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Protein

Nuclear pore complex protein Nup160

Gene

NUP160

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

Functioni

Involved in poly(A)+ RNA transport.1 Publication

GO - Molecular functioni

  • nucleocytoplasmic transporter activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000030066-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-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
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-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.

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 Nup160
Alternative name(s):
160 kDa nucleoporin
Nucleoporin Nup160
Gene namesi
Name:NUP160
Synonyms:KIAA0197, NUP120
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:18017. NUP160.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nuclear envelope Source: Reactome
  • nuclear pore Source: UniProtKB
  • nuclear pore outer ring Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000030066.
PharmGKBiPA31850.

Polymorphism and mutation databases

BioMutaiNUP160.
DMDMi238054372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002048511 – 1436Nuclear pore complex protein Nup160Add BLAST1436

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44PhosphoserineCombined sources1
Modified residuei490PhosphoserineCombined sources1
Modified residuei949PhosphoserineCombined sources1
Modified residuei1157PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ12769.
MaxQBiQ12769.
PaxDbiQ12769.
PeptideAtlasiQ12769.
PRIDEiQ12769.

PTM databases

iPTMnetiQ12769.
PhosphoSitePlusiQ12769.

Expressioni

Gene expression databases

BgeeiENSG00000030066.
CleanExiHS_NUP160.
ExpressionAtlasiQ12769. baseline and differential.
GenevisibleiQ12769. HS.

Organism-specific databases

HPAiCAB019394.

Interactioni

Subunit structurei

Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESRRGP625083EBI-295715,EBI-2834260

Protein-protein interaction databases

BioGridi116879. 59 interactors.
DIPiDIP-31262N.
IntActiQ12769. 26 interactors.
MINTiMINT-4301556.
STRINGi9606.ENSP00000367721.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A9Qelectron microscopy23.001/J/S/a1-1436[»]
ProteinModelPortaliQ12769.
SMRiQ12769.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG4521. Eukaryota.
ENOG410YYM5. LUCA.
GeneTreeiENSGT00390000000972.
HOVERGENiHBG052681.
InParanoidiQ12769.
KOiK14303.
OMAiGFYYMES.
OrthoDBiEOG091G02JO.
PhylomeDBiQ12769.
TreeFamiTF353082.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q12769-1) [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
MLHLSAAPPA PPPEVTATAR PCLCSVGRRG DGGKMAAAGA LERSFVELSG
60 70 80 90 100
AERERPRHFR EFTVCSIGTA NAVAGAVKYS ESAGGFYYVE SGKLFSVTRN
110 120 130 140 150
RFIHWKTSGD TLELMEESLD INLLNNAIRL KFQNCSVLPG GVYVSETQNR
160 170 180 190 200
VIILMLTNQT VHRLLLPHPS RMYRSELVVD SQMQSIFTDI GKVDFTDPCN
210 220 230 240 250
YQLIPAVPGI SPNSTASTAW LSSDGEALFA LPCASGGIFV LKLPPYDIPG
260 270 280 290 300
MVSVVELKQS SVMQRLLTGW MPTAIRGDQS PSDRPLSLAV HCVEHDAFIF
310 320 330 340 350
ALCQDHKLRM WSYKEQMCLM VADMLEYVPV KKDLRLTAGT GHKLRLAYSP
360 370 380 390 400
TMGLYLGIYM HAPKRGQFCI FQLVSTESNR YSLDHISSLF TSQETLIDFA
410 420 430 440 450
LTSTDIWALW HDAENQTVVK YINFEHNVAG QWNPVFMQPL PEEEIVIRDD
460 470 480 490 500
QDPREMYLQS LFTPGQFTNE ALCKALQIFC RGTERNLDLS WSELKKEVTL
510 520 530 540 550
AVENELQGSV TEYEFSQEEF RNLQQEFWCK FYACCLQYQE ALSHPLALHL
560 570 580 590 600
NPHTNMVCLL KKGYLSFLIP SSLVDHLYLL PYENLLTEDE TTISDDVDIA
610 620 630 640 650
RDVICLIKCL RLIEESVTVD MSVIMEMSCY NLQSPEKAAE QILEDMITID
660 670 680 690 700
VENVMEDICS KLQEIRNPIH AIGLLIREMD YETEVEMEKG FNPAQPLNIR
710 720 730 740 750
MNLTQLYGSN TAGYIVCRGV HKIASTRFLI CRDLLILQQL LMRLGDAVIW
760 770 780 790 800
GTGQLFQAQQ DLLHRTAPLL LSYYLIKWGS ECLATDVPLD TLESNLQHLS
810 820 830 840 850
VLELTDSGAL MANRFVSSPQ TIVELFFQEV ARKHIISHLF SQPKAPLSQT
860 870 880 890 900
GLNWPEMITA ITSYLLQLLW PSNPGCLFLE CLMGNCQYVQ LQDYIQLLHP
910 920 930 940 950
WCQVNVGSCR FMLGRCYLVT GEGQKALECF CQAASEVGKE EFLDRLIRSE
960 970 980 990 1000
DGEIVSTPRL QYYDKVLRLL DVIGLPELVI QLATSAITEA GDDWKSQATL
1010 1020 1030 1040 1050
RTCIFKHHLD LGHNSQAYEA LTQIPDSSRQ LDCLRQLVVV LCERSQLQDL
1060 1070 1080 1090 1100
VEFPYVNLHN EVVGIIESRA RAVDLMTHNY YELLYAFHIY RHNYRKAGTV
1110 1120 1130 1140 1150
MFEYGMRLGR EVRTLRGLEK QGNCYLAALN CLRLIRPEYA WIVQPVSGAV
1160 1170 1180 1190 1200
YDRPGASPKR NHDGECTAAP TNRQIEILEL EDLEKECSLA RIRLTLAQHD
1210 1220 1230 1240 1250
PSAVAVAGSS SAEEMVTLLV QAGLFDTAIS LCQTFKLPLT PVFEGLAFKC
1260 1270 1280 1290 1300
IKLQFGGEAA QAEAWAWLAA NQLSSVITTK ESSATDEAWR LLSTYLERYK
1310 1320 1330 1340 1350
VQNNLYHHCV INKLLSHGVP LPNWLINSYK KVDAAELLRL YLNYDLLEEA
1360 1370 1380 1390 1400
VDLVSEYVDA VLGKGHQYFG IEFPLSATAP MVWLPYSSID QLLQALGENS
1410 1420 1430
ANSHNIALSQ KILDKLEDYQ QKVDKATRDL LYRRTL
Length:1,436
Mass (Da):162,121
Last modified:May 26, 2009 - v3
Checksum:i274C063A3CE69F48
GO
Isoform 2 (identifier: Q12769-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     175-224: SELVVDSQMQ...TASTAWLSSD → SVSWLSAISF...QAYFDSYRLK
     225-1436: Missing.

Show »
Length:224
Mass (Da):24,898
Checksum:iC98755EBCB0E1BC7
GO
Isoform 3 (identifier: Q12769-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-250: Missing.
     367-367: Q → QRRGFAMLPGLKLLSSSSPPTSASQCAGITSVNHSTQPEFF
     694-695: AQ → GK
     696-1436: Missing.

Show »
Length:485
Mass (Da):55,554
Checksum:i4650AE42B030DFBC
GO

Sequence cautioni

The sequence AAH09822 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA12110 differs from that shown. Probable cloning artifact. Aberrant splice sites.Curated
The sequence BAB15406 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAG65161 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti152I → K in BAG65161 (PubMed:14702039).Curated1
Sequence conflicti991G → S in BAA12110 (PubMed:8724849).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05540940A → T.1 PublicationCorresponds to variant rs2305984dbSNPEnsembl.1
Natural variantiVAR_055410351T → A.1 PublicationCorresponds to variant rs3816605dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0373501 – 250Missing in isoform 3. 1 PublicationAdd BLAST250
Alternative sequenceiVSP_007093175 – 224SELVV…WLSSD → SVSWLSAISFISQITLGVTN VVLERCLLELKEIWILVIPH QAYFDSYRLK in isoform 2. 2 PublicationsAdd BLAST50
Alternative sequenceiVSP_007094225 – 1436Missing in isoform 2. 2 PublicationsAdd BLAST1212
Alternative sequenceiVSP_037351367Q → QRRGFAMLPGLKLLSSSSPP TSASQCAGITSVNHSTQPEF F in isoform 3. 1 Publication1
Alternative sequenceiVSP_037352694 – 695AQ → GK in isoform 3. 1 Publication2
Alternative sequenceiVSP_037353696 – 1436Missing in isoform 3. 1 PublicationAdd BLAST741

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026236 mRNA. Translation: BAB15406.1. Different initiation.
AK302396 mRNA. Translation: BAG63710.1.
AK304308 mRNA. Translation: BAG65161.1. Different initiation.
AC021443 Genomic DNA. No translation available.
AC023232 Genomic DNA. No translation available.
BC008700 mRNA. Translation: AAH08700.1.
BC009822 mRNA. Translation: AAH09822.1. Different initiation.
BC125227 mRNA. Translation: AAI25228.1.
BC125228 mRNA. Translation: AAI25229.1.
D83781 mRNA. Translation: BAA12110.1. Sequence problems.
CCDSiCCDS31484.1. [Q12769-1]
CCDS81567.1. [Q12769-2]
PIRiG02870.
RefSeqiNP_001305328.1. NM_001318399.1. [Q12769-2]
NP_056046.1. NM_015231.2. [Q12769-1]
UniGeneiHs.643526.
Hs.744107.

Genome annotation databases

EnsembliENST00000378460; ENSP00000367721; ENSG00000030066. [Q12769-1]
ENST00000526870; ENSP00000431495; ENSG00000030066. [Q12769-2]
GeneIDi23279.
KEGGihsa:23279.
UCSCiuc001ngm.4. human. [Q12769-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026236 mRNA. Translation: BAB15406.1. Different initiation.
AK302396 mRNA. Translation: BAG63710.1.
AK304308 mRNA. Translation: BAG65161.1. Different initiation.
AC021443 Genomic DNA. No translation available.
AC023232 Genomic DNA. No translation available.
BC008700 mRNA. Translation: AAH08700.1.
BC009822 mRNA. Translation: AAH09822.1. Different initiation.
BC125227 mRNA. Translation: AAI25228.1.
BC125228 mRNA. Translation: AAI25229.1.
D83781 mRNA. Translation: BAA12110.1. Sequence problems.
CCDSiCCDS31484.1. [Q12769-1]
CCDS81567.1. [Q12769-2]
PIRiG02870.
RefSeqiNP_001305328.1. NM_001318399.1. [Q12769-2]
NP_056046.1. NM_015231.2. [Q12769-1]
UniGeneiHs.643526.
Hs.744107.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A9Qelectron microscopy23.001/J/S/a1-1436[»]
ProteinModelPortaliQ12769.
SMRiQ12769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116879. 59 interactors.
DIPiDIP-31262N.
IntActiQ12769. 26 interactors.
MINTiMINT-4301556.
STRINGi9606.ENSP00000367721.

Protein family/group databases

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

PTM databases

iPTMnetiQ12769.
PhosphoSitePlusiQ12769.

Polymorphism and mutation databases

BioMutaiNUP160.
DMDMi238054372.

Proteomic databases

EPDiQ12769.
MaxQBiQ12769.
PaxDbiQ12769.
PeptideAtlasiQ12769.
PRIDEiQ12769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378460; ENSP00000367721; ENSG00000030066. [Q12769-1]
ENST00000526870; ENSP00000431495; ENSG00000030066. [Q12769-2]
GeneIDi23279.
KEGGihsa:23279.
UCSCiuc001ngm.4. human. [Q12769-1]

Organism-specific databases

CTDi23279.
GeneCardsiNUP160.
H-InvDBHIX0009624.
HGNCiHGNC:18017. NUP160.
HPAiCAB019394.
MIMi607614. gene.
neXtProtiNX_Q12769.
OpenTargetsiENSG00000030066.
PharmGKBiPA31850.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4521. Eukaryota.
ENOG410YYM5. LUCA.
GeneTreeiENSGT00390000000972.
HOVERGENiHBG052681.
InParanoidiQ12769.
KOiK14303.
OMAiGFYYMES.
OrthoDBiEOG091G02JO.
PhylomeDBiQ12769.
TreeFamiTF353082.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000030066-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-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
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-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiNUP160. human.
GeneWikiiNUP160.
GenomeRNAii23279.
PROiQ12769.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000030066.
CleanExiHS_NUP160.
ExpressionAtlasiQ12769. baseline and differential.
GenevisibleiQ12769. HS.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiNU160_HUMAN
AccessioniPrimary (citable) accession number: Q12769
Secondary accession number(s): B4DYE8
, B4E2J9, Q08AD3, Q7Z5X6, Q96GB3, Q9H660
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 26, 2009
Last modified: November 30, 2016
This is version 165 of the entry and version 3 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

Caution

It is uncertain whether Met-1 or Met-35 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

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