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Protein

Nuclear pore complex protein Nup205

Gene

NUP205

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

Functioni

Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC.1 Publication

GO - Molecular functioni

  • structural constituent of nuclear pore Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000155561-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.

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 Nup205
Alternative name(s):
205 kDa nucleoporin
Nucleoporin Nup205
Gene namesi
Name:NUP205
Synonyms:C7orf14, KIAA0225
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:18658. NUP205.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • membrane Source: UniProtKB
  • nuclear envelope Source: Reactome
  • nuclear membrane Source: UniProtKB
  • nuclear periphery Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nuclear pore inner ring Source: GO_Central
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nephrotic syndrome 13 (NPHS13)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.
See also OMIM:616893
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0764711995F → S in NPHS13; abrogates interaction with NUP93. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi23165.
MIMi616893. phenotype.
OpenTargetsiENSG00000155561.
PharmGKBiPA38624.

Polymorphism and mutation databases

BioMutaiNUP205.
DMDMi296439283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002048592 – 2012Nuclear pore complex protein Nup205Add BLAST2011

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei3PhosphothreonineCombined sources1
Modified residuei575PhosphoserineCombined sources1
Modified residuei1165PhosphoserineCombined sources1
Modified residuei1167PhosphoserineCombined sources1
Modified residuei1939PhosphoserineCombined sources1
Modified residuei1942PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92621.
MaxQBiQ92621.
PaxDbiQ92621.
PeptideAtlasiQ92621.
PRIDEiQ92621.

PTM databases

iPTMnetiQ92621.
PhosphoSitePlusiQ92621.
SwissPalmiQ92621.

Expressioni

Gene expression databases

BgeeiENSG00000155561.
CleanExiHS_NUP205.
ExpressionAtlasiQ92621. baseline and differential.
GenevisibleiQ92621. HS.

Organism-specific databases

HPAiHPA024574.

Interactioni

Subunit structurei

Part of the nuclear pore complex (NPC). Forms a complex with NUP53, NUP93, NUP155 and lamin B. Does not interact with TPR.3 Publications

Protein-protein interaction databases

BioGridi116777. 62 interactors.
DIPiDIP-44021N.
IntActiQ92621. 38 interactors.
MINTiMINT-2813123.
STRINGi9606.ENSP00000285968.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IJNelectron microscopy21.40D/J/P/V1-2012[»]
5IJOelectron microscopy21.40D/P1-2012[»]
ProteinModelPortaliQ92621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG1835. Eukaryota.
ENOG410XSBR. LUCA.
GeneTreeiENSGT00390000004003.
HOGENOMiHOG000044863.
HOVERGENiHBG052682.
InParanoidiQ92621.
KOiK14310.
OMAiIHLDFYL.
OrthoDBiEOG091G02G9.
PhylomeDBiQ92621.
TreeFamiTF313397.

Family and domain databases

InterProiIPR021827. Nup186/Nup192/Nup205.
[Graphical view]
PfamiPF11894. Nup192. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPLAVNSA ASLWGPYKDI WHKVGNALWR RQPEAVHLLD KILKKHKPDF
60 70 80 90 100
ISLFKNPPKN VQQHEKVQKA STEGVAIQGQ QGTRLLPEQL IKEAFILSDL
110 120 130 140 150
FDIGELAAVE LLLAGEHQQP HFPGLTRGLV AVLLYWDGKR CIANSLKALI
160 170 180 190 200
QSRRGKTWTL ELSPELASMT TRFTDELMEQ GLTYKVLTLV SQIDVNNEFE
210 220 230 240 250
KLQRERGLGS EKHRKEVSDL IKECRQSLAE SLFAWACQSP LGKEDTLLLI
260 270 280 290 300
GHLERVTVEA NGSLDAVNLA LLMALLYCFD ISFIEQSTEE RDDMIHQLPL
310 320 330 340 350
LTEKQYIATI HSRLQDSQLW KLPGLQATVR LAWALALRGI SQLPDVTALA
360 370 380 390 400
EFTEADEAMA ELAIADNVFL FLMESVVVSE YFYQEEFYIR RVHNLITDFL
410 420 430 440 450
ALMPMKVKQL RNRADEDARM IHMSMQMGNE PPISLRRDLE HLMLLIGELY
460 470 480 490 500
KKNPFHLELA LEYWCPTEPL QTPTIMGSYL GVAHQRPPQR QVVLSKFVRQ
510 520 530 540 550
MGDLLPPTIY IPYLKMLQGL ANGPQCAHYC FSLLKVNGSS HVENIQGAGG
560 570 580 590 600
SPVSWEHFFH SLMLYHEHLR KDLPSADSVQ YRHLPSRGIT QKEQDGLIAF
610 620 630 640 650
LQLTSTIITW SENARLALCE HPQWTPVVVI LGLLQCSIPP VLKAELLKTL
660 670 680 690 700
AAFGKSPEIA ASLWQSLEYT QILQTVRIPS QRQAIGIEVE LNEIESRCEE
710 720 730 740 750
YPLTRAFCQL ISTLVESSFP SNLGAGLRPP GFDPYLQFLR DSVFLRFRTR
760 770 780 790 800
AYRRAAEKWE VAEVVLEVFY KLLRDYEPQL EDFVDQFVEL QGEEIIAYKP
810 820 830 840 850
PGFSLMYHLL NESPMLELAL SLLEEGVKQL DTYAPFPGKK HLEKAVQHCL
860 870 880 890 900
ALLNLTLQKE NLFMDLLRES QLALIVCPLE QLLQGINPRT KKADNVVNIA
910 920 930 940 950
RYLYHGNTNP ELAFESAKIL CCISCNSNIQ IKLVGDFTHD QSISQKLMAG
960 970 980 990 1000
FVECLDCEDA EEFVRLEEGS ELEKKLVAIR HETRIHILNL LITSLECNPP
1010 1020 1030 1040 1050
NLALYLLGFE LKKPVSTTNL QDPGVLGCPR TCLHAILNIL EKGTEGRTGP
1060 1070 1080 1090 1100
VAVRESPQLA ELCYQVIYQL CACSDTSGPT MRYLRTSQDF LFSQLQYLPF
1110 1120 1130 1140 1150
SNKEYEISML NQMSWLMKTA SIELRVTSLN RQRSHTQRLL HLLLDDMPVK
1160 1170 1180 1190 1200
PYSDGEGGIE DENRSVSGFL HFDTATKVRR KILNILDSID FSQEIPEPLQ
1210 1220 1230 1240 1250
LDFFDRAQIE QVIANCEHKN LRGQTVCNVK LLHRVLVAEV NALQGMAAIG
1260 1270 1280 1290 1300
QRPLLMEEIS TVLQYVVGRN KLLQCLHAKR HALESWRQLV EIILTACPQD
1310 1320 1330 1340 1350
LIQAEDRQLI IRDILQDVHD KILDDEAAQE LMPVVAGAVF TLTAHLSQAV
1360 1370 1380 1390 1400
LTEQKETSVL GPAEAHYAFM LDSCFTSPPP EENPLVGFAS IGDSSLYIIL
1410 1420 1430 1440 1450
KKLLDFILKT GGGFQRVRTH LYGSLLYYLQ IAQRPDEPDT LEAAKKTMWE
1460 1470 1480 1490 1500
RLTAPEDVFS KLQRENIAII ESYGAALMEV VCRDACDGHE IGRMLALALL
1510 1520 1530 1540 1550
DRIVSVDKQQ QWLLYLSNSG YLKVLVDSLV EDDRTLQSLL TPQPPLLKAL
1560 1570 1580 1590 1600
YTYESKMAFL TRVAKIQQGA LELLRSGVIV RLAQCQVYDM RPETDPQSMF
1610 1620 1630 1640 1650
GMRDPPMFIP TPVDRYRQIL LPALQLCQVI LTSSMAQHLQ AAGQVLQFLI
1660 1670 1680 1690 1700
SHSDTIQAIL RCQDVSAGSL QELALLTGII SKAALPGILS ELDVDVNEGS
1710 1720 1730 1740 1750
LMELQGHIGR FQRQCLGLLS RFGGSDRLRQ FKFQDDNVEG DKVSKKDEIE
1760 1770 1780 1790 1800
LAMQQICANV MEYCQSLMLQ SSPTFQHAVC LFTPSLSETV NRDGPRQDTQ
1810 1820 1830 1840 1850
APVVPYWRLP GLGIIIYLLK QSANDFFSYY DSHRQSVSKL QNVEQLPPDE
1860 1870 1880 1890 1900
IKELCQSVMP AGVDKISTAQ KYVLARRRLV KVINNRAKLL SLCSFIIETC
1910 1920 1930 1940 1950
LFILWRHLEY YLLHCMPTDS QDSLFASRTL FKSRRLQDSF ASETNLDFRS
1960 1970 1980 1990 2000
GLAIVSQHDL DQLQADAINA FGESLQKKLL DIEGLYSKVR SRYSFIQALV
2010
RRIRGLLRIS RN
Length:2,012
Mass (Da):227,922
Last modified:May 18, 2010 - v3
Checksum:iF3B268881000FBAA
GO

Sequence cautioni

The sequence BAA13214 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05056733P → S.Corresponds to variant rs7797639dbSNPEnsembl.1
Natural variantiVAR_0505681356E → Q.3 PublicationsCorresponds to variant rs7810767dbSNPEnsembl.1
Natural variantiVAR_0764711995F → S in NPHS13; abrogates interaction with NUP93. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86978 mRNA. Translation: BAA13214.1. Different initiation.
AC093107 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83855.1.
BC044255 mRNA. Translation: AAH44255.1.
BC136624 mRNA. Translation: AAI36625.1.
BC146784 mRNA. Translation: AAI46785.1.
CCDSiCCDS34759.1.
RefSeqiNP_001316363.1. NM_001329434.1.
NP_055950.1. NM_015135.2.
UniGeneiHs.743250.

Genome annotation databases

EnsembliENST00000285968; ENSP00000285968; ENSG00000155561.
GeneIDi23165.
KEGGihsa:23165.
UCSCiuc003vsw.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86978 mRNA. Translation: BAA13214.1. Different initiation.
AC093107 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83855.1.
BC044255 mRNA. Translation: AAH44255.1.
BC136624 mRNA. Translation: AAI36625.1.
BC146784 mRNA. Translation: AAI46785.1.
CCDSiCCDS34759.1.
RefSeqiNP_001316363.1. NM_001329434.1.
NP_055950.1. NM_015135.2.
UniGeneiHs.743250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IJNelectron microscopy21.40D/J/P/V1-2012[»]
5IJOelectron microscopy21.40D/P1-2012[»]
ProteinModelPortaliQ92621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116777. 62 interactors.
DIPiDIP-44021N.
IntActiQ92621. 38 interactors.
MINTiMINT-2813123.
STRINGi9606.ENSP00000285968.

Protein family/group databases

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

PTM databases

iPTMnetiQ92621.
PhosphoSitePlusiQ92621.
SwissPalmiQ92621.

Polymorphism and mutation databases

BioMutaiNUP205.
DMDMi296439283.

Proteomic databases

EPDiQ92621.
MaxQBiQ92621.
PaxDbiQ92621.
PeptideAtlasiQ92621.
PRIDEiQ92621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285968; ENSP00000285968; ENSG00000155561.
GeneIDi23165.
KEGGihsa:23165.
UCSCiuc003vsw.4. human.

Organism-specific databases

CTDi23165.
DisGeNETi23165.
GeneCardsiNUP205.
HGNCiHGNC:18658. NUP205.
HPAiHPA024574.
MIMi614352. gene.
616893. phenotype.
neXtProtiNX_Q92621.
OpenTargetsiENSG00000155561.
PharmGKBiPA38624.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1835. Eukaryota.
ENOG410XSBR. LUCA.
GeneTreeiENSGT00390000004003.
HOGENOMiHOG000044863.
HOVERGENiHBG052682.
InParanoidiQ92621.
KOiK14310.
OMAiIHLDFYL.
OrthoDBiEOG091G02G9.
PhylomeDBiQ92621.
TreeFamiTF313397.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000155561-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.

Miscellaneous databases

ChiTaRSiNUP205. human.
GeneWikiiNUP205.
GenomeRNAii23165.
PROiQ92621.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000155561.
CleanExiHS_NUP205.
ExpressionAtlasiQ92621. baseline and differential.
GenevisibleiQ92621. HS.

Family and domain databases

InterProiIPR021827. Nup186/Nup192/Nup205.
[Graphical view]
PfamiPF11894. Nup192. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNU205_HUMAN
AccessioniPrimary (citable) accession number: Q92621
Secondary accession number(s): A6H8X3, Q86YC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 138 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: 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.