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Search results 901 to 1000 out of 1029 for Tcp1

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Type Details Score
Publication
9636156 | J:48267
First Author: Furumura M
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: Characterization of genes modulated during pheomelanogenesis using differential display.
Volume: 95
Issue: 13
Pages: 7374-8
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Publication
10336634 | J:55368
First Author: Kubota H
Year: 1999
Journal: Eur J Biochem
Title: Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits.
Volume: 262
Issue: 2
Pages: 492-500
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Publication
27561680 | J:241613
 
First Author: Guo X
Year: 2016
Journal: Nat Commun
Title: VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington's disease.
Volume: 7
Pages: 12646
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Publication
23872636 | J:205312
First Author: Tarkar A
Year: 2013
Journal: Nat Genet
Title: DYX1C1 is required for axonemal dynein assembly and ciliary motility.
Volume: 45
Issue: 9
Pages: 995-1003
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Publication
12383505 | J:79580
First Author: Le Bras S
Year: 2002
Journal: Gene
Title: Transcript map of the Ovum mutant (Om) locus: isolation by exon trapping of new candidate genes for the DDK syndrome.
Volume: 296
Issue: 1-2
Pages: 75-86
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Publication
36792666 | J:333810
First Author: Elenbaas JS
Year: 2023
Journal: Nat Commun
Title: SVEP1 is an endogenous ligand for the orphan receptor PEAR1.
Volume: 14
Issue: 1
Pages: 850
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Publication
24788519 | J:211289
First Author: Fantauzzo KA
Year: 2014
Journal: Genes Dev
Title: PI3K-mediated PDGFRα signaling regulates survival and proliferation in skeletal development through p53-dependent intracellular pathways.
Volume: 28
Issue: 9
Pages: 1005-17
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Publication
11461004 | J:74152
First Author: Yamaza H
Year: 2001
Journal: Int J Dev Biol
Title: Detection of differentially expressed genes in the early developmental stage of the mouse mandible.
Volume: 45
Issue: 4
Pages: 675-80
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Publication
31201419 | J:279039
First Author: Lu Y
Year: 2019
Journal: Biol Reprod
Title: CRISPR/Cas9-mediated genome editing reveals 30 testis-enriched genes dispensable for male fertility in mice†.
Volume: 101
Issue: 2
Pages: 501-511
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Publication
12174196 | J:83520
 
First Author: Fuchs S
Year: 2002
Journal: BMC Genet
Title: Comparative transcription map of the wobbler critical region on mouse chromosome 11 and the homologous region on human chromosome 2p13-14.
Volume: 3
Pages: 14
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Publication
14706451 | J:87785
First Author: Karim SA
Year: 2004
Journal: Genomics
Title: A physical map of the genomic region on mouse chromosome 3 containing the hindshaker (hsh) mutation.
Volume: 83
Issue: 2
Pages: 225-30
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Publication
20516061 | J:168381
First Author: Lee JH
Year: 2010
Journal: J Biol Chem
Title: Identification and characterization of a novel human PP1 phosphatase complex.
Volume: 285
Issue: 32
Pages: 24466-76
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Publication
26442671 | J:285847
 
First Author: Merkulova M
Year: 2015
Journal: Sci Rep
Title: Mapping the H(+) (V)-ATPase interactome: identification of proteins involved in trafficking, folding, assembly and phosphorylation.
Volume: 5
Pages: 14827
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Publication
2896675 | J:9168
First Author: Andersson L
Year: 1988
Journal: J Hered
Title: Genetic polymorphism of a bovine t-complex gene (TCP1) linkage to major histocompatibility genes.
Volume: 79
Issue: 1
Pages: 1-5
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Publication
8733136 | J:32925
First Author: Morrison K
Year: 1996
Journal: Hum Mol Genet
Title: Genetic mapping of the human homologue (T) of mouse T(Brachyury) and a search for allele association between human T and spina bifida.
Volume: 5
Issue: 5
Pages: 669-74
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Publication
22160715 | J:180143
First Author: Lu J
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Histone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher disease.
Volume: 108
Issue: 52
Pages: 21200-5
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Publication
- | J:175597
     
First Author: Overbeek PA
Year: 2011
Journal: MGI Direct Data Submission
Title: Direct Data Submission for Overbeek Lentiviral Transgenic Lines
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Publication
15703188 | J:98076
First Author: Cai J
Year: 2005
Journal: Hum Mol Genet
Title: Gene expression in pharyngeal arch 1 during human embryonic development.
Volume: 14
Issue: 7
Pages: 903-12
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Publication
22421546 | J:185743
First Author: Cotney J
Year: 2012
Journal: Genome Res
Title: Chromatin state signatures associated with tissue-specific gene expression and enhancer activity in the embryonic limb.
Volume: 22
Issue: 6
Pages: 1069-80
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Publication
32541003 | J:291493
 
First Author: Najas S
Year: 2020
Journal: Development
Title: A SMAD1/5-YAP signalling module drives radial glia self-amplification and growth of the developing cerebral cortex.
Volume: 147
Issue: 13
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Protein Domain
IPR012717 | Chap_CCT_delta
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Protein Domain
IPR012716 | Chap_CCT_beta
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Protein Domain
IPR012715 | Chap_CCT_alpha
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT alpha subunit (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Protein Domain
IPR012719 | Chap_CCT_gamma
Type: Family
Description: Proteins in this entry consist exclusively of the CCT gamma chain from animals, plants, fungi, and other eukaryotes.Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].
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Protein Domain
IPR012718 | Chap_CCT_epsi
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Protein Domain
IPR012722 | Chap_CCT_zeta
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Protein Domain
IPR012721 | Chap_CCT_theta
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT theta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Protein Domain
IPR012720 | Chap_CCT_eta
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
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Publication
1352040 | -
First Author: Hemmingsen SM
Year: 1992
Journal: Nature
Title: What is a chaperonin?
Volume: 357
Issue: 6380
Pages: 650
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Publication
1352857 | -
First Author: Ellis J
Year: 1992
Journal: Nature
Title: Protein folding. Cytosolic chaperonin confirmed.
Volume: 358
Issue: 6383
Pages: 191
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Publication
1630492 | -
First Author: Lewis VA
Year: 1992
Journal: Nature
Title: T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol.
Volume: 358
Issue: 6383
Pages: 249-52
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Publication
7846767 | J:21876
First Author: Kim S
Year: 1994
Journal: Trends Biochem Sci
Title: Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.
Volume: 19
Issue: 12
Pages: 543-8
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Publication
20194787 | -
First Author: Cong Y
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Volume: 107
Issue: 11
Pages: 4967-72
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Publication
18595008 | -
First Author: Brackley KI
Year: 2009
Journal: Cell Stress Chaperones
Title: Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation.
Volume: 14
Issue: 1
Pages: 23-31
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Publication
15027029 | -
First Author: Gómez-Puertas P
Year: 2004
Journal: J Mol Recognit
Title: The substrate recognition mechanisms in chaperonins.
Volume: 17
Issue: 2
Pages: 85-94
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Publication
11340060 | -
 
First Author: Thirumalai D
Year: 2001
Journal: Annu Rev Biophys Biomol Struct
Title: Chaperonin-mediated protein folding.
Volume: 30
Pages: 245-69
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Publication
10753735 | -
First Author: Leroux MR
Year: 2000
Journal: Curr Biol
Title: Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.
Volume: 10
Issue: 7
Pages: R260-4
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Publication
10550210 | -
First Author: Gutsche I
Year: 1999
Journal: J Mol Biol
Title: Group II chaperonins: new TRiC(k)s and turns of a protein folding machine.
Volume: 293
Issue: 2
Pages: 295-312
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Publication
11580264 | -
First Author: Steinbacher S
Year: 2001
Journal: J Struct Biol
Title: Review: nucleotide binding to the thermoplasma thermosome: implications for the functional cycle of group II chaperonins.
Volume: 135
Issue: 2
Pages: 147-56
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Publication
12354605 | -
First Author: Valpuesta JM
Year: 2002
Journal: FEBS Lett
Title: Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.
Volume: 529
Issue: 1
Pages: 11-6
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Publication
14651920 | J:86843
First Author: Easterday MC
Year: 2003
Journal: Dev Biol
Title: Neural progenitor genes. Germinal zone expression and analysis of genetic overlap in stem cell populations.
Volume: 264
Issue: 2
Pages: 309-22
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Publication
- | J:279207
     
First Author: Mager J
Year: 2019
Journal: MGI Direct Data Submission
Title: A Catalog of Early Lethal KOMP Phenotypes
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Publication
11172053 | J:67552
First Author: Jiang CH
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: The effects of aging on gene expression in the hypothalamus and cortex of mice.
Volume: 98
Issue: 4
Pages: 1930-4
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Publication
11044607 | J:65653
First Author: Wertz K
Year: 2000
Journal: Mech Dev
Title: Large-scale screen for genes involved in gonad development.
Volume: 98
Issue: 1-2
Pages: 51-70
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Protein Domain
IPR012714 | Thermosome_arc
Type: Family
Description: Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [, ]. Chaperonins are involved in productive folding of proteins []. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome []. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [], related to the cpn60/groEL chaperonin family (see ).The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place []. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle []with 6 to 8 other different, but homologous, subunits []. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [, , ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [, ].Thermosome (or cpn60) is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacteria), a toroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins []. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. TF55 from thermophilic bacteria is also included in this entry.
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Publication
23055941 | J:193640
First Author: Lo JC
Year: 2012
Journal: PLoS Genet
Title: RAB-like 2 has an essential role in male fertility, sperm intra-flagellar transport, and tail assembly.
Volume: 8
Issue: 10
Pages: e1002969
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Publication
11591653 | J:103507
First Author: Suzuki H
Year: 2001
Journal: Genome Res
Title: Protein-protein interaction panel using mouse full-length cDNAs.
Volume: 11
Issue: 10
Pages: 1758-65
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Protein
A0A1W2P6Q3
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
A0A1W2P871
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
A0A0N4SUI8
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein
A0A1W2P828
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
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Protein
Q8VEI1
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
A0A1W2P8B6
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Publication
16107646 | J:100324
First Author: Bulfone A
Year: 2005
Journal: J Neurosci
Title: Telencephalic embryonic subtractive sequences: a unique collection of neurodevelopmental genes.
Volume: 25
Issue: 33
Pages: 7586-600
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Publication
12466855 | J:80501
First Author: Gitton Y
Year: 2002
Journal: Nature
Title: A gene expression map of human chromosome 21 orthologues in the mouse.
Volume: 420
Issue: 6915
Pages: 586-90
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Publication
12466854 | J:80502
First Author: Reymond A
Year: 2002
Journal: Nature
Title: Human chromosome 21 gene expression atlas in the mouse.
Volume: 420
Issue: 6915
Pages: 582-6
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Protein
P80317
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
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Protein
P11983
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
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Protein
P80314
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
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Protein
P80315
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
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Protein
P80316
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
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Protein
P80318
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
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Protein
P80313
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
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Protein
P42932
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
•
•
•
•
•
Protein
Q61390
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q564F4
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
•
•
•
•
•
Protein
Q3THH8
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
•
•
•
•
•
Protein
Q3TI05
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q542X7
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
•
•
•
•
•
Protein
Q52KG9
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q3U4U6
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
•
•
•
•
•
Protein
Q9WVS5
Organism: Mus musculus/domesticus
Length: 547  
Fragment?: false
•
•
•
•
•
Protein
Q6A0F1
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: true
•
•
•
•
•
Protein
B1AT05
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: false
•
•
•
•
•
Protein
Q8BVT1
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: false
•
•
•
•
•
Protein
Q8C5Q5
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
•
•
•
•
•
Protein
E9Q133
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: false
•
•
•
•
•
Protein
Q497N0
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q3TII0
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
•
•
•
•
•
Protein
Q3TET0
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
•
•
•
•
•
Protein
G5E839
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: false
•
•
•
•
•
Protein
Q9JJD8
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
•
•
•
•
•
Protein
Q3TJN2
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
•
•
•
•
•
Protein
Q3TW97
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q3UJP4
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
•
•
•
•
•
Protein
Q3UJZ8
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
•
•
•
•
•
Protein
Q8BVY8
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
•
•
•
•
•
Protein
H3BL49
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
•
•
•
•
•
Protein
Q9CS06
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: true
•
•
•
•
•
Protein
Q3UDB1
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: true
•
•
•
•
•
Protein
Q3TI62
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q3TIX8
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
•
•
•
•
•
Protein
Q3UKQ2
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
•
•
•
•
•
Protein
Q3UIJ0
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P7B7
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
•
•
•
•
•
Protein
A0A0N4SV00
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
•
•
•
•
•
Protein
Q3TIJ7
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
•
•
•
•
•
Protein
Q3U0I3
Organism: Mus musculus/domesticus
Length: 521  
Fragment?: false
•
•
•
•
•
Protein
Q3UL22
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
•
•
•
•
•
Publication
- | J:342609
       
First Author: UniProt
Year: 2021
Title: Electronic Gene Ontology annotations created by ARBA machine learning models
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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