Tag | Content |
---|
CPLM ID | CPLM-004889 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nucleoporin NUP1 |
Protein Synonyms/Alias | Nuclear pore protein NUP1 |
Gene Name | NUP1 |
Gene Synonyms/Alias | YOR098C; YOR3182C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
---|
568 | TPATIVKKPTFTFGQ | acetylation | [1] | 675 | KPLFSFGKSDAAKEP | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex. |
Sequence Annotation | REPEAT 336 338 FXF 1. REPEAT 384 386 FXF 2. REPEAT 406 409 FXFG 1. REPEAT 422 425 FXFG 2. REPEAT 448 451 FXFG 3. REPEAT 484 487 FXFG 4. REPEAT 510 513 FXFG 5. REPEAT 525 528 FXFG 6. REPEAT 543 546 FXFG 7. REPEAT 571 574 FXFG 8. REPEAT 591 593 FXF 3. REPEAT 614 616 FXF 4. REPEAT 636 638 FXF 5. REPEAT 657 659 FXF 6. REPEAT 671 674 FXFG 9. REPEAT 689 691 FXF 7. REPEAT 708 711 FXFG 10. REPEAT 727 730 FXFG 11. REPEAT 753 755 FXF 8. REPEAT 800 803 FXFG 12. REPEAT 819 821 FXF 9. REPEAT 866 868 FXF 10. REPEAT 885 888 FXFG 13. REPEAT 929 931 FXF 11. REPEAT 1008 1009 FG 1. REPEAT 1027 1028 FG 2. REPEAT 1038 1039 FG 3. REGION 1040 1076 Interaction with KAP95. MOD_RES 54 54 Phosphoserine. MOD_RES 161 161 Phosphoserine. MOD_RES 381 381 Phosphothreonine. MOD_RES 383 383 Phosphoserine; by CHEK2. MOD_RES 449 449 Phosphoserine; by CHEK2. MOD_RES 592 592 Phosphoserine; by CHEK2. MOD_RES 615 615 Phosphoserine; by CHEK2. MOD_RES 637 637 Phosphoserine; by CHEK2. MOD_RES 656 656 Phosphoserine; by CHEK2. MOD_RES 672 672 Phosphoserine; by CHEK2. MOD_RES 754 754 Phosphoserine; by CHEK2. |
Keyword | 3D-structure; Complete proteome; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Translocation; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1076 AA |
Protein Sequence | MSSNTSSVMS SPRVEKRSFS STLKSFFTNP NKKRPSSKKV FSSNLSYANH LEESDVEDTL 60 HVNKRKRVSG TSQHSDSLTQ NNNNAPIIIY GTENTERPPL LPILPIQRLR LLREKQRVRN 120 MRELGLIQST EFPSITSSVI LGSQSKSDEG GSYLCTSSTP SPIKNGSCTR QLAGKSGEDT 180 NVGLPILKSL KNRSNRKRFH SQSKGTVWSA NFEYDLSEYD AIQKKDNKDK EGNAGGDQKT 240 SENRNNIKSS ISNGNLATGP NLTSEIEDLR ADINSNRLSN PQKNLLLKGP ASTVAKTAPI 300 QESFVPNSER SGTPTLKKNI EPKKDKESIV LPTVGFDFIK DNETPSKKTS PKATSSAGAV 360 FKSSVEMGKT DKSTKTAEAP TLSFNFSQKA NKTKAVDNTV PSTTLFNFGG KSDTVTSASQ 420 PFKFGKTSEK SENHTESDAP PKSTAPIFSF GKQEENGDEG DDENEPKRKR RLPVSEDTNT 480 KPLFDFGKTG DQKETKKGES EKDASGKPSF VFGASDKQAE GTPLFTFGKK ADVTSNIDSS 540 AQFTFGKAAT AKETHTKPSE TPATIVKKPT FTFGQSTSEN KISEGSAKPT FSFSKSEEER 600 KSSPISNEAA KPSFSFPGKP VDVQAPTDDK TLKPTFSFTE PAQKDSSVVS EPKKPSFTFA 660 SSKTSQPKPL FSFGKSDAAK EPPGSNTSFS FTKPPANETD KRPTPPSFTF GGSTTNNTTT 720 TSTKPSFSFG APESMKSTAS TAAANTEKLS NGFSFTKFNH NKEKSNSPTS FFDGSASSTP 780 IPVLGKPTDA TGNTTSKSAF SFGTANTNGT NASANSTSFS FNAPATGNGT TTTSNTSGTN 840 IAGTFNVGKP DQSIASGNTN GAGSAFGFSS SGTAATGAAS NQSSFNFGNN GAGGLNPFTS 900 ATSSTNANAG LFNKPPSTNA QNVNVPSAFN FTGNNSTPGG GSVFNMNGNT NANTVFAGSN 960 NQPHQSQTPS FNTNSSFTPS TVPNINFSGL NGGITNTATN ALRPSDIFGA NAASGSNSNV 1020 TNPSSIFGGA GGVPTTSFGQ PQSAPNQMGM GTNNGMSMGG GVMANRKIAR MRHSKR 1076 |
Gene Ontology | GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. GO:0044613; C:nuclear pore central transport channel; IDA:SGD. GO:0044615; C:nuclear pore nuclear basket; IDA:SGD. GO:0005487; F:nucleocytoplasmic transporter activity; IPI:SGD. GO:0017056; F:structural constituent of nuclear pore; IMP:SGD. GO:0006607; P:NLS-bearing substrate import into nucleus; IMP:SGD. GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD. GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD. GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |