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NSFL1 cofactor p47 (UBX domain-containing protein 2C) (p97 cofactor p47)

 NSF1C_HUMAN             Reviewed;         370 AA.
Q9UNZ2; A2A2L1; B2RD74; Q5JXA4; Q5JXA5; Q7Z533; Q9H102; Q9NVL9;
Q9UI06;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
25-OCT-2017, entry version 161.
RecName: Full=NSFL1 cofactor p47;
AltName: Full=UBX domain-containing protein 2C;
AltName: Full=p97 cofactor p47;
Name=NSFL1C; Synonyms=UBXN2C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Yue P., Yu L., Zhou Y., Zhao Y., Yang Y.M., Zhao S.Y.;
"Cloning of a novel human cDNA homology to R.norvegicus p47 mRNA.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-290.
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
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., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 11-22; 77-93; 114-124; 157-172; 189-214; 260-301
AND 357-368, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-272, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-272, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-272, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-102; SER-114;
SER-140; SER-192 AND SER-272, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
STRUCTURE BY NMR OF 171-270, AND INTERACTION WITH CTSL.
PubMed=15498563; DOI=10.1016/j.febslet.2004.09.037;
Soukenik M., Diehl A., Leidert M., Sievert V., Buessow K., Leitner D.,
Labudde D., Ball L.J., Lechner A., Naegler D.K., Oschkinat H.;
"The SEP domain of p47 acts as a reversible competitive inhibitor of
cathepsin L.";
FEBS Lett. 576:358-362(2004).
-!- FUNCTION: Reduces the ATPase activity of VCP. Necessary for the
fragmentation of Golgi stacks during mitosis and for VCP-mediated
reassembly of Golgi stacks after mitosis. May play a role in VCP-
mediated formation of transitional endoplasmic reticulum (tER) (By
similarity). Inhibits the activity of CTSL (in vitro).
{ECO:0000250}.
-!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and
VCP. NSFL1C forms a homotrimer that binds to one end of a VCP
homohexamer. The complex binds to membranes enriched in
phosphatidylethanolamine-containing lipids and promotes Golgi
membrane fusion. Interaction with VCIP135 leads to dissociation of
the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-
ubiquitinated proteins via its N-terminal UBA-like domain when
bound to VCP (By similarity). {ECO:0000250}.
-!- INTERACTION:
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-721577, EBI-10175326;
P55072:VCP; NbExp=8; IntAct=EBI-721577, EBI-355164;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Golgi apparatus,
Golgi stack {ECO:0000250}. Chromosome {ECO:0000250}.
Note=Predominantly nuclear in interphase cells. Bound to the axial
elements of sex chromosomes in pachytene spermatocytes. A small
proportion of the protein is cytoplasmic, associated with Golgi
stacks (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9UNZ2-1; Sequence=Displayed;
Name=2;
IsoId=Q9UNZ2-4; Sequence=VSP_009263;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9UNZ2-5; Sequence=VSP_009262;
Name=4;
IsoId=Q9UNZ2-6; Sequence=VSP_041062;
-!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
interaction with Golgi membranes and is required for the
fragmentation of the Golgi stacks during mitosis (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF17199.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAF17199.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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EMBL; AF086909; AAP97139.1; -; mRNA.
EMBL; AF112211; AAF17199.1; ALT_SEQ; mRNA.
EMBL; AF078856; AAD44488.1; -; mRNA.
EMBL; AK297403; BAG59842.1; -; mRNA.
EMBL; AK001511; BAA91731.1; -; mRNA.
EMBL; AK315433; BAG37821.1; -; mRNA.
EMBL; AL109658; CAB96827.1; -; Genomic_DNA.
EMBL; AL109658; CAI22730.1; -; Genomic_DNA.
EMBL; AL109658; CAI22731.1; -; Genomic_DNA.
EMBL; AL109658; CAM28306.1; -; Genomic_DNA.
EMBL; CH471133; EAX10629.1; -; Genomic_DNA.
EMBL; CH471133; EAX10631.1; -; Genomic_DNA.
EMBL; BC002801; AAH02801.1; -; mRNA.
CCDS; CCDS13015.1; -. [Q9UNZ2-1]
CCDS; CCDS13016.1; -. [Q9UNZ2-4]
CCDS; CCDS56175.1; -. [Q9UNZ2-5]
RefSeq; NP_001193665.1; NM_001206736.1. [Q9UNZ2-5]
RefSeq; NP_057227.2; NM_016143.4. [Q9UNZ2-1]
RefSeq; NP_061327.2; NM_018839.4. [Q9UNZ2-4]
RefSeq; XP_006723657.1; XM_006723594.2. [Q9UNZ2-6]
UniGene; Hs.12865; -.
PDB; 1SS6; NMR; -; A=171-270.
PDBsum; 1SS6; -.
ProteinModelPortal; Q9UNZ2; -.
SMR; Q9UNZ2; -.
BioGrid; 121014; 83.
DIP; DIP-39611N; -.
IntAct; Q9UNZ2; 25.
MINT; MINT-3083194; -.
STRING; 9606.ENSP00000418529; -.
iPTMnet; Q9UNZ2; -.
PhosphoSitePlus; Q9UNZ2; -.
BioMuta; NSFL1C; -.
DMDM; 41017512; -.
REPRODUCTION-2DPAGE; IPI00100197; -.
EPD; Q9UNZ2; -.
PaxDb; Q9UNZ2; -.
PeptideAtlas; Q9UNZ2; -.
PRIDE; Q9UNZ2; -.
TopDownProteomics; Q9UNZ2-1; -. [Q9UNZ2-1]
TopDownProteomics; Q9UNZ2-4; -. [Q9UNZ2-4]
TopDownProteomics; Q9UNZ2-5; -. [Q9UNZ2-5]
DNASU; 55968; -.
Ensembl; ENST00000216879; ENSP00000216879; ENSG00000088833. [Q9UNZ2-1]
Ensembl; ENST00000353088; ENSP00000338643; ENSG00000088833. [Q9UNZ2-4]
Ensembl; ENST00000476071; ENSP00000418529; ENSG00000088833. [Q9UNZ2-5]
GeneID; 55968; -.
KEGG; hsa:55968; -.
UCSC; uc002wfc.3; human. [Q9UNZ2-1]
CTD; 55968; -.
DisGeNET; 55968; -.
EuPathDB; HostDB:ENSG00000088833.17; -.
GeneCards; NSFL1C; -.
HGNC; HGNC:15912; NSFL1C.
HPA; HPA047108; -.
HPA; HPA050628; -.
MIM; 606610; gene.
neXtProt; NX_Q9UNZ2; -.
OpenTargets; ENSG00000088833; -.
PharmGKB; PA31794; -.
eggNOG; KOG2086; Eukaryota.
eggNOG; ENOG410YGXU; LUCA.
GeneTree; ENSGT00520000055567; -.
HOVERGEN; HBG054517; -.
InParanoid; Q9UNZ2; -.
KO; K14012; -.
OMA; MRGEIPQ; -.
OrthoDB; EOG091G0QFZ; -.
PhylomeDB; Q9UNZ2; -.
TreeFam; TF312973; -.
SIGNOR; Q9UNZ2; -.
ChiTaRS; NSFL1C; human.
EvolutionaryTrace; Q9UNZ2; -.
GeneWiki; NSFL1C; -.
GenomeRNAi; 55968; -.
PRO; PR:Q9UNZ2; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000088833; -.
CleanEx; HS_NSFL1C; -.
ExpressionAtlas; Q9UNZ2; baseline and differential.
Genevisible; Q9UNZ2; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:1990730; C:VCP-NSFL1C complex; ISS:ParkinsonsUK-UCL.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0031468; P:nuclear envelope reassembly; IBA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
InterPro; IPR036241; NSFL1C_SEP_dom_sf.
InterPro; IPR012989; SEP_domain.
InterPro; IPR009060; UBA-like.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR001012; UBX_dom.
Pfam; PF08059; SEP; 1.
Pfam; PF00789; UBX; 1.
SMART; SM00553; SEP; 1.
SMART; SM00166; UBX; 1.
SUPFAM; SSF102848; SSF102848; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS51399; SEP; 1.
PROSITE; PS50033; UBX; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
Direct protein sequencing; Golgi apparatus; Lipid-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 370 NSFL1 cofactor p47.
/FTId=PRO_0000210988.
DOMAIN 179 244 SEP. {ECO:0000255|PROSITE-
ProRule:PRU00732}.
DOMAIN 291 368 UBX. {ECO:0000255|PROSITE-
ProRule:PRU00215}.
MOTIF 109 115 Nuclear localization signal.
MOTIF 172 175 Nuclear localization signal.
COMPBIAS 84 90 Poly-Glu.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 167 167 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9CZ44}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CZ44}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 124 MAAERQEALREFVAVTGAEEDRARFFLESAGWDLQIALASF
YEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQ
DEDEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLF
K -> MTKMKMRRKRKAR (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041062.
VAR_SEQ 93 93 R -> RSR (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_009262.
VAR_SEQ 149 179 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_009263.
VARIANT 290 290 D -> N (in dbSNP:rs9575).
{ECO:0000269|PubMed:11042152}.
/FTId=VAR_017481.
CONFLICT 39 40 AS -> EL (in Ref. 1; AAP97139).
{ECO:0000305}.
STRAND 171 173 {ECO:0000244|PDB:1SS6}.
STRAND 180 193 {ECO:0000244|PDB:1SS6}.
STRAND 198 200 {ECO:0000244|PDB:1SS6}.
TURN 204 206 {ECO:0000244|PDB:1SS6}.
HELIX 207 215 {ECO:0000244|PDB:1SS6}.
HELIX 220 223 {ECO:0000244|PDB:1SS6}.
STRAND 231 239 {ECO:0000244|PDB:1SS6}.
STRAND 245 250 {ECO:0000244|PDB:1SS6}.
STRAND 255 259 {ECO:0000244|PDB:1SS6}.
HELIX 260 262 {ECO:0000244|PDB:1SS6}.
STRAND 265 268 {ECO:0000244|PDB:1SS6}.
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


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