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P52948

- NUP98_HUMAN

UniProt

P52948 - NUP98_HUMAN

Protein

Nuclear pore complex protein Nup98-Nup96

Gene

NUP98

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei531 – 5322Breakpoint for translocation to form NUP98-CCDC28A
    Sitei531 – 5322Breakpoint for translocation to form NUP98-PHF23 oncogene

    GO - Molecular functioni

    1. peptide binding Source: Ensembl
    2. protein binding Source: UniProtKB
    3. structural constituent of nuclear pore Source: UniProtKB
    4. transporter activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. DNA replication Source: UniProtKB
    4. glucose transport Source: Reactome
    5. hexose transport Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. mitotic nuclear envelope disassembly Source: Reactome
    8. mRNA transport Source: UniProtKB-KW
    9. nuclear pore complex assembly Source: UniProtKB
    10. nuclear pore organization Source: UniProtKB
    11. nucleocytoplasmic transport Source: UniProtKB
    12. protein import into nucleus, docking Source: UniProtKB
    13. regulation of glucose transport Source: Reactome
    14. small molecule metabolic process Source: Reactome
    15. transmembrane transport Source: Reactome
    16. viral process Source: Reactome

    Keywords - Biological processi

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

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_682. Mitotic Prometaphase.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    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
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8068. NUP98.

    Subcellular locationi

    Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleusnuclear pore complex
    Note: Nup96 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.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nuclear envelope Source: UniProtKB
    3. nuclear inclusion body Source: UniProtKB
    4. nuclear membrane Source: UniProtKB
    5. nuclear periphery Source: UniProtKB
    6. nuclear pore Source: UniProtKB
    7. nuclear pore nuclear basket Source: UniProtKB
    8. nuclear pore outer ring Source: UniProtKB
    9. nucleoplasm Source: Reactome

    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 PHF23.1 Publication
    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 WHSC1L1.1 Publication
    A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1.1 Publication
    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 LNP1.1 Publication
    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 4.1 Publication
    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.1 Publication

    Organism-specific databases

    PharmGKBiPA31856.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 880880Nuclear pore complex protein Nup98PRO_0000019929Add
    BLAST
    Chaini881 – 1817937Nuclear pore complex protein Nup96PRO_0000019930Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei524 – 5241Phosphoserine1 Publication
    Modified residuei603 – 6031N6-acetyllysine1 Publication
    Modified residuei608 – 6081Phosphoserine5 Publications
    Modified residuei612 – 6121Phosphoserine6 Publications
    Modified residuei618 – 6181Phosphoserine1 Publication
    Modified residuei623 – 6231Phosphoserine5 Publications
    Modified residuei625 – 6251Phosphoserine1 Publication
    Modified residuei653 – 6531PhosphoserineBy similarity
    Modified residuei670 – 6701Phosphothreonine1 Publication
    Modified residuei673 – 6731Phosphoserine1 Publication
    Modified residuei681 – 6811Phosphoserine1 Publication
    Modified residuei683 – 6831Phosphoserine1 Publication
    Modified residuei839 – 8391Phosphoserine4 Publications
    Modified residuei888 – 8881Phosphoserine6 Publications
    Modified residuei934 – 9341Phosphoserine2 Publications
    Modified residuei1000 – 10001Phosphothreonine1 Publication
    Modified residuei1023 – 10231Phosphoserine1 Publication
    Modified residuei1028 – 10281Phosphoserine2 Publications
    Modified residuei1043 – 10431Phosphoserine1 Publication
    Modified residuei1060 – 10601Phosphoserine2 Publications
    Modified residuei1070 – 10701Phosphothreonine1 Publication

    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

    MaxQBiP52948.
    PaxDbiP52948.
    PRIDEiP52948.

    PTM databases

    PhosphoSiteiP52948.

    Miscellaneous databases

    PMAP-CutDBP52948.

    Expressioni

    Gene expression databases

    ArrayExpressiP52948.
    BgeeiP52948.
    GenevestigatoriP52948.

    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. 48 interactions.
    DIPiDIP-32484N.
    IntActiP52948. 22 interactions.
    MINTiMINT-121544.

    Structurei

    Secondary structure

    1
    1817
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi168 – 1725
    Beta strandi181 – 1866
    Helixi189 – 1913
    Turni193 – 1975
    Helixi200 – 20910
    Beta strandi741 – 7455
    Helixi747 – 7537
    Beta strandi761 – 7699
    Turni770 – 7723
    Beta strandi773 – 78210
    Helixi788 – 7914
    Beta strandi792 – 7954
    Beta strandi798 – 8014
    Helixi805 – 8073
    Beta strandi819 – 8235
    Turni831 – 8333
    Helixi840 – 8456
    Helixi848 – 85811
    Beta strandi862 – 8676
    Turni868 – 8714
    Beta strandi872 – 8798

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP52948.
    SMRiP52948. Positions 158-213, 729-880.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52948.

    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 RAE1Add
    BLAST
    Regioni214 – 480267FG repeats 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 480474Gly/Thr-richAdd
    BLAST
    Compositional biasi890 – 8945Poly-Glu

    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

    eggNOGiNOG12793.
    HOVERGENiHBG052702.
    KOiK14297.
    OMAiTSFHEES.
    OrthoDBiEOG77WWBT.
    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. Align

    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

    MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG     50
    LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS 100
    LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP 150
    SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL 200
    EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF 250
    AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF 300
    SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF 350
    GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG 400
    TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG 450
    NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV 500
    LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY 550
    KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL 600
    VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD 650
    EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG 700
    LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL 750
    AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV 800
    VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG 850
    RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS 900
    TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM 950
    VDITQEPVLD TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT 1000
    DEEDVDMALD QRFSRLPSKA DTSQEICSPR LPISASHSSK TRSLVGGLLQ 1050
    SKFTSGAFLS PSVSVQECRT PRAASLMNIP STSSWSVPPP LTSVFTMPSP 1100
    APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG RSFRVGWGPN 1150
    WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK 1200
    LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA 1250
    DWVKEASGDL PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL 1300
    ERRRAFSRWL SCTATPQIEE EVSLTQKNSP VEAVFSYLTG KRISEACSLA 1350
    QQSGDHRLAL LLSQFVGSQS VRELLTMQLV DWHQLQADSF IQDERLRIFA 1400
    LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA SISRALSMYE 1450
    EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS 1500
    DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA 1550
    SYAGQLESEG LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA 1600
    KETFLTQKLR VPAKWIHEAK AVRAHMESDK HLEALCLFKA EHWNRCHKLI 1650
    IRHLASDAII NENYDYLKGF LEDLAPPERS SLIQDWETSG LVYLDYIRVI 1700
    EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD RLAQSDMAKR 1750
    VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE 1800
    LRSLTQSYLR ELAVGSL 1817
    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 AAD22395.1 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: Frameshift at position 1551.
    The sequence AAF19342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti318 – 3181L → S in AAH41136. (PubMed:15489334)Curated
    Sequence conflicti376 – 3761S → G in AAH41136. (PubMed:15489334)Curated
    Sequence conflicti756 – 7572EK → VF in AAD22395. (PubMed:10087256)Curated
    Sequence conflicti756 – 7572EK → VF in AAD22396. (PubMed:10087256)Curated
    Sequence conflicti1281 – 12811G → A in AAD22395. (PubMed:10087256)Curated
    Sequence conflicti1281 – 12811G → A in AAD22396. (PubMed:10087256)Curated
    Sequence conflicti1281 – 12811G → A in AAL56659. 1 PublicationCurated
    Sequence conflicti1534 – 15363ALN → DLK in AAD22395. (PubMed:10087256)Curated
    Sequence conflicti1594 – 15941E → D in AAF19342. 1 PublicationCurated
    Sequence conflicti1598 – 15981S → T in AAL56659. 1 PublicationCurated
    Sequence conflicti1639 – 16391K → N in AAF19342. 1 PublicationCurated
    Sequence conflicti1680 – 16801S → T in AAF19342. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1669 – 16691G → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035859

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei393 – 40917Missing in isoform 2, isoform 4 and isoform 5. 7 PublicationsVSP_003619Add
    BLAST
    Alternative sequencei932 – 9376SQSPEV → VEKKGQ in isoform 3 and isoform 4. 3 PublicationsVSP_007942
    Alternative sequencei938 – 1817880Missing in isoform 3 and isoform 4. 3 PublicationsVSP_007943Add
    BLAST
    Alternative sequencei1085 – 1188104WSVPP…VAVKP → C in isoform 6. 1 PublicationVSP_038328Add
    BLAST
    Alternative sequencei1502 – 157675RHYDL…IDNSG → S in isoform 2. 1 PublicationVSP_007944Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_005387.5. [P52948-3]
    NP_057404.2. NM_016320.4. [P52948-5]
    NP_624357.1. NM_139131.3. [P52948-4]
    NP_624358.2. NM_139132.3. [P52948-2]
    XP_005253007.1. XM_005252950.1. [P52948-1]
    UniGeneiHs.524750.

    Genome annotation databases

    EnsembliENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5]
    ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2]
    ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4]
    ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3]
    GeneIDi4928.
    KEGGihsa:4928.
    UCSCiuc001lyh.3. human. [P52948-5]
    uc001lyi.3. human. [P52948-2]
    uc001lyj.2. human. [P52948-4]
    uc001lyk.2. human. [P52948-3]

    Polymorphism databases

    DMDMi308153660.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31347.1. [P52948-2 ]
    CCDS41605.1. [P52948-3 ]
    CCDS41606.1. [P52948-4 ]
    CCDS7746.1. [P52948-5 ]
    PIRi T43443.
    RefSeqi NP_005378.4. NM_005387.5. [P52948-3 ]
    NP_057404.2. NM_016320.4. [P52948-5 ]
    NP_624357.1. NM_139131.3. [P52948-4 ]
    NP_624358.2. NM_139132.3. [P52948-2 ]
    XP_005253007.1. XM_005252950.1. [P52948-1 ]
    UniGenei Hs.524750.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KO6 X-ray 3.00 A/C 695-880 [» ]
    B/D 881-941 [» ]
    2Q5X X-ray 1.90 A 733-887 [» ]
    2Q5Y X-ray 2.30 A/C 729-880 [» ]
    3MMY X-ray 1.65 B/D/F/H 158-213 [» ]
    ProteinModelPortali P52948.
    SMRi P52948. Positions 158-213, 729-880.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110982. 48 interactions.
    DIPi DIP-32484N.
    IntActi P52948. 22 interactions.
    MINTi MINT-121544.

    Protein family/group databases

    MEROPSi S59.001.

    PTM databases

    PhosphoSitei P52948.

    Polymorphism databases

    DMDMi 308153660.

    Proteomic databases

    MaxQBi P52948.
    PaxDbi P52948.
    PRIDEi P52948.

    Protocols and materials databases

    DNASUi 4928.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324932 ; ENSP00000316032 ; ENSG00000110713 . [P52948-5 ]
    ENST00000355260 ; ENSP00000347404 ; ENSG00000110713 . [P52948-2 ]
    ENST00000397004 ; ENSP00000380199 ; ENSG00000110713 . [P52948-4 ]
    ENST00000397007 ; ENSP00000380202 ; ENSG00000110713 . [P52948-3 ]
    GeneIDi 4928.
    KEGGi hsa:4928.
    UCSCi uc001lyh.3. human. [P52948-5 ]
    uc001lyi.3. human. [P52948-2 ]
    uc001lyj.2. human. [P52948-4 ]
    uc001lyk.2. human. [P52948-3 ]

    Organism-specific databases

    CTDi 4928.
    GeneCardsi GC11M003697.
    HGNCi HGNC:8068. NUP98.
    MIMi 601021. gene.
    neXtProti NX_P52948.
    PharmGKBi PA31856.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG052702.
    KOi K14297.
    OMAi TSFHEES.
    OrthoDBi EOG77WWBT.
    PhylomeDBi P52948.
    TreeFami TF343335.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_682. Mitotic Prometaphase.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    Miscellaneous databases

    ChiTaRSi NUP98. human.
    EvolutionaryTracei P52948.
    GeneWikii NUP98.
    GenomeRNAii 4928.
    NextBioi 18979.
    PMAP-CutDB P52948.
    PROi P52948.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52948.
    Bgeei P52948.
    Genevestigatori P52948.

    Family and domain databases

    Gene3Di 3.30.1610.10. 1 hit.
    InterProi IPR021967. Nup96.
    IPR007230. Peptidase_S59.
    [Graphical view ]
    Pfami PF04096. Nucleoporin2. 1 hit.
    PF12110. Nup96. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82215. SSF82215. 1 hit.
    PROSITEi PS51434. NUP_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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. 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] [Europe PMC] [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. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH WHSC1L1.
    16. "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.
    17. "Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
      Hase M.E., Cordes V.C.
      Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF INTERACTION WITH TPR, SUBCELLULAR LOCATION.
    18. "Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
      Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
      Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
    19. "Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
      Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
      Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
    20. "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] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PSIP1/LEDGF.
    21. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-839 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: CHROMOSOMAL TRANSLOCATION WITH LNP1.
    23. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; SER-1028 AND SER-1060, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "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] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PHF23.
      Tissue: Peripheral blood.
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-839; SER-888; SER-934; THR-1000; SER-1023; SER-1028; SER-1043; SER-1060 AND THR-1070, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618; SER-623 AND SER-625, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
      Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
      EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    33. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-608; SER-612; SER-623; THR-670; SER-673; SER-681; SER-839; SER-888 AND SER-934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-623; SER-683; SER-839 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98.
    37. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, INTERACTION WITH NUP96.
    38. "Structural constraints on autoprocessing of the human nucleoporin Nup98."
      Sun Y., Guo H.C.
      Protein Sci. 17:494-505(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 733-887, SUBUNIT, AUTOPROTEOLYTIC PROCESSING.
    39. "Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1."
      Ren Y., Seo H.S., Blobel G., Hoelz A.
      Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 158-213 IN COMPLEX WITH RAE1.
    40. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1669.

    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: October 1, 2014
    This is version 160 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

    External Data

    Dasty 3