| Type |
Details |
Score |
| Protein Domain |
| Type: |
Domain |
| Description: |
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].The potyviridae are a family of positive strand RNA viruses, members of which include Zucchini yellow mosaic virus, and Turnip mosaic virus (strain Japanese) which cause considerable losses of crops worldwide.This entry represents a C-terminal region from various plant potyvirus P1 proteins (found at the N terminus of the polyprotein). The C terminus of P1 is a serine peptidase belonging to MEROPS peptidase family S30 (clan PA(S)). It is the protease responsible for autocatalytic cleavage between P1 and the helper component protease, which is a cysteine peptidase belonging to MEROPS peptidase family C6 [, ]. The P1 protein may be involved in virus-host interactions [], and evasion of immune responses []. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Potyviruses form one of the most numerous groups of plant viruses and are a major cause of crop loss worldwide. The helper-component proteinase (HC-Pro) is an indispensable, multifunctional protein of members of the genus Potyvirus and other viruses of the family Potyviridae. It is directly involved in diverse steps of viral infection, such as aphid plant-to-plant transmission, polyprotein processing, and suppression of host antiviral RNA silencing. HC-Pro is generally divided into three functional domains: a N-terminal domain, a central region, and a cysteine protease domain (CPD) in the C-terminal region. The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. Cysteine and histidine residues form the catalytic dyad at the active site. The HC-Pro CPD domain constitutes the peptidase family C6 of the CA clan [].The HC-Pro CPD domain adopts a compact oval-shaped alpha/beta fold. The secondary structure elements include four α-helices (alpha1-alpha4) and two short β-strands (beta1 and beta2) arranged in the order alpha1-alpha2-alpha3-beta1-beta2-alpha4. In addition, two 3(10) helices are located between alpha3 and beta1 and downstream of alpha4. The four helices form a helix bundle packed against one face of a short β-hairpin formed by strands beta1 and beta2. The catalytic residue Cys is located at the N terminus of helix alpha1, and the other catalytic residue His is located on strand beta2. The substrate binding cleft is lined by the loop connecting helices alpha2 and alpha3 and the N-terminal region of helix alpha1 on one side and by strand beta2 on the other side [].This superfamily represents the CPD domain of the HC-Pro protein. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the CPD domain of the HC-Pro protein. Potyviruses form one of the most numerous groups of plant viruses and are a major cause of crop loss worldwide. The helper-component proteinase (HC-Pro) is an indispensable, multifunctional protein of members of the genus Potyvirus and other viruses of the family Potyviridae. It is directly involved in diverse steps of viral infection, such as aphid plant-to-plant transmission, polyprotein processing, and suppression of host antiviral RNA silencing. HC-Pro is generally divided into three functional domains: a N-terminal domain, a central region, and a cysteine protease domain (CPD) in the C-terminal region. The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. Cysteine and histidine residues form the catalytic dyad at the active site. The HC-Pro CPD domain constitutes the peptidase family C6 of the CA clan [].The HC-Pro CPD domain adopts a compact oval-shaped alpha/beta fold. The secondary structure elements include four α-helices (alpha1-alpha4) and two short β-strands (beta1 and beta2) arranged in the order alpha1-alpha2-alpha3-beta1-beta2-alpha4. In addition, two 3(10) helices are located between alpha3 and beta1 and downstream of alpha4. The four helices form a helix bundle packed against one face of a short β-hairpin formed by strands beta1 and beta2. The catalytic residue Cys is located at the N terminus of helix alpha1, and the other catalytic residue His is located on strand beta2. The substrate binding cleft is lined by the loop connecting helices alpha2 and alpha3 and the N-terminal region of helix alpha1 on one side and by strand beta2 on the other side []. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
380
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
382
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
446
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
321
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
372
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
430
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
373
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
382
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Xue F |
| Year: |
1993 |
| Journal: |
Cell |
| Title: |
kelch encodes a component of intercellular bridges in Drosophila egg chambers. |
| Volume: |
72 |
| Issue: |
5 |
| Pages: |
681-93 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Way M |
| Year: |
1995 |
| Journal: |
J Cell Biol |
| Title: |
Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm. |
| Volume: |
128 |
| Issue: |
1-2 |
| Pages: |
51-60 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ito N |
| Year: |
1994 |
| Journal: |
J Mol Biol |
| Title: |
Crystal structure of a free radical enzyme, galactose oxidase. |
| Volume: |
238 |
| Issue: |
5 |
| Pages: |
794-814 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ito N |
| Year: |
1991 |
| Journal: |
Nature |
| Title: |
Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. |
| Volume: |
350 |
| Issue: |
6313 |
| Pages: |
87-90 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schughart K |
| Year: |
1988 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structure and expression of Hox-2.2, a murine homeobox-containing gene. |
| Volume: |
85 |
| Issue: |
15 |
| Pages: |
5582-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gulati GS |
| Year: |
2019 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Neogenin-1 distinguishes between myeloid-biased and balanced Hoxb5 + mouse long-term hematopoietic stem cells. |
| Volume: |
116 |
| Issue: |
50 |
| Pages: |
25115-25125 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ura K |
| Year: |
1991 |
| Journal: |
Nucleic Acids Res |
| Title: |
Possible role of DNA topoisomerase II on transcription of the homeobox gene Hox-2.1 in F9 embryonal carcinoma cells. |
| Volume: |
19 |
| Issue: |
22 |
| Pages: |
6087-92 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Münke M |
| Year: |
1986 |
| Journal: |
Cytogenet Cell Genet |
| Title: |
The murine Hox-2 cluster of homeo box containing genes maps distal on chromosome 11 near the tail-short (Ts) locus. |
| Volume: |
42 |
| Issue: |
4 |
| Pages: |
236-40 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Utset MF |
| Year: |
1987 |
| Journal: |
Science |
| Title: |
Region-specific expression of two mouse homeo box genes. |
| Volume: |
235 |
| Issue: |
4794 |
| Pages: |
1379-82 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Safaei R |
| Year: |
1997 |
| Journal: |
Brain Res Dev Brain Res |
| Title: |
A target of the HoxB5 gene from the mouse nervous system. |
| Volume: |
100 |
| Issue: |
1 |
| Pages: |
5-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hershko AY |
| Year: |
2003 |
| Journal: |
Gene |
| Title: |
Methylation of HoxA5 and HoxB5 and its relevance to expression during mouse development. |
| Volume: |
302 |
| Issue: |
1-2 |
| Pages: |
65-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Holland PW |
| Year: |
1988 |
| Journal: |
Development |
| Title: |
Spatially restricted patterns of expression of the homeobox-containing gene Hox 2.1. during mouse embryogenesis. |
| Volume: |
102 |
| Issue: |
1 |
| Pages: |
159-74 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Munton RP |
| Year: |
2007 |
| Journal: |
Mol Cell Proteomics |
| Title: |
Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. |
| Volume: |
6 |
| Issue: |
2 |
| Pages: |
283-93 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Boj SF |
| Year: |
2012 |
| Journal: |
Cell |
| Title: |
Diabetes risk gene and Wnt effector Tcf7l2/TCF4 controls hepatic response to perinatal and adult metabolic demand. |
| Volume: |
151 |
| Issue: |
7 |
| Pages: |
1595-607 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Larsen BM |
| Year: |
2015 |
| Journal: |
Development |
| Title: |
Mesenchymal Hox6 function is required for mouse pancreatic endocrine cell differentiation. |
| Volume: |
142 |
| Issue: |
22 |
| Pages: |
3859-68 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Catela C |
| Year: |
2022 |
| Journal: |
Elife |
| Title: |
Control of spinal motor neuron terminal differentiation through sustained Hoxc8 gene activity. |
| Volume: |
11 |
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hanley O |
| Year: |
2016 |
| Journal: |
Neuron |
| Title: |
Parallel Pbx-Dependent Pathways Govern the Coalescence and Fate of Motor Columns. |
| Volume: |
91 |
| Issue: |
5 |
| Pages: |
1005-1020 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lammert F |
| Year: |
2001 |
| Journal: |
Gastroenterology |
| Title: |
Chromosomal organization of candidate genes involved in cholesterol gallstone formation: a murine gallstone map. |
| Volume: |
120 |
| Issue: |
1 |
| Pages: |
221-38 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
571
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
568
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
735
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
554
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
717
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
613
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
705
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
705
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
717
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
208
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
204
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
705
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
146
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
554
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pósfai J |
| Year: |
1988 |
| Journal: |
Gene |
| Title: |
Sequence motifs specific for cytosine methyltransferases. |
| Volume: |
74 |
| Issue: |
1 |
| Pages: |
261-5 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lauster R |
| Year: |
1989 |
| Journal: |
J Mol Biol |
| Title: |
Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains. |
| Volume: |
206 |
| Issue: |
2 |
| Pages: |
305-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hauser CA |
| Year: |
1985 |
| Journal: |
Cell |
| Title: |
Expression of homologous homeo-box-containing genes in differentiated human teratocarcinoma cells and mouse embryos. |
| Volume: |
43 |
| Issue: |
1 |
| Pages: |
19-28 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Frohman MA |
| Year: |
1990 |
| Journal: |
Development |
| Title: |
Isolation of the mouse Hox-2.9 gene; analysis of embryonic expression suggests that positional information along the anterior-posterior axis is specified by mesoderm. |
| Volume: |
110 |
| Issue: |
2 |
| Pages: |
589-607 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yamauchi Y |
| Year: |
1999 |
| Journal: |
Dev Biol |
| Title: |
A novel transgenic technique that allows specific marking of the neural crest cell lineage in mice. |
| Volume: |
212 |
| Issue: |
1 |
| Pages: |
191-203 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wu Y |
| Year: |
2003 |
| Journal: |
Mol Cell Biol |
| Title: |
HoxB5 is an upstream transcriptional switch for differentiation of the vascular endothelium from precursor cells. |
| Volume: |
23 |
| Issue: |
16 |
| Pages: |
5680-91 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Volpe MV |
| Year: |
1997 |
| Journal: |
Histochem Cell Biol |
| Title: |
Hoxb-5 expression in the developing mouse lung suggests a role in branching morphogenesis and epithelial cell fate. |
| Volume: |
108 |
| Issue: |
6 |
| Pages: |
495-504 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chinoy MR |
| Year: |
2002 |
| Journal: |
J Surg Res |
| Title: |
Mesenchymal nuclear transcription factors in nitrofen-induced hypoplastic lung. |
| Volume: |
108 |
| Issue: |
2 |
| Pages: |
203-11 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
766
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
458
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
751
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
837
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
633
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
875
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
709
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
493
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
588
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
752
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
711
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
420
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
493
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
469
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
302
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
209
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
751
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
393
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
818
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
441
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
553
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
844
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
717
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
107
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
758
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
145
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
814
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
709
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
131
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
148
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
588
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Choi MY |
| Year: |
2006 |
| Journal: |
Development |
| Title: |
A dynamic expression survey identifies transcription factors relevant in mouse digestive tract development. |
| Volume: |
133 |
| Issue: |
20 |
| Pages: |
4119-29 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kondrashov N |
| Year: |
2011 |
| Journal: |
Cell |
| Title: |
Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning. |
| Volume: |
145 |
| Issue: |
3 |
| Pages: |
383-397 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Thut CJ |
| Year: |
2001 |
| Journal: |
Dev Biol |
| Title: |
A large-scale in situ screen provides molecular evidence for the induction of eye anterior segment structures by the developing lens. |
| Volume: |
231 |
| Issue: |
1 |
| Pages: |
63-76 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
640
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
604
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
640
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
640
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lussier M |
| Year: |
1990 |
| Journal: |
Gene |
| Title: |
The mouse keratin 19-encoding gene: sequence, structure and chromosomal assignment. |
| Volume: |
95 |
| Issue: |
2 |
| Pages: |
203-13 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kam MK |
| Year: |
2014 |
| Journal: |
Int J Biochem Cell Biol |
| Title: |
Homeobox b5 (Hoxb5) regulates the expression of Forkhead box D3 gene (Foxd3) in neural crest. |
| Volume: |
55 |
|
| Pages: |
144-52 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mock B |
| Year: |
1987 |
| Journal: |
Nucleic Acids Res |
| Title: |
A TaqI restriction fragment length polymorphism at the Hox-2.1 locus cosegregates with the Dlb-1 locus on mouse chromosome 11. |
| Volume: |
15 |
| Issue: |
5 |
| Pages: |
2397 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sharpe J |
| Year: |
1998 |
| Journal: |
EMBO J |
| Title: |
Selectivity, sharing and competitive interactions in the regulation of Hoxb genes. |
| Volume: |
17 |
| Issue: |
6 |
| Pages: |
1788-98 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
686
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
529
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
107
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
486
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
197
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
527
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
584
 |
| Fragment?: |
false |
|
•
•
•
•
•
|