Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear pore complex protein Nup153

Gene

Nup153

Organism
Rattus norvegicus (Rat)
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 (By similarity). 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) (By similarity).By similarity

Cofactori

Zn2+Note: Binds at least 4 zinc ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi664Zinc 12 Publications1
Metal bindingi667Zinc 12 Publications1
Metal bindingi678Zinc 12 Publications1
Metal bindingi681Zinc 12 Publications1
Metal bindingi727Zinc 22 Publications1
Metal bindingi730Zinc 22 Publications1
Metal bindingi741Zinc 22 Publications1
Metal bindingi744Zinc 22 Publications1
Metal bindingi795Zinc 32 Publications1
Metal bindingi798Zinc 32 Publications1
Metal bindingi809Zinc 32 Publications1
Metal bindingi812Zinc 32 Publications1
Metal bindingi852Zinc 42 Publications1
Metal bindingi855Zinc 42 Publications1
Metal bindingi866Zinc 42 Publications1
Metal bindingi869Zinc 42 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri657 – 687RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri721 – 750RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri789 – 818RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri846 – 875RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30

GO - Molecular functioni

  • chromatin binding Source: RGD
  • double-stranded DNA binding Source: RGD
  • nuclear localization sequence binding Source: RGD
  • nucleocytoplasmic transporter activity Source: UniProtKB
  • protein anchor Source: UniProtKB
  • Ran GTPase binding Source: RGD
  • structural constituent of nuclear pore Source: UniProtKB
  • zinc ion binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup153
Alternative name(s):
153 kDa nucleoporin
Nucleoporin Nup153
Gene namesi
Name:Nup153
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3216. Nup153.

Subcellular locationi

  • Nucleus
  • Nucleus membrane
  • Nucleusnuclear pore complex

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

GO - Cellular componenti

  • annulate lamellae Source: RGD
  • 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
  • nucleoplasmic side of nuclear pore Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi714F → A: Reduces affinity for RAN; when associated with A-718. 1 Publication1
Mutagenesisi718F → A: Reduces affinity for RAN; when associated with A-714. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002048432 – 1468Nuclear pore complex protein Nup153Add BLAST1467

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei97PhosphothreonineCombined sources1
Modified residuei103PhosphothreonineBy similarity1
Modified residuei183PhosphoserineBy similarity1
Modified residuei186PhosphoserineBy similarity1
Modified residuei193PhosphoserineBy similarity1
Modified residuei204PhosphoserineBy similarity1
Modified residuei210PhosphoserineBy similarity1
Modified residuei241PhosphoserineBy similarity1
Modified residuei258PhosphoserineBy similarity1
Modified residuei321PhosphoserineBy similarity1
Modified residuei331PhosphoserineCombined sources1
Modified residuei334PhosphoserineBy similarity1
Modified residuei335PhosphoserineBy similarity1
Modified residuei339PhosphoserineCombined sources1
Modified residuei344PhosphoserineBy similarity1
Cross-linki354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei370PhosphothreonineBy similarity1
Modified residuei385N6-acetyllysineBy similarity1
Modified residuei389PhosphothreonineBy similarity1
Modified residuei500PhosphoserineBy similarity1
Modified residuei516PhosphoserineBy similarity1
Modified residuei529PhosphoserineBy similarity1
Glycosylationi534O-linked (GlcNAc)By similarity1
Glycosylationi544O-linked (GlcNAc)By similarity1
Modified residuei607PhosphoserineBy similarity1
Modified residuei619PhosphoserineBy similarity1
Modified residuei633PhosphoserineBy similarity1
Modified residuei717N6-acetyllysineBy similarity1
Modified residuei886PhosphoserineBy similarity1
Glycosylationi902O-linked (GlcNAc)By similarity1
Modified residuei947N6-acetyllysineBy similarity1
Glycosylationi1106O-linked (GlcNAc)By similarity1
Modified residuei1450PhosphoserineBy similarity1
Modified residuei1454PhosphoserineBy similarity1
Modified residuei1456PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis.
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP49791.
PRIDEiP49791.

PTM databases

iPTMnetiP49791.
PhosphoSitePlusiP49791.

Interactioni

Subunit structurei

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 HIKESHI, SENP2 and XPO5 (By similarity). Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner.By similarity2 Publications

GO - Molecular functioni

  • protein anchor Source: UniProtKB
  • Ran GTPase binding Source: RGD

Protein-protein interaction databases

DIPiDIP-46027N.
IntActiP49791. 1 interactor.
STRINGi10116.ENSRNOP00000001979.

Structurei

Secondary structure

11468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni665 – 667Combined sources3
Turni679 – 681Combined sources3
Beta strandi725 – 727Combined sources3
Turni728 – 730Combined sources3
Beta strandi732 – 734Combined sources3
Turni742 – 744Combined sources3
Turni796 – 798Combined sources3
Turni810 – 812Combined sources3
Turni853 – 855Combined sources3
Turni867 – 869Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K0CNMR-A703-755[»]
3CH5X-ray2.10B703-754[»]
3GJ3X-ray1.79B723-750[»]
3GJ4X-ray2.15B/D790-817[»]
3GJ5X-ray1.79B/D848-876[»]
3GJ6X-ray2.70B658-686[»]
3GJ7X-ray1.93B/D658-750[»]
3GJ8X-ray1.82B/D790-876[»]
ProteinModelPortaliP49791.
SMRiP49791.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49791.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 15Gly-richAdd BLAST12
Compositional biasi442 – 446Poly-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 fingeri721 – 750RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri789 – 818RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri846 – 875RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4719. Eukaryota.
ENOG41107SV. LUCA.
HOGENOMiHOG000088610.
HOVERGENiHBG052679.
InParanoidiP49791.
PhylomeDBiP49791.

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]

Sequencei

Sequence statusi: Complete.

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

P49791-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGAGGIGG GGGGGKIRTR RCHQGPVKPY QQGRPQHQGI LSRVTESVKN
60 70 80 90 100
IVPGWLQRYF NKSENACSCS VNADEVPRWP ENREDEREIY VDENTNTDDG
110 120 130 140 150
RTTPEPTGSN TEEPSTTSTA SNYPDVLTRP SLHRSHLNFS VLESPALHCQ
160 170 180 190 200
PSTSSAFPIG SSGFSLVKEI KDSTSQHDDD NISTTSGFSS RASEKDIAVS
210 220 230 240 250
KNTSLPPLWS PEAERSHSLS QHTAISSKKP AFNLSAFGTL STSLGNSSIL
260 270 280 290 300
KTSQLGDSPF YPGKTTYGGA AAAVRQNKVR STPYQAPVRR QMKAKQLNAQ
310 320 330 340 350
SYGVTSSTAR RILQSLEKMS SPLADAKRIP SAVSSPLNSP LDRSGIDSTV
360 370 380 390 400
FQAKKEKVDS QYPPVQRLMT PKPVSIATNR TVYFKPSLTP SGDLRKTNQR
410 420 430 440 450
IDKKNSTVDE KNISRQNREQ ESGFSYPNFS IPAANGLSSG VGGGGGKMRR
460 470 480 490 500
ERTTHFVASK PSEEEEVEVP LLPQISLPIS SSSLPTFNFS SPAISAASSS
510 520 530 540 550
SVSPSQPLSN KVQMTSLGST GNPVFTFSSP IVKSTQADVL PPASIGFTFS
560 570 580 590 600
VPLAKTELSG PNSSSETVLS SSVTAQDNTV VNSSSSKKRS APCEDPFTPA
610 620 630 640 650
KILREGSVLD ILKTPGFMSP KVDSPALQPT TTSSIVYTRP AISTFSSSGV
660 670 680 690 700
EFGESLKAGS SWQCDTCLLQ NKVTDNKCIA CQAAKLPLKE TAKQTGIGTP
710 720 730 740 750
SKSDKPASTS GTGFGDKFKP AIGTWDCDTC LVQNKPEAVK CVACETPKPG
760 770 780 790 800
TGVKRALPLT VASESPVTAS SSTTVTTGTL GFGDKFKRPV GSWECPVCCV
810 820 830 840 850
SNKAEDSRCV SCTSEKPGLV SASSSNSVPV SLPSGGCLGL DKFKKPEGSW
860 870 880 890 900
DCEVCLVQNK ADSTKCIACE SAKPGTKSEF KGFGTSSSLN PAPSAFKFGI
910 920 930 940 950
PSSSSGLSQT FTSTGNFKFG DQGGFKLGTS SDSGSTNTMN TNFKFPKPTG
960 970 980 990 1000
DFKFGVLPDS KPEEIKNDSK NDNFQFGPSS GLSNPASSAP FQFGVSTLGQ
1010 1020 1030 1040 1050
QEKKEELPQS SSAGFSFGAG VANPSSAAID TTVTSENKSG FNFGTIDTKS
1060 1070 1080 1090 1100
VSVTPFTYKT TEAKKEDASA TKGGFTFGKV DSAALSSPSM FVLGRTEEKQ
1110 1120 1130 1140 1150
QEPVTSTSLV FGKKADNEEP KCQPVFSFGN SEQTKDESSS KPTFSFSVAK
1160 1170 1180 1190 1200
PSVKESDQLA KATFAFGNQT NTTTDQGAAK PAFSFLNSSS SSSSTPATSS
1210 1220 1230 1240 1250
SASIFGSSTS SSSPPVAAFV FGQASNPVSS SAFGNSAESS TSQPLLFPQD
1260 1270 1280 1290 1300
GKPATTSSTA SAAPPFVFGT GASSNSTVSS GFTFGATTTS SSSGSFFVFG
1310 1320 1330 1340 1350
TGHSAPSASP AFGANQTPTF GQSQGASQPN PPSFGSISSS TALFSAGSQP
1360 1370 1380 1390 1400
VPPPTFGTVS SSSQPPVFGQ QPSQSAFGSG TANASSVFQF GSSTTNFNFT
1410 1420 1430 1440 1450
NNNPSGVFTF GASPSTPAAA AQPSGSGGFS FSQSPASFTV GSNGKNMFSS
1460
SGTSVSGRKI KTAVRRKK
Length:1,468
Mass (Da):152,824
Last modified:October 1, 1996 - v1
Checksum:iC3DFD9697C556A7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06821 mRNA. No translation available.
PIRiA44345.
UniGeneiRn.1347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06821 mRNA. No translation available.
PIRiA44345.
UniGeneiRn.1347.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K0CNMR-A703-755[»]
3CH5X-ray2.10B703-754[»]
3GJ3X-ray1.79B723-750[»]
3GJ4X-ray2.15B/D790-817[»]
3GJ5X-ray1.79B/D848-876[»]
3GJ6X-ray2.70B658-686[»]
3GJ7X-ray1.93B/D658-750[»]
3GJ8X-ray1.82B/D790-876[»]
ProteinModelPortaliP49791.
SMRiP49791.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46027N.
IntActiP49791. 1 interactor.
STRINGi10116.ENSRNOP00000001979.

PTM databases

iPTMnetiP49791.
PhosphoSitePlusiP49791.

Proteomic databases

PaxDbiP49791.
PRIDEiP49791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi3216. Nup153.

Phylogenomic databases

eggNOGiKOG4719. Eukaryota.
ENOG41107SV. LUCA.
HOGENOMiHOG000088610.
HOVERGENiHBG052679.
InParanoidiP49791.
PhylomeDBiP49791.

Miscellaneous databases

EvolutionaryTraceiP49791.
PROiP49791.

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_RAT
AccessioniPrimary (citable) accession number: P49791
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.