Full text data of NSFL1C
NSFL1C
(UBXN2C)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
NSFL1 cofactor p47 (UBX domain-containing protein 2C; p97 cofactor p47)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
NSFL1 cofactor p47 (UBX domain-containing protein 2C; p97 cofactor p47)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00022830
IPI00022830 Similar to DJ776F14.1 CD34+ hematopoietic stem/progenitor cells, reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic and nuclear n/a expected molecular weight found in band found in band around 62 kdDa
IPI00022830 Similar to DJ776F14.1 CD34+ hematopoietic stem/progenitor cells, reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic and nuclear n/a expected molecular weight found in band found in band around 62 kdDa
UniProt
Q9UNZ2
ID NSF1C_HUMAN Reviewed; 370 AA.
AC Q9UNZ2; A2A2L1; B2RD74; Q5JXA4; Q5JXA5; Q7Z533; Q9H102; Q9NVL9;
read moreAC Q9UI06;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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
RP 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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP AND 357-368, AND 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP STRUCTURE BY NMR OF 171-270, AND INTERACTION WITH CTSL.
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. Necessary for the
CC fragmentation of Golgi stacks during mitosis and for VCP-mediated
CC reassembly of Golgi stacks after mitosis. May play a role in VCP-
CC mediated formation of transitional endoplasmic reticulum (tER) (By
CC similarity). Inhibits the activity of CTSL (in vitro).
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and
CC VCP. NSFL1C forms a homotrimer that binds to one end of a VCP
CC homohexamer. The complex binds to membranes enriched in
CC phosphatidylethanolamine-containing lipids and promotes Golgi
CC membrane fusion. Interaction with VCIP135 leads to dissociation of
CC the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-
CC ubiquitinated proteins via its N-terminal UBA-like domain when
CC bound to VCP (By similarity).
CC -!- INTERACTION:
CC P55072:VCP; NbExp=4; IntAct=EBI-721577, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Golgi apparatus,
CC Golgi stack (By similarity). Chromosome (By similarity).
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
CC stacks (By similarity).
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 Note=No experimental confirmation available;
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
CC fragmentation of the Golgi stacks during mitosis (By similarity).
CC -!- SIMILARITY: Belongs to the NSFL1C family.
CC -!- SIMILARITY: Contains 1 SEP domain.
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17199.1; Type=Frameshift; Positions=Several;
CC Sequence=AAF17199.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
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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; CAB96827.1; -; Genomic_DNA.
DR EMBL; AL109658; CAI22730.1; -; Genomic_DNA.
DR EMBL; AL109658; CAI22731.1; -; Genomic_DNA.
DR EMBL; AL109658; CAM28306.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10629.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10631.1; -; Genomic_DNA.
DR EMBL; BC002801; AAH02801.1; -; mRNA.
DR RefSeq; NP_001193665.1; NM_001206736.1.
DR RefSeq; NP_057227.2; NM_016143.4.
DR RefSeq; NP_061327.2; NM_018839.4.
DR UniGene; Hs.12865; -.
DR PDB; 1SS6; NMR; -; A=171-270.
DR PDBsum; 1SS6; -.
DR ProteinModelPortal; Q9UNZ2; -.
DR SMR; Q9UNZ2; 1-46, 171-370.
DR DIP; DIP-39611N; -.
DR IntAct; Q9UNZ2; 14.
DR MINT; MINT-3083194; -.
DR STRING; 9606.ENSP00000216879; -.
DR PhosphoSite; Q9UNZ2; -.
DR DMDM; 41017512; -.
DR REPRODUCTION-2DPAGE; IPI00100197; -.
DR PaxDb; Q9UNZ2; -.
DR PRIDE; Q9UNZ2; -.
DR DNASU; 55968; -.
DR Ensembl; ENST00000216879; ENSP00000216879; ENSG00000088833.
DR Ensembl; ENST00000353088; ENSP00000338643; ENSG00000088833.
DR Ensembl; ENST00000381658; ENSP00000371074; ENSG00000088833.
DR Ensembl; ENST00000476071; ENSP00000418529; ENSG00000088833.
DR GeneID; 55968; -.
DR KEGG; hsa:55968; -.
DR UCSC; uc002wfc.3; human.
DR CTD; 55968; -.
DR GeneCards; GC20M001422; -.
DR HGNC; HGNC:15912; NSFL1C.
DR HPA; HPA047105; -.
DR HPA; HPA047108; -.
DR HPA; HPA050628; -.
DR MIM; 606610; gene.
DR neXtProt; NX_Q9UNZ2; -.
DR PharmGKB; PA31794; -.
DR eggNOG; NOG252689; -.
DR HOVERGEN; HBG054517; -.
DR KO; K14012; -.
DR OMA; FNHTHRV; -.
DR OrthoDB; EOG7ZKSBB; -.
DR PhylomeDB; Q9UNZ2; -.
DR EvolutionaryTrace; Q9UNZ2; -.
DR GeneWiki; NSFL1C; -.
DR GenomeRNAi; 55968; -.
DR NextBio; 61389; -.
DR PRO; PR:Q9UNZ2; -.
DR ArrayExpress; Q9UNZ2; -.
DR Bgee; Q9UNZ2; -.
DR CleanEx; HS_NSFL1C; -.
DR Genevestigator; Q9UNZ2; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR001012; UBX.
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 PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Complete proteome;
KW Direct protein sequencing; Golgi apparatus; Lipid-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 370 NSFL1 cofactor p47.
FT /FTId=PRO_0000210988.
FT DOMAIN 179 244 SEP.
FT DOMAIN 291 368 UBX.
FT MOTIF 109 115 Nuclear localization signal.
FT MOTIF 172 175 Nuclear localization signal.
FT COMPBIAS 84 90 Poly-Glu.
FT MOD_RES 114 114 Phosphoserine.
FT MOD_RES 140 140 Phosphoserine.
FT MOD_RES 167 167 Phosphotyrosine (By similarity).
FT MOD_RES 176 176 Phosphoserine (By similarity).
FT MOD_RES 272 272 Phosphoserine.
FT VAR_SEQ 1 124 MAAERQEALREFVAVTGAEEDRARFFLESAGWDLQIALASF
FT YEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQ
FT DEDEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLF
FT K -> MTKMKMRRKRKAR (in isoform 4).
FT /FTId=VSP_041062.
FT VAR_SEQ 93 93 R -> RSR (in isoform 3).
FT /FTId=VSP_009262.
FT VAR_SEQ 149 179 Missing (in isoform 2).
FT /FTId=VSP_009263.
FT VARIANT 290 290 D -> N (in dbSNP:rs9575).
FT /FTId=VAR_017481.
FT CONFLICT 39 40 AS -> EL (in Ref. 1; AAP97139).
FT STRAND 171 173
FT STRAND 180 193
FT STRAND 198 200
FT TURN 204 206
FT HELIX 207 215
FT HELIX 220 223
FT STRAND 231 239
FT STRAND 245 250
FT STRAND 255 259
FT HELIX 260 262
FT STRAND 265 268
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
//
ID NSF1C_HUMAN Reviewed; 370 AA.
AC Q9UNZ2; A2A2L1; B2RD74; Q5JXA4; Q5JXA5; Q7Z533; Q9H102; Q9NVL9;
read moreAC Q9UI06;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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
RP 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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP AND 357-368, AND 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP STRUCTURE BY NMR OF 171-270, AND INTERACTION WITH CTSL.
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. Necessary for the
CC fragmentation of Golgi stacks during mitosis and for VCP-mediated
CC reassembly of Golgi stacks after mitosis. May play a role in VCP-
CC mediated formation of transitional endoplasmic reticulum (tER) (By
CC similarity). Inhibits the activity of CTSL (in vitro).
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and
CC VCP. NSFL1C forms a homotrimer that binds to one end of a VCP
CC homohexamer. The complex binds to membranes enriched in
CC phosphatidylethanolamine-containing lipids and promotes Golgi
CC membrane fusion. Interaction with VCIP135 leads to dissociation of
CC the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-
CC ubiquitinated proteins via its N-terminal UBA-like domain when
CC bound to VCP (By similarity).
CC -!- INTERACTION:
CC P55072:VCP; NbExp=4; IntAct=EBI-721577, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Golgi apparatus,
CC Golgi stack (By similarity). Chromosome (By similarity).
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
CC stacks (By similarity).
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 Note=No experimental confirmation available;
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
CC fragmentation of the Golgi stacks during mitosis (By similarity).
CC -!- SIMILARITY: Belongs to the NSFL1C family.
CC -!- SIMILARITY: Contains 1 SEP domain.
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17199.1; Type=Frameshift; Positions=Several;
CC Sequence=AAF17199.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
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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; CAB96827.1; -; Genomic_DNA.
DR EMBL; AL109658; CAI22730.1; -; Genomic_DNA.
DR EMBL; AL109658; CAI22731.1; -; Genomic_DNA.
DR EMBL; AL109658; CAM28306.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10629.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10631.1; -; Genomic_DNA.
DR EMBL; BC002801; AAH02801.1; -; mRNA.
DR RefSeq; NP_001193665.1; NM_001206736.1.
DR RefSeq; NP_057227.2; NM_016143.4.
DR RefSeq; NP_061327.2; NM_018839.4.
DR UniGene; Hs.12865; -.
DR PDB; 1SS6; NMR; -; A=171-270.
DR PDBsum; 1SS6; -.
DR ProteinModelPortal; Q9UNZ2; -.
DR SMR; Q9UNZ2; 1-46, 171-370.
DR DIP; DIP-39611N; -.
DR IntAct; Q9UNZ2; 14.
DR MINT; MINT-3083194; -.
DR STRING; 9606.ENSP00000216879; -.
DR PhosphoSite; Q9UNZ2; -.
DR DMDM; 41017512; -.
DR REPRODUCTION-2DPAGE; IPI00100197; -.
DR PaxDb; Q9UNZ2; -.
DR PRIDE; Q9UNZ2; -.
DR DNASU; 55968; -.
DR Ensembl; ENST00000216879; ENSP00000216879; ENSG00000088833.
DR Ensembl; ENST00000353088; ENSP00000338643; ENSG00000088833.
DR Ensembl; ENST00000381658; ENSP00000371074; ENSG00000088833.
DR Ensembl; ENST00000476071; ENSP00000418529; ENSG00000088833.
DR GeneID; 55968; -.
DR KEGG; hsa:55968; -.
DR UCSC; uc002wfc.3; human.
DR CTD; 55968; -.
DR GeneCards; GC20M001422; -.
DR HGNC; HGNC:15912; NSFL1C.
DR HPA; HPA047105; -.
DR HPA; HPA047108; -.
DR HPA; HPA050628; -.
DR MIM; 606610; gene.
DR neXtProt; NX_Q9UNZ2; -.
DR PharmGKB; PA31794; -.
DR eggNOG; NOG252689; -.
DR HOVERGEN; HBG054517; -.
DR KO; K14012; -.
DR OMA; FNHTHRV; -.
DR OrthoDB; EOG7ZKSBB; -.
DR PhylomeDB; Q9UNZ2; -.
DR EvolutionaryTrace; Q9UNZ2; -.
DR GeneWiki; NSFL1C; -.
DR GenomeRNAi; 55968; -.
DR NextBio; 61389; -.
DR PRO; PR:Q9UNZ2; -.
DR ArrayExpress; Q9UNZ2; -.
DR Bgee; Q9UNZ2; -.
DR CleanEx; HS_NSFL1C; -.
DR Genevestigator; Q9UNZ2; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR001012; UBX.
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 PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Complete proteome;
KW Direct protein sequencing; Golgi apparatus; Lipid-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 370 NSFL1 cofactor p47.
FT /FTId=PRO_0000210988.
FT DOMAIN 179 244 SEP.
FT DOMAIN 291 368 UBX.
FT MOTIF 109 115 Nuclear localization signal.
FT MOTIF 172 175 Nuclear localization signal.
FT COMPBIAS 84 90 Poly-Glu.
FT MOD_RES 114 114 Phosphoserine.
FT MOD_RES 140 140 Phosphoserine.
FT MOD_RES 167 167 Phosphotyrosine (By similarity).
FT MOD_RES 176 176 Phosphoserine (By similarity).
FT MOD_RES 272 272 Phosphoserine.
FT VAR_SEQ 1 124 MAAERQEALREFVAVTGAEEDRARFFLESAGWDLQIALASF
FT YEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQ
FT DEDEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLF
FT K -> MTKMKMRRKRKAR (in isoform 4).
FT /FTId=VSP_041062.
FT VAR_SEQ 93 93 R -> RSR (in isoform 3).
FT /FTId=VSP_009262.
FT VAR_SEQ 149 179 Missing (in isoform 2).
FT /FTId=VSP_009263.
FT VARIANT 290 290 D -> N (in dbSNP:rs9575).
FT /FTId=VAR_017481.
FT CONFLICT 39 40 AS -> EL (in Ref. 1; AAP97139).
FT STRAND 171 173
FT STRAND 180 193
FT STRAND 198 200
FT TURN 204 206
FT HELIX 207 215
FT HELIX 220 223
FT STRAND 231 239
FT STRAND 245 250
FT STRAND 255 259
FT HELIX 260 262
FT STRAND 265 268
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
//
MIM
606610
*RECORD*
*FIELD* NO
606610
*FIELD* TI
*606610 NSFL1 COFACTOR; NSFL1C
;;p47
*FIELD* TX
CLONING
The ATPases NSF (601633) and p97 (VCP; 601023) are involved in the
read moreheterotypic fusion of transport vesicles with their target membranes and
the homotypic fusion of membrane compartments. By biochemical
purification of a 47-kD protein complexed with p97 in rat liver cytosol,
followed by micropeptide sequence analysis and PCR with degenerate
primers, Kondo et al. (1997) isolated a cDNA encoding rat p47. Rat p47
binds specifically to p97. Northern blot analysis revealed ubiquitous
expression of a 1.5-kb p47 transcript in rat tissues. Kondo et al.
(1997) also identified a human EST with approximately 89% sequence
identity to rat p47. They concluded that the p97/p47 complex is probably
the active component in the fusion reaction that leads to cisternal
regrowth.
Zhang et al. (2000) screened CD34 (142230)-positive hemopoietic
stem/progenitor cells for novel cDNAs and obtained a human homolog of
p47. The deduced human p47 protein has 370 amino acids. Northern blot
and macroarray analyses revealed abundant and ubiquitous expression of
p47.
GENE STRUCTURE
Zhang et al. (2000) determined that human p47 is encoded by a single
exon.
MAPPING
Zhang et al. (2000) mapped the p47 gene to the distal end of chromosome
20p by STS analysis.
*FIELD* RF
1. Kondo, H.; Rabouille, C.; Newman, R.; Levine, T. P.; Pappin, D.;
Freemont, P.; Warren, G.: p47 is a cofactor for p97-mediated membrane
fusion. Nature 388: 75-78, 1997.
2. Zhang, Q.-H.; Ye, M.; Wu, X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CD
Paul J. Converse: 1/14/2002
*FIELD* ED
mgross: 01/04/2007
mgross: 1/14/2002
*RECORD*
*FIELD* NO
606610
*FIELD* TI
*606610 NSFL1 COFACTOR; NSFL1C
;;p47
*FIELD* TX
CLONING
The ATPases NSF (601633) and p97 (VCP; 601023) are involved in the
read moreheterotypic fusion of transport vesicles with their target membranes and
the homotypic fusion of membrane compartments. By biochemical
purification of a 47-kD protein complexed with p97 in rat liver cytosol,
followed by micropeptide sequence analysis and PCR with degenerate
primers, Kondo et al. (1997) isolated a cDNA encoding rat p47. Rat p47
binds specifically to p97. Northern blot analysis revealed ubiquitous
expression of a 1.5-kb p47 transcript in rat tissues. Kondo et al.
(1997) also identified a human EST with approximately 89% sequence
identity to rat p47. They concluded that the p97/p47 complex is probably
the active component in the fusion reaction that leads to cisternal
regrowth.
Zhang et al. (2000) screened CD34 (142230)-positive hemopoietic
stem/progenitor cells for novel cDNAs and obtained a human homolog of
p47. The deduced human p47 protein has 370 amino acids. Northern blot
and macroarray analyses revealed abundant and ubiquitous expression of
p47.
GENE STRUCTURE
Zhang et al. (2000) determined that human p47 is encoded by a single
exon.
MAPPING
Zhang et al. (2000) mapped the p47 gene to the distal end of chromosome
20p by STS analysis.
*FIELD* RF
1. Kondo, H.; Rabouille, C.; Newman, R.; Levine, T. P.; Pappin, D.;
Freemont, P.; Warren, G.: p47 is a cofactor for p97-mediated membrane
fusion. Nature 388: 75-78, 1997.
2. Zhang, Q.-H.; Ye, M.; Wu, X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CD
Paul J. Converse: 1/14/2002
*FIELD* ED
mgross: 01/04/2007
mgross: 1/14/2002