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P49790

- NU153_HUMAN

UniProt

P49790 - NU153_HUMAN

Protein

Nuclear pore complex protein Nup153

Gene

NUP153

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC).3 Publications

    Cofactori

    Binds at least 4 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi664 – 6641Zinc 1By similarity
    Metal bindingi667 – 6671Zinc 1By similarity
    Metal bindingi678 – 6781Zinc 1By similarity
    Metal bindingi681 – 6811Zinc 1By similarity
    Metal bindingi728 – 7281Zinc 2
    Metal bindingi731 – 7311Zinc 2
    Metal bindingi742 – 7421Zinc 2
    Metal bindingi745 – 7451Zinc 2
    Metal bindingi799 – 7991Zinc 3By similarity
    Metal bindingi802 – 8021Zinc 3By similarity
    Metal bindingi813 – 8131Zinc 3By similarity
    Metal bindingi816 – 8161Zinc 3By similarity
    Metal bindingi857 – 8571Zinc 4By similarity
    Metal bindingi860 – 8601Zinc 4By similarity
    Metal bindingi871 – 8711Zinc 4By similarity
    Metal bindingi874 – 8741Zinc 4By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri657 – 68731RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri722 – 75130RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri793 – 82230RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri851 – 88030RanBP2-type 4PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. nucleocytoplasmic transporter activity Source: UniProtKB
    4. protein anchor Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. structural constituent of nuclear pore Source: UniProtKB
    7. transporter activity Source: ProtInc
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. glucose transport Source: Reactome
    4. hexose transport Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear envelope disassembly Source: Reactome
    7. mRNA transport Source: UniProtKB-KW
    8. negative regulation of RNA export from nucleus Source: UniProtKB
    9. nuclear pore complex assembly Source: UniProtKB
    10. protein transport Source: UniProtKB-KW
    11. regulation of glucose transport Source: Reactome
    12. small molecule metabolic process Source: Reactome
    13. transmembrane transport Source: Reactome
    14. viral entry into host cell Source: UniProtKB-KW
    15. viral penetration into host nucleus Source: UniProtKB-KW
    16. viral process Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, mRNA transport, Protein transport, Translocation, Transport, Viral penetration into host nucleus, Virus entry into host cell

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    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_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.
    SignaLinkiP49790.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear pore complex protein Nup153
    Alternative name(s):
    153 kDa nucleoporin
    Nucleoporin Nup153
    Gene namesi
    Name:NUP153
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8062. NUP153.

    Subcellular locationi

    Nucleus. Nucleus membrane. Nucleusnuclear pore complex
    Note: Tightly associated with the nuclear membrane and lamina By similarity. Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear inclusion body Source: UniProtKB
    3. nuclear membrane Source: UniProtKB
    4. nuclear periphery Source: UniProtKB
    5. nuclear pore Source: UniProtKB
    6. nuclear pore nuclear basket Source: UniProtKB
    7. nucleolus Source: HPA
    8. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31848.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 14751474Nuclear pore complex protein Nup153PRO_0000204842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei192 – 1921Phosphoserine2 Publications
    Modified residuei209 – 2091Phosphoserine5 Publications
    Modified residuei240 – 2401Phosphoserine2 Publications
    Modified residuei257 – 2571Phosphoserine2 Publications
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei338 – 3381Phosphoserine6 Publications
    Modified residuei343 – 3431Phosphoserine1 Publication
    Modified residuei369 – 3691Phosphothreonine1 Publication
    Modified residuei384 – 3841N6-acetyllysine1 Publication
    Modified residuei500 – 5001Phosphoserine1 Publication
    Modified residuei516 – 5161Phosphoserine1 Publication
    Modified residuei522 – 5221Phosphoserine2 Publications
    Modified residuei529 – 5291Phosphoserine1 Publication
    Glycosylationi534 – 5341O-linked (GlcNAc)1 Publication
    Glycosylationi544 – 5441O-linked (GlcNAc)1 Publication
    Modified residuei588 – 5881Phosphothreonine1 Publication
    Modified residuei614 – 6141Phosphoserine2 Publications
    Modified residuei619 – 6191Phosphoserine2 Publications
    Modified residuei633 – 6331Phosphoserine2 Publications
    Modified residuei687 – 6871Phosphoserine2 Publications
    Modified residuei718 – 7181N6-acetyllysine1 Publication
    Glycosylationi908 – 9081O-linked (GlcNAc)1 Publication
    Glycosylationi909 – 9091O-linked (GlcNAc)1 Publication
    Modified residuei954 – 9541N6-acetyllysine1 Publication
    Glycosylationi1113 – 11131O-linked (GlcNAc)1 Publication
    Glycosylationi1156 – 11561O-linked (GlcNAc)1 Publication
    Modified residuei1457 – 14571Phosphoserine1 Publication
    Modified residuei1463 – 14631Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis By similarity.By similarity
    Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.
    O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.9 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP49790.
    PaxDbiP49790.
    PRIDEiP49790.

    PTM databases

    PhosphoSiteiP49790.

    Miscellaneous databases

    PMAP-CutDBP49790.

    Expressioni

    Gene expression databases

    ArrayExpressiP49790.
    BgeeiP49790.
    CleanExiHS_NUP153.
    GenevestigatoriP49790.

    Organism-specific databases

    HPAiHPA027896.
    HPA027897.
    HPA027898.

    Interactioni

    Subunit structurei

    Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner By similarity. Part of the nuclear pore complex (NPC). Interacts with TPR (via coiled coil region); the interaction is direct and provides a link between the core structure and the TPR-containing nuclear basket of the nuclear pore complex (NPC). Interacts with HIV-1 integrase; this interaction might play a role in nuclear import of HIV pre-integration complex. Interacts with hepatitis B virus capsid protein; this interaction probably plays a role in nuclear import of HBV genome. Interacts with C11orf73/Hikeshi, SENP2 and XPO5.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-286779,EBI-286779
    EPHB2P293232EBI-286779,EBI-1059294
    MAPK14Q16539-32EBI-286779,EBI-6932370

    Protein-protein interaction databases

    BioGridi115297. 46 interactions.
    DIPiDIP-38185N.
    IntActiP49790. 22 interactions.
    MINTiMINT-121422.
    STRINGi9606.ENSP00000262077.

    Structurei

    Secondary structure

    1
    1475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi723 – 7275
    Beta strandi729 – 7313
    Beta strandi743 – 7453
    Helixi755 – 7573
    Beta strandi794 – 7963
    Beta strandi800 – 8023
    Beta strandi814 – 8163
    Beta strandi858 – 8603
    Beta strandi872 – 8743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EBQNMR-A722-761[»]
    2EBRNMR-A851-890[»]
    2EBVNMR-A773-822[»]
    2GQENMR-A722-750[»]
    ProteinModelPortaliP49790.
    SMRiP49790. Positions 661-686, 722-761, 777-822, 855-890.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49790.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 1411Gly-richAdd
    BLAST
    Compositional biasi443 – 4475Poly-Gly

    Domaini

    Contains F-X-F-G repeats.

    Sequence similaritiesi

    Belongs to the NUP153 family.Curated
    Contains 4 RanBP2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri657 – 68731RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri722 – 75130RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri793 – 82230RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri851 – 88030RanBP2-type 4PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000088610.
    HOVERGENiHBG052679.
    InParanoidiP49790.
    KOiK14296.
    OrthoDBiEOG73JKTK.
    PhylomeDBiP49790.
    TreeFamiTF323517.

    Family and domain databases

    InterProiIPR013913. Nucleoporin_Nup153.
    IPR018892. Retro-transposon_transp_CS.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PfamiPF08604. Nup153. 1 hit.
    PF10599. Nup_retrotrp_bd. 1 hit.
    PF00641. zf-RanBP. 4 hits.
    [Graphical view]
    SMARTiSM00547. ZnF_RBZ. 4 hits.
    [Graphical view]
    PROSITEiPS01358. ZF_RANBP2_1. 4 hits.
    PS50199. ZF_RANBP2_2. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49790-1) [UniParc]FASTAAdd to Basket

    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

    MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI     50
    VPGWLQRYFN KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR 100
    ITPEPAVSNT EEPSTTSTAS NYPDVLTRPS LHRSHLNFSM LESPALHCQP 150
    STSSAFPIGS SGFSLVKEIK DSTSQHDDDN ISTTSGFSSR ASDKDITVSK 200
    NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS PSLGNSSILK 250
    TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS 300
    YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF 350
    QAKREKVDSQ YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI 400
    DNKCSTGYEK NMTPGQNREQ RESGFSYPNF SLPAANGLSS GVGGGGGKMR 450
    RERTRFVASK PLEEEEMEVP VLPKISLPIT SSSLPTFNFS SPEITTSSPS 500
    PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL PPSSIGFTFS 550
    VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA 600
    EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI 650
    GFGESLKAGS SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP 700
    NKSGKTTLSA SGTGFGDKFK PVIGTWDCDT CLVQNKPEAI KCVACETPKP 750
    GTCVKRALTL TVVSESAETM TASSSSCTVT TGTLGFGDKF KRPIGSWECS 800
    VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG GSLGLEKFKK 850
    PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS 900
    SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF 950
    KFSKPIGDFK FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF 1000
    GVSNLGQEEK KEELPKSSSA GFSFGTGVIN STPAPANTIV TSENKSSFNL 1050
    GTIETKSASV APFTCKTSEA KKEEMPATKG GFSFGNVEPA SLPSASVFVL 1100
    GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ TKDENSSKST 1150
    FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS 1200
    STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ 1250
    SLLFSQDSKL ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA 1300
    GSSFVFGTGP SAPSASPAFG ANQTPTFGQS QGASQPNPPG FGSISSSTAL 1350
    FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ SAFGSGTTPN SSSAFQFGSS 1400
    TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ SPAAFTVGSN 1450
    GKNVFSSSGT SFSGRKIKTA VRRRK 1475
    Length:1,475
    Mass (Da):153,938
    Last modified:September 23, 2008 - v2
    Checksum:iD07455A691F7CD1F
    GO
    Isoform 2 (identifier: P49790-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         574-615: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,433
    Mass (Da):149,396
    Checksum:i109D4036D0912D37
    GO
    Isoform 3 (identifier: P49790-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         465-465: E → ERQGLTVLPKLISSSCAQAIIPSWPLKVLRLQ

    Show »
    Length:1,506
    Mass (Da):157,338
    Checksum:i9D997D081B22CCD3
    GO

    Sequence cautioni

    The sequence BAE06106.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111E → G in BAG58514. (PubMed:14702039)Curated
    Sequence conflicti454 – 4552TR → HA in CAA80982. (PubMed:8110839)Curated
    Sequence conflicti813 – 8131C → S in BAG58514. (PubMed:14702039)Curated
    Sequence conflicti836 – 8361S → C in BAG58514. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901D → N.1 Publication
    Corresponds to variant rs16879902 [ dbSNP | Ensembl ].
    VAR_046554
    Natural varianti248 – 2481I → V.
    Corresponds to variant rs2228375 [ dbSNP | Ensembl ].
    VAR_046555
    Natural varianti381 – 3811V → F.1 Publication
    Corresponds to variant rs17857419 [ dbSNP | Ensembl ].
    VAR_070841
    Natural varianti402 – 4021N → K.
    Corresponds to variant rs6906499 [ dbSNP | Ensembl ].
    VAR_046556
    Natural varianti821 – 8211P → L.
    Corresponds to variant rs6905654 [ dbSNP | Ensembl ].
    VAR_046557
    Natural varianti827 – 8271A → T.1 Publication
    Corresponds to variant rs2274136 [ dbSNP | Ensembl ].
    VAR_046558
    Natural varianti1388 – 13881T → A.
    Corresponds to variant rs45475293 [ dbSNP | Ensembl ].
    VAR_046559

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei465 – 4651E → ERQGLTVLPKLISSSCAQAI IPSWPLKVLRLQ in isoform 3. 1 PublicationVSP_055134
    Alternative sequencei574 – 61542Missing in isoform 2. 1 PublicationVSP_054265Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z25535 mRNA. Translation: CAA80982.1.
    AK295644 mRNA. Translation: BAG58514.1.
    AB210024 mRNA. Translation: BAE06106.1. Different initiation.
    AL138824, AL138724, AL157776 Genomic DNA. Translation: CAI12246.1.
    AL157776, AL138724, AL138824 Genomic DNA. Translation: CAI16393.1.
    AL138724, AL138824, AL157776 Genomic DNA. Translation: CAI40945.1.
    BC052965 mRNA. Translation: AAH52965.1.
    CCDSiCCDS4541.1. [P49790-1]
    CCDS64359.1. [P49790-3]
    PIRiS42718.
    RefSeqiNP_001265138.1. NM_001278209.1.
    NP_001265139.1. NM_001278210.1. [P49790-2]
    NP_005115.2. NM_005124.3. [P49790-1]
    UniGeneiHs.601591.

    Genome annotation databases

    EnsembliENST00000262077; ENSP00000262077; ENSG00000124789. [P49790-1]
    ENST00000537253; ENSP00000444029; ENSG00000124789. [P49790-3]
    GeneIDi9972.
    KEGGihsa:9972.
    UCSCiuc003ncd.2. human. [P49790-1]

    Polymorphism databases

    DMDMi206729891.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z25535 mRNA. Translation: CAA80982.1 .
    AK295644 mRNA. Translation: BAG58514.1 .
    AB210024 mRNA. Translation: BAE06106.1 . Different initiation.
    AL138824 , AL138724 , AL157776 Genomic DNA. Translation: CAI12246.1 .
    AL157776 , AL138724 , AL138824 Genomic DNA. Translation: CAI16393.1 .
    AL138724 , AL138824 , AL157776 Genomic DNA. Translation: CAI40945.1 .
    BC052965 mRNA. Translation: AAH52965.1 .
    CCDSi CCDS4541.1. [P49790-1 ]
    CCDS64359.1. [P49790-3 ]
    PIRi S42718.
    RefSeqi NP_001265138.1. NM_001278209.1.
    NP_001265139.1. NM_001278210.1. [P49790-2 ]
    NP_005115.2. NM_005124.3. [P49790-1 ]
    UniGenei Hs.601591.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EBQ NMR - A 722-761 [» ]
    2EBR NMR - A 851-890 [» ]
    2EBV NMR - A 773-822 [» ]
    2GQE NMR - A 722-750 [» ]
    ProteinModelPortali P49790.
    SMRi P49790. Positions 661-686, 722-761, 777-822, 855-890.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115297. 46 interactions.
    DIPi DIP-38185N.
    IntActi P49790. 22 interactions.
    MINTi MINT-121422.
    STRINGi 9606.ENSP00000262077.

    PTM databases

    PhosphoSitei P49790.

    Polymorphism databases

    DMDMi 206729891.

    Proteomic databases

    MaxQBi P49790.
    PaxDbi P49790.
    PRIDEi P49790.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262077 ; ENSP00000262077 ; ENSG00000124789 . [P49790-1 ]
    ENST00000537253 ; ENSP00000444029 ; ENSG00000124789 . [P49790-3 ]
    GeneIDi 9972.
    KEGGi hsa:9972.
    UCSCi uc003ncd.2. human. [P49790-1 ]

    Organism-specific databases

    CTDi 9972.
    GeneCardsi GC06M017559.
    H-InvDB HIX0032892.
    HIX0200901.
    HGNCi HGNC:8062. NUP153.
    HPAi HPA027896.
    HPA027897.
    HPA027898.
    MIMi 603948. gene.
    neXtProti NX_P49790.
    PharmGKBi PA31848.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000088610.
    HOVERGENi HBG052679.
    InParanoidi P49790.
    KOi K14296.
    OrthoDBi EOG73JKTK.
    PhylomeDBi P49790.
    TreeFami TF323517.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    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_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.
    SignaLinki P49790.

    Miscellaneous databases

    EvolutionaryTracei P49790.
    GeneWikii NUP153.
    GenomeRNAii 9972.
    NextBioi 35472301.
    PMAP-CutDB P49790.
    PROi P49790.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49790.
    Bgeei P49790.
    CleanExi HS_NUP153.
    Genevestigatori P49790.

    Family and domain databases

    InterProi IPR013913. Nucleoporin_Nup153.
    IPR018892. Retro-transposon_transp_CS.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    Pfami PF08604. Nup153. 1 hit.
    PF10599. Nup_retrotrp_bd. 1 hit.
    PF00641. zf-RanBP. 4 hits.
    [Graphical view ]
    SMARTi SM00547. ZnF_RBZ. 4 hits.
    [Graphical view ]
    PROSITEi PS01358. ZF_RANBP2_1. 4 hits.
    PS50199. ZF_RANBP2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153."
      McMorrow I., Bastos R., Horton H., Burke B.
      Biochim. Biophys. Acta 1217:219-223(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT THR-827.
      Tissue: Hippocampus.
    3. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Myeloma.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1), VARIANTS ASN-90 AND PHE-381.
      Tissue: Testis.
    6. Bienvenut W.V., Dozynkiewicz M., Norman J.C.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 251-263; 295-309; 367-379; 706-718 AND 1046-1056, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
      Brownawell A.M., Macara I.G.
      J. Cell Biol. 156:53-64(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XPO5.
    8. "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.
    9. "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: FUNCTION IN ANCHORING TPR, INTERACTION WITH TPR.
    10. "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.
    11. "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-338 AND THR-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-209; SER-338 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-257 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-240; SER-257; SER-330; SER-334; SER-338; SER-343; THR-369; SER-522; SER-529; SER-614; SER-619; SER-1457 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1."
      Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.
      J. Virol. 83:6522-6533(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV INTEGRASE.
    18. "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-334; SER-338; SER-516; SER-522 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-384; LYS-718 AND LYS-954, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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.
    21. "Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis."
      Nakano H., Funasaka T., Hashizume C., Wong R.W.
      J. Biol. Chem. 285:10841-10849(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TPR.
    22. "Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket."
      Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J., Stoeber M., Pante N., Kann M.
      PLoS Pathog. 6:E1000741-E1000741(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
    23. "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis."
      Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.
      Sci. Signal. 3:RA2-RA2(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-534; SER-544; SER-908; SER-909; SER-1113 AND THR-1156.
    24. "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-192; SER-209; SER-240; SER-338; SER-500; SER-614; SER-619; SER-633; SER-687 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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-192; SER-209 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage."
      Kose S., Furuta M., Imamoto N.
      Cell 149:578-589(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C11ORF73.
    28. "Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA."
      Rajanala K., Nandicoori V.K.
      PLoS ONE 7:E29921-E29921(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RNA EXPORT, INTERACTION WITH MAPK1, SUBCELLULAR LOCATION.
    29. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Solution structure of the second and third ZF-RANBP domains from human nuclear pore complex protein NUP153."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 722-822.
    31. "Solution structure of the second ZF-ranbp domain from human nuclear pore complex protein nup153."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 722-761.

    Entry informationi

    Entry nameiNU153_HUMAN
    AccessioniPrimary (citable) accession number: P49790
    Secondary accession number(s): B4DIK2
    , E7EPX5, F6QR24, Q4LE47, Q5T9I7, Q7Z743
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 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 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3