NSF1C_HUMAN
ID NSF1C_HUMAN Reviewed; 370 AA.
AC Q9UNZ2; A2A2L1; B2RD74; Q5JXA4; Q5JXA5; Q7Z533; Q9H102; Q9NVL9; Q9UI06;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=NSFL1 cofactor p47;
DE AltName: Full=UBX domain-containing protein 2C;
DE AltName: Full=p97 cofactor p47;
GN Name=NSFL1C; Synonyms=UBXN2C;
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 3).
RA Yue P., Yu L., Zhou Y., Zhao Y., Yang Y.M., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to R.norvegicus p47 mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-290.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP PROTEIN SEQUENCE OF 11-22; 77-93; 114-124; 157-172; 189-214; 260-301 AND
RP 357-368, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-272, AND
RP IDENTIFICATION BY MASS 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-272, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-272, AND
RP IDENTIFICATION BY MASS 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP FUNCTION.
RX PubMed=23649807; DOI=10.1083/jcb.201209107;
RA Kress E., Schwager F., Holtackers R., Seiler J., Prodon F., Zanin E.,
RA Eiteneuer A., Toya M., Sugimoto A., Meyer H., Meraldi P., Gotta M.;
RT "The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the
RT centrosomal recruitment of Aurora A.";
RL J. Cell Biol. 201:559-575(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-102; SER-114;
RP SER-140; SER-192 AND SER-272, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP 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 [21]
RP STRUCTURE BY NMR OF 171-270, AND FUNCTION.
RX PubMed=15498563; DOI=10.1016/j.febslet.2004.09.037;
RA Soukenik M., Diehl A., Leidert M., Sievert V., Buessow K., Leitner D.,
RA Labudde D., Ball L.J., Lechner A., Naegler D.K., Oschkinat H.;
RT "The SEP domain of p47 acts as a reversible competitive inhibitor of
RT cathepsin L.";
RL FEBS Lett. 576:358-362(2004).
CC -!- FUNCTION: Reduces the ATPase activity of VCP (By similarity). Necessary
CC for the fragmentation of Golgi stacks during mitosis and for VCP-
CC mediated reassembly of Golgi stacks after mitosis (By similarity). May
CC play a role in VCP-mediated formation of transitional endoplasmic
CC reticulum (tER) (By similarity). Inhibits the activity of CTSL (in
CC vitro) (PubMed:15498563). Together with UBXN2B/p37, regulates the
CC centrosomal levels of kinase AURKA/Aurora A during mitotic progression
CC by promoting AURKA removal from centrosomes in prophase
CC (PubMed:23649807). Also, regulates spindle orientation during mitosis
CC (PubMed:23649807). {ECO:0000250|UniProtKB:O35987,
CC ECO:0000269|PubMed:15498563, ECO:0000269|PubMed:23649807}.
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP.
CC NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer.
CC The complex binds to membranes enriched in phosphatidylethanolamine-
CC containing lipids and promotes Golgi membrane fusion. Interaction with
CC VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP.
CC Binds ubiquitin and mono-ubiquitinated proteins via its N-terminal UBA-
CC like domain when bound to VCP (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UNZ2; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-721577, EBI-10175326;
CC Q9UNZ2; Q13148: TARDBP; NbExp=4; IntAct=EBI-721577, EBI-372899;
CC Q9UNZ2; P55072: VCP; NbExp=20; IntAct=EBI-721577, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35987}. Golgi
CC apparatus, Golgi stack {ECO:0000250|UniProtKB:O35987}. Chromosome
CC {ECO:0000250|UniProtKB:O35987}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O35987}.
CC Note=Predominantly nuclear in interphase cells. Bound to the axial
CC elements of sex chromosomes in pachytene spermatocytes. A small
CC proportion of the protein is cytoplasmic, associated with Golgi stacks.
CC Localizes to centrosome during mitotic prophase and metaphase.
CC {ECO:0000250|UniProtKB:O35987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UNZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNZ2-4; Sequence=VSP_009263;
CC Name=3;
CC IsoId=Q9UNZ2-5; Sequence=VSP_009262;
CC Name=4;
CC IsoId=Q9UNZ2-6; Sequence=VSP_041062;
CC -!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
CC interaction with Golgi membranes and is required for the fragmentation
CC of the Golgi stacks during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17199.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF17199.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF086909; AAP97139.1; -; mRNA.
DR EMBL; AF112211; AAF17199.1; ALT_SEQ; mRNA.
DR EMBL; AF078856; AAD44488.1; -; mRNA.
DR EMBL; AK297403; BAG59842.1; -; mRNA.
DR EMBL; AK001511; BAA91731.1; -; mRNA.
DR EMBL; AK315433; BAG37821.1; -; mRNA.
DR EMBL; AL109658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10629.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10631.1; -; Genomic_DNA.
DR EMBL; BC002801; AAH02801.1; -; mRNA.
DR CCDS; CCDS13015.1; -. [Q9UNZ2-1]
DR CCDS; CCDS13016.1; -. [Q9UNZ2-4]
DR CCDS; CCDS56175.1; -. [Q9UNZ2-5]
DR RefSeq; NP_001193665.1; NM_001206736.1. [Q9UNZ2-5]
DR RefSeq; NP_057227.2; NM_016143.4. [Q9UNZ2-1]
DR RefSeq; NP_061327.2; NM_018839.4. [Q9UNZ2-4]
DR RefSeq; XP_006723657.1; XM_006723594.2. [Q9UNZ2-6]
DR PDB; 1SS6; NMR; -; A=171-270.
DR PDBsum; 1SS6; -.
DR AlphaFoldDB; Q9UNZ2; -.
DR BMRB; Q9UNZ2; -.
DR SMR; Q9UNZ2; -.
DR BioGRID; 121014; 140.
DR ComplexPortal; CPX-262; NSFL1C-VCP complex.
DR DIP; DIP-39611N; -.
DR IntAct; Q9UNZ2; 34.
DR MINT; Q9UNZ2; -.
DR STRING; 9606.ENSP00000418529; -.
DR iPTMnet; Q9UNZ2; -.
DR MetOSite; Q9UNZ2; -.
DR PhosphoSitePlus; Q9UNZ2; -.
DR BioMuta; NSFL1C; -.
DR DMDM; 41017512; -.
DR REPRODUCTION-2DPAGE; IPI00100197; -.
DR CPTAC; CPTAC-101; -.
DR CPTAC; CPTAC-102; -.
DR EPD; Q9UNZ2; -.
DR jPOST; Q9UNZ2; -.
DR MassIVE; Q9UNZ2; -.
DR MaxQB; Q9UNZ2; -.
DR PaxDb; Q9UNZ2; -.
DR PeptideAtlas; Q9UNZ2; -.
DR PRIDE; Q9UNZ2; -.
DR ProteomicsDB; 85346; -. [Q9UNZ2-1]
DR ProteomicsDB; 85347; -. [Q9UNZ2-4]
DR ProteomicsDB; 85348; -. [Q9UNZ2-5]
DR ProteomicsDB; 85349; -. [Q9UNZ2-6]
DR TopDownProteomics; Q9UNZ2-1; -. [Q9UNZ2-1]
DR TopDownProteomics; Q9UNZ2-4; -. [Q9UNZ2-4]
DR TopDownProteomics; Q9UNZ2-5; -. [Q9UNZ2-5]
DR Antibodypedia; 23083; 110 antibodies from 27 providers.
DR DNASU; 55968; -.
DR Ensembl; ENST00000216879.9; ENSP00000216879.4; ENSG00000088833.18. [Q9UNZ2-1]
DR Ensembl; ENST00000353088.6; ENSP00000338643.2; ENSG00000088833.18. [Q9UNZ2-4]
DR Ensembl; ENST00000476071.5; ENSP00000418529.1; ENSG00000088833.18. [Q9UNZ2-5]
DR GeneID; 55968; -.
DR KEGG; hsa:55968; -.
DR MANE-Select; ENST00000216879.9; ENSP00000216879.4; NM_016143.5; NP_057227.2.
DR UCSC; uc002wfc.3; human. [Q9UNZ2-1]
DR CTD; 55968; -.
DR DisGeNET; 55968; -.
DR GeneCards; NSFL1C; -.
DR HGNC; HGNC:15912; NSFL1C.
DR HPA; ENSG00000088833; Low tissue specificity.
DR MIM; 606610; gene.
DR neXtProt; NX_Q9UNZ2; -.
DR OpenTargets; ENSG00000088833; -.
DR PharmGKB; PA31794; -.
DR VEuPathDB; HostDB:ENSG00000088833; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_029402_0_0_1; -.
DR InParanoid; Q9UNZ2; -.
DR OMA; EHQAFYA; -.
DR OrthoDB; 1175850at2759; -.
DR PhylomeDB; Q9UNZ2; -.
DR TreeFam; TF312973; -.
DR PathwayCommons; Q9UNZ2; -.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR SignaLink; Q9UNZ2; -.
DR SIGNOR; Q9UNZ2; -.
DR BioGRID-ORCS; 55968; 50 hits in 1084 CRISPR screens.
DR ChiTaRS; NSFL1C; human.
DR EvolutionaryTrace; Q9UNZ2; -.
DR GeneWiki; NSFL1C; -.
DR GenomeRNAi; 55968; -.
DR Pharos; Q9UNZ2; Tbio.
DR PRO; PR:Q9UNZ2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UNZ2; protein.
DR Bgee; ENSG00000088833; Expressed in right adrenal gland and 210 other tissues.
DR ExpressionAtlas; Q9UNZ2; baseline and differential.
DR Genevisible; Q9UNZ2; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990730; C:VCP-NSFL1C complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; IGI:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IGI:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.420.210; -; 1.
DR InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00553; SEP; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF102848; SSF102848; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; Lipid-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="NSFL1 cofactor p47"
FT /id="PRO_0000210988"
FT DOMAIN 179..244
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 291..368
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 54..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..115
FT /note="Nuclear localization signal"
FT MOTIF 172..175
FT /note="Nuclear localization signal"
FT COMPBIAS 54..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ44"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ44"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..124
FT /note="MAAERQEALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVT
FT ISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEDEEEEEGQRFYAGGSERSGQQIVGPPR
FT KKSPNELVDDLFK -> MTKMKMRRKRKAR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041062"
FT VAR_SEQ 93
FT /note="R -> RSR (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_009262"
FT VAR_SEQ 149..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009263"
FT VARIANT 290
FT /note="D -> N (in dbSNP:rs9575)"
FT /evidence="ECO:0000269|PubMed:11042152"
FT /id="VAR_017481"
FT CONFLICT 39..40
FT /note="AS -> EL (in Ref. 1; AAP97139)"
FT /evidence="ECO:0000305"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1SS6"
FT STRAND 180..193
FT /evidence="ECO:0007829|PDB:1SS6"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1SS6"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1SS6"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:1SS6"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1SS6"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1SS6"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:1SS6"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1SS6"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1SS6"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1SS6"
SQ SEQUENCE 370 AA; 40573 MW; 79364617F940B9F9 CRC64;
MAAERQEALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
VSRGTAPSDN RVTSFRDLIH DQDEDEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
DLFKGAKEHG AVAVERVTKS PGETSKPRPF AGGGYRLGAA PEEESAYVAG EKRQHSSQDV
HVVLKLWKSG FSLDNGELRS YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD
EDFVKPKGAF KAFTGEGQKL GSTAPQVLST SSPAQQAENE AKASSSILID ESEPTTNIQI
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFILM TTFPNKELAD ESQTLKEANL
LNAVIVQRLT
