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Protein

NSFL1 cofactor p47

Gene

Nsfl1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

GO - Molecular functioni

  • ATPase binding Source: RGD
  • lipid binding Source: UniProtKB-KW
  • ubiquitin binding Source: BHF-UCL

GO - Biological processi

  • Golgi organization Source: RGD
  • membrane fusion Source: RGD
  • nuclear envelope reassembly Source: GO_Central
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NSFL1 cofactor p47
Alternative name(s):
XY body-associated protein XY40
p97 cofactor p47
Gene namesi
Name:Nsfl1c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi619952. Nsfl1c.

Subcellular locationi

  • Nucleus
  • Golgi apparatusGolgi stack
  • Chromosome

  • 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.

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • cytosol Source: ParkinsonsUK-UCL
  • Golgi stack Source: UniProtKB-SubCell
  • intermediate filament cytoskeleton Source: Ensembl
  • nucleoplasm Source: Ensembl
  • nucleus Source: GO_Central
  • plasma membrane Source: Ensembl
  • VCP-NSFL1C complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411F → A: Reduces ubiquitin binding and Golgi reassembly. 1 Publication
Mutagenesisi57 – 571T → A: No effect on phosphorylation. 1 Publication
Mutagenesisi112 – 1121K → T: Strongly reduces nuclear location. 1 Publication
Mutagenesisi114 – 1141S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi140 – 1401S → A: Abolishes phosphorylation by CDK1. 1 Publication
Mutagenesisi140 – 1401S → D: Strongly reduces binding to Golgi membranes. 1 Publication
Mutagenesisi173 – 1731R → T: Strongly reduces nuclear location. 1 Publication
Mutagenesisi272 – 2721S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi301 – 3011R → A: Reduced interaction with VCP. 1 Publication
Mutagenesisi342 – 3454TFPN → AG: Strongly reduced interaction with VCP. 1 Publication
Mutagenesisi343 – 3431F → S: Reduced interaction with VCP. 1 Publication
Mutagenesisi345 – 3451N → A: Reduced interaction with VCP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370NSFL1 cofactor p47PRO_0000210990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei140 – 1401Phosphoserine; by CDK11 Publication
Modified residuei167 – 1671PhosphotyrosineBy similarity
Modified residuei176 – 1761PhosphoserineCombined sources
Modified residuei192 – 1921PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated during mitosis. Phosphorylation inhibits interaction with Golgi membranes and is required for the fragmentation of the Golgi stacks during mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35987.
PRIDEiO35987.

PTM databases

iPTMnetiO35987.
PhosphoSiteiO35987.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, spleen, lung, liver, muscle, kidney and testis.3 Publications

Developmental stagei

Highly expressed in pachytene spermatocytes during spermatogenesis.

Gene expression databases

ExpressionAtlasiO35987. baseline and differential.
GenevisibleiO35987. RN.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VcpP4646210EBI-1993760,EBI-399011
VcpQ018533EBI-1993760,EBI-80597From a different organism.

GO - Molecular functioni

  • ATPase binding Source: RGD
  • ubiquitin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi249844. 4 interactions.
IntActiO35987. 16 interactions.
MINTiMINT-1954288.
STRINGi10116.ENSRNOP00000011654.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512Combined sources
Helixi20 – 2910Combined sources
Helixi35 – 439Combined sources
Beta strandi181 – 1877Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi198 – 2003Combined sources
Helixi206 – 21510Combined sources
Helixi221 – 2244Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi232 – 2376Combined sources
Turni239 – 2413Combined sources
Helixi275 – 28612Combined sources
Beta strandi298 – 3025Combined sources
Turni303 – 3064Combined sources
Beta strandi307 – 3115Combined sources
Beta strandi314 – 3163Combined sources
Helixi318 – 32811Combined sources
Helixi331 – 3333Combined sources
Beta strandi337 – 3415Combined sources
Turni342 – 3454Combined sources
Helixi355 – 3584Combined sources
Beta strandi364 – 3696Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I42NMR-A282-370[»]
1JRUNMR-A282-370[»]
1S3SX-ray2.90G/H/I244-370[»]
1V92NMR-A1-46[»]
1VAZNMR-A171-246[»]
ProteinModelPortaliO35987.
SMRiO35987. Positions 1-46, 171-246, 253-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35987.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini179 – 24466SEPPROSITE-ProRule annotationAdd
BLAST
Domaini291 – 36878UBXPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi109 – 1157Nuclear localization signal
Motifi172 – 1754Nuclear localization signal

Sequence similaritiesi

Belongs to the NSFL1C family.Curated
Contains 1 SEP domain.PROSITE-ProRule annotation
Contains 1 UBX domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2086. Eukaryota.
ENOG410YGXU. LUCA.
GeneTreeiENSGT00520000055567.
HOGENOMiHOG000159961.
HOVERGENiHBG054517.
InParanoidiO35987.
KOiK14012.
OMAiQTIGDVY.
OrthoDBiEOG7ZKSBB.
PhylomeDBiO35987.

Family and domain databases

InterProiIPR012989. SEP_domain.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF08059. SEP. 1 hit.
PF00789. UBX. 1 hit.
[Graphical view]
SMARTiSM00553. SEP. 1 hit.
SM00166. UBX. 1 hit.
[Graphical view]
SUPFAMiSSF102848. SSF102848. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS51399. SEP. 1 hit.
PS50033. UBX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEERQDALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI
60 70 80 90 100
VTISQATPSS VSRGTAPSDN RVTSFRDLIH DQDEEEEEEE GQRFYAGGSE
110 120 130 140 150
RSGQQIVGPP RKKSPNELVD DLFKGAKEHG AVAVERVTKS PGETSKPRPF
160 170 180 190 200
AGGGYRLGAA PEEESAYVAG ERRRHSGQDV HVVLKLWKTG FSLDNGDLRS
210 220 230 240 250
YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD EDFVKPKGAF
260 270 280 290 300
KAFTGEGQKL GSTAPQVLNT SSPAQQAENE AKASSSILIN EAEPTTNIQI
310 320 330 340 350
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFVLM TTFPNKELAD
360 370
ENQTLKEANL LNAVIVQRLT
Length:370
Mass (Da):40,680
Last modified:January 1, 1998 - v1
Checksum:i60C81402E5C58134
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10769 mRNA. Translation: CAA71742.1.
AB002086 mRNA. Translation: BAA21659.1.
BC072464 mRNA. Translation: AAH72464.1.
RefSeqiNP_114187.1. NM_031981.2.
UniGeneiRn.2771.

Genome annotation databases

EnsembliENSRNOT00000011654; ENSRNOP00000011654; ENSRNOG00000008604.
GeneIDi83809.
KEGGirno:83809.
UCSCiRGD:619952. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10769 mRNA. Translation: CAA71742.1.
AB002086 mRNA. Translation: BAA21659.1.
BC072464 mRNA. Translation: AAH72464.1.
RefSeqiNP_114187.1. NM_031981.2.
UniGeneiRn.2771.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I42NMR-A282-370[»]
1JRUNMR-A282-370[»]
1S3SX-ray2.90G/H/I244-370[»]
1V92NMR-A1-46[»]
1VAZNMR-A171-246[»]
ProteinModelPortaliO35987.
SMRiO35987. Positions 1-46, 171-246, 253-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249844. 4 interactions.
IntActiO35987. 16 interactions.
MINTiMINT-1954288.
STRINGi10116.ENSRNOP00000011654.

PTM databases

iPTMnetiO35987.
PhosphoSiteiO35987.

Proteomic databases

PaxDbiO35987.
PRIDEiO35987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011654; ENSRNOP00000011654; ENSRNOG00000008604.
GeneIDi83809.
KEGGirno:83809.
UCSCiRGD:619952. rat.

Organism-specific databases

CTDi55968.
RGDi619952. Nsfl1c.

Phylogenomic databases

eggNOGiKOG2086. Eukaryota.
ENOG410YGXU. LUCA.
GeneTreeiENSGT00520000055567.
HOGENOMiHOG000159961.
HOVERGENiHBG054517.
InParanoidiO35987.
KOiK14012.
OMAiQTIGDVY.
OrthoDBiEOG7ZKSBB.
PhylomeDBiO35987.

Miscellaneous databases

EvolutionaryTraceiO35987.
PROiO35987.

Gene expression databases

ExpressionAtlasiO35987. baseline and differential.
GenevisibleiO35987. RN.

Family and domain databases

InterProiIPR012989. SEP_domain.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF08059. SEP. 1 hit.
PF00789. UBX. 1 hit.
[Graphical view]
SMARTiSM00553. SEP. 1 hit.
SM00166. UBX. 1 hit.
[Graphical view]
SUPFAMiSSF102848. SSF102848. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS51399. SEP. 1 hit.
PS50033. UBX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization and expression pattern of XY body-associated protein XY40 of the rat."
    Alsheimer M., Imamichi Y., Heid H., Benavente R.
    Chromosoma 106:308-314(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 200-209; 283-292 AND 323-328, TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Spermatocyte.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-22; 94-101; 157-172; 189-214; 260-282; 323-346 AND 357-368, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH VCP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 200-214 AND 283-301, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  5. "Meiosis-specific protein selectively associated with sex chromosomes of rat pachytene spermatocytes."
    Smith A., Benavente R.
    Proc. Natl. Acad. Sci. U.S.A. 89:6938-6942(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro."
    Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.
    Cell 92:603-610(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX5A.
  7. "The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97."
    Meyer H.H., Kondo H., Warren G.
    FEBS Lett. 437:255-257(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways."
    Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.
    EMBO J. 19:2181-2192(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCP.
  9. Cited for: FUNCTION.
  10. "Phospholipid species act as modulators in p97/p47-mediated fusion of Golgi membranes."
    Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M., Hoekstra D.
    Biochemistry 41:9813-9823(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEMBRANES.
  11. "Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4."
    Meyer H.H., Wang Y., Warren G.
    EMBO J. 21:5645-5652(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PHE-41.
  12. "VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo."
    Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B., Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.
    J. Cell Biol. 159:855-866(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCIP135.
  13. "The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle."
    Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M., Zhang X., Kondo H.
    J. Cell Biol. 161:1067-1079(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-140, MUTAGENESIS OF THR-57; LYS-112; SER-114; SER-140; ARG-173 AND SER-272, SUBCELLULAR LOCATION.
  14. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly."
    Yuan X., Shaw A., Zhang X., Kondo H., Lally J., Freemont P.S., Matthews S.
    J. Mol. Biol. 311:255-263(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 282-370, INTERACTION WITH VCP.
  17. "Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47."
    Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.
    EMBO J. 23:1030-1039(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 244-370, INTERACTION WITH VCP, MUTAGENESIS OF ARG-301; 342-THR--ASN-345; PHE-343 AND ASN-345.
  18. "Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97."
    Yuan X., Simpson P., McKeown C., Kondo H., Uchiyama K., Wallis R., Dreveny I., Keetch C., Zhang X., Robinson C., Freemont P., Matthews S.
    EMBO J. 23:1463-1473(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-46 IN COMPLEX WITH UBIQUITIN, STRUCTURE BY NMR OF 171-246, INTERACTION WITH VCP.

Entry informationi

Entry nameiNSF1C_RAT
AccessioniPrimary (citable) accession number: O35987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.