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Protein

NSFL1 cofactor p47

Gene

NSFL1C

Organism
Homo sapiens (Human)
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) (By similarity). Inhibits the activity of CTSL (in vitro).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

SIGNORiQ9UNZ2.

Names & Taxonomyi

Protein namesi
Recommended name:
NSFL1 cofactor p47
Alternative name(s):
UBX domain-containing protein 2C
p97 cofactor p47
Gene namesi
Name:NSFL1C
Synonyms:UBXN2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15912. NSFL1C.

Subcellular locationi

  • Nucleus By similarity
  • Golgi apparatusGolgi stack By similarity
  • Chromosome By similarity

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Golgi apparatus, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31794.

Polymorphism and mutation databases

BioMutaiNSFL1C.
DMDMi41017512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370NSFL1 cofactor p47PRO_0000210988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei167 – 1671PhosphotyrosineBy similarity
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated during mitosis. Phosphorylation inhibits interaction with Golgi membranes and is required for the fragmentation of the Golgi stacks during mitosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UNZ2.
MaxQBiQ9UNZ2.
PaxDbiQ9UNZ2.
PRIDEiQ9UNZ2.
TopDownProteomicsiQ9UNZ2-1. [Q9UNZ2-1]
Q9UNZ2-4. [Q9UNZ2-4]
Q9UNZ2-5. [Q9UNZ2-5]

2D gel databases

REPRODUCTION-2DPAGEIPI00100197.

PTM databases

iPTMnetiQ9UNZ2.
PhosphoSiteiQ9UNZ2.

Expressioni

Gene expression databases

BgeeiQ9UNZ2.
CleanExiHS_NSFL1C.
ExpressionAtlasiQ9UNZ2. baseline and differential.
GenevisibleiQ9UNZ2. HS.

Organism-specific databases

HPAiHPA047108.
HPA050628.

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HEL-S-70V9HW803EBI-721577,EBI-10175326
VCPP550725EBI-721577,EBI-355164

GO - Molecular functioni

Protein-protein interaction databases

BioGridi121014. 71 interactions.
DIPiDIP-39611N.
IntActiQ9UNZ2. 25 interactions.
MINTiMINT-3083194.
STRINGi9606.ENSP00000418529.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi171 – 1733Combined sources
Beta strandi180 – 19314Combined sources
Beta strandi198 – 2003Combined sources
Turni204 – 2063Combined sources
Helixi207 – 2159Combined sources
Helixi220 – 2234Combined sources
Beta strandi231 – 2399Combined sources
Beta strandi245 – 2506Combined sources
Beta strandi255 – 2595Combined sources
Helixi260 – 2623Combined sources
Beta strandi265 – 2684Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SS6NMR-A171-270[»]
ProteinModelPortaliQ9UNZ2.
SMRiQ9UNZ2. Positions 1-46, 171-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNZ2.

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi84 – 907Poly-Glu

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.
HOVERGENiHBG054517.
InParanoidiQ9UNZ2.
KOiK14012.
OMAiQTIGDVY.
OrthoDBiEOG7ZKSBB.
PhylomeDBiQ9UNZ2.
TreeFamiTF312973.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UNZ2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAERQEALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI
60 70 80 90 100
VTISQATPSS VSRGTAPSDN RVTSFRDLIH DQDEDEEEEE GQRFYAGGSE
110 120 130 140 150
RSGQQIVGPP RKKSPNELVD DLFKGAKEHG AVAVERVTKS PGETSKPRPF
160 170 180 190 200
AGGGYRLGAA PEEESAYVAG EKRQHSSQDV HVVLKLWKSG FSLDNGELRS
210 220 230 240 250
YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD EDFVKPKGAF
260 270 280 290 300
KAFTGEGQKL GSTAPQVLST SSPAQQAENE AKASSSILID ESEPTTNIQI
310 320 330 340 350
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFILM TTFPNKELAD
360 370
ESQTLKEANL LNAVIVQRLT
Length:370
Mass (Da):40,573
Last modified:January 16, 2004 - v2
Checksum:i79364617F940B9F9
GO
Isoform 2 (identifier: Q9UNZ2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-179: Missing.

Note: No experimental confirmation available.
Show »
Length:339
Mass (Da):37,325
Checksum:iCF165EC48BB54B96
GO
Isoform 3 (identifier: Q9UNZ2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-93: R → RSR

Show »
Length:372
Mass (Da):40,816
Checksum:i4EFCFE27D995031F
GO
Isoform 4 (identifier: Q9UNZ2-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: MAAERQEALR...PNELVDDLFK → MTKMKMRRKRKAR

Show »
Length:259
Mass (Da):28,522
Checksum:i5400E8D45F25448A
GO

Sequence cautioni

The sequence AAF17199.1 differs from that shown.Sequencing errors.Curated
The sequence AAF17199.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 402AS → EL in AAP97139 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti290 – 2901D → N.1 Publication
Corresponds to variant rs9575 [ dbSNP | Ensembl ].
VAR_017481

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 124124MAAER…DDLFK → MTKMKMRRKRKAR in isoform 4. 1 PublicationVSP_041062Add
BLAST
Alternative sequencei93 – 931R → RSR in isoform 3. 1 PublicationVSP_009262
Alternative sequencei149 – 17931Missing in isoform 2. 1 PublicationVSP_009263Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086909 mRNA. Translation: AAP97139.1.
AF112211 mRNA. Translation: AAF17199.1. Sequence problems.
AF078856 mRNA. Translation: AAD44488.1.
AK297403 mRNA. Translation: BAG59842.1.
AK001511 mRNA. Translation: BAA91731.1.
AK315433 mRNA. Translation: BAG37821.1.
AL109658 Genomic DNA. Translation: CAB96827.1.
AL109658 Genomic DNA. Translation: CAI22730.1.
AL109658 Genomic DNA. Translation: CAI22731.1.
AL109658 Genomic DNA. Translation: CAM28306.1.
CH471133 Genomic DNA. Translation: EAX10629.1.
CH471133 Genomic DNA. Translation: EAX10631.1.
BC002801 mRNA. Translation: AAH02801.1.
CCDSiCCDS13015.1. [Q9UNZ2-1]
CCDS13016.1. [Q9UNZ2-4]
CCDS56175.1. [Q9UNZ2-5]
RefSeqiNP_001193665.1. NM_001206736.1. [Q9UNZ2-5]
NP_057227.2. NM_016143.4. [Q9UNZ2-1]
NP_061327.2. NM_018839.4. [Q9UNZ2-4]
XP_006723657.1. XM_006723594.2. [Q9UNZ2-6]
UniGeneiHs.12865.

Genome annotation databases

EnsembliENST00000216879; ENSP00000216879; ENSG00000088833. [Q9UNZ2-1]
ENST00000353088; ENSP00000338643; ENSG00000088833. [Q9UNZ2-4]
ENST00000476071; ENSP00000418529; ENSG00000088833. [Q9UNZ2-5]
GeneIDi55968.
KEGGihsa:55968.
UCSCiuc002wfc.3. human. [Q9UNZ2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086909 mRNA. Translation: AAP97139.1.
AF112211 mRNA. Translation: AAF17199.1. Sequence problems.
AF078856 mRNA. Translation: AAD44488.1.
AK297403 mRNA. Translation: BAG59842.1.
AK001511 mRNA. Translation: BAA91731.1.
AK315433 mRNA. Translation: BAG37821.1.
AL109658 Genomic DNA. Translation: CAB96827.1.
AL109658 Genomic DNA. Translation: CAI22730.1.
AL109658 Genomic DNA. Translation: CAI22731.1.
AL109658 Genomic DNA. Translation: CAM28306.1.
CH471133 Genomic DNA. Translation: EAX10629.1.
CH471133 Genomic DNA. Translation: EAX10631.1.
BC002801 mRNA. Translation: AAH02801.1.
CCDSiCCDS13015.1. [Q9UNZ2-1]
CCDS13016.1. [Q9UNZ2-4]
CCDS56175.1. [Q9UNZ2-5]
RefSeqiNP_001193665.1. NM_001206736.1. [Q9UNZ2-5]
NP_057227.2. NM_016143.4. [Q9UNZ2-1]
NP_061327.2. NM_018839.4. [Q9UNZ2-4]
XP_006723657.1. XM_006723594.2. [Q9UNZ2-6]
UniGeneiHs.12865.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SS6NMR-A171-270[»]
ProteinModelPortaliQ9UNZ2.
SMRiQ9UNZ2. Positions 1-46, 171-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121014. 71 interactions.
DIPiDIP-39611N.
IntActiQ9UNZ2. 25 interactions.
MINTiMINT-3083194.
STRINGi9606.ENSP00000418529.

PTM databases

iPTMnetiQ9UNZ2.
PhosphoSiteiQ9UNZ2.

Polymorphism and mutation databases

BioMutaiNSFL1C.
DMDMi41017512.

2D gel databases

REPRODUCTION-2DPAGEIPI00100197.

Proteomic databases

EPDiQ9UNZ2.
MaxQBiQ9UNZ2.
PaxDbiQ9UNZ2.
PRIDEiQ9UNZ2.
TopDownProteomicsiQ9UNZ2-1. [Q9UNZ2-1]
Q9UNZ2-4. [Q9UNZ2-4]
Q9UNZ2-5. [Q9UNZ2-5]

Protocols and materials databases

DNASUi55968.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216879; ENSP00000216879; ENSG00000088833. [Q9UNZ2-1]
ENST00000353088; ENSP00000338643; ENSG00000088833. [Q9UNZ2-4]
ENST00000476071; ENSP00000418529; ENSG00000088833. [Q9UNZ2-5]
GeneIDi55968.
KEGGihsa:55968.
UCSCiuc002wfc.3. human. [Q9UNZ2-1]

Organism-specific databases

CTDi55968.
GeneCardsiNSFL1C.
HGNCiHGNC:15912. NSFL1C.
HPAiHPA047108.
HPA050628.
MIMi606610. gene.
neXtProtiNX_Q9UNZ2.
PharmGKBiPA31794.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2086. Eukaryota.
ENOG410YGXU. LUCA.
GeneTreeiENSGT00520000055567.
HOVERGENiHBG054517.
InParanoidiQ9UNZ2.
KOiK14012.
OMAiQTIGDVY.
OrthoDBiEOG7ZKSBB.
PhylomeDBiQ9UNZ2.
TreeFamiTF312973.

Enzyme and pathway databases

SIGNORiQ9UNZ2.

Miscellaneous databases

ChiTaRSiNSFL1C. human.
EvolutionaryTraceiQ9UNZ2.
GeneWikiiNSFL1C.
GenomeRNAii55968.
PROiQ9UNZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNZ2.
CleanExiHS_NSFL1C.
ExpressionAtlasiQ9UNZ2. baseline and differential.
GenevisibleiQ9UNZ2. HS.

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. "Cloning of a novel human cDNA homology to R.norvegicus p47 mRNA."
    Yue P., Yu L., Zhou Y., Zhao Y., Yang Y.M., Zhao S.Y.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    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.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-290.
    Tissue: Umbilical cord blood.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
    Tissue: Brain.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Placenta.
  8. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-22; 77-93; 114-124; 157-172; 189-214; 260-301 AND 357-368, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L."
    Soukenik M., Diehl A., Leidert M., Sievert V., Buessow K., Leitner D., Labudde D., Ball L.J., Lechner A., Naegler D.K., Oschkinat H.
    FEBS Lett. 576:358-362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 171-270, INTERACTION WITH CTSL.

Entry informationi

Entry nameiNSF1C_HUMAN
AccessioniPrimary (citable) accession number: Q9UNZ2
Secondary accession number(s): A2A2L1
, B2RD74, Q5JXA4, Q5JXA5, Q7Z533, Q9H102, Q9NVL9, Q9UI06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: June 8, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.