NU154_DROME
ID NU154_DROME Reviewed; 1365 AA.
AC Q9V463; O62536; O62610; O62613; Q9VKL5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nuclear pore complex protein Nup154 {ECO:0000305};
DE AltName: Full=154 kDa nucleoporin {ECO:0000305};
DE AltName: Full=Nucleoporin Nup154 {ECO:0000303|PubMed:9732281};
DE AltName: Full=Tulipan {ECO:0000303|PubMed:9732281};
GN Name=Nup154 {ECO:0000303|PubMed:9732281, ECO:0000312|FlyBase:FBgn0021761};
GN Synonyms=Nup155 {ECO:0000303|PubMed:22718353, ECO:0000312|EMBL:AAF53051.1};
GN ORFNames=CG4579 {ECO:0000312|FlyBase:FBgn0021761};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:CAA76635.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:CAA76635.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:CAA76635.1};
RX PubMed=9732281; DOI=10.1083/jcb.142.5.1195;
RA Gigliotti S., Callaini G., Andone S., Riparbelli M.G., Pernas-Alonso R.,
RA Hoffmann G., Graziani F., Malva C.;
RT "Nup154, a new Drosophila gene essential for male and female gametogenesis
RT is related to the nup155 vertebrate nucleoporin gene.";
RL J. Cell Biol. 142:1195-1207(1998).
RN [2] {ECO:0000312|EMBL:AAC05385.1, ECO:0000312|EMBL:AAC05386.1, ECO:0000312|EMBL:AAC06247.1, ECO:0000312|EMBL:AAC06248.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=10511559; DOI=10.1093/genetics/153.2.799;
RA Kiger A.A., Gigliotti S., Fuller M.T.;
RT "Developmental genetics of the essential Drosophila nucleoporin nup154:
RT allelic differences due to an outward-directed promoter in the P-element 3'
RT end.";
RL Genetics 153:799-812(1999).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:AAD46884.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAD46884.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAD46884.1};
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17410542; DOI=10.1002/cm.20206;
RA Riparbelli M.G., Gigliotti S., Callaini G.;
RT "The Drosophila nucleoporin gene nup154 is required for correct
RT microfilament dynamics and cell death during oogenesis.";
RL Cell Motil. Cytoskeleton 64:590-604(2007).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CUP, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17277377; DOI=10.1534/genetics.106.062844;
RA Grimaldi M.R., Cozzolino L., Malva C., Graziani F., Gigliotti S.;
RT "nup154 genetically interacts with cup and plays a cell-type-specific
RT function during Drosophila melanogaster egg-chamber development.";
RL Genetics 175:1751-1759(2007).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21696798; DOI=10.1016/j.tice.2011.05.001;
RA Colozza G., Montembault E., Quenerch'du E., Riparbelli M.G., D'Avino P.P.,
RA Callaini G.;
RT "Drosophila nucleoporin Nup154 controls cell viability, proliferation and
RT nuclear accumulation of Mad transcription factor.";
RL Tissue Cell 43:254-261(2011).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NUP93-1 AND NUP35, AND SUBCELLULAR LOCATION.
RX PubMed=22718353; DOI=10.1242/jcs.105809;
RA Busayavalasa K., Chen X., Farrants A.K., Wagner N., Sabri N.;
RT "The Nup155-mediated organisation of inner nuclear membrane proteins is
RT independent of Nup155 anchoring to the metazoan nuclear pore complex.";
RL J. Cell Sci. 125:4214-4218(2012).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26341556; DOI=10.1101/gad.264341.115;
RA Breuer M., Ohkura H.;
RT "A negative loop within the nuclear pore complex controls global chromatin
RT organization.";
RL Genes Dev. 29:1789-1794(2015).
CC -!- FUNCTION: Component of the nuclear pore complex (PubMed:17410542). Has
CC a role in the organization of the inner nuclear membrane proteins at
CC the nuclear envelope (PubMed:22718353). In germ cells, plays a role in
CC the nuclear localization of components of the dpp signaling pathways,
CC such as Medea and phosphorylated Mad (PubMed:21696798). Binds to
CC chromatin, and together with Nup62 and Nup93-1, contributes to
CC karyosome morphology and chromatin organization including attachment to
CC the nuclear envelope in oocytes and nurse cells (PubMed:22718353,
CC PubMed:26341556). Has a role in female fertility including egg chamber
CC development; in nurse cells, has a role in the organization of F-actin
CC in subcortical and cytoplasmic actin filaments important for the
CC transfer of cytoplasm from nurse cells to the growing oocytes
CC (PubMed:9732281, PubMed:10511559, PubMed:17410542, PubMed:17277377).
CC Has a role in male spermatogenesis and fertility (PubMed:9732281,
CC PubMed:10511559). Has a role in germ line cell proliferation
CC (PubMed:21696798). {ECO:0000269|PubMed:10511559,
CC ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:21696798, ECO:0000269|PubMed:22718353,
CC ECO:0000269|PubMed:26341556, ECO:0000269|PubMed:9732281,
CC ECO:0000303|PubMed:17410542}.
CC -!- SUBUNIT: Interacts (via N-terminus) with Nup93-1 (PubMed:22718353).
CC Interacts with Nup35 (PubMed:22718353). Interacts with cup
CC (PubMed:17277377). {ECO:0000269|PubMed:17277377,
CC ECO:0000269|PubMed:22718353}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:17410542}. Chromosome {ECO:0000269|PubMed:22718353,
CC ECO:0000269|PubMed:9732281}. Nucleus {ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:9732281}. Nucleus membrane
CC {ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17410542}; Cytoplasmic side
CC {ECO:0000269|PubMed:17410542}. Nucleus membrane
CC {ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17410542}; Nucleoplasmic side
CC {ECO:0000269|PubMed:17410542}. Cytoplasm {ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:22718353}. Note=Increased localization to chromatin
CC before interphase (PubMed:22718353). Distributed along filamentous
CC structures that extend radially on the nuclear side of the pore complex
CC (PubMed:17410542). {ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:22718353}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo (at protein level)
CC (PubMed:9732281). Expressed in ovaries; more specifically in the
CC germarium and throughout egg chamber development both in germ line and
CC nurse cells (at protein level) (PubMed:9732281, PubMed:17410542,
CC PubMed:17277377). Expressed in spermatocytes (at protein level)
CC (PubMed:9732281). In embryos, detected during germ-band elongation and
CC in the developing mesoderm (PubMed:10511559). At stage 11, mostly
CC prominent in the central nervous system and gut (PubMed:10511559). By
CC stage 14, detected in the brain and dorsal vessel (PubMed:10511559). At
CC the end of embryogenesis restricted to lymph glands (hematopoietic
CC organ), gonadal germline and specific neurons in the brain
CC (PubMed:10511559). In larvae, detected in the imaginal disks, certain
CC regions of the brain and all tissues containing dividing cells
CC (PubMed:10511559). In larval, detected in testes and in all germline
CC cells up through the meiotic stages (PubMed:10511559). In adult,
CC detected in testes, ovaries in germanium region 2 and throughout later
CC stage of oogenesis (PubMed:10511559). {ECO:0000269|PubMed:10511559,
CC ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542,
CC ECO:0000269|PubMed:9732281}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:10511559). RNAi-mediated
CC knockdown results in failed nuclear import of phosphorylated Mad in
CC response to activation of the dpp signaling cascade (PubMed:21696798).
CC RNAi-mediated knockdown results in altered karyosome morphology, in the
CC reduction of Nup62 association with the nuclear envelope and its
CC accumulation in the cytoplasm (PubMed:26341556). RNAi-mediated
CC knockdown of Nup62 in combination with Nup154 rescues the phenotype of
CC the Nup62 knockdown restablishing correct kariosome morphology and
CC chromatin detachment from the nuclear envelope (PubMed:26341556).
CC {ECO:0000269|PubMed:10511559, ECO:0000269|PubMed:21696798,
CC ECO:0000269|PubMed:26341556}.
CC -!- SIMILARITY: Belongs to the non-repetitive/WGA-negative nucleoporin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05385.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC06248.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y17111; CAA76635.1; -; mRNA.
DR EMBL; AF051397; AAC05385.1; ALT_SEQ; mRNA.
DR EMBL; AF051398; AAC05386.1; -; mRNA.
DR EMBL; AF051396; AAC06247.1; -; Genomic_DNA.
DR EMBL; AF051396; AAC06248.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014134; AAF53050.3; -; Genomic_DNA.
DR EMBL; AE014134; AAF53051.1; -; Genomic_DNA.
DR EMBL; AE014134; AHN54341.1; -; Genomic_DNA.
DR EMBL; AF160944; AAD46884.1; -; mRNA.
DR PIR; T13031; T13031.
DR PIR; T13991; T13991.
DR RefSeq; NP_001285827.1; NM_001298898.1.
DR RefSeq; NP_477287.1; NM_057939.4.
DR RefSeq; NP_477288.3; NM_057940.4.
DR AlphaFoldDB; Q9V463; -.
DR SMR; Q9V463; -.
DR IntAct; Q9V463; 3.
DR MINT; Q9V463; -.
DR STRING; 7227.FBpp0088820; -.
DR PaxDb; Q9V463; -.
DR PRIDE; Q9V463; -.
DR EnsemblMetazoa; FBtr0089881; FBpp0088820; FBgn0021761.
DR EnsemblMetazoa; FBtr0340224; FBpp0309199; FBgn0021761.
DR EnsemblMetazoa; FBtr0340225; FBpp0309200; FBgn0021761.
DR GeneID; 34527; -.
DR KEGG; dme:Dmel_CG4579; -.
DR UCSC; CG4579-RA; d. melanogaster.
DR UCSC; CG4579-RB; d. melanogaster.
DR CTD; 34527; -.
DR FlyBase; FBgn0021761; Nup154.
DR VEuPathDB; VectorBase:FBgn0021761; -.
DR eggNOG; KOG1900; Eukaryota.
DR GeneTree; ENSGT00390000016532; -.
DR HOGENOM; CLU_000429_0_0_1; -.
DR InParanoid; Q9V463; -.
DR OMA; EYYSRMI; -.
DR OrthoDB; 140051at2759; -.
DR PhylomeDB; Q9V463; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR SignaLink; Q9V463; -.
DR BioGRID-ORCS; 34527; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34527; -.
DR PRO; PR:Q9V463; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0021761; Expressed in ovariole (Drosophila) and 32 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044611; C:nuclear pore inner ring; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0055050; P:astral spindle assembly involved in male meiosis; IMP:UniProtKB.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR GO; GO:0030715; P:oocyte growth in germarium-derived egg chamber; IGI:UniProtKB.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:1905938; P:positive regulation of germ cell proliferation; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IMP:FlyBase.
DR GO; GO:0045477; P:regulation of nurse cell apoptotic process; IMP:UniProtKB.
DR GO; GO:1905879; P:regulation of oogenesis; IMP:UniProtKB.
DR GO; GO:1905475; P:regulation of protein localization to membrane; IMP:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0035220; P:wing disc development; IMP:UniProtKB.
DR Gene3D; 1.20.120.1880; -; 1.
DR Gene3D; 1.25.40.440; -; 1.
DR Gene3D; 1.25.40.450; -; 1.
DR InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR004870; Nucleoporin_Nup155.
DR InterPro; IPR042533; Nucleoporin_Nup155_C_1.
DR InterPro; IPR042537; Nucleoporin_Nup155_C_2.
DR InterPro; IPR042538; Nucleoporin_Nup155_C_3.
DR PANTHER; PTHR10350; PTHR10350; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1365
FT /note="Nuclear pore complex protein Nup154"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442728"
FT REGION 1..508
FT /note="Required for binding to Nup93-1 and anchoring to the
FT nuclear pore complex"
FT /evidence="ECO:0000269|PubMed:22718353"
FT REGION 508..986
FT /note="Required for binding to chromatin"
FT /evidence="ECO:0000269|PubMed:22718353"
FT CONFLICT 1003
FT /note="V -> E (in Ref. 1; CAA76635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="A -> P (in Ref. 2; AAC05385/AAC05386/AAC06247/
FT AAC06248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1365 AA; 153895 MW; 0ADFC7E8B6BD18B3 CRC64;
MTLPQAQLDF FTTATSMLEW HYNLERNKPG LLELTGVSQH GRATMSGLND YDYQSLSFLK
SDRTHNLQQM RTVTKSAIPN EILEHFKHIK CHCTMGLFPE IGRAWLTIDS EIYIWTFNQT
RDVAYYDGLS HLIVSVGLVK PKPGVFVQDV KYLLVLTTPI EVIVLGVTFG ESSYNEMQLM
NRPVFVIGTD NVSISVIKGT DDGRIFLGGR DGCLYEIYYQ AESSWFGKRC KKINLSQGLV
SYMVPSFLKV FSEVDPIEHI EIDNSRKLLY VLTEKGVIEA WDISTSYTTA RRLGRITQND
ITNQAVSLIT TVDPSIFKSV KAICPLSADD ADKLHLVAVT QCGVRLFFST TSLNVKQQFG
PAVPCSPGEN TGFGQPAVQP PLSPNAEAPK GLYLLHVRLP PGYTPNATTN KPKQVHAAHY
TEGTMLMITT QQHEQDLLWS LSSAPSVNFT YLVESTALES LDGVVWGLAE VHEPSTPQRK
SPLNSARHAR KVALLTNQGT HIIEVLKMVD VLRQILLSCN GPHHEEVKMF FQSQNQREAC
VTALLLATSD TYRGSDVALW AAQAFMLYGG EPCYQHQKFL NASNRNMANQ TLGPNTTNVR
ERQSMFMSTP MPNSVANSPV GFPGSQFNQP ISPIGNMQPP QVAVSNENSP IVFSAKHDGL
YMYVSRMLHS VWQMRCVNEQ FCSNLSQSEC ALLLSDLRSL RSFLEVHSVH DISSTTRVSF
DNHLDRTNSY NTIMMGNTLL PIPEQRVLSE QAQVEETRSL SALNLFVKHA CEVISLWNIL
NSHSFQLICV QLSPEHQKLL TCSTFRDLLI TRSEVCAFLI ISLINLYLKD AAGVSEVSKN
LRENCPNLYR HEDDVTYKAT ELLMNAKNCT SATEKEHMLR TTLHMCKEAA PTLPLHSICM
QFISADFFEG VIELSAVCAS KSDPEEVGVH FYNNGEPADD REGYTCFATR MAYYKEVQLM
LDHIYQRVCN KTHVQDKSIN PLKGTAKASD AKNGATQTIP KIVAHTLKVK DPLIHITLYE
WLLAHDMLKE LLDVVEPSLG EFLRRSVSQN VDNVVLIDLL WKYYEKNSHH SQAAHILDNL
AMTRSENINL EQRIEYLVRA VMCMRNGNVG SSLSNGIFLK ELEDKLDIAR VQKSVLAAMT
ELASDKLEAA TAVKELNYAL YDITQLYQHF AEPFDLWECQ LSILNCSHHN DPLLIESVWG
QIINSVVDKP GTTSERCNRL FTKIEILVRE YGESGVCFPF AFLIRELEVK ACQLRFPEGI
VPEKLVSMNL DIELLLEYYS RMISMNERVW ANEGNEWHLI QSVIRVVSLL ADNAQSIWYR
SKRRIVGKAQ DIVAGCLNIC YQKPDTNRLQ HSLKELQSQL QRLLI
