NU107_MOUSE
ID NU107_MOUSE Reviewed; 926 AA.
AC Q8BH74; Q99KH5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nuclear pore complex protein Nup107;
DE AltName: Full=107 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup107;
GN Name=Nup107;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, 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).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-60 AND ARG-69, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [5]
RP INTERACTION WITH ZNF106, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28072389; DOI=10.7554/elife.19032;
RA Celona B., Dollen J.V., Vatsavayai S.C., Kashima R., Johnson J.R.,
RA Tang A.A., Hata A., Miller B.L., Huang E.J., Krogan N.J., Seeley W.W.,
RA Black B.L.;
RT "Suppression of C9orf72 RNA repeat-induced neurotoxicity by the ALS-
RT associated RNA-binding protein Zfp106.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance. Required for the assembly of peripheral proteins
CC into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis.
CC {ECO:0000250|UniProtKB:P57740}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (By similarity). Forms
CC part of the Nup160 subcomplex in the nuclear pore which is composed of
CC NUP160, NUP133, NUP107 and Nup96; this complex plays a role in RNA
CC export and in tethering Nup98 and NUP153 to the nucleus (By
CC similarity). Does not interact with TPR (By similarity). Interacts with
CC ZNF106 (PubMed:28072389). {ECO:0000250|UniProtKB:P57740,
CC ECO:0000269|PubMed:28072389}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P57740}.
CC Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}.
CC Note=Located on both the cytoplasmic and nuclear sides of the NPC core
CC structure. During mitosis, localizes to the kinetochores. Dissociates
CC from the dissasembled NPC structure late during prophase of mitosis.
CC {ECO:0000250|UniProtKB:P57740}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup84/Nup107 family.
CC {ECO:0000305}.
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DR EMBL; AK088069; BAC40127.1; -; mRNA.
DR EMBL; AK088303; BAC40270.1; -; mRNA.
DR EMBL; AK088625; BAC40461.1; -; mRNA.
DR EMBL; BC004655; AAH04655.1; -; mRNA.
DR EMBL; BC057591; AAH57591.1; -; mRNA.
DR CCDS; CCDS36068.1; -.
DR RefSeq; NP_598771.1; NM_134010.2.
DR AlphaFoldDB; Q8BH74; -.
DR SMR; Q8BH74; -.
DR BioGRID; 222088; 72.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8BH74; 53.
DR STRING; 10090.ENSMUSP00000063590; -.
DR iPTMnet; Q8BH74; -.
DR PhosphoSitePlus; Q8BH74; -.
DR SwissPalm; Q8BH74; -.
DR EPD; Q8BH74; -.
DR jPOST; Q8BH74; -.
DR MaxQB; Q8BH74; -.
DR PaxDb; Q8BH74; -.
DR PeptideAtlas; Q8BH74; -.
DR PRIDE; Q8BH74; -.
DR ProteomicsDB; 291920; -.
DR Antibodypedia; 16892; 246 antibodies from 36 providers.
DR DNASU; 103468; -.
DR Ensembl; ENSMUST00000064848; ENSMUSP00000063590; ENSMUSG00000052798.
DR GeneID; 103468; -.
DR KEGG; mmu:103468; -.
DR UCSC; uc007hdo.1; mouse.
DR CTD; 57122; -.
DR MGI; MGI:2143854; Nup107.
DR VEuPathDB; HostDB:ENSMUSG00000052798; -.
DR eggNOG; KOG1964; Eukaryota.
DR GeneTree; ENSGT00390000012080; -.
DR InParanoid; Q8BH74; -.
DR OMA; MAHIVLF; -.
DR OrthoDB; 671846at2759; -.
DR PhylomeDB; Q8BH74; -.
DR TreeFam; TF324259; -.
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; 103468; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Nup107; mouse.
DR PRO; PR:Q8BH74; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BH74; protein.
DR Bgee; ENSMUSG00000052798; Expressed in primitive streak and 239 other tissues.
DR ExpressionAtlas; Q8BH74; baseline and differential.
DR Genevisible; Q8BH74; MM.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0008585; P:female gonad development; ISO:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0072006; P:nephron development; ISS:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR007252; Nup84/Nup107.
DR PANTHER; PTHR13003; PTHR13003; 1.
DR Pfam; PF04121; Nup84_Nup100; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; Kinetochore; Membrane; Methylation;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..926
FT /note="Nuclear pore complex protein Nup107"
FT /id="PRO_0000204832"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 60
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 60
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 69
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57740"
SQ SEQUENCE 926 AA; 106717 MW; 4489666D13A1BD3A CRC64;
MDRSGFGGMS SPVIRDAEVT RTARKHSAHK RVLIQANQED NFGTATPRSQ IIPRTPSSFR
QPFVTPSSRS LLRHPDISYI LGTEGRSPRH TQSSGYLGNL SMVTNLDDSN WAAAFSSQRL
GLYTNTEHHS MTEDVNLSTV MLREDDPGEA ASMSMFSDFL HSFLKHSSTT VFDLVEEYEN
ICGSQVNILS KIVSRATPGL QKFSKTASML WLLQQEMVTW RLLASLYRDR IQSSLEEENM
FAIAGINASE KMVVETLFQR DSLVRQSQLV VDWLESIAKD EIGEFSDNIE FYAKSVYWEN
TLHSLKQRQL LSHMGSTRPL VTELDPDAPI RQKLPLDDLD REDEVRLLKY LFTLIRAGMT
EEAQRLCKRC GQAWRAATLE GWKLYHDPNV NGGTELEPVE GNPYRRIWKI SCWRMAEDEL
FNKYERAIYA ALSGNLKQLL PVCDTWEDTV WAYFRVMVDS LVEQEIRTSV MTQDDSEELP
REYMEANWTL EKVFEELQAT DKKRVLEENQ EHYHIVQKFL ILGDVDGLMD EFSKWLSKSG
SSLPGHLLRF MTHLILFLRT LGLQTKEEVS IEVLKTYIQL LISEKHTSLI AFYTCHLPQD
LAVAQYALFL EGVTEFEQRH QCLELAKEAD LDVATITKTV VENICKKDNG EFSHHDLAPS
LDTGTTEEDR LKIDVIDWLV FDPAQRAEAL RQGNAIMRKF LALKKHEAAK EVFVKIPQDS
IAEIYNQWEE QGMESPLPAE DDNAIREHLC IRAYLEAHET FNEWFKHMNS APQKPTLLSQ
ATFTEKVAYE HREKKYEMDH NIWKGHLDAL TADVKEKMYN VLLFVDGGWM VDVREDAEDD
PERTHQMVLL RKLCLPMLCF LLHTILHSTG QYQECLQLAD MVSSERHKLY LVFSKEELRK
LLQKLRESSL MLLDQGLDPL GYEIQS
