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P35658 (NU214_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear pore complex protein Nup214
Alternative name(s):
214 kDa nucleoporin
Nucleoporin Nup214
Protein CAN
Gene names
Name:NUP214
Synonyms:CAIN, CAN, KIAA0023
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2090 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.7 Ref.8 Ref.15

Subcellular location

Nucleusnuclear pore complex. Note: Cytoplasmic filaments.

Tissue specificity

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

Domain

Contains FG repeats. Ref.21 Ref.23

The beta-propeller contains long interblade connector loops, and mediates interaction with DDX19B. Ref.21 Ref.23

Post-translational modification

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

Involvement in disease

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.

Sequence caution

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

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentNuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
Repeat
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

mRNA export from nucleus

Inferred from electronic annotation. Source: Ensembl

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

protein export from nucleus

Inferred from mutant phenotype PubMed 12191473. Source: MGI

protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of glucose transport

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear pore

Traceable author statement Ref.6. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionnucleocytoplasmic transporter activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 11545741. Source: UniProtKB

transporter activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35658-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35658-2)

The sequence of this isoform differs from the canonical sequence as follows:
     590-601: KFTAAATSTPVS → N
Note: No experimental confirmation available.
Isoform 3 (identifier: P35658-3)

The sequence of this isoform differs from the canonical sequence as follows:
     648-648: S → SA
Note: No experimental confirmation available.
Isoform 4 (identifier: P35658-4)

The sequence of this isoform differs from the canonical sequence as follows:
     590-601: KFTAAATSTPVS → N
     648-648: S → SA
Isoform 5 (identifier: P35658-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.20
Chain2 – 20902089Nuclear pore complex protein Nup214
PRO_0000204861

Regions

Repeat41 – 9353Blade 1
Repeat94 – 15057Blade 2
Repeat151 – 19343Blade 3
Repeat194 – 23946Blade 4
Repeat240 – 30364Blade 5
Repeat304 – 35956Blade 6
Repeat360 – 40445Blade 7
Region41 – 404364Seven-bladed beta propeller
Region481 – 2076159611 X 5 AA approximate repeats
Region740 – 76829Leucine-zipper 1
Region861 – 88222Leucine-zipper 2
Region1409 – 208467618 X 4 AA approximate repeats
Region1427 – 208565911 X 3 AA approximate repeats
Coiled coil680 – 1209530 Ref.23
Compositional bias1213 – 2090878Pro/Ser/Thr-rich

Sites

Site812 – 8132Breakpoint

Amino acid modifications

Modified residue21N-acetylglycine Ref.20
Modified residue4301Phosphoserine Ref.10 Ref.13 Ref.16
Modified residue4331Phosphoserine Ref.19
Modified residue4341Phosphothreonine Ref.13 Ref.19
Modified residue4371Phosphothreonine Ref.13 Ref.19
Modified residue4391Phosphothreonine Ref.10 Ref.13
Modified residue6511Phosphoserine Ref.12
Modified residue6571Phosphoserine Ref.17 Ref.19
Modified residue6661Phosphoserine Ref.13
Modified residue6701Phosphothreonine Ref.17 Ref.19
Modified residue6781Phosphoserine Ref.17 Ref.19
Modified residue9401Phosphoserine Ref.12 Ref.17 Ref.19
Modified residue9701Phosphoserine Ref.13
Modified residue9741Phosphoserine Ref.13
Modified residue9891Phosphoserine Ref.16
Modified residue10231Phosphoserine Ref.13
Modified residue10451Phosphoserine Ref.17
Modified residue10811Phosphoserine Ref.17
Modified residue11341Phosphothreonine Ref.17
Modified residue11501Phosphothreonine Ref.17
Modified residue11561Phosphothreonine Ref.17
Modified residue11811Phosphoserine Ref.12
Modified residue13121Phosphothreonine Ref.17
Modified residue19631Phosphoserine Ref.13
Modified residue19851Phosphoserine Ref.17

Natural variations

Alternative sequence590 – 60112KFTAA…STPVS → N in isoform 2, isoform 4 and isoform 5.
VSP_034896
Alternative sequence6481S → SA in isoform 3 and isoform 4.
VSP_034897
Alternative sequence1139 – 114810Missing in isoform 5.
VSP_034898
Alternative sequence2026 – 209065FGSSS…GGWRS → SLAMSLSPTLKGRLLLMRPK AGGGREQAAPGRKSNESRSL GHLCMERALTSPLKVWEQQQ HHILRHARESECPHFRITVP TDFWFWDPE in isoform 5.
VSP_034899
Natural variant4241G → A in a breast cancer sample; somatic mutation. Ref.24
VAR_035856
Natural variant5741P → S. Ref.1 Ref.5
Corresponds to variant rs103612 [ dbSNP | Ensembl ].
VAR_045691
Natural variant13781P → L in a breast cancer sample; somatic mutation. Ref.24
VAR_035857
Natural variant13921A → V in a breast cancer sample; somatic mutation. Ref.24
VAR_035858
Natural variant15921G → A.
Corresponds to variant rs28594669 [ dbSNP | Ensembl ].
VAR_061533

Experimental info

Mutagenesis3531V → A: Reduced binding to DDX19B. Ref.22
Mutagenesis3591D → R: Impairs interaction with DDX19B. Ref.22
Sequence conflict1491G → A in CAA45535. Ref.1
Sequence conflict1751A → D in CAA45535. Ref.1
Sequence conflict1091 – 10922AA → QL in CAA45535. Ref.1
Sequence conflict18721S → N in AAH45620. Ref.5

Secondary structure

................................................................................... 2090
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: EE6F0F3DE3D522C6

FASTA2,090213,620
        10         20         30         40         50         60 
MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS LLAVSNKYGL VFAGGASGLQ 

        70         80         90        100        110        120 
IFPTKNLLIQ NKPGDDPNKI VDKVQGLLVP MKFPIHHLAL SCDNLTLSAC MMSSEYGSII 

       130        140        150        160        170        180 
AFFDVRTFSN EAKQQKRPFA YHKLLKDAGG MVIDMKWNPT VPSMVAVCLA DGSIAVLQVT 

       190        200        210        220        230        240 
ETVKVCATLP STVAVTSVCW SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP 

       250        260        270        280        290        300 
VRVLDVLWIG TYVFAIVYAA ADGTLETSPD VVMALLPKKE EKHPEIFVNF MEPCYGSCTE 

       310        320        330        340        350        360 
RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQSDQINWES WLLEDSSRAE LPVTDKSDDS 

       370        380        390        400        410        420 
LPMGVVVDYT NQVEITISDE KTLPPAPVLM LLSTDGVLCP FYMINQNPGV KSLIKTPERL 

       430        440        450        460        470        480 
SLEGERQPKS PGSTPTTPTS SQAPQKLDAS AAAAPASLPP SSPAAPIATF SLLPAGGAPT 

       490        500        510        520        530        540 
VFSFGSSSLK SSATVTGEPP SYSSGSDSSK AAPGPGPSTF SFVPPSKASL APTPAASPVA 

       550        560        570        580        590        600 
PSAASFSFGS SGFKPTLEST PVPSVSAPNI AMKPSFPPST SAVKVNLSEK FTAAATSTPV 

       610        620        630        640        650        660 
SSSQSAPPMS PFSSASKPAA SGPLSHPTPL SAPPSSVPLK SSVLPSPSGR SAQGSSSPVP 

       670        680        690        700        710        720 
SMVQKSPRIT PPAAKPGSPQ AKSLQPAVAE KQGHQWKDSD PVMAGIGEEI AHFQKELEEL 

       730        740        750        760        770        780 
KARTSKACFQ VGTSEEMKML RTESDDLHTF LLEIKETTES LHGDISSLKT TLLEGFAGVE 

       790        800        810        820        830        840 
EAREQNERNR DSGYLHLLYK RPLDPKSEAQ LQEIRRLHQY VKFAVQDVND VLDLEWDQHL 

       850        860        870        880        890        900 
EQKKKQRHLL VPERETLFNT LANNREIINQ QRKRLNHLVD SLQQLRLYKQ TSLWSLSSAV 

       910        920        930        940        950        960 
PSQSSIHSFD SDLESLCNAL LKTTIESHTK SLPKVPAKLS PMKQAQLRNF LAKRKTPPVR 

       970        980        990       1000       1010       1020 
STAPASLSRS AFLSQRYYED LDEVSSTSSV SQSLESEDAR TSCKDDEAVV QAPRHAPVVR 

      1030       1040       1050       1060       1070       1080 
TPSIQPSLLP HAAPFAKSHL VHGSSPGVMG TSVATSASKI IPQGADSTML ATKTVKHGAP 

      1090       1100       1110       1120       1130       1140 
SPSHPISAPQ AAAAAALRRQ MASQAPAVNT LTESTLKNVP QVVNVQELKN NPATPSTAMG 

      1150       1160       1170       1180       1190       1200 
SSVPYSTAKT PHPVLTPVAA NQAKQGSLIN SLKPSGPTPA SGQLSSGDKA SGTAKIETAV 

      1210       1220       1230       1240       1250       1260 
TSTPSASGQF SKPFSFSPSG TGFNFGIITP TPSSNFTAAQ GATPSTKESS QPDAFSSGGG 

      1270       1280       1290       1300       1310       1320 
SKPSYEAIPE SSPPSGITSA SNTTPGEPAA SSSRPVAPSG TALSTTSSKL ETPPSKLGEL 

      1330       1340       1350       1360       1370       1380 
LFPSSLAGET LGSFSGLRVG QADDSTKPTN KASSTSLTST QPTKTSGVPS GFNFTAPPVL 

      1390       1400       1410       1420       1430       1440 
GKHTEPPVTS SATTTSVAPP AATSTSSTAV FGSLPVTSAG SSGVISFGGT SLSAGKTSFS 

      1450       1460       1470       1480       1490       1500 
FGSQQTNSTV PPSAPPPTTA ATPLPTSFPT LSFGSLLSSA TTPSLPMSAG RSTEEATSSA 

      1510       1520       1530       1540       1550       1560 
LPEKPGDSEV SASAASLLEE QQSAQLPQAP PQTSDSVKKE PVLAQPAVSN SGTAASSTSL 

      1570       1580       1590       1600       1610       1620 
VALSAEATPA TTGVPDARTE AVPPASSFSV PGQTAVTAAA ISSAGPVAVE TSSTPIASST 

      1630       1640       1650       1660       1670       1680 
TSIVAPGPSA EAAAFGTVTS GSSVFAQPPA ASSSSAFNQL TNNTATAPSA TPVFGQVAAS 

      1690       1700       1710       1720       1730       1740 
TAPSLFGQQT GSTASTAAAT PQVSSSGFSS PAFGTTAPGV FGQTTFGQAS VFGQSASSAA 

      1750       1760       1770       1780       1790       1800 
SVFSFSQPGF SSVPAFGQPA SSTPTSTSGS VFGAASSTSS SSSFSFGQSS PNTGGGLFGQ 

      1810       1820       1830       1840       1850       1860 
SNAPAFGQSP GFGQGGSVFG GTSAATTTAA TSGFSFCQAS GFGSSNTGSV FGQAASTGGI 

      1870       1880       1890       1900       1910       1920 
VFGQQSSSSS GSVFGSGNTG RGGGFFSGLG GKPSQDAANK NPFSSASGGF GSTATSNTSN 

      1930       1940       1950       1960       1970       1980 
LFGNSGAKTF GGFASSSFGE QKPTGTFSSG GGSVASQGFG FSSPNKTGGF GAAPVFGSPP 

      1990       2000       2010       2020       2030       2040 
TFGGSPGFGG VPAFGSAPAF TSPLGSTGGK VFGEGTAAAS AGGFGFGSSS NTTSFGTLAS 

      2050       2060       2070       2080       2090 
QNAPTFGSLS QQTSGFGTQS SGFSGFGSGT GGFSFGSNNS SVQGFGGWRS 

« Hide

Isoform 2 [UniParc].

Checksum: 159D32101C9DF54A
Show »

FASTA2,079212,571
Isoform 3 [UniParc].

Checksum: 765727236C2B47C8
Show »

FASTA2,091213,691
Isoform 4 [UniParc].

Checksum: A5ECD51E41D40F1F
Show »

FASTA2,080212,643
Isoform 5 [UniParc].

Checksum: 4C67CE62D57E590F
Show »

FASTA2,093215,401

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-424; LEU-1378 AND VAL-1392.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6940.1. [P35658-1]
PIRS26058.
RefSeqNP_005076.3. NM_005085.3. [P35658-1]
UniGeneHs.654530.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OITX-ray1.65A1-434[»]
3FHCX-ray2.80A1-405[»]
3FMOX-ray2.51A1-450[»]
3FMPX-ray3.19A/C1-450[»]
ProteinModelPortalP35658.
SMRP35658. Positions 1-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113717. 51 interactions.
DIPDIP-38367N.
IntActP35658. 18 interactions.
MINTMINT-121482.
STRING9606.ENSP00000352400.

PTM databases

PhosphoSiteP35658.

Polymorphism databases

DMDM205831380.

Proteomic databases

MaxQBP35658.
PaxDbP35658.
PRIDEP35658.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359428; ENSP00000352400; ENSG00000126883. [P35658-1]
ENST00000411637; ENSP00000396576; ENSG00000126883. [P35658-4]
ENST00000451030; ENSP00000405014; ENSG00000126883. [P35658-3]
GeneID8021.
KEGGhsa:8021.
UCSCuc004caf.1. human. [P35658-2]
uc004cag.3. human. [P35658-1]
uc004cah.3. human. [P35658-4]

Organism-specific databases

CTD8021.
GeneCardsGC09P134000.
HGNCHGNC:8064. NUP214.
HPAHPA018404.
HPA048789.
MIM114350. gene.
neXtProtNX_P35658.
Orphanet98277. Acute myeloid leukemia with recurrent genetic anomaly.
PharmGKBPA31851.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG052683.
KOK14317.
OMANERNRDS.
OrthoDBEOG7V765H.
PhylomeDBP35658.
TreeFamTF323517.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.
REACT_71. Gene Expression.
SignaLinkP35658.

Gene expression databases

ArrayExpressP35658.
BgeeP35658.
CleanExHS_NUP214.
GenevestigatorP35658.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
[Graphical view]
SMARTSM00320. WD40. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNUP214. human.
EvolutionaryTraceP35658.
GeneWikiNUP214.
GenomeRNAi8021.
NextBio30584.
PROP35658.
SOURCESearch...

Entry information

Entry nameNU214_HUMAN
AccessionPrimary (citable) accession number: P35658
Secondary accession number(s): A6NFQ0 expand/collapse secondary AC list , Q15010, Q3KQZ0, Q5JUP7, Q75R47, Q86XD3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM