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Protein

Nuclear pore complex protein Nup214

Gene

NUP214

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei812 – 813Breakpoint2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126883-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP35658.
SIGNORiP35658.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8064. NUP214.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi353V → A: Reduced binding to DDX19B. 1 Publication1
Mutagenesisi359D → R: Impairs interaction with DDX19B. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi8021.
MalaCardsiNUP214.
OpenTargetsiENSG00000126883.
Orphaneti402014. 'Acute myeloid leukemia with t(6;9)(p23;q34)'.
PharmGKBiPA31851.

Polymorphism and mutation databases

BioMutaiNUP214.
DMDMi205831380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002048612 – 2090Nuclear pore complex protein Nup214Add BLAST2089

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineCombined sources1
Modified residuei30PhosphoserineCombined sources1
Modified residuei416PhosphothreonineCombined sources1
Modified residuei421PhosphoserineCombined sources1
Modified residuei430PhosphoserineCombined sources1
Modified residuei433PhosphoserineCombined sources1
Modified residuei434PhosphothreonineCombined sources1
Modified residuei437PhosphothreonineCombined sources1
Modified residuei439PhosphothreonineCombined sources1
Modified residuei651PhosphoserineCombined sources1
Modified residuei657PhosphoserineCombined sources1
Modified residuei666PhosphoserineCombined sources1
Modified residuei670PhosphothreonineCombined sources1
Modified residuei678PhosphoserineCombined sources1
Modified residuei760PhosphoserineCombined sources1
Modified residuei940PhosphoserineCombined sources1
Modified residuei970PhosphoserineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei989PhosphoserineCombined sources1
Modified residuei1021PhosphothreonineCombined sources1
Modified residuei1023PhosphoserineCombined sources1
Modified residuei1045PhosphoserineCombined sources1
Modified residuei1056PhosphoserineCombined sources1
Modified residuei1081PhosphoserineCombined sources1
Modified residuei1134PhosphothreonineCombined sources1
Modified residuei1150PhosphothreonineCombined sources1
Modified residuei1156PhosphothreonineCombined sources1
Modified residuei1181PhosphoserineCombined sources1
Modified residuei1312PhosphothreonineCombined sources1
Modified residuei1353PhosphoserineCombined sources1
Modified residuei1963PhosphoserineCombined sources1
Modified residuei1985PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP35658.
MaxQBiP35658.
PaxDbiP35658.
PeptideAtlasiP35658.
PRIDEiP35658.

PTM databases

iPTMnetiP35658.
PhosphoSitePlusiP35658.

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

BgeeiENSG00000126883.
CleanExiHS_NUP214.
ExpressionAtlasiP35658. baseline and differential.
GenevisibleiP35658. HS.

Organism-specific databases

HPAiHPA018404.
HPA048789.

Interactioni

Subunit structurei

Homodimer. Interacts with NUP214; this interaction increases upon lipopolysaccharide (LPS) stimulation (PubMed:14766228). Interacts with DDX19 (PubMed:19219046, PubMed:19208808). Interacts with NUP88 (PubMed:9049309). Interacts with XPO1 (PubMed:9049309). Interacts with XPO5 (PubMed:11777942).5 Publications
(Microbial infection) Interacts with human herpes virus 1 (HHV-1) protein UL25; this interaction might be essential to the capsid docking onto the host nuclear pore.1 Publication

Protein-protein interaction databases

BioGridi113717. 78 interactors.
DIPiDIP-38367N.
IntActiP35658. 39 interactors.
MINTiMINT-121482.
STRINGi9606.ENSP00000352400.

Structurei

Secondary structure

12090
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi11 – 21Combined sources11
Beta strandi24 – 26Combined sources3
Beta strandi42 – 45Combined sources4
Turni46 – 49Combined sources4
Beta strandi50 – 55Combined sources6
Beta strandi58 – 63Combined sources6
Helixi64 – 67Combined sources4
Beta strandi80 – 82Combined sources3
Beta strandi87 – 89Combined sources3
Beta strandi95 – 100Combined sources6
Beta strandi106 – 113Combined sources8
Turni114 – 116Combined sources3
Beta strandi117 – 124Combined sources8
Helixi125 – 129Combined sources5
Beta strandi139 – 143Combined sources5
Helixi148 – 150Combined sources3
Beta strandi151 – 157Combined sources7
Beta strandi164 – 169Combined sources6
Beta strandi174 – 189Combined sources16
Helixi191 – 193Combined sources3
Beta strandi195 – 200Combined sources6
Beta strandi207 – 211Combined sources5
Beta strandi216 – 219Combined sources4
Beta strandi225 – 229Combined sources5
Beta strandi237 – 239Combined sources3
Beta strandi241 – 250Combined sources10
Beta strandi253 – 260Combined sources8
Beta strandi265 – 267Combined sources3
Beta strandi270 – 275Combined sources6
Beta strandi286 – 289Combined sources4
Beta strandi299 – 301Combined sources3
Beta strandi305 – 310Combined sources6
Helixi311 – 313Combined sources3
Beta strandi315 – 320Combined sources6
Beta strandi323 – 325Combined sources3
Beta strandi327 – 331Combined sources5
Beta strandi338 – 343Combined sources6
Helixi345 – 347Combined sources3
Beta strandi357 – 359Combined sources3
Beta strandi362 – 368Combined sources7
Beta strandi375 – 378Combined sources4
Beta strandi381 – 383Combined sources3
Beta strandi388 – 393Combined sources6
Beta strandi396 – 405Combined sources10
Helixi1925 – 1929Combined sources5
Beta strandi1937 – 1941Combined sources5
Turni1943 – 1945Combined sources3
Helixi2016 – 2019Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OITX-ray1.65A1-434[»]
3FHCX-ray2.80A1-405[»]
3FMOX-ray2.51A1-450[»]
3FMPX-ray3.19A/C1-450[»]
5DISX-ray2.85D1916-2027[»]
ProteinModelPortaliP35658.
SMRiP35658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35658.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati41 – 93Blade 1Add BLAST53
Repeati94 – 150Blade 2Add BLAST57
Repeati151 – 193Blade 3Add BLAST43
Repeati194 – 239Blade 4Add BLAST46
Repeati240 – 303Blade 5Add BLAST64
Repeati304 – 359Blade 6Add BLAST56
Repeati360 – 404Blade 7Add BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 404Seven-bladed beta propellerAdd BLAST364
Regioni481 – 207611 X 5 AA approximate repeatsAdd BLAST1596
Regioni740 – 768Leucine-zipper 1Add BLAST29
Regioni861 – 882Leucine-zipper 2Add BLAST22
Regioni1409 – 208418 X 4 AA approximate repeatsAdd BLAST676
Regioni1427 – 208511 X 3 AA approximate repeatsAdd BLAST659

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili680 – 12091 PublicationAdd BLAST530

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1213 – 2090Pro/Ser/Thr-richAdd BLAST878

Domaini

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG3630. Eukaryota.
ENOG410YBVS. LUCA.
GeneTreeiENSGT00730000111045.
HOVERGENiHBG052683.
InParanoidiP35658.
KOiK14317.
OMAiFNFGIIT.
OrthoDBiEOG091G02Y1.
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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti149G → A in CAA45535 (PubMed:1549122).Curated1
Sequence conflicti175A → D in CAA45535 (PubMed:1549122).Curated1
Sequence conflicti1091 – 1092AA → QL in CAA45535 (PubMed:1549122).Curated2
Sequence conflicti1872S → N in AAH45620 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035856424G → A in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_045691574P → S.2 PublicationsCorresponds to variant rs103612dbSNPEnsembl.1
Natural variantiVAR_0358571378P → L in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs777822003dbSNPEnsembl.1
Natural variantiVAR_0358581392A → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0615331592G → A.Corresponds to variant rs28594669dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_034896590 – 601KFTAA…STPVS → N in isoform 2, isoform 4 and isoform 5. 2 PublicationsAdd BLAST12
Alternative sequenceiVSP_034897648S → SA in isoform 3 and isoform 4. 1 Publication1
Alternative sequenceiVSP_0348981139 – 1148Missing in isoform 5. 1 Publication10
Alternative sequenceiVSP_0348992026 – 2090FGSSS…GGWRS → SLAMSLSPTLKGRLLLMRPK AGGGREQAAPGRKSNESRSL GHLCMERALTSPLKVWEQQQ HHILRHARESECPHFRITVP TDFWFWDPE in isoform 5. 1 PublicationAdd BLAST65

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]
CCDS83429.1. [P35658-4]
PIRiS26058.
RefSeqiNP_001305253.1. NM_001318324.1. [P35658-4]
NP_001305254.1. NM_001318325.1.
NP_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.
UCSCiuc004cag.4. human. [P35658-1]

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.
CCDSiCCDS6940.1. [P35658-1]
CCDS83429.1. [P35658-4]
PIRiS26058.
RefSeqiNP_001305253.1. NM_001318324.1. [P35658-4]
NP_001305254.1. NM_001318325.1.
NP_005076.3. NM_005085.3. [P35658-1]
UniGeneiHs.654530.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OITX-ray1.65A1-434[»]
3FHCX-ray2.80A1-405[»]
3FMOX-ray2.51A1-450[»]
3FMPX-ray3.19A/C1-450[»]
5DISX-ray2.85D1916-2027[»]
ProteinModelPortaliP35658.
SMRiP35658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113717. 78 interactors.
DIPiDIP-38367N.
IntActiP35658. 39 interactors.
MINTiMINT-121482.
STRINGi9606.ENSP00000352400.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP35658.
PhosphoSitePlusiP35658.

Polymorphism and mutation databases

BioMutaiNUP214.
DMDMi205831380.

Proteomic databases

EPDiP35658.
MaxQBiP35658.
PaxDbiP35658.
PeptideAtlasiP35658.
PRIDEiP35658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359428; ENSP00000352400; ENSG00000126883. [P35658-1]
ENST00000411637; ENSP00000396576; ENSG00000126883. [P35658-4]
GeneIDi8021.
KEGGihsa:8021.
UCSCiuc004cag.4. human. [P35658-1]

Organism-specific databases

CTDi8021.
DisGeNETi8021.
GeneCardsiNUP214.
HGNCiHGNC:8064. NUP214.
HPAiHPA018404.
HPA048789.
MalaCardsiNUP214.
MIMi114350. gene.
neXtProtiNX_P35658.
OpenTargetsiENSG00000126883.
Orphaneti402014. 'Acute myeloid leukemia with t(6;9)(p23;q34)'.
PharmGKBiPA31851.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3630. Eukaryota.
ENOG410YBVS. LUCA.
GeneTreeiENSGT00730000111045.
HOVERGENiHBG052683.
InParanoidiP35658.
KOiK14317.
OMAiFNFGIIT.
OrthoDBiEOG091G02Y1.
PhylomeDBiP35658.
TreeFamiTF323517.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126883-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP35658.
SIGNORiP35658.

Miscellaneous databases

ChiTaRSiNUP214. human.
EvolutionaryTraceiP35658.
GeneWikiiNUP214.
GenomeRNAii8021.
PROiP35658.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126883.
CleanExiHS_NUP214.
ExpressionAtlasiP35658. baseline and differential.
GenevisibleiP35658. HS.

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]
ProtoNetiSearch...

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 30, 2016
This is version 173 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.