NU160_MOUSE
ID NU160_MOUSE Reviewed; 1402 AA.
AC Q9Z0W3; Q3TBI7; Q3TP11; Q3U250; Q6A0A7; Q7TME1; Q9CZD9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nuclear pore complex protein Nup160;
DE AltName: Full=160 kDa nucleoporin;
DE AltName: Full=Gene trap locus 1-13 protein;
DE Short=GTL-13;
DE AltName: Full=Nucleoporin Nup160;
GN Name=Nup160; Synonyms=Gtl1-13, Kiaa0197;
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] (ISOFORM 1).
RC STRAIN=129/SvJ;
RA Van de Putte T., Cozijnsen M., Dewulf N., Tylzanowski P., Lonnoy O.,
RA Huylebroeck D.;
RT "Mus musculus mRNA for gtl-13 (gene trap locus-13), similar to human
RT KIAA0197 gene (D83781), complete cds.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-985 AND 1151-1402 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Heart;
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 MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 542-1402 (ISOFORM 1).
RC TISSUE=Natural killer cell;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11564755; DOI=10.1083/jcb.200101081;
RA Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N.,
RA Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., Ellenberg J.,
RA Doye V.;
RT "An evolutionarily conserved NPC subcomplex, which redistributes in part to
RT kinetochores in mammalian cells.";
RL J. Cell Biol. 154:1147-1160(2001).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11684705; DOI=10.1083/jcb.200108007;
RA Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.;
RT "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA
RT export.";
RL J. Cell Biol. 155:339-354(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-1123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and 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).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC (PubMed:11564755, PubMed:11684705). Involved in poly(A)+ RNA transport
CC (PubMed:11684705). {ECO:0000269|PubMed:11564755,
CC ECO:0000269|PubMed:11684705}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:11564755,
CC PubMed:11684705). Forms part of the NUP160 subcomplex in the nuclear
CC pore which is composed of NUP160, NUP133, NUP107 and NUP96
CC (PubMed:11564755, PubMed:11684705). This complex plays a role in RNA
CC export and in tethering NUP98 and NUP153 to the nucleus
CC (PubMed:11564755, PubMed:11684705). {ECO:0000269|PubMed:11564755,
CC ECO:0000269|PubMed:11684705}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0W3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0W3-2; Sequence=VSP_018500, VSP_018501;
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DR EMBL; AF104415; AAD17922.2; -; mRNA.
DR EMBL; AK012715; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK155492; BAE33292.1; -; mRNA.
DR EMBL; AK164802; BAE37926.1; -; mRNA.
DR EMBL; AK171218; BAE42322.1; -; mRNA.
DR EMBL; BC052450; AAH52450.1; -; mRNA.
DR EMBL; BC054523; AAH54523.1; -; mRNA.
DR EMBL; AK172911; BAD32189.1; -; mRNA.
DR CCDS; CCDS16413.1; -. [Q9Z0W3-1]
DR RefSeq; NP_067487.1; NM_021512.2. [Q9Z0W3-1]
DR RefSeq; XP_006500031.1; XM_006499968.3. [Q9Z0W3-1]
DR AlphaFoldDB; Q9Z0W3; -.
DR SMR; Q9Z0W3; -.
DR BioGRID; 208486; 5.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q9Z0W3; 3.
DR MINT; Q9Z0W3; -.
DR STRING; 10090.ENSMUSP00000059289; -.
DR iPTMnet; Q9Z0W3; -.
DR PhosphoSitePlus; Q9Z0W3; -.
DR SwissPalm; Q9Z0W3; -.
DR EPD; Q9Z0W3; -.
DR jPOST; Q9Z0W3; -.
DR MaxQB; Q9Z0W3; -.
DR PaxDb; Q9Z0W3; -.
DR PeptideAtlas; Q9Z0W3; -.
DR PRIDE; Q9Z0W3; -.
DR ProteomicsDB; 253034; -. [Q9Z0W3-1]
DR ProteomicsDB; 253035; -. [Q9Z0W3-2]
DR Antibodypedia; 26888; 239 antibodies from 32 providers.
DR DNASU; 59015; -.
DR Ensembl; ENSMUST00000057481; ENSMUSP00000059289; ENSMUSG00000051329. [Q9Z0W3-1]
DR GeneID; 59015; -.
DR KEGG; mmu:59015; -.
DR UCSC; uc008ksw.1; mouse. [Q9Z0W3-1]
DR UCSC; uc008ksy.1; mouse. [Q9Z0W3-2]
DR CTD; 23279; -.
DR MGI; MGI:1926227; Nup160.
DR VEuPathDB; HostDB:ENSMUSG00000051329; -.
DR eggNOG; KOG4521; Eukaryota.
DR GeneTree; ENSGT00390000000972; -.
DR HOGENOM; CLU_005083_0_0_1; -.
DR InParanoid; Q9Z0W3; -.
DR OMA; CQFDQAY; -.
DR OrthoDB; 284127at2759; -.
DR PhylomeDB; Q9Z0W3; -.
DR TreeFam; TF353082; -.
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; 59015; 25 hits in 70 CRISPR screens.
DR ChiTaRS; Nup160; mouse.
DR PRO; PR:Q9Z0W3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z0W3; protein.
DR Bgee; ENSMUSG00000051329; Expressed in spermatid and 247 other tissues.
DR Genevisible; Q9Z0W3; MM.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0072006; P:nephron development; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR PANTHER; PTHR21286; PTHR21286; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW Transport.
FT CHAIN 1..1402
FT /note="Nuclear pore complex protein Nup160"
FT /id="PRO_0000204852"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12769"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12769"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 836..839
FT /note="WPSN -> YPFA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018500"
FT VAR_SEQ 840..1402
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018501"
FT CONFLICT 562..563
FT /note="Missing (in Ref. 3; AAH52450/AAH54523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1314
FT /note="E -> G (in Ref. 2; AK012715)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="N -> D (in Ref. 2; AK012715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1402 AA; 158232 MW; 3BF5D9F057D28772 CRC64;
MAAAGSLERS FVELSGAERE RPRHFREFTV CDIGTASAAF GTVKYSESAG GFYYVESGKL
FSITRNRFIH WKTSGDTLEL VEESLDLNLL NNAVRLKFQN YNILPGGVHV SETQNHVIIL
ILTNQTVHRL ILPHPSRMYR SELVTESQMQ SIFTDIGKVD FRDPCNSQLI PSVPGLSPGS
TTSAAWLSSD GEALFALPSA SGGIFVLKLP PYDVPGIASV VELKQSSVMQ RLLTGWMPTA
IRGDHGPSDR ALSLAVHCVE HDAFIFALCQ DHKLRMWSYK DQMCLMVADM LEYVPVNKDL
RLTAGTGHKL RLAYSPSMGL YLGIYMHAPK RGQFCVFQLV STENNRYSLD HISSLFTSQE
TLVDFALTST DIWALWHDAE NQTIVKYINF EHNVAGQWNP VFMQPLPEEE IVIRDDQDPR
EMYLRSLFTP GHFINAALCK ALQIFCRGTE RNLDLSWNEL KKEITLAVEN ELQGSVTEYE
FSQDEFRTLQ QEFWCKFYAC VLQYQEALSH PLALHLNPVT NMVCLLKKGY LSFLVPSSLV
DHLYLLPDEH LLTEDETTIS DDADVARDVL CLIKCLRMIG ESVTMDMAVL METSCYNLQS
PEKAAEHILE DLITIDVENV MEDICSKLQE IRNPVHAIGL LIREMDYETE VEMEKGFDPA
QPLNVRMNLS QLYGSSTAGY IVCRGVYKIA STRFLICRDL LILQQLLTRL GDAVILGAGQ
LFQAQQDLLH RTAPLLLSYY LIKWASQCLA TDVPVDTLES NLQHLSVLEL TDSGALMANK
LVSSPQTIME LFFQEVARKQ IISHLFSQPK APLSQTGLNW PEMITAVTGY LLQLLWPSNP
GCLFLECLMG NCQYVQLQDY IQLLHPWCQV NVGSCRFMLG RCYLVTGEVQ KALECFCQAA
SEVGKEEFLD RLIRSEDGEI VSTPKLQYYD KVLRLLDVVG LPELVIQLAT SAITEAGDDW
KSQATLRTCI FKHHLDLGHN SQAYEALTQI PDSSRQLDCL RQLVVVLCER SQLQDLVEFP
YVNLHNEVVG IIESRARAVD LMTHNYYELL YAFHIYRHNY RKAGTVMFEY GMRLGREVRT
LRGLEKQGNC YLAAINCLRL IRPEYAWIVQ PASGAVSDRP GASPKRNHDG ECTAAPTNRQ
IEILELEDLE KEYSLARIRL TLARHDPSVI AIAGSSSAKE MSALLVQAGL FDTAISLCQT
FTLPLTPVFE GLAFKCIKLQ FGGEAAQGEA WSWLATNQLS SVITTKESSA TDEAWRLLST
YLERYKVQNN LYHHCVINKL LSHGVPLPNW LINSYKKVDA AELLRLYLNY DLLEEAVDLV
SEYVDAVLGK GHQYFGIEFP LSATAPMVWL PYSSIDQLLQ ALGENSANSH NIILSQKILD
KLEDYQQKVD KATRDLLYRR DL
