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P35658

- NU214_HUMAN

UniProt

P35658 - NU214_HUMAN

Protein

Nuclear pore complex protein Nup214

Gene

NUP214

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei812 – 8132Breakpoint

    GO - Molecular functioni

    1. nucleocytoplasmic transporter activity Source: Ensembl
    2. protein binding Source: UniProtKB
    3. transporter activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. gene expression Source: Reactome
    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 export from nucleus Source: Ensembl
    9. mRNA metabolic process Source: Reactome
    10. protein export from nucleus Source: MGI
    11. protein import into nucleus Source: Ensembl
    12. regulation of cell cycle Source: Ensembl
    13. regulation of glucose transport Source: Reactome
    14. RNA metabolic process Source: Reactome
    15. small molecule metabolic process Source: Reactome
    16. transmembrane transport Source: Reactome
    17. viral process Source: Reactome

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_25218. HuR stabilizes mRNA.
    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.
    SignaLinkiP35658.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear pore complex protein Nup214
    Alternative name(s):
    214 kDa nucleoporin
    Nucleoporin Nup214
    Protein CAN
    Gene namesi
    Name:NUP214
    Synonyms:CAIN, CAN, KIAA0023
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8064. NUP214.

    Subcellular locationi

    Nucleusnuclear pore complex
    Note: Cytoplasmic filaments.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. focal adhesion Source: HPA
    3. intracellular membrane-bounded organelle Source: HPA
    4. nuclear pore Source: ProtInc
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving NUP214 is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia. Translocation t(6;9)(p23;q34) with DEK. It results in the formation of a DEK-CAN fusion gene.
    A chromosomal aberration involving NUP214 is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with SET.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi353 – 3531V → A: Reduced binding to DDX19B. 1 Publication
    Mutagenesisi359 – 3591D → R: Impairs interaction with DDX19B. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti98277. Acute myeloid leukemia with recurrent genetic anomaly.
    PharmGKBiPA31851.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 20902089Nuclear pore complex protein Nup214PRO_0000204861Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei430 – 4301Phosphoserine3 Publications
    Modified residuei433 – 4331Phosphoserine1 Publication
    Modified residuei434 – 4341Phosphothreonine2 Publications
    Modified residuei437 – 4371Phosphothreonine2 Publications
    Modified residuei439 – 4391Phosphothreonine2 Publications
    Modified residuei651 – 6511Phosphoserine1 Publication
    Modified residuei657 – 6571Phosphoserine2 Publications
    Modified residuei666 – 6661Phosphoserine1 Publication
    Modified residuei670 – 6701Phosphothreonine2 Publications
    Modified residuei678 – 6781Phosphoserine2 Publications
    Modified residuei940 – 9401Phosphoserine3 Publications
    Modified residuei970 – 9701Phosphoserine1 Publication
    Modified residuei974 – 9741Phosphoserine1 Publication
    Modified residuei989 – 9891Phosphoserine1 Publication
    Modified residuei1023 – 10231Phosphoserine1 Publication
    Modified residuei1045 – 10451Phosphoserine1 Publication
    Modified residuei1081 – 10811Phosphoserine1 Publication
    Modified residuei1134 – 11341Phosphothreonine1 Publication
    Modified residuei1150 – 11501Phosphothreonine1 Publication
    Modified residuei1156 – 11561Phosphothreonine1 Publication
    Modified residuei1181 – 11811Phosphoserine1 Publication
    Modified residuei1312 – 13121Phosphothreonine1 Publication
    Modified residuei1963 – 19631Phosphoserine1 Publication
    Modified residuei1985 – 19851Phosphoserine1 Publication

    Post-translational modificationi

    Probably glycosylated as it reacts with wheat germ agglutinin (WGA).

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP35658.
    PaxDbiP35658.
    PRIDEiP35658.

    PTM databases

    PhosphoSiteiP35658.

    Expressioni

    Tissue specificityi

    Expressed in thymus, spleen, bone marrow, kidney, brain and testis, but hardly in all other tissues or in whole embryos during development.

    Gene expression databases

    ArrayExpressiP35658.
    BgeeiP35658.
    CleanExiHS_NUP214.
    GenevestigatoriP35658.

    Organism-specific databases

    HPAiHPA018404.
    HPA048789.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DDX19, NUP88, XPO1 and XPO5. Interacts with human herpes virus 1 (HHV-1) protein UL25; this interaction might be essential to the capsid docking onto the host nuclear pore.5 Publications

    Protein-protein interaction databases

    BioGridi113717. 51 interactions.
    DIPiDIP-38367N.
    IntActiP35658. 18 interactions.
    MINTiMINT-121482.
    STRINGi9606.ENSP00000352400.

    Structurei

    Secondary structure

    1
    2090
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Beta strandi11 – 2111
    Beta strandi24 – 263
    Beta strandi42 – 454
    Turni46 – 494
    Beta strandi50 – 556
    Beta strandi58 – 636
    Helixi64 – 674
    Beta strandi80 – 823
    Beta strandi87 – 893
    Beta strandi95 – 1006
    Beta strandi106 – 1138
    Turni114 – 1163
    Beta strandi117 – 1248
    Helixi125 – 1295
    Beta strandi139 – 1435
    Helixi148 – 1503
    Beta strandi151 – 1577
    Beta strandi164 – 1696
    Beta strandi174 – 18916
    Helixi191 – 1933
    Beta strandi195 – 2006
    Beta strandi207 – 2115
    Beta strandi216 – 2194
    Beta strandi225 – 2295
    Beta strandi237 – 2393
    Beta strandi241 – 25010
    Beta strandi253 – 2608
    Beta strandi265 – 2673
    Beta strandi270 – 2756
    Beta strandi286 – 2894
    Beta strandi299 – 3013
    Beta strandi305 – 3106
    Helixi311 – 3133
    Beta strandi315 – 3206
    Beta strandi323 – 3253
    Beta strandi327 – 3315
    Beta strandi338 – 3436
    Helixi345 – 3473
    Beta strandi357 – 3593
    Beta strandi362 – 3687
    Beta strandi375 – 3784
    Beta strandi381 – 3833
    Beta strandi388 – 3936
    Beta strandi396 – 40510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OITX-ray1.65A1-434[»]
    3FHCX-ray2.80A1-405[»]
    3FMOX-ray2.51A1-450[»]
    3FMPX-ray3.19A/C1-450[»]
    ProteinModelPortaliP35658.
    SMRiP35658. Positions 1-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35658.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati41 – 9353Blade 1Add
    BLAST
    Repeati94 – 15057Blade 2Add
    BLAST
    Repeati151 – 19343Blade 3Add
    BLAST
    Repeati194 – 23946Blade 4Add
    BLAST
    Repeati240 – 30364Blade 5Add
    BLAST
    Repeati304 – 35956Blade 6Add
    BLAST
    Repeati360 – 40445Blade 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 404364Seven-bladed beta propellerAdd
    BLAST
    Regioni481 – 2076159611 X 5 AA approximate repeatsAdd
    BLAST
    Regioni740 – 76829Leucine-zipper 1Add
    BLAST
    Regioni861 – 88222Leucine-zipper 2Add
    BLAST
    Regioni1409 – 208467618 X 4 AA approximate repeatsAdd
    BLAST
    Regioni1427 – 208565911 X 3 AA approximate repeatsAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili680 – 12095301 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1213 – 2090878Pro/Ser/Thr-richAdd
    BLAST

    Domaini

    Contains FG repeats.
    The beta-propeller contains long interblade connector loops, and mediates interaction with DDX19B.

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG052683.
    KOiK14317.
    OMAiNERNRDS.
    OrthoDBiEOG7V765H.
    PhylomeDBiP35658.
    TreeFamiTF323517.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    [Graphical view]
    SMARTiSM00320. WD40. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35658-1) [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

    MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS LLAVSNKYGL     50
    VFAGGASGLQ IFPTKNLLIQ NKPGDDPNKI VDKVQGLLVP MKFPIHHLAL 100
    SCDNLTLSAC MMSSEYGSII AFFDVRTFSN EAKQQKRPFA YHKLLKDAGG 150
    MVIDMKWNPT VPSMVAVCLA DGSIAVLQVT ETVKVCATLP STVAVTSVCW 200
    SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP VRVLDVLWIG 250
    TYVFAIVYAA ADGTLETSPD VVMALLPKKE EKHPEIFVNF MEPCYGSCTE 300
    RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQSDQINWES WLLEDSSRAE 350
    LPVTDKSDDS LPMGVVVDYT NQVEITISDE KTLPPAPVLM LLSTDGVLCP 400
    FYMINQNPGV KSLIKTPERL SLEGERQPKS PGSTPTTPTS SQAPQKLDAS 450
    AAAAPASLPP SSPAAPIATF SLLPAGGAPT VFSFGSSSLK SSATVTGEPP 500
    SYSSGSDSSK AAPGPGPSTF SFVPPSKASL APTPAASPVA PSAASFSFGS 550
    SGFKPTLEST PVPSVSAPNI AMKPSFPPST SAVKVNLSEK FTAAATSTPV 600
    SSSQSAPPMS PFSSASKPAA SGPLSHPTPL SAPPSSVPLK SSVLPSPSGR 650
    SAQGSSSPVP SMVQKSPRIT PPAAKPGSPQ AKSLQPAVAE KQGHQWKDSD 700
    PVMAGIGEEI AHFQKELEEL KARTSKACFQ VGTSEEMKML RTESDDLHTF 750
    LLEIKETTES LHGDISSLKT TLLEGFAGVE EAREQNERNR DSGYLHLLYK 800
    RPLDPKSEAQ LQEIRRLHQY VKFAVQDVND VLDLEWDQHL EQKKKQRHLL 850
    VPERETLFNT LANNREIINQ QRKRLNHLVD SLQQLRLYKQ TSLWSLSSAV 900
    PSQSSIHSFD SDLESLCNAL LKTTIESHTK SLPKVPAKLS PMKQAQLRNF 950
    LAKRKTPPVR STAPASLSRS AFLSQRYYED LDEVSSTSSV SQSLESEDAR 1000
    TSCKDDEAVV QAPRHAPVVR TPSIQPSLLP HAAPFAKSHL VHGSSPGVMG 1050
    TSVATSASKI IPQGADSTML ATKTVKHGAP SPSHPISAPQ AAAAAALRRQ 1100
    MASQAPAVNT LTESTLKNVP QVVNVQELKN NPATPSTAMG SSVPYSTAKT 1150
    PHPVLTPVAA NQAKQGSLIN SLKPSGPTPA SGQLSSGDKA SGTAKIETAV 1200
    TSTPSASGQF SKPFSFSPSG TGFNFGIITP TPSSNFTAAQ GATPSTKESS 1250
    QPDAFSSGGG SKPSYEAIPE SSPPSGITSA SNTTPGEPAA SSSRPVAPSG 1300
    TALSTTSSKL ETPPSKLGEL LFPSSLAGET LGSFSGLRVG QADDSTKPTN 1350
    KASSTSLTST QPTKTSGVPS GFNFTAPPVL GKHTEPPVTS SATTTSVAPP 1400
    AATSTSSTAV FGSLPVTSAG SSGVISFGGT SLSAGKTSFS FGSQQTNSTV 1450
    PPSAPPPTTA ATPLPTSFPT LSFGSLLSSA TTPSLPMSAG RSTEEATSSA 1500
    LPEKPGDSEV SASAASLLEE QQSAQLPQAP PQTSDSVKKE PVLAQPAVSN 1550
    SGTAASSTSL VALSAEATPA TTGVPDARTE AVPPASSFSV PGQTAVTAAA 1600
    ISSAGPVAVE TSSTPIASST TSIVAPGPSA EAAAFGTVTS GSSVFAQPPA 1650
    ASSSSAFNQL TNNTATAPSA TPVFGQVAAS TAPSLFGQQT GSTASTAAAT 1700
    PQVSSSGFSS PAFGTTAPGV FGQTTFGQAS VFGQSASSAA SVFSFSQPGF 1750
    SSVPAFGQPA SSTPTSTSGS VFGAASSTSS SSSFSFGQSS PNTGGGLFGQ 1800
    SNAPAFGQSP GFGQGGSVFG GTSAATTTAA TSGFSFCQAS GFGSSNTGSV 1850
    FGQAASTGGI VFGQQSSSSS GSVFGSGNTG RGGGFFSGLG GKPSQDAANK 1900
    NPFSSASGGF GSTATSNTSN LFGNSGAKTF GGFASSSFGE QKPTGTFSSG 1950
    GGSVASQGFG FSSPNKTGGF GAAPVFGSPP TFGGSPGFGG VPAFGSAPAF 2000
    TSPLGSTGGK VFGEGTAAAS AGGFGFGSSS NTTSFGTLAS QNAPTFGSLS 2050
    QQTSGFGTQS SGFSGFGSGT GGFSFGSNNS SVQGFGGWRS 2090
    Length:2,090
    Mass (Da):213,620
    Last modified:July 22, 2008 - v2
    Checksum:iEE6F0F3DE3D522C6
    GO
    Isoform 2 (identifier: P35658-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         590-601: KFTAAATSTPVS → N

    Note: No experimental confirmation available.

    Show »
    Length:2,079
    Mass (Da):212,571
    Checksum:i159D32101C9DF54A
    GO
    Isoform 3 (identifier: P35658-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         648-648: S → SA

    Note: No experimental confirmation available.

    Show »
    Length:2,091
    Mass (Da):213,691
    Checksum:i765727236C2B47C8
    GO
    Isoform 4 (identifier: P35658-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         590-601: KFTAAATSTPVS → N
         648-648: S → SA

    Show »
    Length:2,080
    Mass (Da):212,643
    Checksum:iA5ECD51E41D40F1F
    GO
    Isoform 5 (identifier: P35658-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         590-601: KFTAAATSTPVS → N
         1139-1148: Missing.
         2026-2090: FGSSSNTTSF...SVQGFGGWRS → SLAMSLSPTL...PTDFWFWDPE

    Show »
    Length:2,093
    Mass (Da):215,401
    Checksum:i4C67CE62D57E590F
    GO

    Sequence cautioni

    The sequence BAD07398.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491G → A in CAA45535. (PubMed:1549122)Curated
    Sequence conflicti175 – 1751A → D in CAA45535. (PubMed:1549122)Curated
    Sequence conflicti1091 – 10922AA → QL in CAA45535. (PubMed:1549122)Curated
    Sequence conflicti1872 – 18721S → N in AAH45620. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti424 – 4241G → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035856
    Natural varianti574 – 5741P → S.2 Publications
    Corresponds to variant rs103612 [ dbSNP | Ensembl ].
    VAR_045691
    Natural varianti1378 – 13781P → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035857
    Natural varianti1392 – 13921A → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035858
    Natural varianti1592 – 15921G → A.
    Corresponds to variant rs28594669 [ dbSNP | Ensembl ].
    VAR_061533

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei590 – 60112KFTAA…STPVS → N in isoform 2, isoform 4 and isoform 5. 2 PublicationsVSP_034896Add
    BLAST
    Alternative sequencei648 – 6481S → SA in isoform 3 and isoform 4. 1 PublicationVSP_034897
    Alternative sequencei1139 – 114810Missing in isoform 5. 1 PublicationVSP_034898
    Alternative sequencei2026 – 209065FGSSS…GGWRS → SLAMSLSPTLKGRLLLMRPK AGGGREQAAPGRKSNESRSL GHLCMERALTSPLKVWEQQQ HHILRHARESECPHFRITVP TDFWFWDPE in isoform 5. 1 PublicationVSP_034899Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64228 mRNA. Translation: CAA45535.1.
    AB159230 mRNA. Translation: BAD07398.1. Different initiation.
    D14689 mRNA. Translation: BAA03515.1.
    AL157938 Genomic DNA. Translation: CAI41111.1.
    BC045620 mRNA. Translation: AAH45620.2.
    BC105998 mRNA. Translation: AAI05999.1.
    CCDSiCCDS6940.1. [P35658-1]
    PIRiS26058.
    RefSeqiNP_005076.3. NM_005085.3. [P35658-1]
    UniGeneiHs.654530.

    Genome annotation databases

    EnsembliENST00000359428; ENSP00000352400; ENSG00000126883. [P35658-1]
    ENST00000411637; ENSP00000396576; ENSG00000126883. [P35658-4]
    ENST00000451030; ENSP00000405014; ENSG00000126883. [P35658-3]
    GeneIDi8021.
    KEGGihsa:8021.
    UCSCiuc004caf.1. human. [P35658-2]
    uc004cag.3. human. [P35658-1]
    uc004cah.3. human. [P35658-4]

    Polymorphism databases

    DMDMi205831380.

    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
    X64228 mRNA. Translation: CAA45535.1 .
    AB159230 mRNA. Translation: BAD07398.1 . Different initiation.
    D14689 mRNA. Translation: BAA03515.1 .
    AL157938 Genomic DNA. Translation: CAI41111.1 .
    BC045620 mRNA. Translation: AAH45620.2 .
    BC105998 mRNA. Translation: AAI05999.1 .
    CCDSi CCDS6940.1. [P35658-1 ]
    PIRi S26058.
    RefSeqi NP_005076.3. NM_005085.3. [P35658-1 ]
    UniGenei Hs.654530.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OIT X-ray 1.65 A 1-434 [» ]
    3FHC X-ray 2.80 A 1-405 [» ]
    3FMO X-ray 2.51 A 1-450 [» ]
    3FMP X-ray 3.19 A/C 1-450 [» ]
    ProteinModelPortali P35658.
    SMRi P35658. Positions 1-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113717. 51 interactions.
    DIPi DIP-38367N.
    IntActi P35658. 18 interactions.
    MINTi MINT-121482.
    STRINGi 9606.ENSP00000352400.

    PTM databases

    PhosphoSitei P35658.

    Polymorphism databases

    DMDMi 205831380.

    Proteomic databases

    MaxQBi P35658.
    PaxDbi P35658.
    PRIDEi P35658.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359428 ; ENSP00000352400 ; ENSG00000126883 . [P35658-1 ]
    ENST00000411637 ; ENSP00000396576 ; ENSG00000126883 . [P35658-4 ]
    ENST00000451030 ; ENSP00000405014 ; ENSG00000126883 . [P35658-3 ]
    GeneIDi 8021.
    KEGGi hsa:8021.
    UCSCi uc004caf.1. human. [P35658-2 ]
    uc004cag.3. human. [P35658-1 ]
    uc004cah.3. human. [P35658-4 ]

    Organism-specific databases

    CTDi 8021.
    GeneCardsi GC09P134000.
    HGNCi HGNC:8064. NUP214.
    HPAi HPA018404.
    HPA048789.
    MIMi 114350. gene.
    neXtProti NX_P35658.
    Orphaneti 98277. Acute myeloid leukemia with recurrent genetic anomaly.
    PharmGKBi PA31851.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG052683.
    KOi K14317.
    OMAi NERNRDS.
    OrthoDBi EOG7V765H.
    PhylomeDBi P35658.
    TreeFami TF323517.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_25218. HuR stabilizes mRNA.
    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 P35658.

    Miscellaneous databases

    ChiTaRSi NUP214. human.
    EvolutionaryTracei P35658.
    GeneWikii NUP214.
    GenomeRNAii 8021.
    NextBioi 30584.
    PROi P35658.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35658.
    Bgeei P35658.
    CleanExi HS_NUP214.
    Genevestigatori P35658.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    [Graphical view ]
    SMARTi SM00320. WD40. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA."
      Von Lindern M., Fornerod M., Van Baal S., Jaegle M., De Wit T., Buijs A., Grosveld G.
      Mol. Cell. Biol. 12:1687-1697(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-574.
      Tissue: Testis.
    2. "Homo sapiens mRNA for KIAA0023 splice variant 1 protein."
      Nagase T., Kikuno R., Ohara O.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] (ISOFORMS 1 AND 4), VARIANT SER-574.
      Tissue: Placenta and Testis.
    6. "The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm."
      Kraemer D., Wozniak R.W., Blobel G., Radu A.
      Proc. Natl. Acad. Sci. U.S.A. 91:1519-1523(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and the novel nuclear pore component Nup88."
      Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D., Murti K.G., Fransen J., Grosveld G.
      EMBO J. 16:807-816(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XPO1.
    8. "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.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-430 AND THR-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-651; SER-940 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; THR-434; THR-437; THR-439; SER-666; SER-970; SER-974; SER-1023 AND SER-1963, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25."
      Pasdeloup D., Blondel D., Isidro A.L., Rixon F.J.
      J. Virol. 83:6610-6623(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-1 PROTEIN UL25.
    16. "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-430 AND SER-989, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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-657; THR-670; SER-678; SER-940; SER-1045; SER-1081; THR-1134; THR-1150; THR-1156; THR-1312 AND SER-1985, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-433; THR-434; THR-437; SER-657; THR-670; SER-678 AND SER-940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    21. "Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN."
      Napetschnig J., Blobel G., Hoelz A.
      Proc. Natl. Acad. Sci. U.S.A. 104:1783-1788(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-434, BETA-PROPELLER DOMAIN.
    22. "The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner."
      von Moeller H., Basquin C., Conti E.
      Nat. Struct. Mol. Biol. 16:247-254(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-405 IN COMPLEX WITH DDX19B, MUTAGENESIS OF VAL-353 AND ASP-359.
    23. "Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19."
      Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G., Hoelz A.
      Proc. Natl. Acad. Sci. U.S.A. 106:3089-3094(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-450 IN COMPLEX WITH DDX19B, COILED-COIL DOMAIN.
    24. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-424; LEU-1378 AND VAL-1392.

    Entry informationi

    Entry nameiNU214_HUMAN
    AccessioniPrimary (citable) accession number: P35658
    Secondary accession number(s): A6NFQ0
    , Q15010, Q3KQZ0, Q5JUP7, Q75R47, Q86XD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 148 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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

    External Data

    Dasty 3