Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01139

- NGF_MOUSE

UniProt

P01139 - NGF_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-nerve growth factor

Gene

Ngf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades through those receptor tyrosine kinase to regulate neuronal proliferation, differentiation and survival.

GO - Molecular functioni

  1. receptor signaling protein activity Source: MGI

GO - Biological processi

  1. circadian rhythm Source: UniProtKB
  2. extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  3. intracellular signal transduction Source: GOC
  4. negative regulation of neuron apoptotic process Source: MGI
  5. nerve growth factor signaling pathway Source: MGI
  6. neuron apoptotic process Source: MGI
  7. neuron projection morphogenesis Source: MGI
  8. peripheral nervous system development Source: MGI
  9. positive regulation of axon extension Source: MGI
  10. positive regulation of neuron maturation Source: MGI
  11. positive regulation of neuron projection development Source: MGI
  12. positive regulation of neurotrophin TRK receptor signaling pathway Source: MGI
  13. positive regulation of protein autophosphorylation Source: MGI
  14. positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  15. regulation of neuron differentiation Source: MGI
  16. regulation of neurotransmitter secretion Source: MGI
  17. regulation of release of sequestered calcium ion into cytosol Source: MGI
  18. sensory perception of pain Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

ReactomeiREACT_202086. p75NTR negatively regulates cell cycle via SC1.
REACT_202271. NRIF signals cell death from the nucleus.
REACT_202778. Retrograde neurotrophin signalling.
REACT_205300. PI3K/AKT activation.
REACT_206713. NGF processing.
REACT_207546. NFG and proNGF binds to p75NTR.
REACT_209641. NRAGE signals death through JNK.
REACT_210754. NADE modulates death signalling.
REACT_212952. Signalling to STAT3.
REACT_213333. TRKA activation by NGF.
REACT_214242. Axonal growth stimulation.
REACT_214670. p75NTR recruits signalling complexes.
REACT_217312. Ceramide signalling.
REACT_218887. NF-kB is activated and signals survival.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-nerve growth factor
Short name:
Beta-NGF
Gene namesi
Name:Ngf
Synonyms:Ngfb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:97321. Ngf.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 1211031 PublicationPRO_0000019601Add
BLAST
Chaini122 – 241120Beta-nerve growth factorPRO_0000019602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi136 ↔ 201
Disulfide bondi179 ↔ 229
Disulfide bondi189 ↔ 231

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01139.
PRIDEiP01139.

PTM databases

PhosphoSiteiP01139.

Expressioni

Inductioni

Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain.1 Publication

Gene expression databases

BgeeiP01139.
CleanExiMM_NGF.
ExpressionAtlasiP01139. baseline and differential.
GenevestigatoriP01139.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi201764. 1 interaction.
DIPiDIP-59840N.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi133 – 1364
Beta strandi138 – 1447
Beta strandi148 – 1514
Beta strandi156 – 1594
Beta strandi161 – 1655
Beta strandi168 – 1714
Beta strandi174 – 1807
Turni194 – 1963
Beta strandi197 – 21317
Beta strandi218 – 23518

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BETX-ray2.30A131-237[»]
1BTGX-ray2.50A/B/C130-239[»]
1SGFX-ray3.15B/Y122-239[»]
3IJ2X-ray3.75A/B19-241[»]
4EAXX-ray2.30A/B/C/D122-241[»]
ProteinModelPortaliP01139.
SMRiP01139. Positions 131-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01139.

Family & Domainsi

Sequence similaritiesi

Belongs to the NGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG44820.
GeneTreeiENSGT00390000007725.
HOVERGENiHBG006494.
InParanoidiP01139.
KOiK02582.
PhylomeDBiP01139.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR020408. Nerve_growth_factor-like.
IPR002072. Nerve_growth_factor-rel.
IPR020425. Nerve_growth_factor_bsu.
IPR020437. Nerve_growth_factor_bsu_mml.
IPR019846. Nerve_growth_factor_CS.
[Graphical view]
PANTHERiPTHR11589. PTHR11589. 1 hit.
PfamiPF00243. NGF. 1 hit.
[Graphical view]
PIRSFiPIRSF001789. NGF. 1 hit.
PRINTSiPR01925. MAMLNGFBETA.
PR00268. NGF.
PR01913. NGFBETA.
ProDomiPD002052. Nerve_growth_factor-rel. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00140. NGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00248. NGF_1. 1 hit.
PS50270. NGF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01139-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSMLFYTLIT AFLIGVQAEP YTDSNVPEGD SVPEAHWTKL QHSLDTALRR
60 70 80 90 100
ARSAPTAPIA ARVTGQTRNI TVDPRLFKKR RLHSPRVLFS TQPPPTSSDT
110 120 130 140 150
LDLDFQAHGT IPFNRTHRSK RSSTHPVFHM GEFSVCDSVS VWVGDKTTAT
160 170 180 190 200
DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY
210 220 230 240
CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G
Length:241
Mass (Da):27,077
Last modified:January 1, 1990 - v2
Checksum:i164465E1DC550081
GO

Sequence cautioni

The sequence AAA37687.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAA39818.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAA39820.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAA39821.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA24221.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2419LSRKATRRG → CSAGRLQEEADLPAAPFPTC PLHTLLGPSLPQPVNYFKL in AAB26820. (PubMed:1284621)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35075 mRNA. Translation: AAA39818.1. Different initiation.
V00836 mRNA. Translation: CAA24221.1. Different initiation.
K01759 mRNA. Translation: AAA39820.1. Different initiation.
M14805 mRNA. Translation: AAA39821.1. Different initiation.
M17298, M17296, M17297 Genomic DNA. Translation: AAA37687.1. Different initiation.
S62089 mRNA. Translation: AAB26820.2.
CCDSiCCDS51025.1.
RefSeqiNP_001106168.1. NM_001112698.2.
NP_038637.1. NM_013609.3.
XP_006501171.1. XM_006501108.1.
XP_006501172.1. XM_006501109.1.
XP_006501173.1. XM_006501110.1.
UniGeneiMm.1259.

Genome annotation databases

EnsembliENSMUST00000035952; ENSMUSP00000040345; ENSMUSG00000027859.
GeneIDi18049.
KEGGimmu:18049.
UCSCiuc012cuz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35075 mRNA. Translation: AAA39818.1 . Different initiation.
V00836 mRNA. Translation: CAA24221.1 . Different initiation.
K01759 mRNA. Translation: AAA39820.1 . Different initiation.
M14805 mRNA. Translation: AAA39821.1 . Different initiation.
M17298 , M17296 , M17297 Genomic DNA. Translation: AAA37687.1 . Different initiation.
S62089 mRNA. Translation: AAB26820.2 .
CCDSi CCDS51025.1.
RefSeqi NP_001106168.1. NM_001112698.2.
NP_038637.1. NM_013609.3.
XP_006501171.1. XM_006501108.1.
XP_006501172.1. XM_006501109.1.
XP_006501173.1. XM_006501110.1.
UniGenei Mm.1259.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BET X-ray 2.30 A 131-237 [» ]
1BTG X-ray 2.50 A/B/C 130-239 [» ]
1SGF X-ray 3.15 B/Y 122-239 [» ]
3IJ2 X-ray 3.75 A/B 19-241 [» ]
4EAX X-ray 2.30 A/B/C/D 122-241 [» ]
ProteinModelPortali P01139.
SMRi P01139. Positions 131-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201764. 1 interaction.
DIPi DIP-59840N.

PTM databases

PhosphoSitei P01139.

Proteomic databases

MaxQBi P01139.
PRIDEi P01139.

Protocols and materials databases

DNASUi 18049.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035952 ; ENSMUSP00000040345 ; ENSMUSG00000027859 .
GeneIDi 18049.
KEGGi mmu:18049.
UCSCi uc012cuz.1. mouse.

Organism-specific databases

CTDi 4803.
MGIi MGI:97321. Ngf.

Phylogenomic databases

eggNOGi NOG44820.
GeneTreei ENSGT00390000007725.
HOVERGENi HBG006494.
InParanoidi P01139.
KOi K02582.
PhylomeDBi P01139.

Enzyme and pathway databases

Reactomei REACT_202086. p75NTR negatively regulates cell cycle via SC1.
REACT_202271. NRIF signals cell death from the nucleus.
REACT_202778. Retrograde neurotrophin signalling.
REACT_205300. PI3K/AKT activation.
REACT_206713. NGF processing.
REACT_207546. NFG and proNGF binds to p75NTR.
REACT_209641. NRAGE signals death through JNK.
REACT_210754. NADE modulates death signalling.
REACT_212952. Signalling to STAT3.
REACT_213333. TRKA activation by NGF.
REACT_214242. Axonal growth stimulation.
REACT_214670. p75NTR recruits signalling complexes.
REACT_217312. Ceramide signalling.
REACT_218887. NF-kB is activated and signals survival.

Miscellaneous databases

EvolutionaryTracei P01139.
NextBioi 293175.
PROi P01139.
SOURCEi Search...

Gene expression databases

Bgeei P01139.
CleanExi MM_NGF.
ExpressionAtlasi P01139. baseline and differential.
Genevestigatori P01139.

Family and domain databases

Gene3Di 2.10.90.10. 1 hit.
InterProi IPR029034. Cystine-knot_cytokine.
IPR020408. Nerve_growth_factor-like.
IPR002072. Nerve_growth_factor-rel.
IPR020425. Nerve_growth_factor_bsu.
IPR020437. Nerve_growth_factor_bsu_mml.
IPR019846. Nerve_growth_factor_CS.
[Graphical view ]
PANTHERi PTHR11589. PTHR11589. 1 hit.
Pfami PF00243. NGF. 1 hit.
[Graphical view ]
PIRSFi PIRSF001789. NGF. 1 hit.
PRINTSi PR01925. MAMLNGFBETA.
PR00268. NGF.
PR01913. NGFBETA.
ProDomi PD002052. Nerve_growth_factor-rel. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00140. NGF. 1 hit.
[Graphical view ]
SUPFAMi SSF57501. SSF57501. 1 hit.
PROSITEi PS00248. NGF_1. 1 hit.
PS50270. NGF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and nucleotide sequence of a cDNA encoding the precursor of mouse nerve growth factor."
    Scott J., Selby M.J., Urdea M.S., Quiroga M., Bell G.I., Rutter W.J.
    Nature 302:538-540(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Submandibular gland.
  2. "Human beta-nerve growth factor gene sequence highly homologous to that of mouse."
    Ullrich A., Gray A., Berman C., Dull T.J.
    Nature 303:821-825(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence homology of human and mouse beta-NGF subunit genes."
    Ullrich A., Gray A., Berman C., Coussens L., Dull T.J.
    Cold Spring Harb. Symp. Quant. Biol. 48:435-442(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Mouse nerve growth factor gene: structure and expression."
    Selby M.J., Edwards R., Sharp F., Rutter W.J.
    Mol. Cell. Biol. 7:3057-3064(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6.
    Tissue: Submandibular gland.
  5. "Production and secretion of nerve growth factor by clonal striated muscle cell line, G8-1."
    Yamamoto T., Yamakuni T., Okabe N., Amano T.
    Neurochem. Int. 21:251-258(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  6. "Amino acid sequences of mouse 2.5S nerve growth factor. II. Isolation and characterization of the thermolytic and peptic peptides and the complete covalent structure."
    Angeletti R.H., Hermodson M.A., Bradshaw R.A.
    Biochemistry 12:100-115(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 122-239.
  7. "p75 neurotrophin receptor is a clock gene that regulates oscillatory components of circadian and metabolic networks."
    Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., Sassone-Corsi P., Ptacek L.J., Akassoglou K.
    J. Neurosci. 33:10221-10234(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor."
    McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A., Blundell T.L.
    Nature 354:411-414(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  9. "Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites."
    Holland D.R., Cousens L.S., Meng W., Matthews B.W.
    J. Mol. Biol. 239:385-400(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  10. "Structure of mouse 7S NGF: a complex of nerve growth factor with four binding proteins."
    Bax B., Blundell T.L., Murray-Rust J., McDonald N.Q.
    Structure 5:1275-1285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 7S COMPLEX.
    Strain: Swiss Webster.
    Tissue: Submandibular gland.

Entry informationi

Entry nameiNGF_MOUSE
AccessioniPrimary (citable) accession number: P01139
Secondary accession number(s): Q63864, Q6LDB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 140 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3