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Search results 1801 to 1900 out of 2368 for Tpr

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Type Details Score
Protein
A0A140LI57
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
A2AIV3
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: false
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Protein
A2ALS2
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: true
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Protein
A8IK50
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
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Protein
F6TP19
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
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Protein
Q3UR12
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Publication
15612916 | -
First Author: Carbonnelle E
Year: 2005
Journal: Mol Microbiol
Title: Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function.
Volume: 55
Issue: 1
Pages: 54-64
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Publication
9418847 | -
First Author: Arrebola R
Year: 1998
Journal: Mol Cell Biol
Title: Tau91, an essential subunit of yeast transcription factor IIIC, cooperates with tau138 in DNA binding.
Volume: 18
Issue: 1
Pages: 1-9
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Publication
21784982 | -
First Author: Zeytuni N
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly.
Volume: 108
Issue: 33
Pages: E480-7
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Publication
23818233 | -
First Author: Wagner JM
Year: 2014
Journal: Proteins
Title: Crystal structure of the N-terminal domain of EccA? ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis.
Volume: 82
Issue: 1
Pages: 159-63
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Publication
21612577 | -
First Author: von Loeffelholz O
Year: 2011
Journal: Biochem J
Title: OEP61 is a chaperone receptor at the plastid outer envelope.
Volume: 438
Issue: 1
Pages: 143-53
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Publication
22899711 | -
First Author: Schweiger R
Year: 2012
Journal: J Cell Sci
Title: AtTPR7 is a chaperone-docking protein of the Sec translocon in Arabidopsis.
Volume: 125
Issue: Pt 21
Pages: 5196-207
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Publication
27932497 | -
First Author: Hirano T
Year: 2017
Journal: Mol Biol Cell
Title: Intraflagellar transport-A complex mediates ciliary entry and retrograde trafficking of ciliary G protein-coupled receptors.
Volume: 28
Issue: 3
Pages: 429-439
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Publication
29191911 | -
First Author: Wang X
Year: 2017
Journal: Science
Title: 3.9 ? structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP.
Volume: 358
Issue: 6367
Pages: 1206-1209
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Publication
27097373 | -
First Author: Lau WC
Year: 2016
Journal: Cell Cycle
Title: Structure of the human dimeric ATM kinase.
Volume: 15
Issue: 8
Pages: 1117-24
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Publication
26678875 | -
First Author: Aylett CH
Year: 2016
Journal: Science
Title: Architecture of human mTOR complex 1.
Volume: 351
Issue: 6268
Pages: 48-52
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Publication
27072897 | -
 
First Author: Bareti? D
Year: 2016
Journal: Nat Commun
Title: Tor forms a dimer through an N-terminal helical solenoid with a complex topology.
Volume: 7
Pages: 11016
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Publication
12640452 | -
First Author: O'Driscoll M
Year: 2003
Journal: Nat Genet
Title: A splicing mutation affecting expression of ataxia-telangiectasia and Rad3-related protein (ATR) results in Seckel syndrome.
Volume: 33
Issue: 4
Pages: 497-501
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Publication
9111320 | -
First Author: Smith JJ
Year: 1997
Journal: Mol Cell Biol
Title: The peroxin Pex17p of the yeast Yarrowia lipolytica is associated peripherally with the peroxisomal membrane and is required for the import of a subset of matrix proteins.
Volume: 17
Issue: 5
Pages: 2511-20
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Publication
25936803 | -
First Author: Stelter P
Year: 2015
Journal: Mol Cell
Title: Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension.
Volume: 58
Issue: 5
Pages: 854-62
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Protein Domain
IPR053319 | OEP61
Type: Family
Description: Outer envelope protein 61 is involved in protein import into the endoplasmic reticulum and chloroplasts. It is thought to act as chaperone docking proteins during post-translational protein translocation into the ER. It also implicated in chaperone-mediated targeting of proteins to chloroplasts, interacting specifically with chloroplast precursors to facilitate their delivery to the chloroplast translocase. The TPR region within this protein is essential for interaction with HSP70-1, and the linker domain is crucial for the selective recognition of chloroplast precursor complexes, distinguishing it from mitochondrial precursors [, ].
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Protein Domain
IPR063281 | ACL4_C
Type: Domain
Description: This entry represents the C-terminal domain of ACL4 (Assembly chaperone of RPL4). ACL4 acts as a chaperone for the L4 ribosomal subunit encoded by RPL4A and RPL4B, required for hierarchical ribosome assembly []. The protein shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present. The full-length protein contains N-terminal TPR repeats and is distributed throughout the cell but enriched in the nucleus. The specific function of this C-terminal domain remains to be determined.
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Protein Domain
IPR063140 | RMD9_N
Type: Domain
Description: This entry represents the N-terminal mitochondrial transit peptide TPR domain found in RMD9 proteins from ascomycetes. RMD9 is an RNA-binding protein that localisesto the mitochondrial inner membrane and binds the 3'-UTR of mitochondrial mRNAs []. The transit peptide directs the protein to the mitochondrial matrix where it is cleaved off during import. The peptide varies in length from 12 residues in Eremothecium gossypii to 108 residues in Debaryomyces hansenii. The mature protein following transit peptide cleavage is involved in mitochondrial mRNA processing and stability. RMD9 proteins function as monomers and phosphorylation promotes RNA binding activity.
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Protein Domain
IPR005631 | SDH
Type: Family
Description: This family includes the highly conserved mitochondrial and bacterial proteins Sdh5/SDHAF2/SdhE.Both yeast and human Sdh5/SDHAF2 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Mutational inactivation of Sdh5 confers tumor susceptibility in humans [].This family was previously annotated in Pfam as being a divergent TPR repeat but structural evidence has indicated this is not true.
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Protein Domain
IPR063506 | ECM9_middle
Type: Domain
Description: This entry represents the middle domain of protein ECM9. This domain contains a TPR fold. This domain is also present in proteins annotated as Protein prenylyltransferase in fungi.ECM9 proteins are involved in cell wall organisation and biogenesis in fungi []. The proteins belong to the protein prenylyltransferase superfamily and show similarity to Rab-protein geranylgeranyltransferase complex components. ECM9 is found in the cytoplasm and is associated with endoplasmic reticulum to Golgi vesicle-mediated transport processes. The protein is present at approximately 846 molecules per cell during log phase growth.
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Protein Domain
IPR063902 | SUV2_C
Type: Domain
Description: This entry represents the C-terminal TPR domain of the SUV2 protein found in plants. The specific function of this C-terminal domain remains to be determined.SUV2 is a DNA damage response protein required for tolerance to various DNA-damaging agents and cell cycle checkpoint control. The full-length protein contains a nuclear localisation signal and coiled-coil region in this N-terminal domain, followed by a C-terminal phosphatase tensin-type domain. SUV2 functions in G2/M cell cycle arrest in response to DNA damage and aluminium-dependent root growth inhibition [, ].
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Protein Domain
IPR040478 | FKBP_N_2
Type: Domain
Description: This is the N-terminal domain of the beta chain found in Drosophila melanogaster protein Protein Bride of doubletime (also known as BDBT, a FK506-Binding Protein) which stimulates the DBT circadian function. The domain contains the DBT-binding site. The domain is structurally homologous to the peptidyl prolyl isomerase (PPIase) regions of FK506-binding proteins despite low sequence homology. BDBT is structurally related to the immunophilin FKBP51 and it shares a common domain organisation consisting of PPIase-like and TPR domains with non-canonical immunophilins such as FKBP38 or FKBPL [].
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Protein Domain
IPR049078 | T7SS_EccA1-like_N
Type: Domain
Description: This domain is found at the N-terminal end of ESX-1 secretion system protein EccA1 from Mycobacterium tuberculosis () and similar proteins predominantly from Actinobacteria. EccA1 is part of the ESX-1 specialised secretion system (a cluster of the type VII secretion system, T7SS). EccA1 contains a C-terminal ATPase domain (and ) and a tetratricopeptide repeat (TPR) containing N-terminal domain, represented in this entry. The six tandem TPR motifs of this domain, packed in parallel, create a series of repeating antiparallel ��-helices that give rise to an overall superhelix structure () [, ].
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Protein Domain
IPR049132 | FAN1-like_euk
Type: Family
Description: Fanconi-associated nuclease 1 (FAN1) is a DNA structure-specific nuclease involved in the processing of DNA interstrand crosslinks (ICLs). It maintains genomic stability and prevents tissue decline in several organs. This protein possesses preferential endonuclease activity toward 5' flap structures. FAN1 is present in most eukaryotes and some bacterial sequences. It consists of four characterised domains: UBZ, SAP, TPR and VRR nuclease (). However, monocellular eukaryote and bacterial homologues lack the UBZ domain []. The N-terminal helical domain of FAN1 can be subdivided in a winged-helix (WH) DNA-binding domain, represented in this entry, and a SAP domain (bacterial and eukaryotic ) [, , , , ].
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Protein Domain
IPR035625 | Tfc3-like_eWH
Type: Domain
Description: Tfc3 (also known as Tau138) is one of three subunits of the tauB subcomplex of yeast transcription factor IIIC. This extended winged-helix domain of tau138 appears to interact with the TPR (tetratricopeptide repeat) array of tauA subunit tau131, and may therefore play a role in linking tauA, tauB, and TFIIIB to regulate the formation of the RNA polymerase III pre-initiation complex [, ].Proteins containing this domain also include mammalian general transcription factor 3C polypeptide 1 (Gtf3c1), which is a transcription factor IIIC box B binding subunit [].
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Protein Domain
IPR056939 | Znf_RING_Vps8
Type: Domain
Description: Vps8 is one of the Golgi complex components necessary for vacuolar sorting. It is the core component of the endosomal tethering complex CORVET (class C core vacuole/endosome tethering). Vps8 co-operates with Vps21-GTP to mediate endosomal clustering in a reaction that is dependent on Vps3. Vps8 is the only CORVET subunit that is enriched on late endosomes, suggesting that it is a marker for the maturation of late endosomes []. These proteins consist of a ��-propeller at the N-terminal followed by a long, central TPR domain and a RING zinc finger at the C-terminal. This entry represents the RING zinc finger found in Vps8 from mammals and similar sequences mainly found in vertebrates.
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Protein Domain
IPR059219 | Pex8_N
Type: Domain
Description: This domain is found towards the N-terminal end of the Peroxisomal biogenesis factor 8 protein (PEX8), Peroxisomal membrane protein PEX17 and related proteins from fungal species. PEX17 is involved in peroxisome biosynthesis. This protein is required for the import of a subset of matrix proteins into peroxisomes []. PEX8 is essential component of the machinery required for the import of both PTS1 and PTS2 (and perhaps all) peroxisomal matrix proteins []. Binding of PEX8 to the N terminus of PEX5 cargo receptor induces a conformational change of the TPR domains and decrease their binding affinity to cargo, facilitating the release of the PTS1 proteins within the peroxisome [].
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Protein Domain
IPR056152 | Beta-prop_IFT122_2nd
Type: Domain
Description: This entry represents the second ��-propeller of IFT122, which is a crucial subunit for IFT-A integrity [].Intraflagellar transport protein 122 homolog (IFT122) is one of the core components (together with WDR19/IFT144 and IFT140) of the IFT-A complex which is required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), being involved in cilia function and/or assembly [, ]. IFT-A polymerises interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins [].
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Protein Domain
IPR056155 | Beta-prop_IFT140_2nd
Type: Domain
Description: This entry represents the second ��-propeller of IFT140.IFT140 is one of the core components (together with WDR19/IFT144 and IFT122) of the IFT-A complex which is required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), being involved in cilia function and/or assembly [, ]. IFT-A polymerises interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins []. The ��-propeller domains of IFT140 contact the ��-propeller domains of IFT121 from the adjacent complex [].
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Protein Domain
IPR056154 | Beta-prop_IFT140_1st
Type: Domain
Description: This entry represents the first ��-propeller of IFT140.IFT140 is one of the core components (together with WDR19/IFT144 and IFT122) of the IFT-A complex which is required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), being involved in cilia function and/or assembly [, ]. IFT-A polymerises interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins []. The ��-propeller domains of IFT140 contact the ��-propeller domains of IFT121 from the adjacent complex [].
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Protein Domain
IPR046924 | CATASP
Type: Domain
Description: This is a small, rapidly-evolving domain predicted to possess a compact, four-helix structure. Along with a gene encoding a TPR repeat region fused to a CASPASE domain and a gene encoding the CATRA module (CATRA-N CATRA-C) C-terminally fused to a diverse range of conflict effector domains, forms the three gene island making up the CATRA conflict systems. Plays a possible inhibitory role in the CATRA system which is relieved upon sensing of an invasive molecule or is directly cleaved by the CASPASE domain [].
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Protein Domain
IPR056803 | ATR-like_N-HEAT
Type: Domain
Description: This region of HEAT repeats is found in human Serine/threonine-protein kinase ATR and similar proteins from vertebrates. This entry represents the N-HEAT region.ATR acts as a DNA damage sensor and is associated with severe disorders such as Seckel syndrome 1. This protein is organised into a large N-terminal ��-solenoid containing HEAT repeats, a FAT (FRAP, ATM, TRRAP) domain (), a kinase domain (), and a C-terminal short segment referred to as FATC (). N-terminal part has two continuous HEAT repeat regions, the N-HEAT and the M-HEAT. The FAT domain contains TPR (tetratricopeptide) repeats followed by a HEAT repeat domain [].
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Protein Domain
IPR056838 | Zn_ribbon_IFT122
Type: Domain
Description: This zinc ribbon domain is found in the human Intraflagellar transport protein 122 homolog (IFT122) and related animal proteins. IFT122 contains two zinc ribbon domains toward the C-terminal. This one is the first of the pair.Intraflagellar transport protein 122 homolog (IFT122) is one of the core components (together with WDR19/IFT144 and IFT140) of the IFT-A complex which is required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), being involved in cilia function and/or assembly [, ]. IFT-A polymerises interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins [].
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Protein Domain
IPR052628 | CFAP70
Type: Family
Description: This family of proteins is involved in the structural and functional organization of cilia and flagella. Members of this family are axoneme-binding proteins that contribute to the regulation of ciliary and flagellar motility, as well as the determination of cilium length. While the conserved TPR domains within these proteins are not essential for ciliary targeting, the N-terminal region is crucial for proper localization to cilia and/or interaction with the axoneme structure. These proteins are implicated in the regulation of the outer dynein arm, which is a critical component for the movement of cilia and flagella.
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Protein Domain
IPR057564 | HEAT_ATR
Type: Domain
Description: This region of HEAT repeats is found towards the C-terminal of the FAT domain in human Serine/threonine-protein kinase ATR and similar eukaryotic proteins.ATR acts as a DNA damage sensor and is associated with severe disorders such as Seckel syndrome 1. This protein is organised into a large N-terminal ��-solenoid containing HEAT repeats, a FAT (FRAP, ATM, TRRAP) domain (), a kinase domain (), and a C-terminal short segment referred to as FATC (). N-terminal part has two continuous HEAT repeat regions, the N-HEAT and the M-HEAT. The FAT domain contains TPR (tetratricopeptide) repeats followed by a HEAT repeat domain [].
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Protein Domain
IPR057855 | Beta-prop_WDR19_1st
Type: Domain
Description: This entry represents the first ��-propeller of WRD19 (also known as IFT144) from animals and the orthologue from C.elegans DYF2. This domain is also found in the WD repeat-containing protein 39-A/B from Salmo salar.WDR19 is a core component of the IFT complex A (IFT-A, together with IFT140 and IFT122), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), being involved in cilia function and/or assembly [, ]. IFT-A polymerises interacts with IFT-B, and uses an array of ��-propeller and TPR domains to create 'carriages' of the IFT train that engage TULP adaptor proteins [].
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Publication
2140597 | J:10525
First Author: Capetanaki Y
Year: 1990
Journal: Oncogene
Title: Mouse vimentin: structural relationship to fos, jun, CREB and tpr.
Volume: 5
Issue: 5
Pages: 645-55
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Publication
12719437 | J:385615
First Author: Blumer JB
Year: 2003
Journal: J Biol Chem
Title: Interaction of activator of G-protein signaling 3 (AGS3) with LKB1, a serine/threonine kinase involved in cell polarity and cell cycle progression: phosphorylation of the G-protein regulatory (GPR) motif as a regulatory mechanism for the interaction of GPR motifs with Gi alpha.
Volume: 278
Issue: 26
Pages: 23217-20
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Publication
10100923 | J:53877
First Author: Melo LG
Year: 1999
Journal: Regul Pept
Title: Chronic hypertension in ANP knockout mice: contribution of peripheral resistance.
Volume: 79
Issue: 2-3
Pages: 109-15
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Publication
11290414 | J:68891
First Author: Chaudhuri M
Year: 2001
Journal: Gene
Title: Cloning and characterization of a novel serine/threonine protein phosphatase type 5 from Trypanosoma brucei.
Volume: 266
Issue: 1-2
Pages: 1-13
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Publication
12482845 | J:82139
First Author: Odunuga OO
Year: 2003
Journal: J Biol Chem
Title: Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.
Volume: 278
Issue: 9
Pages: 6896-904
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Publication
15284070 | J:95760
First Author: Walsh EK
Year: 2004
Journal: Am J Physiol Heart Circ Physiol
Title: Control of myocardial oxygen consumption in transgenic mice overexpressing vascular eNOS.
Volume: 287
Issue: 5
Pages: H2115-21
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Publication
23539217 | J:218875
First Author: He J
Year: 2013
Journal: Arterioscler Thromb Vasc Biol
Title: Liver kinase B1 is required for thromboxane receptor-dependent nuclear factor-?B activation and inflammatory responses.
Volume: 33
Issue: 6
Pages: 1297-305
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Publication
12752376 | J:84411
First Author: Wang Y
Year: 2003
Journal: Eur J Neurosci
Title: A hot spot for hotfoot mutations in the gene encoding the delta2 glutamate receptor.
Volume: 17
Issue: 8
Pages: 1581-90
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Protein
P12672
Organism: Mus musculus/domesticus
Length: 412  
Fragment?: false
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Protein
Q80VA5
Organism: Mus musculus/domesticus
Length: 1289  
Fragment?: false
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Protein
Q6NZL6
Organism: Mus musculus/domesticus
Length: 1363  
Fragment?: false
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Protein
G3UW83
Organism: Mus musculus/domesticus
Length: 1363  
Fragment?: false
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Protein
A2AFX4
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
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Protein
A2AFX6
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
F8VPP8
Organism: Mus musculus/domesticus
Length: 982  
Fragment?: false
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Protein
A0A494B911
Organism: Mus musculus/domesticus
Length: 1228  
Fragment?: false
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Protein
F6U4F1
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: true
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Protein
G3X9F6
Organism: Mus musculus/domesticus
Length: 1346  
Fragment?: false
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Protein
Q3TBH5
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: true
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Protein
Q3TD36
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: true
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Protein
Q3TXV8
Organism: Mus musculus/domesticus
Length: 1346  
Fragment?: false
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Protein
Q3UDI4
Organism: Mus musculus/domesticus
Length: 1346  
Fragment?: false
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Protein
Q3UPD8
Organism: Mus musculus/domesticus
Length: 1228  
Fragment?: false
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Protein
Q8R1A5
Organism: Mus musculus/domesticus
Length: 1150  
Fragment?: true
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Protein
P28663
Organism: Mus musculus/domesticus
Length: 298  
Fragment?: false
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Protein
P54729
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
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Protein
P61202
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
P61406
Organism: Mus musculus/domesticus
Length: 1418  
Fragment?: false
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Protein
Q3V1T4
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: false
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Protein
Q8BG32
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q8C0T9
Organism: Mus musculus/domesticus
Length: 1614  
Fragment?: false
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Protein
Q8CG70
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: false
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Protein
Q8CG71
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
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Protein
Q8R3K3
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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Protein
Q9DB05
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
A2BGJ5
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
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Protein
O89079
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
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Protein
P63154
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
Q6W3F0
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
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Protein
Q8BK72
Organism: Mus musculus/domesticus
Length: 415  
Fragment?: false
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Protein
Q9CWZ7
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
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Protein
Q5SW19
Organism: Mus musculus/domesticus
Length: 1315  
Fragment?: false
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Protein
Q99LI7
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
E9Q9T4
Organism: Mus musculus/domesticus
Length: 1609  
Fragment?: false
•
•
•
•
•
Protein
E9Q7B0
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
•
•
•
•
•
Protein
H7BX23
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
•
•
•
•
•
Protein
Q3TTT2
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
•
•
•
•
•
Protein
A0A0G2JGQ4
Organism: Mus musculus/domesticus
Length: 638  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J140
Organism: Mus musculus/domesticus
Length: 1353  
Fragment?: false
•
•
•
•
•
Protein
A0A494BA20
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
•
•
•
•
•
Protein
A0A494BAE3
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
•
•
•
•
•
Protein
A0A494BAX2
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: false
•
•
•
•
•
Protein
A2A7Q5
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: false
•
•
•
•
•
Protein
A6PW84
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
•
•
•
•
•
Protein
B9EJT6
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
•
•
•
•
•
Protein
D3Z315
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: true
•
•
•
•
•
Protein
D3Z4B2
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: true
•
•
•
•
•
Protein
E9Q6I5
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
•
•
•
•
•
Protein
F6XIG5
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
•
•
•
•
•




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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom