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P49790

- NU153_HUMAN

UniProt

P49790 - NU153_HUMAN

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Protein

Nuclear pore complex protein Nup153

Gene

NUP153

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi664 – 6641Zinc 1By similarity
Metal bindingi667 – 6671Zinc 1By similarity
Metal bindingi678 – 6781Zinc 1By similarity
Metal bindingi681 – 6811Zinc 1By similarity
Metal bindingi728 – 7281Zinc 2
Metal bindingi731 – 7311Zinc 2
Metal bindingi742 – 7421Zinc 2
Metal bindingi745 – 7451Zinc 2
Metal bindingi799 – 7991Zinc 3By similarity
Metal bindingi802 – 8021Zinc 3By similarity
Metal bindingi813 – 8131Zinc 3By similarity
Metal bindingi816 – 8161Zinc 3By similarity
Metal bindingi857 – 8571Zinc 4By similarity
Metal bindingi860 – 8601Zinc 4By similarity
Metal bindingi871 – 8711Zinc 4By similarity
Metal bindingi874 – 8741Zinc 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri657 – 68731RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri722 – 75130RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri793 – 82230RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri851 – 88030RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. nucleocytoplasmic transporter activity Source: UniProtKB
  4. protein anchor Source: UniProtKB
  5. structural constituent of nuclear pore Source: UniProtKB
  6. transporter activity Source: ProtInc
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. glucose transport Source: Reactome
  4. hexose transport Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear envelope disassembly Source: Reactome
  7. mRNA transport Source: UniProtKB-KW
  8. negative regulation of RNA export from nucleus Source: UniProtKB
  9. nuclear pore complex assembly Source: UniProtKB
  10. protein transport Source: UniProtKB-KW
  11. regulation of glucose transport Source: Reactome
  12. small molecule metabolic process Source: Reactome
  13. transmembrane transport Source: Reactome
  14. viral entry into host cell Source: UniProtKB-KW
  15. viral penetration into host nucleus Source: UniProtKB-KW
  16. viral process Source: Reactome
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

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
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.
SignaLinkiP49790.

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
ProteomesiUP000005640: 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

  1. cytoplasm Source: HPA
  2. nuclear inclusion body Source: UniProtKB
  3. nuclear membrane Source: UniProtKB
  4. nuclear periphery Source: UniProtKB
  5. nuclear pore Source: UniProtKB
  6. nuclear pore nuclear basket Source: UniProtKB
  7. nucleolus Source: HPA
  8. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 14751474Nuclear pore complex protein Nup153PRO_0000204842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei192 – 1921Phosphoserine2 Publications
Modified residuei209 – 2091Phosphoserine5 Publications
Modified residuei240 – 2401Phosphoserine2 Publications
Modified residuei257 – 2571Phosphoserine2 Publications
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei334 – 3341Phosphoserine2 Publications
Modified residuei338 – 3381Phosphoserine6 Publications
Modified residuei343 – 3431Phosphoserine1 Publication
Modified residuei369 – 3691Phosphothreonine1 Publication
Modified residuei384 – 3841N6-acetyllysine1 Publication
Modified residuei500 – 5001Phosphoserine1 Publication
Modified residuei516 – 5161Phosphoserine1 Publication
Modified residuei522 – 5221Phosphoserine2 Publications
Modified residuei529 – 5291Phosphoserine1 Publication
Glycosylationi534 – 5341O-linked (GlcNAc)1 Publication
Glycosylationi544 – 5441O-linked (GlcNAc)1 Publication
Modified residuei588 – 5881Phosphothreonine1 Publication
Modified residuei614 – 6141Phosphoserine2 Publications
Modified residuei619 – 6191Phosphoserine2 Publications
Modified residuei633 – 6331Phosphoserine2 Publications
Modified residuei687 – 6871Phosphoserine2 Publications
Modified residuei718 – 7181N6-acetyllysine1 Publication
Glycosylationi908 – 9081O-linked (GlcNAc)1 Publication
Glycosylationi909 – 9091O-linked (GlcNAc)1 Publication
Modified residuei954 – 9541N6-acetyllysine1 Publication
Glycosylationi1113 – 11131O-linked (GlcNAc)1 Publication
Glycosylationi1156 – 11561O-linked (GlcNAc)1 Publication
Modified residuei1457 – 14571Phosphoserine1 Publication
Modified residuei1463 – 14631Phosphoserine3 Publications

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.9 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP49790.
PaxDbiP49790.
PRIDEiP49790.

PTM databases

PhosphoSiteiP49790.

Miscellaneous databases

PMAP-CutDBP49790.

Expressioni

Gene expression databases

BgeeiP49790.
CleanExiHS_NUP153.
ExpressionAtlasiP49790. baseline and differential.
GenevestigatoriP49790.

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 C11orf73/Hikeshi, SENP2 and XPO5.By similarity8 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115297. 52 interactions.
DIPiDIP-38185N.
IntActiP49790. 22 interactions.
MINTiMINT-121422.
STRINGi9606.ENSP00000262077.

Structurei

Secondary structure

1
1475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi723 – 7275Combined sources
Beta strandi729 – 7313Combined sources
Beta strandi743 – 7453Combined sources
Helixi755 – 7573Combined sources
Beta strandi794 – 7963Combined sources
Beta strandi800 – 8023Combined sources
Beta strandi814 – 8163Combined sources
Beta strandi858 – 8603Combined sources
Beta strandi872 – 8743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBQNMR-A722-761[»]
2EBRNMR-A851-890[»]
2EBVNMR-A773-822[»]
2GQENMR-A722-750[»]
ProteinModelPortaliP49790.
SMRiP49790. Positions 661-686, 722-761, 777-822, 855-890.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49790.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 1411Gly-richAdd
BLAST
Compositional biasi443 – 4475Poly-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 fingeri722 – 75130RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri793 – 82230RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri851 – 88030RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00700000104544.
HOGENOMiHOG000088610.
HOVERGENiHBG052679.
InParanoidiP49790.
KOiK14296.
OrthoDBiEOG73JKTK.
PhylomeDBiP49790.
TreeFamiTF323517.

Family and domain databases

InterProiIPR013913. Nucleoporin_Nup153.
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]
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. Align

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 BAE06106.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111E → G in BAG58514. (PubMed:14702039)Curated
Sequence conflicti454 – 4552TR → HA in CAA80982. (PubMed:8110839)Curated
Sequence conflicti813 – 8131C → S in BAG58514. (PubMed:14702039)Curated
Sequence conflicti836 – 8361S → C in BAG58514. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901D → N.1 Publication
Corresponds to variant rs16879902 [ dbSNP | Ensembl ].
VAR_046554
Natural varianti248 – 2481I → V.
Corresponds to variant rs2228375 [ dbSNP | Ensembl ].
VAR_046555
Natural varianti381 – 3811V → F.1 Publication
Corresponds to variant rs17857419 [ dbSNP | Ensembl ].
VAR_070841
Natural varianti402 – 4021N → K.
Corresponds to variant rs6906499 [ dbSNP | Ensembl ].
VAR_046556
Natural varianti821 – 8211P → L.
Corresponds to variant rs6905654 [ dbSNP | Ensembl ].
VAR_046557
Natural varianti827 – 8271A → T.1 Publication
Corresponds to variant rs2274136 [ dbSNP | Ensembl ].
VAR_046558
Natural varianti1388 – 13881T → A.
Corresponds to variant rs45475293 [ dbSNP | Ensembl ].
VAR_046559

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei465 – 4651E → ERQGLTVLPKLISSSCAQAI IPSWPLKVLRLQ in isoform 3. 1 PublicationVSP_055134
Alternative sequencei574 – 61542Missing in isoform 2. 1 PublicationVSP_054265Add
BLAST

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.2. human. [P49790-1]

Polymorphism databases

DMDMi206729891.

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 .
CCDSi CCDS4541.1. [P49790-1 ]
CCDS64359.1. [P49790-3 ]
CCDS75407.1. [P49790-2 ]
PIRi S42718.
RefSeqi NP_001265138.1. NM_001278209.1. [P49790-3 ]
NP_001265139.1. NM_001278210.1. [P49790-2 ]
NP_005115.2. NM_005124.3. [P49790-1 ]
UniGenei Hs.601591.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EBQ NMR - A 722-761 [» ]
2EBR NMR - A 851-890 [» ]
2EBV NMR - A 773-822 [» ]
2GQE NMR - A 722-750 [» ]
ProteinModelPortali P49790.
SMRi P49790. Positions 661-686, 722-761, 777-822, 855-890.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115297. 52 interactions.
DIPi DIP-38185N.
IntActi P49790. 22 interactions.
MINTi MINT-121422.
STRINGi 9606.ENSP00000262077.

PTM databases

PhosphoSitei P49790.

Polymorphism databases

DMDMi 206729891.

Proteomic databases

MaxQBi P49790.
PaxDbi P49790.
PRIDEi P49790.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262077 ; ENSP00000262077 ; ENSG00000124789 . [P49790-1 ]
ENST00000537253 ; ENSP00000444029 ; ENSG00000124789 . [P49790-3 ]
ENST00000613258 ; ENSP00000478627 ; ENSG00000124789 . [P49790-2 ]
GeneIDi 9972.
KEGGi hsa:9972.
UCSCi uc003ncd.2. human. [P49790-1 ]

Organism-specific databases

CTDi 9972.
GeneCardsi GC06M017615.
H-InvDB HIX0032892.
HIX0200901.
HGNCi HGNC:8062. NUP153.
HPAi HPA027896.
HPA027897.
HPA027898.
MIMi 603948. gene.
neXtProti NX_P49790.
PharmGKBi PA31848.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00700000104544.
HOGENOMi HOG000088610.
HOVERGENi HBG052679.
InParanoidi P49790.
KOi K14296.
OrthoDBi EOG73JKTK.
PhylomeDBi P49790.
TreeFami TF323517.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
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 P49790.

Miscellaneous databases

ChiTaRSi NUP153. human.
EvolutionaryTracei P49790.
GeneWikii NUP153.
GenomeRNAii 9972.
NextBioi 35472301.
PMAP-CutDB P49790.
PROi P49790.
SOURCEi Search...

Gene expression databases

Bgeei P49790.
CleanExi HS_NUP153.
ExpressionAtlasi P49790. baseline and differential.
Genevestigatori P49790.

Family and domain databases

InterProi IPR013913. Nucleoporin_Nup153.
IPR018892. Retro-transposon_transp_CS.
IPR001876. Znf_RanBP2.
[Graphical view ]
Pfami PF08604. Nup153. 1 hit.
PF10599. Nup_retrotrp_bd. 1 hit.
PF00641. zf-RanBP. 4 hits.
[Graphical view ]
SMARTi SM00547. ZnF_RBZ. 4 hits.
[Graphical view ]
PROSITEi PS01358. ZF_RANBP2_1. 4 hits.
PS50199. ZF_RANBP2_2. 4 hits.
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Publicationsi

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  1. "Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153."
    McMorrow I., Bastos R., Horton H., Burke B.
    Biochim. Biophys. Acta 1217:219-223(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT THR-827.
    Tissue: Hippocampus.
  3. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
    Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Myeloma.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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] (ISOFORM 1), VARIANTS ASN-90 AND PHE-381.
    Tissue: Testis.
  6. Bienvenut W.V., Dozynkiewicz M., Norman J.C.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 251-263; 295-309; 367-379; 706-718 AND 1046-1056, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "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.
  8. "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.
  9. "Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
    Hase M.E., Cordes V.C.
    Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANCHORING TPR, INTERACTION WITH TPR.
  10. "Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
    Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
    Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND THR-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-209; SER-338 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-240; SER-257; SER-330; SER-334; SER-338; SER-343; THR-369; SER-522; SER-529; SER-614; SER-619; SER-1457 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1."
    Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.
    J. Virol. 83:6522-6533(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV INTEGRASE.
  18. "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-334; SER-338; SER-516; SER-522 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-718 AND LYS-954, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
    Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
    EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  21. "Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis."
    Nakano H., Funasaka T., Hashizume C., Wong R.W.
    J. Biol. Chem. 285:10841-10849(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TPR.
  22. "Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket."
    Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J., Stoeber M., Pante N., Kann M.
    PLoS Pathog. 6:E1000741-E1000741(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
  23. "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis."
    Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.
    Sci. Signal. 3:RA2-RA2(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-534; SER-544; SER-908; SER-909; SER-1113 AND THR-1156.
  24. "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-192; SER-209; SER-240; SER-338; SER-500; SER-614; SER-619; SER-633; SER-687 AND SER-1463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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-192; SER-209 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage."
    Kose S., Furuta M., Imamoto N.
    Cell 149:578-589(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C11ORF73.
  28. "Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA."
    Rajanala K., Nandicoori V.K.
    PLoS ONE 7:E29921-E29921(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RNA EXPORT, INTERACTION WITH MAPK1, SUBCELLULAR LOCATION.
  29. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Solution structure of the second and third ZF-RANBP domains from human nuclear pore complex protein NUP153."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 722-822.
  31. "Solution structure of the second ZF-ranbp domain from human nuclear pore complex protein nup153."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 722-761.

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 26, 2014
This is version 140 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

External Data

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