NUP85_MOUSE
ID NUP85_MOUSE Reviewed; 656 AA.
AC Q8R480; A2A9W9; A2A9X0; Q9CYI9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Nuclear pore complex protein Nup85;
DE AltName: Full=85 kDa nucleoporin;
DE AltName: Full=FROUNT;
DE AltName: Full=Nucleoporin Nup85;
DE AltName: Full=Pericentrin-1;
GN Name=Nup85; Synonyms=Pcnt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15995708; DOI=10.1038/ni1222;
RA Terashima Y., Onai N., Murai M., Enomoto M., Poonpiriya V., Hamada T.,
RA Motomura K., Suwa M., Ezaki T., Haga T., Kanegasaki S., Matsushima K.;
RT "Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte
RT chemotaxis.";
RL Nat. Immunol. 6:827-835(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH NUP160; NUP133 AND SEC13.
RX PubMed=12718872; DOI=10.1016/s1097-2765(03)00116-3;
RA Harel A., Orjalo A.V., Vincent T., Lachish-Zalait A., Vasu S., Shah S.,
RA Zimmerman E., Elbaum M., Forbes D.J.;
RT "Removal of a single pore subcomplex results in vertebrate nuclei devoid of
RT nuclear pores.";
RL Mol. Cell 11:853-864(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Essential component of the nuclear pore complex (NPC) that
CC seems to be required for NPC assembly and maintenance. As part of the
CC NPC Nup107-160 subcomplex plays a role in RNA export and in tethering
CC NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to
CC be required for spindle assembly during mitosis. NUP85 is required for
CC membrane clustering of CCL2-activated CCR2. Seems to be involved in
CC CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to
CC the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion
CC cascade. Involved in nephrogenesis. {ECO:0000250|UniProtKB:Q9BW27}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). Component of the
CC NPC Nup107-160 subcomplex, consisting of at least NUP107, NUP98/Nup96,
CC NUP160, NUP133, NUP85, NUP37, NUP43 and SEC13. Interacts with NUP160,
CC NUP133 and SEC13 (PubMed:12718872). Interacts with NUP37, NUP107 and
CC NUP43. Interacts with CCR2. {ECO:0000250|UniProtKB:Q9BW27,
CC ECO:0000269|PubMed:12718872}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the
CC kinetochores and spindle poles. Upon CCl2 stimulation translocates from
CC the cytoplasm to the membrane and colocalizes with CCR2 at the front of
CC migrating cells. {ECO:0000250|UniProtKB:Q9BW27}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM23011.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM23012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF498263; AAM18529.1; -; mRNA.
DR EMBL; AK017632; BAB30848.1; -; mRNA.
DR EMBL; AL645470; CAM23011.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL645470; CAM23012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL645470; CAM23013.1; -; Genomic_DNA.
DR EMBL; BC079856; AAH79856.1; -; mRNA.
DR CCDS; CCDS25640.1; -.
DR RefSeq; NP_001002929.3; NM_001002929.4.
DR AlphaFoldDB; Q8R480; -.
DR SMR; Q8R480; -.
DR BioGRID; 243059; 20.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8R480; 2.
DR MINT; Q8R480; -.
DR STRING; 10090.ENSMUSP00000021085; -.
DR iPTMnet; Q8R480; -.
DR PhosphoSitePlus; Q8R480; -.
DR SwissPalm; Q8R480; -.
DR EPD; Q8R480; -.
DR MaxQB; Q8R480; -.
DR PaxDb; Q8R480; -.
DR PeptideAtlas; Q8R480; -.
DR PRIDE; Q8R480; -.
DR ProteomicsDB; 293782; -.
DR Antibodypedia; 32118; 232 antibodies from 31 providers.
DR DNASU; 445007; -.
DR Ensembl; ENSMUST00000021085; ENSMUSP00000021085; ENSMUSG00000020739.
DR GeneID; 445007; -.
DR KEGG; mmu:445007; -.
DR UCSC; uc007mhx.2; mouse.
DR CTD; 79902; -.
DR MGI; MGI:3046173; Nup85.
DR VEuPathDB; HostDB:ENSMUSG00000020739; -.
DR eggNOG; KOG2271; Eukaryota.
DR GeneTree; ENSGT00390000000204; -.
DR HOGENOM; CLU_027342_0_0_1; -.
DR InParanoid; Q8R480; -.
DR OMA; ELMEWLN; -.
DR OrthoDB; 588551at2759; -.
DR PhylomeDB; Q8R480; -.
DR TreeFam; TF323240; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 445007; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Nup85; mouse.
DR PRO; PR:Q8R480; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R480; protein.
DR Bgee; ENSMUSG00000020739; Expressed in optic fissure and 263 other tissues.
DR ExpressionAtlas; Q8R480; baseline and differential.
DR Genevisible; Q8R480; MM.
DR GO; GO:0005737; C:cytoplasm; ISA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISA:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0031727; F:CCR2 chemokine receptor binding; ISA:MGI.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISA:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR GO; GO:0048246; P:macrophage chemotaxis; IDA:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0072006; P:nephron development; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR InterPro; IPR011502; Nucleoporin_Nup85.
DR PANTHER; PTHR13373; PTHR13373; 1.
DR Pfam; PF07575; Nucleopor_Nup85; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinetochore;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..656
FT /note="Nuclear pore complex protein Nup85"
FT /id="PRO_0000324188"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW27"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 649
FT /note="R -> G (in Ref. 2; BAB30848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 74776 MW; 42289D345DDE3F5E CRC64;
MEELDCEPAV TWIPGVNSKK KQMCFDWGPG EMLLCETSFN QTGKSEKVPS CPFIYIIRKD
VDVYSQILRK LFNESHGIFV GLQKIEEELS GKSRKAQLVR VSKNYRSVIR ACMEEMHQVA
IAAKDPASGR QFSSQVSILS AMELIWNLCE ILFIEVAPAG PLLLHLLDWV RLHVCEVDSL
SADVLGGDNP SKHENFWDLV TVLVLQGRLD EARQMLAKEA DANPSCAGMC RVLGDLMRTM
PILSPGNTQT LTELELKWQH WREECERHLQ DNTFAANPRL ESLCKIMLGD EAALLEQKEL
LSNWYHFLVT RLLYSNPTVK PIDLHFYAQS SLDMFLGGES SPEPLDNILM AAFEFDIHQV
IKECSIALSN WWFVAHLTDL LDHCRLLQSH NLYFGSNMRE FLLLEYASGL FAHHSLWQLG
VDYFDYCPEL GRVSLELHIE RIPLNTEQKA LKVLRICEQR QMTEQVKSIC KILAMKAVRN
NRLGSALSWS IRAKDAAFAT LVSDRFLRDY CERGCFSDLD LIDNLGSAMM LSDRLTFLGK
YREFHRLYGE KRFGDAASLL LSLMTSQIAP RSFWMTLLTD ALPLLEQKQV IFSAEQTYEL
MRCLEDLASG RPECGEPDAQ RLQDDDIETT KVEMLRLALA RNLARAIIRE GSLEGS
