NDC1_HUMAN
ID NDC1_HUMAN Reviewed; 674 AA.
AC Q9BTX1; B4DHA3; B4DQQ5; G3XA81; Q8NB76; Q9H9T6; Q9NSG3; Q9NSG4; Q9NVZ7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nucleoporin NDC1;
DE Short=hNDC1;
DE AltName: Full=Transmembrane protein 48;
GN Name=NDC1; Synonyms=TMEM48;
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), VARIANT ASP-154, FUNCTION,
RP SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RX PubMed=16702233; DOI=10.1083/jcb.200601001;
RA Stavru F., Hulsmann B.B., Spang A., Hartmann E., Cordes V.C., Gorlich D.;
RT "NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore
RT complexes.";
RL J. Cell Biol. 173:509-519(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-674 (ISOFORM 3).
RC TISSUE=Brain, and Teratocarcinoma;
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 MRNA] (ISOFORM 2).
RA Rhodes S., Huckle E.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-154.
RC 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12958361; DOI=10.1126/science.1088176;
RA Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.;
RT "Nuclear membrane proteins with potential disease links found by
RT subtractive proteomics.";
RL Science 301:1380-1382(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND PHOSPHORYLATION.
RX PubMed=16600873; DOI=10.1016/j.molcel.2006.02.015;
RA Mansfeld J., Guettinger S., Hawryluk-Gara L.A., Pante N., Mall M., Galy V.,
RA Haselmann U., Muehlhaeusser P., Wozniak R.W., Mattaj I.W., Kutay U.,
RA Antonin W.;
RT "The conserved transmembrane nucleoporin NDC1 is required for nuclear pore
RT complex assembly in vertebrate cells.";
RL Mol. Cell 22:93-103(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; THR-440; SER-445;
RP THR-449; SER-471 AND SER-474, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AAAS.
RX PubMed=19782045; DOI=10.1016/j.bbrc.2009.09.080;
RA Kind B., Koehler K., Lorenz M., Huebner A.;
RT "The nuclear pore complex protein ALADIN is anchored via NDC1 but not via
RT POM121 and GP210 in the nuclear envelope.";
RL Biochem. Biophys. Res. Commun. 390:205-210(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-414; SER-445;
RP SER-471 AND SER-474, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND THR-414, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), which plays a
CC key role in de novo assembly and insertion of NPC in the nuclear
CC envelope. Required for NPC and nuclear envelope assembly, possibly by
CC forming a link between the nuclear envelope membrane and soluble
CC nucleoporins, thereby anchoring the NPC in the membrane.
CC {ECO:0000269|PubMed:16600873, ECO:0000269|PubMed:16702233}.
CC -!- SUBUNIT: Interacts with the NUP35/NUP53 (By similarity). Interacts with
CC AAAS, anchoring it to the nuclear envelope.
CC {ECO:0000250|UniProtKB:Q6AXN4, ECO:0000269|PubMed:19782045}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane;
CC Multi-pass membrane protein. Note=Central core structure of the nuclear
CC pore complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9BTX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTX1-2; Sequence=VSP_018396;
CC Name=3;
CC IsoId=Q9BTX1-3; Sequence=VSP_018397;
CC Name=4;
CC IsoId=Q9BTX1-4; Sequence=VSP_018398, VSP_018399;
CC Name=5;
CC IsoId=Q9BTX1-5; Sequence=VSP_055332;
CC Name=6;
CC IsoId=Q9BTX1-6; Sequence=VSP_055331;
CC -!- MISCELLANEOUS: Depletion of NDC1 from HeLa cells interferes with the
CC assembly of phenylalanine-glycine (FG) repeat Nups into nuclear pore
CC complexes.
CC -!- SIMILARITY: Belongs to the NDC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ141696; AAZ73087.1; -; mRNA.
DR EMBL; AK001269; BAA91592.1; -; mRNA.
DR EMBL; AK022618; BAB14135.1; ALT_INIT; mRNA.
DR EMBL; AK091439; BAC03665.1; ALT_INIT; mRNA.
DR EMBL; AK298909; BAG61017.1; -; mRNA.
DR EMBL; AK295000; BAG58064.1; -; mRNA.
DR EMBL; AL354612; CAB89725.1; -; mRNA.
DR EMBL; AL354613; CAB89726.1; -; mRNA.
DR EMBL; AL049745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06731.1; -; Genomic_DNA.
DR EMBL; BC003082; AAH03082.1; -; mRNA.
DR CCDS; CCDS583.1; -. [Q9BTX1-1]
DR RefSeq; NP_001162023.1; NM_001168551.1. [Q9BTX1-5]
DR RefSeq; NP_060557.3; NM_018087.4. [Q9BTX1-1]
DR AlphaFoldDB; Q9BTX1; -.
DR BioGRID; 120831; 187.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q9BTX1; 52.
DR MINT; Q9BTX1; -.
DR STRING; 9606.ENSP00000360483; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9BTX1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BTX1; -.
DR PhosphoSitePlus; Q9BTX1; -.
DR SwissPalm; Q9BTX1; -.
DR BioMuta; NDC1; -.
DR DMDM; 97180263; -.
DR EPD; Q9BTX1; -.
DR jPOST; Q9BTX1; -.
DR MassIVE; Q9BTX1; -.
DR MaxQB; Q9BTX1; -.
DR PaxDb; Q9BTX1; -.
DR PeptideAtlas; Q9BTX1; -.
DR PRIDE; Q9BTX1; -.
DR ProteomicsDB; 33675; -.
DR ProteomicsDB; 79021; -. [Q9BTX1-1]
DR ProteomicsDB; 79022; -. [Q9BTX1-2]
DR ProteomicsDB; 79023; -. [Q9BTX1-3]
DR ProteomicsDB; 79024; -. [Q9BTX1-4]
DR Antibodypedia; 33093; 71 antibodies from 17 providers.
DR DNASU; 55706; -.
DR Ensembl; ENST00000371429.4; ENSP00000360483.3; ENSG00000058804.12. [Q9BTX1-1]
DR GeneID; 55706; -.
DR KEGG; hsa:55706; -.
DR MANE-Select; ENST00000371429.4; ENSP00000360483.3; NM_018087.5; NP_060557.3.
DR UCSC; uc001cvs.4; human. [Q9BTX1-1]
DR CTD; 55706; -.
DR DisGeNET; 55706; -.
DR GeneCards; NDC1; -.
DR HGNC; HGNC:25525; NDC1.
DR HPA; ENSG00000058804; Low tissue specificity.
DR MIM; 610115; gene.
DR neXtProt; NX_Q9BTX1; -.
DR OpenTargets; ENSG00000058804; -.
DR PharmGKB; PA142670764; -.
DR VEuPathDB; HostDB:ENSG00000058804; -.
DR eggNOG; KOG4358; Eukaryota.
DR GeneTree; ENSGT00390000014590; -.
DR HOGENOM; CLU_027343_0_0_1; -.
DR InParanoid; Q9BTX1; -.
DR OMA; MIYSWIQ; -.
DR OrthoDB; 556184at2759; -.
DR PhylomeDB; Q9BTX1; -.
DR TreeFam; TF324843; -.
DR PathwayCommons; Q9BTX1; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
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-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-6784531; tRNA processing in the nucleus.
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-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q9BTX1; -.
DR SIGNOR; Q9BTX1; -.
DR BioGRID-ORCS; 55706; 442 hits in 1052 CRISPR screens.
DR ChiTaRS; NDC1; human.
DR GeneWiki; TMEM48; -.
DR GenomeRNAi; 55706; -.
DR Pharos; Q9BTX1; Tbio.
DR PRO; PR:Q9BTX1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BTX1; protein.
DR Bgee; ENSG00000058804; Expressed in secondary oocyte and 186 other tissues.
DR Genevisible; Q9BTX1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; 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:HPA.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
DR GO; GO:0051664; P:nuclear pore localization; IMP:UniProtKB.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR019049; Nucleoporin_prot_Ndc1/Nup.
DR PANTHER; PTHR13269; PTHR13269; 1.
DR Pfam; PF09531; Ndc1_Nup; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..674
FT /note="Nucleoporin NDC1"
FT /id="PRO_0000235240"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..68
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..165
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..272
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 394..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055331"
FT VAR_SEQ 93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_018396"
FT VAR_SEQ 95..135
FT /note="VPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVI -> I (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055332"
FT VAR_SEQ 376..492
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018397"
FT VAR_SEQ 509..542
FT /note="GKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYF -> APRGLHSGCFFRCP
FT NAYLGIRRSVALSSSIIYRG (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_018398"
FT VAR_SEQ 543..674
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_018399"
FT VARIANT 154
FT /note="G -> D (in dbSNP:rs17849721)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16702233"
FT /id="VAR_026388"
FT CONFLICT 261
FT /note="V -> A (in Ref. 2; BAG58064)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="Q -> R (in Ref. 2; BAG58064)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="K -> R (in Ref. 2; BAG61017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 674 AA; 76305 MW; 78368FEB232895D9 CRC64;
MATAVSRPCA GRSRDILWRV LGWRIVASIV WSVLFLPICT TVFIIFSRID LFHPIQWLSD
SFSDLYSSYV IFYFLLLSVV IIIISIFNVE FYAVVPSIPC SRLALIGKII HPQQLMHSFI
HAAMGMVMAW CAAVITQGQY SFLVVPCTGT NSFGSPAAQT CLNEYHLFFL LTGAFMGYSY
SLLYFVNNMN YLPFPIIQQY KFLRFRRSLL LLVKHSCVES LFLVRNFCIL YYFLGYIPKA
WISTAMNLHI DEQVHRPLDT VSGLLNLSLL YHVWLCGVFL LTTWYVSWIL FKIYATEAHV
FPVQPPFAEG SDECLPKVLN SNPPPIIKYL ALQDLMLLSQ YSPSRRQEVF SLSQPGGHPH
NWTAISRECL NLLNGMTQKL ILYQEAAATN GRVSSSYPVE PKKLNSPEET AFQTPKSSQM
PRPSVPPLVK TSLFSSKLST PDVVSPFGTP FGSSVMNRMA GIFDVNTCYG SPQSPQLIRR
GPRLWTSASD QQMTEFSNPS PSTSISAEGK TMRQPSVIYS WIQNKREQIK NFLSKRVLIM
YFFSKHPEAS IQAVFSDAQM HIWALEGLSH LVAASFTEDR FGVVQTTLPA ILNTLLTLQE
AVDKYFKLPH ASSKPPRISG SLVDTSYKTL RFAFRASLKT AIYRITTTFG EHLNAVQASA
EHQKRLQQFL EFKE
