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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi664 – 6641Zinc 12 Publications
Metal bindingi667 – 6671Zinc 12 Publications
Metal bindingi678 – 6781Zinc 12 Publications
Metal bindingi681 – 6811Zinc 12 Publications
Metal bindingi727 – 7271Zinc 22 Publications
Metal bindingi730 – 7301Zinc 22 Publications
Metal bindingi741 – 7411Zinc 22 Publications
Metal bindingi744 – 7441Zinc 22 Publications
Metal bindingi795 – 7951Zinc 32 Publications
Metal bindingi798 – 7981Zinc 32 Publications
Metal bindingi809 – 8091Zinc 32 Publications
Metal bindingi812 – 8121Zinc 32 Publications
Metal bindingi852 – 8521Zinc 42 Publications
Metal bindingi855 – 8551Zinc 42 Publications
Metal bindingi866 – 8661Zinc 42 Publications
Metal bindingi869 – 8691Zinc 42 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri657 – 68731RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri721 – 75030RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri789 – 81830RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri846 – 87530RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST

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 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi714 – 7141F → A: Reduces affinity for RAN; when associated with A-718. 1 Publication
Mutagenesisi718 – 7181F → A: Reduces affinity for RAN; when associated with A-714. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 14681467Nuclear pore complex protein Nup153PRO_0000204843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei97 – 971PhosphothreonineCombined sources
Modified residuei103 – 1031PhosphothreonineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei210 – 2101PhosphoserineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei258 – 2581PhosphoserineBy similarity
Modified residuei321 – 3211PhosphoserineBy similarity
Modified residuei331 – 3311PhosphoserineCombined sources
Modified residuei334 – 3341PhosphoserineBy similarity
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineBy similarity
Cross-linki354 – 354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei370 – 3701PhosphothreonineBy similarity
Modified residuei385 – 3851N6-acetyllysineBy similarity
Modified residuei389 – 3891PhosphothreonineBy similarity
Modified residuei500 – 5001PhosphoserineBy similarity
Modified residuei516 – 5161PhosphoserineBy similarity
Modified residuei529 – 5291PhosphoserineBy similarity
Glycosylationi534 – 5341O-linked (GlcNAc)By similarity
Glycosylationi544 – 5441O-linked (GlcNAc)By similarity
Modified residuei607 – 6071PhosphoserineBy similarity
Modified residuei619 – 6191PhosphoserineBy similarity
Modified residuei633 – 6331PhosphoserineBy similarity
Modified residuei717 – 7171N6-acetyllysineBy similarity
Modified residuei886 – 8861PhosphoserineBy similarity
Glycosylationi902 – 9021O-linked (GlcNAc)By similarity
Modified residuei947 – 9471N6-acetyllysineBy similarity
Glycosylationi1106 – 11061O-linked (GlcNAc)By similarity
Modified residuei1450 – 14501PhosphoserineBy similarity
Modified residuei1454 – 14541PhosphoserineBy similarity
Modified residuei1456 – 14561PhosphoserineBy similarity

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.
PhosphoSiteiP49791.

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 C11orf73/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 interaction.
STRINGi10116.ENSRNOP00000001979.

Structurei

Secondary structure

1
1468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni665 – 6673Combined sources
Turni679 – 6813Combined sources
Beta strandi725 – 7273Combined sources
Turni728 – 7303Combined sources
Beta strandi732 – 7343Combined sources
Turni742 – 7443Combined sources
Turni796 – 7983Combined sources
Turni810 – 8123Combined sources
Turni853 – 8553Combined sources
Turni867 – 8693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 713-749, 774-818, 850-885.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49791.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 1512Gly-richAdd
BLAST
Compositional biasi442 – 4465Poly-Gly

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri657 – 68731RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri721 – 75030RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri789 – 81830RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri846 – 87530RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST

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
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. Positions 713-749, 774-818, 850-885.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP49791.
PhosphoSiteiP49791.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm."
    Sukegawa J., Blobel G.
    Cell 72:29-38(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 602-613; 622-645 AND 971-993.
    Strain: Buffalo.
    Tissue: Liver.
  2. "Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
    Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
    J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex."
    Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.
    Mol. Biol. Cell 16:2382-2394(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-97; SER-331 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex."
    Schrader N., Koerner C., Koessmeier K., Bangert J.A., Wittinghofer A., Stoll R., Vetter I.R.
    Structure 16:1116-1125(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 703-755 IN COMPLEX WITH RAN AND ZINC, INTERACTION WITH RAN, MUTAGENESIS OF PHE-714 AND PHE-718.
  6. "Crystallographic and biochemical analysis of the Ran-binding zinc finger domain."
    Partridge J.R., Schwartz T.U.
    J. Mol. Biol. 391:375-389(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 658-817 IN COMPLEX WITH RAN AND ZINC.

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: July 6, 2016
This is version 115 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.