GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Matrix protein 1 (M1)

 M1_I34A1                Reviewed;         252 AA.
P03485; A4GXH8; Q20N36; Q77HF4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
16-JAN-2019, entry version 138.
RecName: Full=Matrix protein 1 {ECO:0000255|HAMAP-Rule:MF_04068};
Short=M1 {ECO:0000255|HAMAP-Rule:MF_04068};
Name=M {ECO:0000255|HAMAP-Rule:MF_04068};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6927841; DOI=10.1093/nar/8.9.1965;
Winter G., Fields S.;
"Cloning of influenza cDNA into M13: the sequence of the RNA segment
encoding the A/PR/8/34 matrix protein.";
Nucleic Acids Res. 8:1965-1974(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A/Puerto Rico/8/34/Mount Sinai;
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
PubMed=7241645;
Hall R.M., Air G.M.;
"Variation in nucleotide sequences coding for the N-terminal regions
of the matrix and nonstructural proteins of influenza A viruses.";
J. Virol. 38:1-7(1981).
[6]
INTERACTION WITH NEP PROTEIN.
PubMed=8356796; DOI=10.1006/viro.1993.1473;
Yasuda J., Nakada S., Kato A., Toyoda T., Ishihama A.;
"Molecular assembly of influenza virus: association of the NS2 protein
with virion matrix.";
Virology 196:249-255(1993).
[7]
HOMOMULTIMERIZATION.
PubMed=9780049;
Zhao H., Ekstrom M., Garoff H.;
"The M1 and NP proteins of influenza A virus form homo- but not
heterooligomeric complexes when coexpressed in BHK-21 cells.";
J. Gen. Virol. 79:2435-2446(1998).
[8]
INTERACTION WITH MEMBRANE AND VIRAL RNP.
PubMed=11222100; DOI=10.1006/viro.2000.0804;
Baudin F., Petit I., Weissenhorn W., Ruigrok R.W.;
"In vitro dissection of the membrane and RNP binding activities of
influenza virus M1 protein.";
Virology 281:102-108(2001).
[9]
FUNCTION.
PubMed=11531417; DOI=10.1006/viro.2001.1067;
Huang X., Liu T., Muller J., Levandowski R.A., Ye Z.;
"Effect of influenza virus matrix protein and viral RNA on
ribonucleoprotein formation and nuclear export.";
Virology 287:405-416(2001).
[10]
REVIEW.
PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
Nayak D.P., Hui E.K., Barman S.;
"Assembly and budding of influenza virus.";
Virus Res. 106:147-165(2004).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-66.
PubMed=1565634; DOI=10.1073/pnas.89.8.3429;
Garboczi D.N., Hung D.T., Wiley D.C.;
"HLA-A2-peptide complexes: refolding and crystallization of molecules
expressed in Escherichia coli and complexed with single antigenic
peptides.";
Proc. Natl. Acad. Sci. U.S.A. 89:3429-3433(1992).
[12]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-158.
PubMed=9164466; DOI=10.1038/nsb0397-239;
Sha B., Luo M.;
"Structure of a bifunctional membrane-RNA binding protein, influenza
virus matrix protein M1.";
Nat. Struct. Biol. 4:239-244(1997).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-164.
PubMed=11162800; DOI=10.1006/viro.2000.0727;
Arzt S., Baudin F., Barge A., Timmins P., Burmeister W.P.,
Ruigrok R.W.;
"Combined results from solution studies on intact influenza virus M1
protein and from a new crystal form of its N-terminal domain show that
M1 is an elongated monomer.";
Virology 279:439-446(2001).
-!- FUNCTION: Plays critical roles in virus replication, from virus
entry and uncoating to assembly and budding of the virus particle.
M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit
viral transcription. Interaction of viral NEP with M1-RNP is
thought to promote nuclear export of the complex, which is
targeted to the virion assembly site at the apical plasma membrane
in polarized epithelial cells. Interactions with NA and HA may
bring M1, a non-raft-associated protein, into lipid rafts. Forms a
continuous shell on the inner side of the lipid bilayer in virion,
where it binds the RNP. During virus entry into cell, the M2 ion
channel acidifies the internal virion core, inducing M1
dissociation from the RNP. M1-free RNPs are transported to the
nucleus, where viral transcription and replication can take place.
{ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:11531417}.
-!- FUNCTION: Determines the virion's shape: spherical or filamentous.
Clinical isolates of influenza are characterized by the presence
of significant proportion of filamentous virions, whereas after
multiple passage on eggs or cell culture, virions have only
spherical morphology. Filamentous virions are thought to be
important to infect neighboring cells, and spherical virions more
suited to spread through aerosol between hosts organisms.
{ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:11531417}.
-!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds
ribonucleocapsid by both interacting with genomic RNA and NP
protein. May interact with HA and NA. Cannot bind NP without
genomic RNA. {ECO:0000255|HAMAP-Rule:MF_04068,
ECO:0000269|PubMed:11222100, ECO:0000269|PubMed:8356796}.
-!- INTERACTION:
P11142:HSPA8 (xeno); NbExp=4; IntAct=EBI-2547543, EBI-351896;
P03466:NP; NbExp=2; IntAct=EBI-2547543, EBI-2547640;
P03508:NS; NbExp=3; IntAct=EBI-2547543, EBI-2547979;
P03433:PA; NbExp=2; IntAct=EBI-2547543, EBI-2547616;
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-
Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-
Rule:MF_04068}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Only the first 9 residues are shared by the 2 isoforms.;
Name=M1;
IsoId=P03485-1; Sequence=Displayed;
Name=M2;
IsoId=P06821-1; Sequence=External;
-!- MISCELLANEOUS: Most abundant protein in virion. When expressed
alone can form virus-like particles in transfected cells.
{ECO:0000255|HAMAP-Rule:MF_04068}.
-!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1
family. {ECO:0000255|HAMAP-Rule:MF_04068}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; V01099; CAA24282.1; -; Genomic_RNA.
EMBL; AF389121; AAM75161.1; -; Genomic_RNA.
EMBL; EF467824; ABO21712.1; -; Viral_cRNA.
EMBL; CY009445; ABD77676.1; -; Genomic_RNA.
RefSeq; NP_040978.1; NC_002016.1. [P03485-1]
PDB; 1AA7; X-ray; 2.08 A; A/B=1-158.
PDB; 1EA3; X-ray; 2.30 A; A/B=1-164.
PDB; 1HHI; X-ray; 2.50 A; C/F=58-66.
PDB; 2VLL; X-ray; 1.60 A; C/F=58-66.
PDB; 2VLR; X-ray; 2.30 A; C/H=58-66.
PDB; 3VDX; X-ray; 3.00 A; A/B/C=3-164.
PDB; 4D9J; X-ray; 3.92 A; A/B/C/D/E/F/G/H/I/J/K/L=3-164.
PDB; 4IQ4; X-ray; 3.50 A; A/B/C/D/E/F=3-164.
PDB; 4ITV; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=3-164.
PDB; 4IVJ; X-ray; 7.35 A; A/B/C=3-164.
PDB; 4QES; X-ray; 4.19 A; A/B/C=3-164.
PDB; 4QF0; X-ray; 6.49 A; A/B/C/D/E/F=3-164.
PDB; 4QFF; X-ray; 7.81 A; A/B/C/D/E/F/G/H/I/J/K/L=3-164.
PDB; 5CQE; X-ray; 2.10 A; A/B=1-164.
PDB; 5E6I; X-ray; 4.00 A; E/K/O/T=58-66.
PDB; 5EUO; X-ray; 2.10 A; I/J=58-66.
PDB; 5ISZ; X-ray; 2.06 A; C=58-66.
PDB; 5JHD; X-ray; 2.46 A; C/H=58-66.
PDB; 5TEZ; X-ray; 1.70 A; C=58-66.
PDBsum; 1AA7; -.
PDBsum; 1EA3; -.
PDBsum; 1HHI; -.
PDBsum; 2VLL; -.
PDBsum; 2VLR; -.
PDBsum; 3VDX; -.
PDBsum; 4D9J; -.
PDBsum; 4IQ4; -.
PDBsum; 4ITV; -.
PDBsum; 4IVJ; -.
PDBsum; 4QES; -.
PDBsum; 4QF0; -.
PDBsum; 4QFF; -.
PDBsum; 5CQE; -.
PDBsum; 5E6I; -.
PDBsum; 5EUO; -.
PDBsum; 5ISZ; -.
PDBsum; 5JHD; -.
PDBsum; 5TEZ; -.
ProteinModelPortal; P03485; -.
SMR; P03485; -.
IntAct; P03485; 50.
MINT; P03485; -.
GeneID; 956527; -.
KEGG; vg:956527; -.
KO; K19393; -.
OrthoDB; 5567at10239; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-192823; Viral mRNA Translation.
EvolutionaryTrace; P03485; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
GO; GO:0019070; P:viral genome maturation; TAS:Reactome.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
Gene3D; 1.10.10.180; -; 1.
Gene3D; 1.20.91.10; -; 1.
HAMAP; MF_04068; INFV_M1; 1.
InterPro; IPR036039; Flu_matrix_M1.
InterPro; IPR013188; Flu_matrix_M1_C.
InterPro; IPR001561; Flu_matrix_M1_N.
InterPro; IPR015423; Flu_matrix_M1_N_sub1.
InterPro; IPR015799; Flu_matrix_M1_N_sub2.
InterPro; IPR037533; INFV_M1.
Pfam; PF00598; Flu_M1; 1.
Pfam; PF08289; Flu_M1_C; 1.
ProDom; PD596253; Flu_matrix_M1_C; 1.
ProDom; PD001061; Flu_matrix_M1_N; 1.
SMART; SM00759; Flu_M1_C; 1.
SUPFAM; SSF48145; SSF48145; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Host nucleus;
Membrane; Reference proteome; RNA-binding; Viral matrix protein;
Virion.
CHAIN 1 252 Matrix protein 1.
/FTId=PRO_0000078864.
REGION 1 164 Membrane-binding. {ECO:0000255|HAMAP-
Rule:MF_04068}.
REGION 165 252 RNP-binding. {ECO:0000255|HAMAP-
Rule:MF_04068}.
MOTIF 101 105 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04068}.
CONFLICT 207 208 SQ -> IR (in Ref. 4; ABD77676).
{ECO:0000305}.
HELIX 3 12 {ECO:0000244|PDB:1AA7}.
HELIX 19 32 {ECO:0000244|PDB:1AA7}.
HELIX 39 47 {ECO:0000244|PDB:1AA7}.
STRAND 50 52 {ECO:0000244|PDB:1AA7}.
HELIX 54 67 {ECO:0000244|PDB:1AA7}.
HELIX 78 83 {ECO:0000244|PDB:1AA7}.
HELIX 86 88 {ECO:0000244|PDB:1AA7}.
HELIX 90 103 {ECO:0000244|PDB:1AA7}.
HELIX 109 116 {ECO:0000244|PDB:1AA7}.
HELIX 121 132 {ECO:0000244|PDB:1AA7}.
HELIX 134 137 {ECO:0000244|PDB:1EA3}.
HELIX 140 157 {ECO:0000244|PDB:1AA7}.
SEQUENCE 252 AA; 27893 MW; 2A54EEC87C3D4638 CRC64;
MSLLTEVETY VLSIIPSGPL KAEIAQRLED VFAGKNTDLE VLMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY RKLKREITFH GAKEISLSYS
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVTTTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK NDLLENLQAY
QKRMGVQMQR FK


Related products :

Catalog number Product name Quantity
EIAAB39943 300 kDa nuclear matrix antigen,Homo sapiens,HSPC075,Human,KIAA0324,Ser_Arg-related nuclear matrix protein of 300 kDa,Serine_arginine repetitive matrix protein 2,Serine_arginine-rich splicing factor-re
E1639p ELISA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
U1639p CLIA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
orb81536 SARS Associated Coronavirus Matrix protein The E.coli derived 30kDa recombinant protein contains the Matrix protein 182-216 amino acids immunodominant regions. For research use only. 100
E1639p ELISA kit 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
U1639b CLIA 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T
E1639b ELISA 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T
E1639b ELISA kit 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T
EIAAB39941 Homo sapiens,Human,Ser_Arg-related nuclear matrix protein,Serine_arginine repetitive matrix protein 1,SRm160,SRM160,SR-related nuclear matrix protein of 160 kDa,SRRM1
EIAAB39674 Ecm2,Extracellular matrix protein 2,Matrix glycoprotein Sc1,Mouse,Mus musculus,Sc1,Sparcl1,SPARC-like protein 1
EIAAB47428 CAG repeat protein 1,CAGH1,CAS-interacting zinc finger protein,CIZ,Homo sapiens,Human,NMP4,Nuclear matrix protein 4,Nuclear matrix transcription factor 4,TNRC1,Trinucleotide repeat-containing gene 1 p
EIAAB45178 Mouse,Mus musculus,Ucma,Unique cartilage matrix-associated protein,Upper zone of growth plate and cartilage matrix associated protein
EIAAB12386 ECM2,Extracellular matrix protein 2,Homo sapiens,Human,Matrix glycoprotein SC1_ECM2
A 1009AG.2 Matrix Gla Protein (MGP) antigen: human Matrix Gla Protein (aa 3-15) 1 mg
A 1009AG.1 Matrix Gla Protein (MGP) antigen: human Matrix Gla Protein (aa 3-15) 100
EIAAB47429 Cas-associated zinc finger protein,Ciz,Nmp4,Nuclear matrix protein 4,Nuclear matrix transcription factor 4,Rat,Rattus norvegicus,Zfp384,Zinc finger protein 384,Znf384
MCA2860 MOUSE ANTI INFLUENZA B MATRIX PROTEIN M1, Product Type Monoclonal Antibody, Specificity INFLUENZA B MATRIX PROTEIN M1, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Applicati 0.2 mg
SCH-MCA401 MOUSE ANTI INFLUENZA A MATRIX PROTEIN, Product Type Monoclonal Antibody, Specificity INFLUENZA A MATRIX PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Applications I 1 mg
MCA401 MOUSE ANTI INFLUENZA A MATRIX PROTEIN, Product Type Monoclonal Antibody, Specificity INFLUENZA A MATRIX PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Applications I 1 mg
SCH-OBT0849 MOUSE ANTI INFLUENZA B MATRIX PROTEIN, Product Type Monoclonal Antibody, Specificity INFLUENZA B MATRIX PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Applications C 0.1 mg
OBT0849 MOUSE ANTI INFLUENZA B MATRIX PROTEIN, Product Type Monoclonal Antibody, Specificity INFLUENZA B MATRIX PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Applications C 0.1 mg
SCH-MCA2860 MOUSE ANTI INFLUENZA B MATRIX PROTEIN M1, Product Type Monoclonal Antibody, Specificity INFLUENZA B MATRIX PROTEIN M1, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Applicati 0.2 mg
U2078h CLIA kit Dentin matrix acidic phosphoprotein 1,Dentin matrix protein 1,DMP1,DMP-1,Homo sapiens,Human 96T
E2078h ELISA Dentin matrix acidic phosphoprotein 1,Dentin matrix protein 1,DMP1,DMP-1,Homo sapiens,Human 96T
U2078h CLIA Dentin matrix acidic phosphoprotein 1,Dentin matrix protein 1,DMP1,DMP-1,Homo sapiens,Human 96T

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1438: Influenza A virus infection
WP1049: G Protein Signaling Pathways
WP1060: Matrix Metalloproteinases
WP1165: G Protein Signaling Pathways
WP1176: Matrix Metalloproteinases
WP129: Matrix Metalloproteinases
WP1371: G Protein Signaling Pathways
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[cas9 csn1 SPy_1046] CRISPR-associated endonuclease Cas9/Csn1 (EC 3.1.-.-) (SpCas9) (SpyCas9)
[M] Matrix protein 1 (M1)
[M] Matrix protein 1 (M1)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] M1-1 protoxin (Killer toxin K1) [Cleaved into: M1-1 delta chain; M1-1 alpha chain; M1-1 gamma immunity chain; M1-1 beta chain]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] M1 family aminopeptidase (EC 3.4.11.-) (Pfa-M1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[MBM_07953] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[GLRG_10163] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[hchA BTN44_09930 EP54_12995 EQ90_07165 M1K003_2012 NCTC10654_00648 NCTC11940_00515 NCTC13131_01033 NCTC13196_00644 RK64_03380] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[APM1 At4g33090 F4I10_20] Aminopeptidase M1 (EC 3.4.11.2) (Alpha-aminoacylpeptide hydrolase)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[P] Phosphoprotein (Protein P) (Protein M1)
[nnrD nnrE DU31_11450 DU33_17155 DU34_07685 DU35_07085 DU36_09790 DU37_12565 DU38_10935 DU39_12815 DU40_12880 DU41_14740 DU42_07270 DU44_01295 DU45_16155 DU46_10990 DU47_01255 DU48_07720 DU49_14655 DU50_12285 DU51_19805 DU54_00670 DU55_05370 DU56_15760 DU57_06830 DU59_03855 DU60_14595 DU61_11015 DU62_06475 DU63_06395 DU64_18510 DU65_03810 DU66_17325 DU68_15815 DU69_04530 DU71_00795 DU72_19440 DU73_09980 DU74_18275 DU75_11940 DU76_10140 DU77_00515 DU78_12025 DU79_00590 DU80_09755 DU81_02350 DU82_01250 DU83_01980 DU84_01080 DU85_13135 DU86_12110 DU88_12415] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[RRM1 RR1] Ribonucleoside-diphosphate reductase large subunit (EC 1.17.4.1) (Ribonucleoside-diphosphate reductase subunit M1) (Ribonucleotide reductase large subunit)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]

Bibliography :
[30872764] Super-resolution microscopy reveals significant impact of M2e-specific monoclonal antibodies on influenza A virus filament formation at the host cell surface.
[30825230] Molecular profile of ultrastructure changes of the ligamentum flavum related to lumbar spinal canal stenosis.
[30692667] Influenza virus uses transportin 1 for vRNP debundling during cell entry.
[30669292] Simultaneous Quantitation of a Novel α₁/β₁-Blocker TJ0711 and Its Two Metabolites in Dog Plasma Using LC-MS/MS and Its Application to a Pharmacokinetic Study after Intravenous Infusion.
[30666253] Protective Immunity Induced by Incorporating Multiple Antigenic Proteins of Into Influenza Virus-Like Particles.
[30655797] Lentiviral RNA interference-mediated downregulation of Forkhead box M1 expression suppresses growth of oral squamous cell carcinoma .
[30597671] Three-dimensional nanofibrous polystyrene scaffolds modify macrophage phenotypes and activate macrophage angiogenic potential.
[30595182] Thrombospondin 1 Is Increased in the Aorta and Plasma of Patients With Acute Aortic Dissection.
[30582811] Energetic Fingerprinting of Ligand Binding to Paralogous Proteins: The Case of the Apoptotic Pathway.
[30559459] SOX9 regulated matrix proteins are increased in patients serum and correlate with severity of liver fibrosis.