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Protein

Nuclear pore complex protein Nup153

Gene

NUP153

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Cofactori

Zn2+By similarityNote: Binds at least 4 zinc ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi664Zinc 1By similarity1
Metal bindingi667Zinc 1By similarity1
Metal bindingi678Zinc 1By similarity1
Metal bindingi681Zinc 1By similarity1
Metal bindingi728Zinc 2Combined sources1
Metal bindingi731Zinc 2Combined sources1
Metal bindingi742Zinc 2Combined sources1
Metal bindingi745Zinc 2Combined sources1
Metal bindingi799Zinc 3Combined sources1
Metal bindingi802Zinc 3Combined sources1
Metal bindingi813Zinc 3Combined sources1
Metal bindingi816Zinc 3Combined sources1
Metal bindingi857Zinc 4Combined sources1
Metal bindingi860Zinc 4Combined sources1
Metal bindingi871Zinc 4Combined sources1
Metal bindingi874Zinc 4Combined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri657 – 687RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri722 – 751RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri793 – 822RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri851 – 880RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • nuclear localization sequence binding Source: GO_Central
  • nucleocytoplasmic transporter activity Source: UniProtKB
  • protein anchor Source: UniProtKB
  • structural constituent of nuclear pore Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124789-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-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.
SignaLinkiP49790.
SIGNORiP49790.

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 Nup153
Alternative name(s):
153 kDa nucleoporin
Nucleoporin Nup153
Gene namesi
Name:NUP153
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8062. NUP153.

Subcellular locationi

  • Nucleus
  • Nucleus membrane
  • Nucleusnuclear pore complex

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

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nuclear inclusion body Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nuclear periphery Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nuclear pore central transport channel Source: GO_Central
  • nuclear pore nuclear basket Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi9972.
OpenTargetsiENSG00000124789.
PharmGKBiPA31848.

Polymorphism and mutation databases

DMDMi206729891.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002048422 – 1475Nuclear pore complex protein Nup153Add BLAST1474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei102PhosphothreonineCombined sources1
Modified residuei182PhosphoserineCombined sources1
Modified residuei185PhosphoserineCombined sources1
Modified residuei192PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei209PhosphoserineCombined sources1
Modified residuei240PhosphoserineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei297PhosphoserineCombined sources1
Modified residuei320PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei333PhosphoserineCombined sources1
Modified residuei334PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei343PhosphoserineCombined sources1
Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei369PhosphothreonineCombined sources1
Modified residuei384N6-acetyllysineCombined sources1
Modified residuei388PhosphothreonineCombined sources1
Modified residuei500PhosphoserineCombined sources1
Modified residuei516PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Modified residuei522PhosphoserineCombined sources1
Modified residuei529PhosphoserineCombined sources1
Glycosylationi534O-linked (GlcNAc)1 Publication1
Glycosylationi544O-linked (GlcNAc)1 Publication1
Modified residuei588PhosphothreonineCombined sources1
Modified residuei607PhosphoserineCombined sources1
Modified residuei614PhosphoserineCombined sources1
Modified residuei619PhosphoserineCombined sources1
Modified residuei633PhosphoserineCombined sources1
Modified residuei687PhosphoserineCombined sources1
Modified residuei718N6-acetyllysineCombined sources1
Modified residuei891PhosphoserineCombined sources1
Glycosylationi908O-linked (GlcNAc)1 Publication1
Glycosylationi909O-linked (GlcNAc)1 Publication1
Modified residuei954N6-acetyllysineCombined sources1
Glycosylationi1113O-linked (GlcNAc)1 Publication1
Glycosylationi1156O-linked (GlcNAc)1 Publication1
Modified residuei1457PhosphoserineCombined sources1
Modified residuei1461PhosphoserineCombined sources1
Modified residuei1463PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity).By similarity
Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49790.
MaxQBiP49790.
PaxDbiP49790.
PeptideAtlasiP49790.
PRIDEiP49790.

PTM databases

iPTMnetiP49790.
PhosphoSitePlusiP49790.

Miscellaneous databases

PMAP-CutDBP49790.

Expressioni

Gene expression databases

BgeeiENSG00000124789.
CleanExiHS_NUP153.
GenevisibleiP49790. HS.

Organism-specific databases

HPAiHPA027896.
HPA027897.
HPA027898.

Interactioni

Subunit structurei

Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner (By similarity). Part of the nuclear pore complex (NPC). Interacts with TPR (via coiled coil region); the interaction is direct and provides a link between the core structure and the TPR-containing nuclear basket of the nuclear pore complex (NPC). Interacts with HIV-1 integrase; this interaction might play a role in nuclear import of HIV pre-integration complex. Interacts with hepatitis B virus capsid protein; this interaction probably plays a role in nuclear import of HBV genome. Interacts with HIKESHI, SENP2 and XPO5. Interacts with Epstein-barr virus BGLF4; this interaction allows BGLF4 nuclear entry.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-286779,EBI-286779
EPHB2P293232EBI-286779,EBI-1059294
KPNB1Q149743EBI-286779,EBI-286758
MAPK14Q16539-32EBI-286779,EBI-6932370

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein anchor Source: UniProtKB

Protein-protein interaction databases

BioGridi115297. 117 interactors.
DIPiDIP-38185N.
IntActiP49790. 90 interactors.
MINTiMINT-121422.
STRINGi9606.ENSP00000262077.

Structurei

Secondary structure

11475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi723 – 727Combined sources5
Beta strandi729 – 731Combined sources3
Beta strandi743 – 745Combined sources3
Helixi755 – 757Combined sources3
Beta strandi794 – 796Combined sources3
Beta strandi800 – 802Combined sources3
Beta strandi814 – 816Combined sources3
Beta strandi858 – 860Combined sources3
Beta strandi872 – 874Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBQNMR-A722-761[»]
2EBRNMR-A851-890[»]
2EBVNMR-A773-822[»]
2GQENMR-A722-750[»]
4U0CX-ray1.77B1407-1423[»]
4U0DX-ray3.00M/N/O/P/Q/R1407-1423[»]
ProteinModelPortaliP49790.
SMRiP49790.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49790.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 14Gly-richAdd BLAST11
Compositional biasi443 – 447Poly-Gly5

Domaini

Contains F-X-F-G repeats.

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri657 – 687RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri722 – 751RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri793 – 822RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri851 – 880RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4719. Eukaryota.
ENOG41107SV. LUCA.
GeneTreeiENSGT00700000104544.
HOGENOMiHOG000088610.
HOVERGENiHBG052679.
InParanoidiP49790.
KOiK14296.
OMAiNFKFGDQ.
OrthoDBiEOG091G015X.
PhylomeDBiP49790.
TreeFamiTF323517.

Family and domain databases

InterProiIPR013913. Nup153_N.
IPR018892. Retro-transposon_transp_CS.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF08604. Nup153. 1 hit.
PF10599. Nup_retrotrp_bd. 1 hit.
PF00641. zf-RanBP. 4 hits.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 4 hits.
[Graphical view]
SUPFAMiSSF90209. SSF90209. 4 hits.
PROSITEiPS01358. ZF_RANBP2_1. 4 hits.
PS50199. ZF_RANBP2_2. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI
60 70 80 90 100
VPGWLQRYFN KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR
110 120 130 140 150
ITPEPAVSNT EEPSTTSTAS NYPDVLTRPS LHRSHLNFSM LESPALHCQP
160 170 180 190 200
STSSAFPIGS SGFSLVKEIK DSTSQHDDDN ISTTSGFSSR ASDKDITVSK
210 220 230 240 250
NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS PSLGNSSILK
260 270 280 290 300
TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS
310 320 330 340 350
YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF
360 370 380 390 400
QAKREKVDSQ YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI
410 420 430 440 450
DNKCSTGYEK NMTPGQNREQ RESGFSYPNF SLPAANGLSS GVGGGGGKMR
460 470 480 490 500
RERTRFVASK PLEEEEMEVP VLPKISLPIT SSSLPTFNFS SPEITTSSPS
510 520 530 540 550
PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL PPSSIGFTFS
560 570 580 590 600
VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA
610 620 630 640 650
EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI
660 670 680 690 700
GFGESLKAGS SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP
710 720 730 740 750
NKSGKTTLSA SGTGFGDKFK PVIGTWDCDT CLVQNKPEAI KCVACETPKP
760 770 780 790 800
GTCVKRALTL TVVSESAETM TASSSSCTVT TGTLGFGDKF KRPIGSWECS
810 820 830 840 850
VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG GSLGLEKFKK
860 870 880 890 900
PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS
910 920 930 940 950
SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF
960 970 980 990 1000
KFSKPIGDFK FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF
1010 1020 1030 1040 1050
GVSNLGQEEK KEELPKSSSA GFSFGTGVIN STPAPANTIV TSENKSSFNL
1060 1070 1080 1090 1100
GTIETKSASV APFTCKTSEA KKEEMPATKG GFSFGNVEPA SLPSASVFVL
1110 1120 1130 1140 1150
GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ TKDENSSKST
1160 1170 1180 1190 1200
FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS
1210 1220 1230 1240 1250
STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ
1260 1270 1280 1290 1300
SLLFSQDSKL ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA
1310 1320 1330 1340 1350
GSSFVFGTGP SAPSASPAFG ANQTPTFGQS QGASQPNPPG FGSISSSTAL
1360 1370 1380 1390 1400
FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ SAFGSGTTPN SSSAFQFGSS
1410 1420 1430 1440 1450
TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ SPAAFTVGSN
1460 1470
GKNVFSSSGT SFSGRKIKTA VRRRK
Length:1,475
Mass (Da):153,938
Last modified:September 23, 2008 - v2
Checksum:iD07455A691F7CD1F
GO
Isoform 2 (identifier: P49790-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:1,433
Mass (Da):149,396
Checksum:i109D4036D0912D37
GO
Isoform 3 (identifier: P49790-3) [UniParc]FASTAAdd to basket

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

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

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti111E → G in BAG58514 (PubMed:14702039).Curated1
Sequence conflicti454 – 455TR → HA in CAA80982 (PubMed:8110839).Curated2
Sequence conflicti813C → S in BAG58514 (PubMed:14702039).Curated1
Sequence conflicti836S → C in BAG58514 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04655490D → N.1 PublicationCorresponds to variant rs16879902dbSNPEnsembl.1
Natural variantiVAR_046555248I → V.Corresponds to variant rs2228375dbSNPEnsembl.1
Natural variantiVAR_070841381V → F.1 PublicationCorresponds to variant rs17857419dbSNPEnsembl.1
Natural variantiVAR_046556402N → K.Corresponds to variant rs6906499dbSNPEnsembl.1
Natural variantiVAR_046557821P → L.Corresponds to variant rs6905654dbSNPEnsembl.1
Natural variantiVAR_046558827A → T.1 PublicationCorresponds to variant rs2274136dbSNPEnsembl.1
Natural variantiVAR_0465591388T → A.Corresponds to variant rs45475293dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055134465E → ERQGLTVLPKLISSSCAQAI IPSWPLKVLRLQ in isoform 3. 1 Publication1
Alternative sequenceiVSP_054265574 – 615Missing in isoform 2. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25535 mRNA. Translation: CAA80982.1.
AK295644 mRNA. Translation: BAG58514.1.
AB210024 mRNA. Translation: BAE06106.1. Different initiation.
AL138824, AL138724, AL157776 Genomic DNA. Translation: CAI12246.1.
AL157776, AL138724, AL138824 Genomic DNA. Translation: CAI16393.1.
AL138724, AL138824, AL157776 Genomic DNA. Translation: CAI40945.1.
BC052965 mRNA. Translation: AAH52965.1.
CCDSiCCDS4541.1. [P49790-1]
CCDS64359.1. [P49790-3]
CCDS75407.1. [P49790-2]
PIRiS42718.
RefSeqiNP_001265138.1. NM_001278209.1. [P49790-3]
NP_001265139.1. NM_001278210.1. [P49790-2]
NP_005115.2. NM_005124.3. [P49790-1]
UniGeneiHs.601591.

Genome annotation databases

EnsembliENST00000262077; ENSP00000262077; ENSG00000124789. [P49790-1]
ENST00000537253; ENSP00000444029; ENSG00000124789. [P49790-3]
ENST00000613258; ENSP00000478627; ENSG00000124789. [P49790-2]
GeneIDi9972.
KEGGihsa:9972.
UCSCiuc003ncd.3. human. [P49790-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25535 mRNA. Translation: CAA80982.1.
AK295644 mRNA. Translation: BAG58514.1.
AB210024 mRNA. Translation: BAE06106.1. Different initiation.
AL138824, AL138724, AL157776 Genomic DNA. Translation: CAI12246.1.
AL157776, AL138724, AL138824 Genomic DNA. Translation: CAI16393.1.
AL138724, AL138824, AL157776 Genomic DNA. Translation: CAI40945.1.
BC052965 mRNA. Translation: AAH52965.1.
CCDSiCCDS4541.1. [P49790-1]
CCDS64359.1. [P49790-3]
CCDS75407.1. [P49790-2]
PIRiS42718.
RefSeqiNP_001265138.1. NM_001278209.1. [P49790-3]
NP_001265139.1. NM_001278210.1. [P49790-2]
NP_005115.2. NM_005124.3. [P49790-1]
UniGeneiHs.601591.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBQNMR-A722-761[»]
2EBRNMR-A851-890[»]
2EBVNMR-A773-822[»]
2GQENMR-A722-750[»]
4U0CX-ray1.77B1407-1423[»]
4U0DX-ray3.00M/N/O/P/Q/R1407-1423[»]
ProteinModelPortaliP49790.
SMRiP49790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115297. 117 interactors.
DIPiDIP-38185N.
IntActiP49790. 90 interactors.
MINTiMINT-121422.
STRINGi9606.ENSP00000262077.

Protein family/group databases

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

PTM databases

iPTMnetiP49790.
PhosphoSitePlusiP49790.

Polymorphism and mutation databases

DMDMi206729891.

Proteomic databases

EPDiP49790.
MaxQBiP49790.
PaxDbiP49790.
PeptideAtlasiP49790.
PRIDEiP49790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262077; ENSP00000262077; ENSG00000124789. [P49790-1]
ENST00000537253; ENSP00000444029; ENSG00000124789. [P49790-3]
ENST00000613258; ENSP00000478627; ENSG00000124789. [P49790-2]
GeneIDi9972.
KEGGihsa:9972.
UCSCiuc003ncd.3. human. [P49790-1]

Organism-specific databases

CTDi9972.
DisGeNETi9972.
GeneCardsiNUP153.
H-InvDBHIX0032892.
HIX0200901.
HGNCiHGNC:8062. NUP153.
HPAiHPA027896.
HPA027897.
HPA027898.
MIMi603948. gene.
neXtProtiNX_P49790.
OpenTargetsiENSG00000124789.
PharmGKBiPA31848.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4719. Eukaryota.
ENOG41107SV. LUCA.
GeneTreeiENSGT00700000104544.
HOGENOMiHOG000088610.
HOVERGENiHBG052679.
InParanoidiP49790.
KOiK14296.
OMAiNFKFGDQ.
OrthoDBiEOG091G015X.
PhylomeDBiP49790.
TreeFamiTF323517.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124789-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-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.
SignaLinkiP49790.
SIGNORiP49790.

Miscellaneous databases

ChiTaRSiNUP153. human.
EvolutionaryTraceiP49790.
GeneWikiiNUP153.
GenomeRNAii9972.
PMAP-CutDBP49790.
PROiP49790.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124789.
CleanExiHS_NUP153.
GenevisibleiP49790. HS.

Family and domain databases

InterProiIPR013913. Nup153_N.
IPR018892. Retro-transposon_transp_CS.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF08604. Nup153. 1 hit.
PF10599. Nup_retrotrp_bd. 1 hit.
PF00641. zf-RanBP. 4 hits.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 4 hits.
[Graphical view]
SUPFAMiSSF90209. SSF90209. 4 hits.
PROSITEiPS01358. ZF_RANBP2_1. 4 hits.
PS50199. ZF_RANBP2_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNU153_HUMAN
AccessioniPrimary (citable) accession number: P49790
Secondary accession number(s): B4DIK2
, E7EPX5, F6QR24, Q4LE47, Q5T9I7, Q7Z743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: November 30, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.