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Conserved domains on  [gi|971825769|ref|NP_001305328|]
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nuclear pore complex protein Nup160 isoform 2 [Homo sapiens]

Protein Classification

nucleoporin Nup120/160( domain architecture ID 707697)

nucleoporin Nup120/Nup160 family protein is a component of the nuclear pore complex (NPC) that plays a role in assembly and/or maintenance, and is required for the assembly of peripheral proteins into the NPC

Gene Ontology:  GO:0005643|GO:0017056|GO:0006913
PubMed:  11684705|8557736

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nup160 super family cl26448
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
62-175 1.30e-19

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


The actual alignment was detected with superfamily member pfam11715:

Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 86.75  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825769   62 FTVCSIGTANAVAGAVKY-------SESAGGFYYVESGKLFSV----TRNRFIHWK--TSGDTLELMEESLDINLLNNAI 128
Cdd:pfam11715   1 ITVPSPGVSTSSDDTKASrtfesedDEEAFGRRYVATGGSVYFrksnKYPRFFLWRvlTDGRVLELVDLSLKSSLANLTL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 971825769  129 RLKFQNcSVLPGGVYVSETQNR-VIILMLTNQTVHRLLLPHPSRMYRS 175
Cdd:pfam11715  81 RLDFPS-PILPSCVCFTDSEDGdVLIVIVTTASVHLYSLRLRPDFFRL 127
 
Name Accession Description Interval E-value
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
62-175 1.30e-19

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 86.75  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825769   62 FTVCSIGTANAVAGAVKY-------SESAGGFYYVESGKLFSV----TRNRFIHWK--TSGDTLELMEESLDINLLNNAI 128
Cdd:pfam11715   1 ITVPSPGVSTSSDDTKASrtfesedDEEAFGRRYVATGGSVYFrksnKYPRFFLWRvlTDGRVLELVDLSLKSSLANLTL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 971825769  129 RLKFQNcSVLPGGVYVSETQNR-VIILMLTNQTVHRLLLPHPSRMYRS 175
Cdd:pfam11715  81 RLDFPS-PILPSCVCFTDSEDGdVLIVIVTTASVHLYSLRLRPDFFRL 127
 
Name Accession Description Interval E-value
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
62-175 1.30e-19

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 86.75  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825769   62 FTVCSIGTANAVAGAVKY-------SESAGGFYYVESGKLFSV----TRNRFIHWK--TSGDTLELMEESLDINLLNNAI 128
Cdd:pfam11715   1 ITVPSPGVSTSSDDTKASrtfesedDEEAFGRRYVATGGSVYFrksnKYPRFFLWRvlTDGRVLELVDLSLKSSLANLTL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 971825769  129 RLKFQNcSVLPGGVYVSETQNR-VIILMLTNQTVHRLLLPHPSRMYRS 175
Cdd:pfam11715  81 RLDFPS-PILPSCVCFTDSEDGdVLIVIVTTASVHLYSLRLRPDFFRL 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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