databases

BgeeiENSG00000110713.
ExpressionAtlasiP52948. baseline and differential.
GenevisibleiP52948. HS.

Organism-specific databases

HPAiCAB016725.

Interactioni

Subunit structurei

Part of the nuclear pore complex (NPC). Nup98 interacts directly with Nup96. Nup98 interacts directly with NUP88 and NUP214, subunits of the cytoplasmic filaments of the NPC (By similarity). 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. Interacts with vesicular stomatitis virus protein M.By similarity7 Publications

Protein-protein interaction databases

BioGridi110982. 89 interactors.
DIPiDIP-32484N.
IntActiP52948. 45 interactors.
MINTiMINT-121544.
STRINGi9606.ENSP00000316032.

Structurei

Secondary structure

11817
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi168 – 172Combined sources5
Beta strandi181 – 186Combined sources6
Helixi189 – 191Combined sources3
Turni193 – 197Combined sources5
Helixi200 – 209Combined sources10
Beta strandi741 – 745Combined sources5
Helixi747 – 753Combined sources7
Beta strandi761 – 769Combined sources9
Turni770 – 772Combined sources3
Beta strandi773 – 782Combined sources10
Helixi788 – 791Combined sources4
Beta strandi792 – 795Combined sources4
Beta strandi798 – 801Combined sources4
Helixi805 – 807Combined sources3
Beta strandi819 – 823Combined sources5
Turni831 – 833Combined sources3
Helixi840 – 845Combined sources6
Helixi848 – 858Combined sources11
Beta strandi862 – 867Combined sources6
Turni868 – 871Combined sources4
Beta strandi872 – 879Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KO6X-ray3.00A/C695-880[»]
B/D881-941[»]
2Q5XX-ray1.90A733-887[»]
2Q5YX-ray2.30A/C729-880[»]
3MMYX-ray1.65B/D/F/H158-213[»]
4OWRX-ray3.15B157-213[»]
5A9Qelectron microscopy23.005/E/N/W881-1817[»]
ProteinModelPortaliP52948.
SMRiP52948.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini738 – 880Peptidase S59PROSITE-ProRule annotationAdd BLAST143

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 156FG repeats 1Add BLAST156
Regioni157 – 213GLEBS; interaction with RAE11 PublicationAdd BLAST57
Regioni214 – 480FG repeats 2Add BLAST267

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 480Gly/Thr-richAdd BLAST474
Compositional biasi890 – 894Poly-Glu5

Domaini

Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a direct role in the transport.

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.
HOVERGENiHBG052702.
InParanoidiP52948.
KOiK14297.
OMAiKQHCITA.
OrthoDBiEOG091G00HN.
PhylomeDBiP52948.
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 (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P52948-1) [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 FGTSTGTANT 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 AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG
410 420 430 440 450
TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG
460 470 480 490 500
NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV
510 520 530 540 550
LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY
560 570 580 590 600
KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
610 620 630 640 650
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD
660 670 680 690 700
EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG
710 720 730 740 750
LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL
760 770 780 790 800
AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV
810 820 830 840 850
VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG
860 870 880 890 900
RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS
910 920 930 940 950
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM
960 970 980 990 1000
VDITQEPVLD TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT
1010 1020 1030 1040 1050
DEEDVDMALD QRFSRLPSKA DTSQEICSPR LPISASHSSK TRSLVGGLLQ
1060 1070 1080 1090 1100
SKFTSGAFLS PSVSVQECRT PRAASLMNIP STSSWSVPPP LTSVFTMPSP
1110 1120 1130 1140 1150
APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG RSFRVGWGPN
1160 1170 1180 1190 1200
WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK
1210 1220 1230 1240 1250
LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA
1260 1270 1280 1290 1300
DWVKEASGDL PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL
1310 1320 1330 1340 1350
ERRRAFSRWL SCTATPQIEE EVSLTQKNSP VEAVFSYLTG KRISEACSLA
1360 1370 1380 1390 1400
QQSGDHRLAL LLSQFVGSQS VRELLTMQLV DWHQLQADSF IQDERLRIFA
1410 1420 1430 1440 1450
LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA SISRALSMYE
1460 1470 1480 1490 1500
EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS
1510 1520 1530 1540 1550
DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA
1560 1570 1580 1590 1600
SYAGQLESEG LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA
1610 1620 1630 1640 1650
KETFLTQKLR VPAKWIHEAK AVRAHMESDK HLEALCLFKA EHWNRCHKLI
1660 1670 1680 1690 1700
IRHLASDAII NENYDYLKGF LEDLAPPERS SLIQDWETSG LVYLDYIRVI
1710 1720 1730 1740 1750
EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD RLAQSDMAKR
1760 1770 1780 1790 1800
VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE
1810
LRSLTQSYLR ELAVGSL
Length:1,817
Mass (Da):197,579
Last modified:October 5, 2010 - v4
Checksum:iBC60E5456B936C79
GO
Isoform 2 (identifier: P52948-2) [UniParc]FASTAAdd to basket
Also known as: Nup98-Nup96 precursor splice variant 1

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.
     1502-1576: RHYDLNQLLE...FVLLHIDNSG → S

Show »
Length:1,726
Mass (Da):187,199
Checksum:i0F92C34F9FD7DC92
GO
Isoform 3 (identifier: P52948-3) [UniParc]FASTAAdd to basket
Also known as: Nup98-specific 1

The sequence of this isoform differs from the canonical sequence as follows:
     932-937: SQSPEV → VEKKGQ
     938-1817: Missing.

Show »
Length:937
Mass (Da):97,836
Checksum:i2CB6CE36734F0B82
GO
Isoform 4 (identifier: P52948-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.
     932-937: SQSPEV → VEKKGQ
     938-1817: Missing.

Show »
Length:920
Mass (Da):96,075
Checksum:i129DABAFB69253AD
GO
Isoform 5 (identifier: P52948-5) [UniParc]FASTAAdd to basket
Also known as: Nup196, ADIR2

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.

Show »
Length:1,800
Mass (Da):195,817
Checksum:i4BCA483C2E9E1A8E
GO
Isoform 6 (identifier: P52948-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1085-1188: WSVPPPLTSV...FLPNPVAVKP → C

Show »
Length:1,714
Mass (Da):186,268
Checksum:i158300FBC47A0C0C
GO

Sequence cautioni

The sequence AAD22395 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAD22396 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAF19342 differs from that shown. Reason: Frameshift at position 1551.Curated
The sequence AAF19342 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti318L → S in AAH41136 (PubMed:15489334).Curated1
Sequence conflicti376S → G in AAH41136 (PubMed:15489334).Curated1
Sequence conflicti756 – 757EK → VF in AAD22395 (PubMed:10087256).Curated2
Sequence conflicti756 – 757EK → VF in AAD22396 (PubMed:10087256).Curated2
Sequence conflicti1281G → A in AAD22395 (PubMed:10087256).Curated1
Sequence conflicti1281G → A in AAD22396 (PubMed:10087256).Curated1
Sequence conflicti1281G → A in AAL56659 (Ref. 4) Curated1
Sequence conflicti1534 – 1536ALN → DLK in AAD22395 (PubMed:10087256).Curated3
Sequence conflicti1594E → D in AAF19342 (Ref. 7) Curated1
Sequence conflicti1598S → T in AAL56659 (Ref. 4) Curated1
Sequence conflicti1639K → N in AAF19342 (Ref. 7) Curated1
Sequence conflicti1680S → T in AAF19342 (Ref. 7) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0358591669G → V in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003619393 – 409Missing in isoform 2, isoform 4 and isoform 5. 7 PublicationsAdd BLAST17
Alternative sequenceiVSP_007942932 – 937SQSPEV → VEKKGQ in isoform 3 and isoform 4. 3 Publications6
Alternative sequenceiVSP_007943938 – 1817Missing in isoform 3 and isoform 4. 3 PublicationsAdd BLAST880
Alternative sequenceiVSP_0383281085 – 1188WSVPP…VAVKP → C in isoform 6. 1 PublicationAdd BLAST104
Alternative sequenceiVSP_0079441502 – 1576RHYDL…IDNSG → S in isoform 2. 1 PublicationAdd BLAST75

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41815 mRNA. Translation: AAC50366.1.
AB040538 mRNA. Translation: BAB18537.1.
AF071076 mRNA. Translation: AAD22395.1. Sequence problems.
AF071077 mRNA. Translation: AAD22396.1. Sequence problems.
AF231130 mRNA. Translation: AAL56659.1.
AC060812 Genomic DNA. No translation available.
AC090587 Genomic DNA. No translation available.
BC041136 mRNA. Translation: AAH41136.1.
BC012906 mRNA. Translation: AAH12906.2.
AF116074 mRNA. Translation: AAF19342.1. Sequence problems.
BT007349 mRNA. Translation: AAP36013.1.
AL133601 mRNA. Translation: CAB63736.1.
AL137613 mRNA. Translation: CAB70842.1.
CCDSiCCDS31347.1. [P52948-2]
CCDS41605.1. [P52948-3]
CCDS41606.1. [P52948-4]
CCDS7746.1. [P52948-5]
PIRiT43443.
RefSeqiNP_005378.4. NM_005387.6. [P52948-3]
NP_057404.2. NM_016320.4. [P52948-5]
NP_624357.1. NM_139131.4. [P52948-4]
NP_624358.2. NM_139132.3. [P52948-2]
UniGeneiHs.524750.

Genome annotation databases

EnsembliENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5]
ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2]
ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1]
ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4]
ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3]
GeneIDi4928.
KEGGihsa:4928.
UCSCiuc001lyh.3. human. [P52948-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41815 mRNA. Translation: AAC50366.1.
AB040538 mRNA. Translation: BAB18537.1.
AF071076 mRNA. Translation: AAD22395.1. Sequence problems.
AF071077 mRNA. Translation: AAD22396.1. Sequence problems.
AF231130 mRNA. Translation: AAL56659.1.
AC060812 Genomic DNA. No translation available.
AC090587 Genomic DNA. No translation available.
BC041136 mRNA. Translation: AAH41136.1.
BC012906 mRNA. Translation: AAH12906.2.
AF116074 mRNA. Translation: AAF19342.1. Sequence problems.
BT007349 mRNA. Translation: AAP36013.1.
AL133601 mRNA. Translation: CAB63736.1.
AL137613 mRNA. Translation: CAB70842.1.
CCDSiCCDS31347.1. [P52948-2]
CCDS41605.1. [P52948-3]
CCDS41606.1. [P52948-4]
CCDS7746.1. [P52948-5]
PIRiT43443.
RefSeqiNP_005378.4. NM_005387.6. [P52948-3]
NP_057404.2. NM_016320.4. [P52948-5]
NP_624357.1. NM_139131.4. [P52948-4]
NP_624358.2. NM_139132.3. [P52948-2]
UniGeneiHs.524750.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KO6X-ray3.00A/C695-880[»]
B/D881-941[»]
2Q5XX-ray1.90A733-887[»]
2Q5YX-ray2.30A/C729-880[»]
3MMYX-ray1.65B/D/F/H158-213[»]
4OWRX-ray3.15B157-213[»]
5A9Qelectron microscopy23.005/E/N/W881-1817[»]
ProteinModelPortaliP52948.
SMRiP52948.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110982. 89 interactors.
DIPiDIP-32484N.
IntActiP52948. 45 interactors.
MINTiMINT-121544.
STRINGi9606.ENSP00000316032.

Protein family/group databases

MEROPSiS59.001.

PTM databases

iPTMnetiP52948.
PhosphoSitePlusiP52948.

Polymorphism and mutation databases

BioMutaiNUP98.
DMDMi308153660.

Proteomic databases

EPDiP52948.
MaxQBiP52948.
PaxDbiP52948.
PeptideAtlasiP52948.
PRIDEiP52948.

Protocols and materials databases

DNASUi4928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5]
ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2]
ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1]
ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4]
ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3]
GeneIDi4928.
KEGGihsa:4928.
UCSCiuc001lyh.3. human. [P52948-1]

Organism-specific databases

CTDi4928.
DisGeNETi4928.
GeneCardsiNUP98.
HGNCiHGNC:8068. NUP98.
HPAiCAB016725.
MIMi601021. gene.
neXtProtiNX_P52948.
OpenTargetsiENSG00000110713.
PharmGKBiPA31856.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0845. Eukaryota.
ENOG410XPV4. LUCA.
GeneTreeiENSGT00550000074799.
HOVERGENiHBG052702.
InParanoidiP52948.
KOiK14297.
OMAiKQHCITA.
OrthoDBiEOG091G00HN.
PhylomeDBiP52948.
TreeFamiTF343335.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110713-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiP52948.

Miscellaneous databases

ChiTaRSiNUP98. human.
EvolutionaryTraceiP52948.
GeneWikiiNUP98.
GenomeRNAii4928.
PMAP-CutDBP52948.
PROiP52948.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110713.
ExpressionAtlasiP52948. baseline and differential.
GenevisibleiP52948. HS.

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...

Entry informationi

Entry nameiNUP98_HUMAN
AccessioniPrimary (citable) accession number: P52948
Secondary accession number(s): Q8IUT2
, Q8WYB0, Q96E54, Q9H3Q4, Q9NT02, Q9UF57, Q9UHX0, Q9Y6J4, Q9Y6J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 185 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. 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.