NU107_HUMAN
ID NU107_HUMAN Reviewed; 925 AA.
AC P57740; B4DZ67; Q6PJE1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Nuclear pore complex protein Nup107;
DE AltName: Full=107 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup107;
GN Name=NUP107;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic cancer;
RA Cordes V.C., Hunziker A., Mueller-Pillasch F.;
RT "Sequential assembly of structural modules forming the vertebrate nuclear
RT pore complex.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterus;
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 SUBUNIT, AND 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 SUBUNIT.
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 LACK OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
RX PubMed=12802065; DOI=10.1091/mbc.e02-09-0620;
RA Hase M.E., Cordes V.C.;
RT "Direct interaction with nup153 mediates binding of Tpr to the periphery of
RT the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [8]
RP FUNCTION.
RX PubMed=12552102; DOI=10.1073/pnas.252749899;
RA Boehmer T., Enninga J., Dales S., Blobel G., Zhong H.;
RT "Depletion of a single nucleoporin, Nup107, prevents the assembly of a
RT subset of nucleoporins into the nuclear pore complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:981-985(2003).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15229283; DOI=10.1091/mbc.e04-03-0165;
RA Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
RT "Nucleoporins as components of the nuclear pore complex core structure and
RT Tpr as the architectural element of the nuclear basket.";
RL Mol. Biol. Cell 15:4261-4277(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-11; SER-37; THR-46;
RP THR-55; SER-58; THR-64; SER-69 AND SER-86, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND THR-46, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-11 AND THR-46, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-10; SER-11; SER-37;
RP SER-57; SER-58; THR-64 AND SER-86, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [21]
RP INVOLVEMENT IN NPHS11, VARIANTS NPHS11 TYR-157 AND ALA-831,
RP CHARACTERIZATION OF VARIANTS NPHS11 TYR-157 AND ALA-831, INTERACTION WITH
RP NUP133, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26411495; DOI=10.1016/j.ajhg.2015.08.013;
RA Miyake N., Tsukaguchi H., Koshimizu E., Shono A., Matsunaga S., Shiina M.,
RA Mimura Y., Imamura S., Hirose T., Okudela K., Nozu K., Akioka Y.,
RA Hattori M., Yoshikawa N., Kitamura A., Cheong H.I., Kagami S.,
RA Yamashita M., Fujita A., Miyatake S., Tsurusaki Y., Nakashima M.,
RA Saitsu H., Ohashi K., Imamoto N., Ryo A., Ogata K., Iijima K.,
RA Matsumoto N.;
RT "Biallelic mutations in nuclear pore complex subunit NUP107 cause early-
RT childhood-onset steroid-resistant nephrotic syndrome.";
RL Am. J. Hum. Genet. 97:555-566(2015).
RN [22]
RP INVOLVEMENT IN ODG6, AND VARIANT ODG6 ASN-447.
RX PubMed=26485283; DOI=10.1172/jci83553;
RA Weinberg-Shukron A., Renbaum P., Kalifa R., Zeligson S., Ben-Neriah Z.,
RA Dreifuss A., Abu-Rayyan A., Maatuk N., Fardian N., Rekler D., Kanaan M.,
RA Samson A.O., Levy-Lahad E., Gerlitz O., Zangen D.;
RT "A mutation in the nucleoporin-107 gene causes XX gonadal dysgenesis.";
RL J. Clin. Invest. 125:4295-4304(2015).
RN [23]
RP INVOLVEMENT IN GAMOS7, VARIANT GAMOS7 ILE-101, AND CHARACTERIZATION OF
RP VARIANT GAMOS7 ILE-101.
RX PubMed=28280135; DOI=10.1136/jmedgenet-2016-104237;
RA Rosti R.O., Sotak B.N., Bielas S.L., Bhat G., Silhavy J.L., Aslanger A.D.,
RA Altunoglu U., Bilge I., Tasdemir M., Yzaguirrem A.D., Musaev D.,
RA Infante S., Thuong W., Marin-Valencia I., Nelson S.F., Kayserili H.,
RA Gleeson J.G.;
RT "Homozygous mutation in NUP107 leads to microcephaly with steroid-resistant
RT nephrotic condition similar to Galloway-Mowat syndrome.";
RL J. Med. Genet. 54:399-403(2017).
RN [24]
RP INVOLVEMENT IN GAMOS7, AND VARIANTS GAMOS7 ILE-101 AND TYR-442.
RX PubMed=28117080; DOI=10.1016/j.kint.2016.10.013;
RA Bierzynska A., McCarthy H.J., Soderquest K., Sen E.S., Colby E., Ding W.Y.,
RA Nabhan M.M., Kerecuk L., Hegde S., Hughes D., Marks S., Feather S.,
RA Jones C., Webb N.J., Ognjanovic M., Christian M., Gilbert R.D., Sinha M.D.,
RA Lord G.M., Simpson M., Koziell A.B., Welsh G.I., Saleem M.A.;
RT "Genomic and clinical profiling of a national nephrotic syndrome cohort
RT advocates a precision medicine approach to disease management.";
RL Kidney Int. 91:937-947(2017).
RN [25]
RP FUNCTION, INTERACTION WITH NUP133, INVOLVEMENT IN GAMOS7, INVOLVEMENT IN
RP NPHS11, VARIANT GAMOS7 ILE-101, VARIANTS NPHS11 GLU-710 DEL AND CYS-889,
RP CHARACTERIZATION OF VARIANT GAMOS7 ILE-101, AND CHARACTERIZATION OF VARIANT
RP NPHS11 CYS-889.
RX PubMed=30179222; DOI=10.1172/jci98688;
RA Braun D.A., Lovric S., Schapiro D., Schneider R., Marquez J., Asif M.,
RA Hussain M.S., Daga A., Widmeier E., Rao J., Ashraf S., Tan W., Lusk C.P.,
RA Kolb A., Jobst-Schwan T., Schmidt J.M., Hoogstraten C.A., Eddy K.,
RA Kitzler T.M., Shril S., Moawia A., Schrage K., Khayyat A.I.A., Lawson J.A.,
RA Gee H.Y., Warejko J.K., Hermle T., Majmundar A.J., Hugo H., Budde B.,
RA Motameny S., Altmueller J., Noegel A.A., Fathy H.M., Gale D.P.,
RA Waseem S.S., Khan A., Kerecuk L., Hashmi S., Mohebbi N., Ettenger R.,
RA Serdaroglu E., Alhasan K.A., Hashem M., Goncalves S., Ariceta G.,
RA Ubetagoyena M., Antonin W., Baig S.M., Alkuraya F.S., Shen Q., Xu H.,
RA Antignac C., Lifton R.P., Mane S., Nuernberg P., Khokha M.K.,
RA Hildebrandt F.;
RT "Mutations in multiple components of the nuclear pore complex cause
RT nephrotic syndrome.";
RL J. Clin. Invest. 128:4313-4328(2018).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance (PubMed:12552102, PubMed:15229283, PubMed:30179222).
CC Required for the assembly of peripheral proteins into the NPC
CC (PubMed:15229283, PubMed:12552102). May anchor NUP62 to the NPC
CC (PubMed:15229283). Involved in nephrogenesis (PubMed:30179222).
CC {ECO:0000269|PubMed:12552102, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:30179222}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:11564755,
CC PubMed:12802065, PubMed:15229283, PubMed:26411495). Forms part of the
CC Nup160 subcomplex in the nuclear pore which is composed of NUP160,
CC NUP133, NUP107 and Nup96; this complex plays a role in RNA export and
CC in tethering Nup98 and NUP153 to the nucleus (PubMed:11564755,
CC PubMed:11684705, PubMed:26411495, PubMed:30179222). Does not interact
CC with TPR (PubMed:12802065). Interacts with ZNF106 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BH74, ECO:0000269|PubMed:11564755,
CC ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:26411495,
CC ECO:0000269|PubMed:30179222}.
CC -!- INTERACTION:
CC P57740; Q8WUM0: NUP133; NbExp=14; IntAct=EBI-295687, EBI-295695;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:11564755,
CC ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:26411495}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:26411495}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on
CC both the cytoplasmic and nuclear sides of the NPC core structure
CC (PubMed:11564755). During mitosis, localizes to the kinetochores
CC (PubMed:11564755). Dissociates from the dissasembled NPC structure late
CC during prophase of mitosis (PubMed:11564755).
CC {ECO:0000269|PubMed:11564755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P57740-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57740-2; Sequence=VSP_054263;
CC Name=3;
CC IsoId=P57740-3; Sequence=VSP_054262, VSP_054264;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues.
CC {ECO:0000269|PubMed:26411495}.
CC -!- DISEASE: Nephrotic syndrome 11 (NPHS11) [MIM:616730]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form and progress to end-stage renal failure. NPHS11
CC is an autosomal recessive, steroid-resistant and progressive form with
CC onset in the first decade of life. {ECO:0000269|PubMed:26411495,
CC ECO:0000269|PubMed:30179222}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Ovarian dysgenesis 6 (ODG6) [MIM:618078]: A form of ovarian
CC dysgenesis, a disorder characterized by lack of spontaneous pubertal
CC development, primary amenorrhea, uterine hypoplasia, and
CC hypergonadotropic hypogonadism as a result of streak gonads. ODG6 is an
CC autosomal recessive condition. {ECO:0000269|PubMed:26485283}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- DISEASE: Galloway-Mowat syndrome 7 (GAMOS7) [MIM:618348]: A form of
CC Galloway-Mowat syndrome, a severe renal-neurological disease
CC characterized by early-onset nephrotic syndrome associated with
CC microcephaly, central nervous system abnormalities, developmental
CC delays, and a propensity for seizures. Brain anomalies include gyration
CC defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC and cerebellar hypoplasia. Most patients show facial dysmorphism
CC characterized by a small, narrow forehead, large/floppy ears, deep-set
CC eyes, hypertelorism and micrognathia. Additional variable features are
CC visual impairment and arachnodactyly. Most patients die in early
CC childhood. GAMOS7 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:28117080, ECO:0000269|PubMed:28280135,
CC ECO:0000269|PubMed:30179222}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup84/Nup107 family.
CC {ECO:0000305}.
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DR EMBL; AJ295745; CAC03716.1; -; mRNA.
DR EMBL; AK302773; BAG63979.1; -; mRNA.
DR EMBL; AC090061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017167; AAH17167.1; -; mRNA.
DR EMBL; BC043343; AAH43343.1; -; mRNA.
DR CCDS; CCDS81712.1; -. [P57740-2]
DR CCDS; CCDS8985.1; -. [P57740-1]
DR RefSeq; NP_001317121.1; NM_001330192.1. [P57740-2]
DR RefSeq; NP_065134.1; NM_020401.3. [P57740-1]
DR PDB; 3CQC; X-ray; 2.53 A; A=658-925.
DR PDB; 3CQG; X-ray; 3.00 A; A=658-771, A=802-925.
DR PDB; 3I4R; X-ray; 3.53 A; A=658-925.
DR PDB; 5A9Q; EM; 23.00 A; 4/D/M/V=1-925.
DR PDB; 7PEQ; EM; 35.00 A; AD/BD/CD/DD=1-925.
DR PDBsum; 3CQC; -.
DR PDBsum; 3CQG; -.
DR PDBsum; 3I4R; -.
DR PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; P57740; -.
DR SMR; P57740; -.
DR BioGRID; 121386; 182.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; P57740; -.
DR IntAct; P57740; 103.
DR MINT; P57740; -.
DR STRING; 9606.ENSP00000229179; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; P57740; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P57740; -.
DR MetOSite; P57740; -.
DR PhosphoSitePlus; P57740; -.
DR SwissPalm; P57740; -.
DR BioMuta; NUP107; -.
DR DMDM; 12230339; -.
DR CPTAC; CPTAC-986; -.
DR EPD; P57740; -.
DR jPOST; P57740; -.
DR MassIVE; P57740; -.
DR MaxQB; P57740; -.
DR PaxDb; P57740; -.
DR PeptideAtlas; P57740; -.
DR PRIDE; P57740; -.
DR ProteomicsDB; 5575; -.
DR ProteomicsDB; 57028; -. [P57740-1]
DR ProteomicsDB; 67197; -.
DR Antibodypedia; 16892; 246 antibodies from 36 providers.
DR DNASU; 57122; -.
DR Ensembl; ENST00000229179.9; ENSP00000229179.4; ENSG00000111581.10. [P57740-1]
DR Ensembl; ENST00000378905.6; ENSP00000368185.2; ENSG00000111581.10. [P57740-3]
DR Ensembl; ENST00000539906.5; ENSP00000441448.1; ENSG00000111581.10. [P57740-2]
DR GeneID; 57122; -.
DR KEGG; hsa:57122; -.
DR MANE-Select; ENST00000229179.9; ENSP00000229179.4; NM_020401.4; NP_065134.1.
DR UCSC; uc001suf.4; human. [P57740-1]
DR CTD; 57122; -.
DR DisGeNET; 57122; -.
DR GeneCards; NUP107; -.
DR HGNC; HGNC:29914; NUP107.
DR HPA; ENSG00000111581; Low tissue specificity.
DR MalaCards; NUP107; -.
DR MIM; 607617; gene.
DR MIM; 616730; phenotype.
DR MIM; 618078; phenotype.
DR MIM; 618348; phenotype.
DR neXtProt; NX_P57740; -.
DR OpenTargets; ENSG00000111581; -.
DR Orphanet; 243; 46,XX gonadal dysgenesis.
DR Orphanet; 2065; Galloway-Mowat syndrome.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA134890486; -.
DR VEuPathDB; HostDB:ENSG00000111581; -.
DR eggNOG; KOG1964; Eukaryota.
DR GeneTree; ENSGT00390000012080; -.
DR HOGENOM; CLU_012944_1_0_1; -.
DR InParanoid; P57740; -.
DR OMA; MAHIVLF; -.
DR OrthoDB; 671846at2759; -.
DR PhylomeDB; P57740; -.
DR TreeFam; TF324259; -.
DR PathwayCommons; P57740; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P57740; -.
DR SIGNOR; P57740; -.
DR BioGRID-ORCS; 57122; 565 hits in 1089 CRISPR screens.
DR ChiTaRS; NUP107; human.
DR EvolutionaryTrace; P57740; -.
DR GeneWiki; NUP107; -.
DR GenomeRNAi; 57122; -.
DR Pharos; P57740; Tbio.
DR PRO; PR:P57740; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P57740; protein.
DR Bgee; ENSG00000111581; Expressed in secondary oocyte and 195 other tissues.
DR ExpressionAtlas; P57740; baseline and differential.
DR Genevisible; P57740; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IMP:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP: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 3D-structure; Acetylation; Alternative splicing; Centromere; Chromosome;
KW Disease variant; Epilepsy; Intellectual disability; Kinetochore; Membrane;
KW Methylation; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..925
FT /note="Nuclear pore complex protein Nup107"
FT /id="PRO_0000204831"
FT REGION 20..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BH74"
FT MOD_RES 60
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH74"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054262"
FT VAR_SEQ 1..63
FT /note="MDRSGFGEISSPVIREAEVTRTARKQSAQKRVLLQASQDENFGNTTPRNQVI
FT PRTPSSFRQPF -> MKILVILHQETRLSLELLAHFDSLVLSTNLLFIV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054263"
FT VAR_SEQ 579..666
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054264"
FT VARIANT 101
FT /note="M -> I (in GAMOS7; decreased function in
FT nephrogenesis; unable to fully rescue morpholino-induced
FT nephrogenesis defects in Xenopus; decreased protein amount
FT detected by Western blot in patient cells; affects exon 4
FT splicing resulting in decreased levels of wild-type mature
FT transcript; impairs assembly of nuclear pore complex;
FT dbSNP:rs730882216)"
FT /evidence="ECO:0000269|PubMed:28117080,
FT ECO:0000269|PubMed:28280135, ECO:0000269|PubMed:30179222"
FT /id="VAR_081356"
FT VARIANT 157
FT /note="D -> Y (in NPHS11; no effect on interaction with
FT NUP133; no effect on localization to the nuclear pore;
FT dbSNP:rs864321633)"
FT /evidence="ECO:0000269|PubMed:26411495"
FT /id="VAR_076358"
FT VARIANT 442
FT /note="C -> Y (in GAMOS7; unknown pathological
FT significance; dbSNP:rs745342141)"
FT /evidence="ECO:0000269|PubMed:28117080"
FT /id="VAR_082054"
FT VARIANT 447
FT /note="D -> N (in ODG6; dbSNP:rs1555178358)"
FT /evidence="ECO:0000269|PubMed:26485283"
FT /id="VAR_078571"
FT VARIANT 710
FT /note="Missing (in NPHS11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30179222"
FT /id="VAR_081357"
FT VARIANT 831
FT /note="D -> A (in NPHS11; decreased interaction with
FT NUP133; changed localization to the nuclear pore with
FT relocalization to the cytoplasm; dbSNP:rs864321632)"
FT /evidence="ECO:0000269|PubMed:26411495"
FT /id="VAR_076359"
FT VARIANT 889
FT /note="Y -> C (in NPHS11; decreased function in
FT nephrogenesis; unable to fully rescue morpholino-induced
FT nephrogenesis defects in Xenopus; decreased interaction
FT with NUP133; dbSNP:rs1565707103)"
FT /evidence="ECO:0000269|PubMed:30179222"
FT /id="VAR_081358"
FT CONFLICT 845
FT /note="Q -> R (in Ref. 4; AAH43343)"
FT /evidence="ECO:0000305"
FT HELIX 668..680
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 685..701
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 705..714
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 719..723
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 738..767
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 782..821
FT /evidence="ECO:0007829|PDB:3CQC"
FT TURN 824..826
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 840..867
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 871..875
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 877..882
FT /evidence="ECO:0007829|PDB:3CQC"
FT TURN 884..886
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 888..891
FT /evidence="ECO:0007829|PDB:3CQC"
FT HELIX 894..912
FT /evidence="ECO:0007829|PDB:3CQC"
FT TURN 913..915
FT /evidence="ECO:0007829|PDB:3CQC"
SQ SEQUENCE 925 AA; 106374 MW; CE1E4DA6C832A5A5 CRC64;
MDRSGFGEIS SPVIREAEVT RTARKQSAQK RVLLQASQDE NFGNTTPRNQ VIPRTPSSFR
QPFTPTSRSL LRQPDISCIL GTGGKSPRLT QSSGFFGNLS MVTNLDDSNW AAAFSSQRSG
LFTNTEPHSI TEDVTISAVM LREDDPGEAA SMSMFSDFLQ SFLKHSSSTV FDLVEEYENI
CGSQVNILSK IVSRATPGLQ KFSKTASMLW LLQQEMVTWR LLASLYRDRI QSALEEESVF
AVTAVNASEK TVVEALFQRD SLVRQSQLVV DWLESIAKDE IGEFSDNIEF YAKSVYWENT
LHTLKQRQLT SYVGSVRPLV TELDPDAPIR QKMPLDDLDR EDEVRLLKYL FTLIRAGMTE
EAQRLCKRCG QAWRAATLEG WKLYHDPNVN GGTELEPVEG NPYRRIWKIS CWRMAEDELF
NRYERAIYAA LSGNLKQLLP VCDTWEDTVW AYFRVMVDSL VEQEIQTSVA TLDETEELPR
EYLGANWTLE KVFEELQATD KKRVLEENQE HYHIVQKFLI LGDIDGLMDE FSKWLSKSRN
NLPGHLLRFM THLILFFRTL GLQTKEEVSI EVLKTYIQLL IREKHTNLIA FYTCHLPQDL
AVAQYALFLE SVTEFEQRHH CLELAKEADL DVATITKTVV ENIRKKDNGE FSHHDLAPAL
DTGTTEEDRL KIDVIDWLVF DPAQRAEALK QGNAIMRKFL ASKKHEAAKE VFVKIPQDSI
AEIYNQCEEQ GMESPLPAED DNAIREHLCI RAYLEAHETF NEWFKHMNSV PQKPALIPQP
TFTEKVAHEH KEKKYEMDFG IWKGHLDALT ADVKEKMYNV LLFVDGGWMV DVREDAKEDH
ERTHQMVLLR KLCLPMLCFL LHTILHSTGQ YQECLQLADM VSSERHKLYL VFSKEELRKL
LQKLRESSLM LLDQGLDPLG YEIQL
