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P52948 (NUP98_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear pore complex protein Nup98-Nup96

Cleaved into the following 2 chains:

  1. Nuclear pore complex protein Nup98
    Alternative name(s):
    98 kDa nucleoporin
    Nucleoporin Nup98
  2. Nuclear pore complex protein Nup96
    Alternative name(s):
    96 kDa nucleoporin
    Nucleoporin Nup96
Gene names
Name:NUP98
Synonyms:ADAR2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1817 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The repeat domain in Nup98 has a direct role in the transport.

Subunit structure

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. May interact with RAE1. Interacts with vesicular stomatitis virus protein M. Ref.11 Ref.12 Ref.14 Ref.32

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Nup96 is localized to the nucleoplasmic side of the nuclear pore complex, at or near the nucleoplasmic basket.

Domain

Contains G-L-F-G repeats.

Post-translational modification

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.

Involvement in disease

Note=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.

Note=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.

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

Note=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.

Note=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.

Sequence similarities

Belongs to the nucleoporin GLFG family.

Contains 1 peptidase S59 domain.

Sequence caution

The sequence AAD22395.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

The sequence AAD22396.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

The sequence AAF19342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF19342.1 differs from that shown. Reason: Frameshift at position 1551.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein transport
Translocation
Transport
mRNA transport
   Cellular componentMembrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainRepeat
   PTMAcetylation
Autocatalytic cleavage
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processDNA replication

Inferred from mutant phenotype. Source: UniProtKB

carbohydrate metabolic process

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic prometaphase

Traceable author statement. Source: Reactome

nuclear pore organization

Non-traceable author statement. Source: UniProtKB

protein import into nucleus, docking

Non-traceable author statement. Source: UniProtKB

regulation of glucose transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral reproduction

Traceable author statement. Source: Reactome

   Cellular componentNup107-160 complex

Inferred from direct assay. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: UniProtKB

structural constituent of nuclear pore

Non-traceable author statement. Source: UniProtKB

transporter activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52948-1)

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.
Isoform 2 (identifier: P52948-2)

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
Isoform 3 (identifier: P52948-3)

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.
Isoform 4 (identifier: P52948-4)

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.
     932-937: SQSPEV → VEKKGQ
     938-1817: Missing.
Isoform 5 (identifier: P52948-5)

Also known as: Nup196; ADIR2;

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.
Isoform 6 (identifier: P52948-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 880880Nuclear pore complex protein Nup98
PRO_0000019929
Chain881 – 1817937Nuclear pore complex protein Nup96
PRO_0000019930

Regions

Domain738 – 880143Peptidase S59
Compositional bias7 – 480474Gly/Thr-rich
Compositional bias890 – 8945Poly-Glu

Sites

Site531 – 5322Breakpoint for translocation to form NUP98-PHF23 oncogene

Amino acid modifications

Modified residue6031N6-acetyllysine Ref.31
Modified residue6081Phosphoserine Ref.18 Ref.20 Ref.25 Ref.27 Ref.29 Ref.30
Modified residue6121Phosphoserine Ref.18 Ref.20 Ref.25 Ref.27 Ref.29 Ref.30
Modified residue6181Phosphoserine Ref.30
Modified residue6231Phosphoserine Ref.16 Ref.18 Ref.20 Ref.23 Ref.24 Ref.27 Ref.29 Ref.30
Modified residue6251Phosphoserine Ref.30
Modified residue6701Phosphothreonine Ref.29
Modified residue6731Phosphoserine Ref.29
Modified residue8391Phosphoserine Ref.18 Ref.27
Modified residue8881Phosphoserine Ref.18 Ref.21 Ref.23 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30
Modified residue9161Phosphothreonine Ref.29
Modified residue9341Phosphoserine Ref.23 Ref.26 Ref.27
Modified residue10001Phosphothreonine Ref.27
Modified residue10231Phosphoserine Ref.23 Ref.27 Ref.29
Modified residue10281Phosphoserine Ref.20 Ref.23 Ref.27 Ref.29
Modified residue10431Phosphoserine Ref.27
Modified residue10601Phosphoserine Ref.20 Ref.25 Ref.27 Ref.29
Modified residue10641Phosphoserine Ref.25
Modified residue10701Phosphothreonine Ref.27

Natural variations

Alternative sequence393 – 40917Missing in isoform 2, isoform 4 and isoform 5.
VSP_003619
Alternative sequence932 – 9376SQSPEV → VEKKGQ in isoform 3 and isoform 4.
VSP_007942
Alternative sequence938 – 1817880Missing in isoform 3 and isoform 4.
VSP_007943
Alternative sequence1085 – 1188104WSVPP…VAVKP → C in isoform 6.
VSP_038328
Alternative sequence1502 – 157675RHYDL…IDNSG → S in isoform 2.
VSP_007944
Natural variant16691G → V in a breast cancer sample; somatic mutation. Ref.33
VAR_035859

Experimental info

Sequence conflict3181L → S in AAH41136. Ref.6
Sequence conflict3761S → G in AAH41136. Ref.6
Sequence conflict756 – 7572EK → VF in AAD22395. Ref.3
Sequence conflict756 – 7572EK → VF in AAD22396. Ref.3
Sequence conflict12811G → A in AAD22395. Ref.3
Sequence conflict12811G → A in AAD22396. Ref.3
Sequence conflict12811G → A in AAL56659. Ref.4
Sequence conflict1534 – 15363ALN → DLK in AAD22395. Ref.3
Sequence conflict15941E → D in AAF19342. Ref.7
Sequence conflict15981S → T in AAL56659. Ref.4
Sequence conflict16391K → N in AAF19342. Ref.7
Sequence conflict16801S → T in AAF19342. Ref.7

Secondary structure

........................... 1817
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Nup98-Nup96 precursor) [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: BC60E5456B936C79

FASTA1,817197,579
        10         20         30         40         50         60 
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG 

        70         80         90        100        110        120 
GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS LFSSQNNAFA QNKPTGFGNF 

       130        140        150        160        170        180 
GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST 

       190        200        210        220        230        240 
NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL 

       250        260        270        280        290        300 
FSSSTTNSGF AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF 

       310        320        330        340        350        360 
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQTNTGFGAV 

       370        380        390        400        410        420 
GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG TNTNTSNFGF GTNTSGNSIF 

       430        440        450        460        470        480 
GSKPAPGTLG TGLGAGFGTA LGAGQASLFG NNQPKIGGPL GTGAFGAPGF NTTTATLGFG 

       490        500        510        520        530        540 
APQAPVALTD PNASAAQQAV LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA 

       550        560        570        580        590        600 
QKALTTPTHY KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL 

       610        620        630        640        650        660 
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD EDSLVSHFYT 

       670        680        690        700        710        720 
NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG LEGSSEETSF HDESLQDDRE 

       730        740        750        760        770        780 
EIENNSYHMH PAGIILTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD 

       790        800        810        820        830        840 
VNLTNLNLDD IVHIRRKEVV VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP 

       850        860        870        880        890        900 
DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS 

       910        920        930        940        950        960 
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVLD 

       970        980        990       1000       1010       1020 
TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT DEEDVDMALD QRFSRLPSKA 

      1030       1040       1050       1060       1070       1080 
DTSQEICSPR LPISASHSSK TRSLVGGLLQ SKFTSGAFLS PSVSVQECRT PRAASLMNIP 

      1090       1100       1110       1120       1130       1140 
STSSWSVPPP LTSVFTMPSP APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG 

      1150       1160       1170       1180       1190       1200 
RSFRVGWGPN WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK 

      1210       1220       1230       1240       1250       1260 
LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA DWVKEASGDL 

      1270       1280       1290       1300       1310       1320 
PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL ERRRAFSRWL SCTATPQIEE 

      1330       1340       1350       1360       1370       1380 
EVSLTQKNSP VEAVFSYLTG KRISEACSLA QQSGDHRLAL LLSQFVGSQS VRELLTMQLV 

      1390       1400       1410       1420       1430       1440 
DWHQLQADSF IQDERLRIFA LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA 

      1450       1460       1470       1480       1490       1500 
SISRALSMYE EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS 

      1510       1520       1530       1540       1550       1560 
DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA SYAGQLESEG 

      1570       1580       1590       1600       1610       1620 
LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA KETFLTQKLR VPAKWIHEAK 

      1630       1640       1650       1660       1670       1680 
AVRAHMESDK HLEALCLFKA EHWNRCHKLI IRHLASDAII NENYDYLKGF LEDLAPPERS 

      1690       1700       1710       1720       1730       1740 
SLIQDWETSG LVYLDYIRVI EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD 

      1750       1760       1770       1780       1790       1800 
RLAQSDMAKR VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE 

      1810 
LRSLTQSYLR ELAVGSL 

« Hide

Isoform 2 (Nup98-Nup96 precursor splice variant 1) [UniParc].

Checksum: 0F92C34F9FD7DC92
Show »

FASTA1,726187,199
Isoform 3 (Nup98-specific 1) [UniParc].

Checksum: 2CB6CE36734F0B82
Show »

FASTA93797,836
Isoform 4 [UniParc].

Checksum: 129DABAFB69253AD
Show »

FASTA92096,075
Isoform 5 (Nup196) (ADIR2) [UniParc].

Checksum: 4BCA483C2E9E1A8E
Show »

FASTA1,800195,817
Isoform 6 [UniParc].

Checksum: 158300FBC47A0C0C
Show »

FASTA1,714186,268

References

« Hide 'large scale' references
[1]"The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9."
Borrow J., Shearman A.M., Stanton V.P., Becher R., Collins T., Williams A.J., Dube I., Katz F., Kwong Y.L., Morris C., Ohyashiki K., Toyama K., Rowley J., Housman D.E.
Nat. Genet. 12:159-167(1996) [PubMed: 8563754] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), CHROMOSOMAL TRANSLOCATION WITH HOXA9.
[2]"Molecular analysis of the chromosomal breakpoints and identification of the repetitive sequences near the breakpoints of NUP98 in therapy-related leukemia with inv(11)(p15q22)."
Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[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: 10087256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1648-1664.
[4]"An alternative splice form of NUP98 encodes a 196kDa NUP196 isoform."
Borrow J., Housman D.E.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed: 16554811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 963-1817 (ISOFORM 6).
Tissue: Lung carcinoma.
[7]Xu Y.H., Guo B.C., Yu Y.L.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1176-1817 (ISOFORM 5).
Tissue: Liver.
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1212-1817 (ISOFORM 5).
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1227-1817 (ISOFORM 5).
Tissue: Testis.
[10]"The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion."
Ahuja H.G., Felix C.A., Aplan P.D.
Blood 94:3258-3261(1999) [PubMed: 10556215] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH TOP1.
[11]"RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains."
Pritchard C.E., Fornerod M., Kasper L.H., van Deursen J.M.
J. Cell Biol. 145:237-254(1999) [PubMed: 10209021] [Abstract]
Cited for: INTERACTION WITH RAE1.
[12]"Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98."
von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D., Bachi A., Wu X., Wilm M., Carmo-Fonseca M., Izaurralde E.
Mol. Cell 6:1243-1252(2000) [PubMed: 11106761] [Abstract]
Cited for: INTERACTION WITH VESICULAR STOMATITIS VIRUS PROTEIN M.
[13]"A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia."
Jaju R.J., Fidler C., Haas O.A., Strickson A.J., Watkins F., Clark K., Cross N.C., Cheng J.F., Aplan P.D., Kearney L., Boultwood J., Wainscoat J.S.
Blood 98:1264-1267(2001) [PubMed: 11493482] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH NSD1.
[14]"Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export."
Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.
J. Cell Biol. 155:339-354(2001) [PubMed: 11684705] [Abstract]
Cited for: SUBUNIT.
[15]"NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15)."
Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., Vallespi T., Negrini M., Martelli M.F., Mecucci C.
Blood 99:3857-3860(2002) [PubMed: 11986249] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH WHSC1L1.
[16]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid leukemia."
Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E., Micalizzi C., Panarello C.
Leuk. Res. 29:467-470(2005) [PubMed: 15725483] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH PSIP1/LEDGF.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; SER-839 AND SER-888, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[19]"NUP98 rearrangements in hematopoietic malignancies: a study of the Groupe Francophone de Cytogenetique Hematologique."
Romana S.P., Radford-Weiss I., Ben Abdelali R., Schluth C., Petit A., Dastugue N., Talmant P., Bilhou-Nabera C., Mugneret F., Lafage-Pochitaloff M., Mozziconacci M.-J., Andrieu J., Lai J.-L., Terre C., Rack K., Cornillet-Lefebvre P., Luquet I., Nadal N. expand/collapse author list , Nguyen-Khac F., Perot C., Van den Akker J., Fert-Ferrer S., Cabrol C., Charrin C., Tigaud I., Poirel H., Vekemans M., Bernard O.A., Berger R.
Leukemia 20:696-706(2006) [PubMed: 16467868] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH LNP1.
[20]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; SER-1028 AND SER-1060, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[21]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, MASS SPECTROMETRY.
Tissue: Cervix adenocarcinoma.
[22]"A novel NUP98-PHF23 fusion resulting from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia."
Reader J.C., Meekins J.S., Gojo I., Ning Y.
Leukemia 21:842-844(2007) [PubMed: 17287853] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH PHF23.
Tissue: Peripheral blood.
[23]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-888; SER-934; SER-1023 AND SER-1028, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[25]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-1060 AND SER-1064, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[26]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888 AND SER-934, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[27]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; SER-839; SER-888; SER-934; THR-1000; SER-1023; SER-1028; SER-1043; SER-1060 AND THR-1070, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[28]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, MASS SPECTROMETRY.
Tissue: Liver.
[29]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; THR-670; SER-673; SER-888; THR-916; SER-1023; SER-1028 AND SER-1060, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[30]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618; SER-623; SER-625 AND SER-888, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[31]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, MASS SPECTROMETRY.
[32]"The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98."
Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., Powers M.A.
Mol. Cell 10:347-358(2002) [PubMed: 12191480] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, INTERACTION WITH NUP96.
[33]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1669.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00006038.
IPI00216688.
IPI00337395.
IPI00337397.
IPI00936708.
IPI00953181.
PIRT43443.
RefSeqNP_005378.4. NM_005387.5.
NP_057404.2. NM_016320.4.
NP_624357.1. NM_139131.3.
NP_624358.2. NM_139132.3.
UniGeneHs.524750.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KO6X-ray3.00A/C695-880[»]
B/D881-931[»]
2Q5XX-ray1.90A733-887[»]
2Q5YX-ray2.30A/C729-880[»]
3MMYX-ray1.65B/D/F/H158-213[»]
ProteinModelPortalP52948.
SMRP52948. Positions 158-213, 729-880.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-32484N.
IntActP52948. 11 interactions.
MINTMINT-121544.
STRINGP52948.

Protein family/group databases

MEROPSS59.001.

PTM databases

PhosphoSiteP52948.

Polymorphism databases

DMDM308153660.

Proteomic databases

PRIDEP52948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359171; ENSP00000352091; ENSG00000110713.
GeneID4928.
KEGGhsa:4928.
UCSCuc001lyh.1. human.
uc001lyi.1. human.
uc001lyk.1. human.

Organism-specific databases

CTD4928.
GeneCardsGC11M003696.
HGNCHGNC:8068. NUP98.
MIM601021. gene.
neXtProtNX_P52948.
PharmGKBPA31856.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07907.
HOVERGENHBG052702.
OMADWVKEAS.
PhylomeDBP52948.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_15518. Transmembrane transport of small molecules.
REACT_383. DNA Replication.
REACT_474. Metabolism of carbohydrates.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpressP52948.
BgeeP52948.
GenevestigatorP52948.
GermOnlineENSG00000110713. Homo sapiens.

Family and domain databases

InterProIPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
KOK14297.
PfamPF04096. Nucleoporin2. 1 hit.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMSSF82215. Peptidase_S59. 1 hit.
PROSITEPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio18979.
PMAP-CutDBP52948.
SOURCESearch...

Entry information

Entry nameNUP98_HUMAN
AccessionPrimary (citable) accession number: P52948
Secondary accession number(s): Q8IUT2 expand/collapse secondary AC list , Q8WYB0, Q96E54, Q9H3Q4, Q9NT02, Q9UF57, Q9UHX0, Q9Y6J4, Q9Y6J5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 5, 2010
Last modified: January 25, 2012
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families