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P35658

- NU214_HUMAN

UniProt

P35658 - NU214_HUMAN

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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

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. 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
Complete GO annotation...

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_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
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
Complete GO annotation...

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

BgeeiP35658.
CleanExiHS_NUP214.
ExpressionAtlasiP35658. baseline and differential.
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. 55 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 – 74Combined sources
Beta strandi11 – 2111Combined sources
Beta strandi24 – 263Combined sources
Beta strandi42 – 454Combined sources
Turni46 – 494Combined sources
Beta strandi50 – 556Combined sources
Beta strandi58 – 636Combined sources
Helixi64 – 674Combined sources
Beta strandi80 – 823Combined sources
Beta strandi87 – 893Combined sources
Beta strandi95 – 1006Combined sources
Beta strandi106 – 1138Combined sources
Turni114 – 1163Combined sources
Beta strandi117 – 1248Combined sources
Helixi125 – 1295Combined sources
Beta strandi139 – 1435Combined sources
Helixi148 – 1503Combined sources
Beta strandi151 – 1577Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi174 – 18916Combined sources
Helixi191 – 1933Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi207 – 2115Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi225 – 2295Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 25010Combined sources
Beta strandi253 – 2608Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2756Combined sources
Beta strandi286 – 2894Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi305 – 3106Combined sources
Helixi311 – 3133Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi327 – 3315Combined sources
Beta strandi338 – 3436Combined sources
Helixi345 – 3473Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi362 – 3687Combined sources
Beta strandi375 – 3784Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi396 – 40510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000111045.
HOVERGENiHBG052683.
InParanoidiP35658.
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

        10         20         30         40         50
MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS LLAVSNKYGL
60 70 80 90 100
VFAGGASGLQ IFPTKNLLIQ NKPGDDPNKI VDKVQGLLVP MKFPIHHLAL
110 120 130 140 150
SCDNLTLSAC MMSSEYGSII AFFDVRTFSN EAKQQKRPFA YHKLLKDAGG
160 170 180 190 200
MVIDMKWNPT VPSMVAVCLA DGSIAVLQVT ETVKVCATLP STVAVTSVCW
210 220 230 240 250
SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP VRVLDVLWIG
260 270 280 290 300
TYVFAIVYAA ADGTLETSPD VVMALLPKKE EKHPEIFVNF MEPCYGSCTE
310 320 330 340 350
RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQSDQINWES WLLEDSSRAE
360 370 380 390 400
LPVTDKSDDS LPMGVVVDYT NQVEITISDE KTLPPAPVLM LLSTDGVLCP
410 420 430 440 450
FYMINQNPGV KSLIKTPERL SLEGERQPKS PGSTPTTPTS SQAPQKLDAS
460 470 480 490 500
AAAAPASLPP SSPAAPIATF SLLPAGGAPT VFSFGSSSLK SSATVTGEPP
510 520 530 540 550
SYSSGSDSSK AAPGPGPSTF SFVPPSKASL APTPAASPVA PSAASFSFGS
560 570 580 590 600
SGFKPTLEST PVPSVSAPNI AMKPSFPPST SAVKVNLSEK FTAAATSTPV
610 620 630 640 650
SSSQSAPPMS PFSSASKPAA SGPLSHPTPL SAPPSSVPLK SSVLPSPSGR
660 670 680 690 700
SAQGSSSPVP SMVQKSPRIT PPAAKPGSPQ AKSLQPAVAE KQGHQWKDSD
710 720 730 740 750
PVMAGIGEEI AHFQKELEEL KARTSKACFQ VGTSEEMKML RTESDDLHTF
760 770 780 790 800
LLEIKETTES LHGDISSLKT TLLEGFAGVE EAREQNERNR DSGYLHLLYK
810 820 830 840 850
RPLDPKSEAQ LQEIRRLHQY VKFAVQDVND VLDLEWDQHL EQKKKQRHLL
860 870 880 890 900
VPERETLFNT LANNREIINQ QRKRLNHLVD SLQQLRLYKQ TSLWSLSSAV
910 920 930 940 950
PSQSSIHSFD SDLESLCNAL LKTTIESHTK SLPKVPAKLS PMKQAQLRNF
960 970 980 990 1000
LAKRKTPPVR STAPASLSRS AFLSQRYYED LDEVSSTSSV SQSLESEDAR
1010 1020 1030 1040 1050
TSCKDDEAVV QAPRHAPVVR TPSIQPSLLP HAAPFAKSHL VHGSSPGVMG
1060 1070 1080 1090 1100
TSVATSASKI IPQGADSTML ATKTVKHGAP SPSHPISAPQ AAAAAALRRQ
1110 1120 1130 1140 1150
MASQAPAVNT LTESTLKNVP QVVNVQELKN NPATPSTAMG SSVPYSTAKT
1160 1170 1180 1190 1200
PHPVLTPVAA NQAKQGSLIN SLKPSGPTPA SGQLSSGDKA SGTAKIETAV
1210 1220 1230 1240 1250
TSTPSASGQF SKPFSFSPSG TGFNFGIITP TPSSNFTAAQ GATPSTKESS
1260 1270 1280 1290 1300
QPDAFSSGGG SKPSYEAIPE SSPPSGITSA SNTTPGEPAA SSSRPVAPSG
1310 1320 1330 1340 1350
TALSTTSSKL ETPPSKLGEL LFPSSLAGET LGSFSGLRVG QADDSTKPTN
1360 1370 1380 1390 1400
KASSTSLTST QPTKTSGVPS GFNFTAPPVL GKHTEPPVTS SATTTSVAPP
1410 1420 1430 1440 1450
AATSTSSTAV FGSLPVTSAG SSGVISFGGT SLSAGKTSFS FGSQQTNSTV
1460 1470 1480 1490 1500
PPSAPPPTTA ATPLPTSFPT LSFGSLLSSA TTPSLPMSAG RSTEEATSSA
1510 1520 1530 1540 1550
LPEKPGDSEV SASAASLLEE QQSAQLPQAP PQTSDSVKKE PVLAQPAVSN
1560 1570 1580 1590 1600
SGTAASSTSL VALSAEATPA TTGVPDARTE AVPPASSFSV PGQTAVTAAA
1610 1620 1630 1640 1650
ISSAGPVAVE TSSTPIASST TSIVAPGPSA EAAAFGTVTS GSSVFAQPPA
1660 1670 1680 1690 1700
ASSSSAFNQL TNNTATAPSA TPVFGQVAAS TAPSLFGQQT GSTASTAAAT
1710 1720 1730 1740 1750
PQVSSSGFSS PAFGTTAPGV FGQTTFGQAS VFGQSASSAA SVFSFSQPGF
1760 1770 1780 1790 1800
SSVPAFGQPA SSTPTSTSGS VFGAASSTSS SSSFSFGQSS PNTGGGLFGQ
1810 1820 1830 1840 1850
SNAPAFGQSP GFGQGGSVFG GTSAATTTAA TSGFSFCQAS GFGSSNTGSV
1860 1870 1880 1890 1900
FGQAASTGGI VFGQQSSSSS GSVFGSGNTG RGGGFFSGLG GKPSQDAANK
1910 1920 1930 1940 1950
NPFSSASGGF GSTATSNTSN LFGNSGAKTF GGFASSSFGE QKPTGTFSSG
1960 1970 1980 1990 2000
GGSVASQGFG FSSPNKTGGF GAAPVFGSPP TFGGSPGFGG VPAFGSAPAF
2010 2020 2030 2040 2050
TSPLGSTGGK VFGEGTAAAS AGGFGFGSSS NTTSFGTLAS QNAPTFGSLS
2060 2070 2080 2090
QQTSGFGTQS SGFSGFGSGT GGFSFGSNNS SVQGFGGWRS
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 55 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 ]
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.
GeneTreei ENSGT00730000111045.
HOVERGENi HBG052683.
InParanoidi P35658.
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_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
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

Bgeei P35658.
CleanExi HS_NUP214.
ExpressionAtlasi P35658. baseline and differential.
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 ]
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Publicationsi

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  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: November 26, 2014
This is version 150 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

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