Proteopedia - User contributions [en]

PTEN function

2018-05-05T02:06:45Z

Tanner Young: New page: ==Structure== <scene name='78/786030/Pten_molecule/1'>PTEN</scene> is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal)...

==Structure==

<scene name='78/786030/Pten_molecule/1'>PTEN</scene> is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal) it has 166 residues on the C-terminal (C2 Domain) and 179 on the N-terminal (Phosphatase Domain). PTEN is consisted of Alpha helix and Beta pleated sheets. PTEN has a signature motif that forms a Walker loop (Phosphate-bonding loop) HCXXGXXR which is residues 123-130. The pocket of PTEN is about 8 angstroms deep. There are Cys, Arg, His, and Gly within the Walker loop. His and Gly are both important for the Walker loop, while the Cys and Arg are important for the catalytic ability of the PTEN enzyme. One difference from PTEN compared to other know Protein Tyrosine Phosphatases (PTPs) is the location of two Lys residues in the center of the Walker Loop.

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1. It is composed of a C-terminal and N-Terminal. The C-Terminal is a C2 Domain, this targets proteins to cell membranes. The N-terminal is a Phosphatase Domain, it’s job is to remove phosphate groups from a phosphorolated amino acid.
== Disease ==
The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer. It also works to remove phosphate groups from specific amino acids, such as dephosphorylating tyrosine, serine, and threonine phosphorylated peptides.
== Relevance ==
PTEN’s relevance is that without the PTEN suppressing tumors, you would have a higher increased odds of having multiple cancers, including but not limited to Breast and Prostate cancer. PTEN is one of the enzymes tested for when someone has their genes tested. The user is being testing for Hereditary cancer risk when looking at the portion of the genome containing PTEN.
== Structural highlights ==
PTEN’s main structural points is the N and C terminal along with the Walker loop containing the Cys, His, Arg, and Gly making it stand out.
</StructureSection>
== References ==
<references/>
1. Crystal Structure of the PTEN Tumor Suppressor

Lee, Jie-Oh et al.
Cell , Volume 99 , Issue 3 , 323 - 334

2. Lee, et al. ?Crystal Structure of the PTEN Tumor Suppressor: Implications for Its Phosphoinositide Phosphatase Activity and Membrane Association.? Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1D5R.

3. Lumb, Craig N., and Mark S.P. Sansom. ?PTEN.? Advances in Pediatrics., U.S. National Library of Medicine, 5 Feb. 2013, www.ncbi.nlm.nih.gov/pmc/articles/PMC3566463/.

4. Mehenni, et al. ?LKB1 Interacts with and Phosphorylates PTEN: a Functional Link between Two Proteins Involved in Cancer Predisposing Syndromes | Human Molecular Genetics | Oxford Academic.? OUP Academic, Oxford University Press, 29 June 2005, academic.oup.com/hmg/article/14/15/2209/551725.

5. ?PTEN Gene - Genetics Home Reference.? U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/PTEN.

User:Tanner Young

2018-05-05T02:04:39Z

Tanner Young:

* Full Real Name: Tanner Young

* Position: Student

* Institution (NO ABBREVIATIONS): Maryville University, Missouri

* City, State/Province, Country: Town and Country Missouri, United State of America

* Field of Expertise or Study: Biochemistry
*[[User:Tanner Young/Sandbox 1]]

User:Tanner Young

2018-05-05T02:03:58Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-05-05T01:59:51Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-05-05T01:53:40Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten_molecule/1'>PTEN</scene> is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal) it has 166 residues on the C-terminal (C2 Domain) and 179 on the N-terminal (Phosphatase Domain). PTEN is consisted of Alpha helix and Beta pleated sheets. PTEN has a signature motif that forms a Walker loop (Phosphate-bonding loop) HCXXGXXR which is residues 123-130. The pocket of PTEN is about 8 angstroms deep. There are Cys, Arg, His, and Gly within the Walker loop. His and Gly are both important for the Walker loop, while the Cys and Arg are important for the catalytic ability of the PTEN enzyme. One difference from PTEN compared to other know Protein Tyrosine Phosphatases (PTPs) is the location of two Lys residues in the center of the Walker Loop.

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1. It is composed of a C-terminal and N-Terminal. The C-Terminal is a C2 Domain, this targets proteins to cell membranes. The N-terminal is a Phosphatase Domain, it’s job is to remove phosphate groups from a phosphorolated amino acid.
== Disease ==
The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer. It also works to remove phosphate groups from specific amino acids, such as dephosphorylating tyrosine, serine, and threonine phosphorylated peptides.
== Relevance ==
PTEN’s relevance is that without the PTEN suppressing tumors, you would have a higher increased odds of having multiple cancers, including but not limited to Breast and Prostate cancer. PTEN is one of the enzymes tested for when someone has their genes tested. The user is being testing for Hereditary cancer risk when looking at the portion of the genome containing PTEN.
== Structural highlights ==

</StructureSection>
== References ==
<references/>
1. Crystal Structure of the PTEN Tumor Suppressor

Lee, Jie-Oh et al.
Cell , Volume 99 , Issue 3 , 323 - 334

2. Lee, et al. ?Crystal Structure of the PTEN Tumor Suppressor: Implications for Its Phosphoinositide Phosphatase Activity and Membrane Association.? Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1D5R.

3. Lumb, Craig N., and Mark S.P. Sansom. ?PTEN.? Advances in Pediatrics., U.S. National Library of Medicine, 5 Feb. 2013, www.ncbi.nlm.nih.gov/pmc/articles/PMC3566463/.

4. Mehenni, et al. ?LKB1 Interacts with and Phosphorylates PTEN: a Functional Link between Two Proteins Involved in Cancer Predisposing Syndromes | Human Molecular Genetics | Oxford Academic.? OUP Academic, Oxford University Press, 29 June 2005, academic.oup.com/hmg/article/14/15/2209/551725.

5. ?PTEN Gene - Genetics Home Reference.? U.S. National Library of Medicine, National Institutes of Health, ghr.nlm.nih.gov/gene/PTEN.

File:PTENSTRUCTURE.jpeg

2018-05-02T19:13:04Z

Tanner Young: http://www.cell.com/cell/fulltext/S0092-8674(00)81663-3 Image from that site.

== Summary ==
http://www.cell.com/cell/fulltext/S0092-8674(00)81663-3 Image from that site.
== Licensing ==
{{subst:No license from license selector|Somewebsite}}

User:Tanner Young/Sandbox 1

2018-04-30T20:16:35Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-04-30T20:15:37Z

Tanner Young:

File:PTEN-P-LOOP.jpeg

2018-04-30T20:14:33Z

Tanner Young: https://www.cell.com/cell/fulltext/S0092-8674(00)81663-3

== Summary ==
https://www.cell.com/cell/fulltext/S0092-8674(00)81663-3
== Licensing ==
{{subst:No license from license selector|Somewebsite}}

File:Picture.jpeg

2018-04-30T20:11:11Z

Tanner Young:

File:18DD58B9-6069-4276-ACF9-6A8962FBE8DD.jpeg

2018-04-30T20:09:42Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-04-30T19:47:39Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-04-30T19:23:39Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-04-30T19:07:35Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-04-30T17:44:37Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten/1'>PTEN</scene> is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal) it has 166 residues on the C-terminal (C2 Domain) and 179 on the N-terminal (Phosphatase Domain). PTEN is consisted of Alpha helix and Beta pleated sheets.

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1. It is composed of a C-terminal and N-Terminal. The C-Terminal is a C2 Domain, this targets proteins to cell membranes. The N-terminal is a Phosphatase Domain, it’s job is to remove phosphate groups from a phosphorolated amino acid.
== Disease ==
The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer. It also works to remove phosphate groups from specific amino acids, such as dephosphorylating tyrosine, serine, and threonine phosphorylated peptides.
== Relevance ==
PTEN’s relevance is that without the PTEN suppressing tumors, you would have a higher increased odds of having multiple cancers, including but not limited to Breast and Prostate cancer.
== Structural highlights ==

</StructureSection>
== References ==
<references/>

User:Tanner Young/Sandbox 1

2018-04-24T16:57:06Z

Tanner Young:

User:Tanner Young/Sandbox 1

2018-04-24T16:24:57Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten/1'>PTEN</scene> is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal) it has 166 residues on the C-terminal (C2 Domain) and 179 on the N-terminal (Phosphatase Domain).

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tanner Young/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1. It is composed of a C-terminal and N-Terminal. The C-Terminal is a C2 Domain, this targets proteins to cell membranes. The N-terminal is a Phosphatase Domain, it’s job is to remove phosphate groups from a phosphorolated amino acid.
== Disease ==
The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer. It also works to remove phosphate groups from specific amino acids, such as dephosphorylating tyrosine, serine, and threonine phosphorylated peptides.
== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Tanner Young/Sandbox 1

2018-04-24T16:17:06Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten/1'>PTEN</scene> is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal) it has 166 residues on the C-terminal (C2 Domain) and 179 on the N-terminal (Phosphatase Domain).

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tanner Young/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1.
== Disease ==
The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer.
== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Tanner Young/Sandbox 1

2018-04-23T19:30:33Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten/1'>PTEN</scene> Alpha Helix and Beta pleated sheets

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tanner Young/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1.
== Disease ==
The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer.
== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Tanner Young/Sandbox 1

2018-04-20T01:02:21Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten/1'>PTEN</scene> Alpha Helix and Beta pleated sheets

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tanner Young/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Tanner Young/Sandbox 1

2018-04-20T00:56:45Z

Tanner Young:

==Structure==

<scene name='78/786030/Pten/1'>PTEN</scene>

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tanner Young/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Tanner Young/Sandbox 1

2018-04-20T00:52:32Z

Tanner Young: New page: ==Structure== PTEN Structure <StructureSection load=‘1stp’ size=‘340’ side=‘right’ caption=‘Caption’ scene=‘’> <StructureSection load='1stp' size='340' side='right'...

==Structure==

PTEN Structure

<StructureSection load=‘1stp’ size=‘340’ side=‘right’ caption=‘Caption’ scene=‘’>

<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Tanner Young/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Tanner Young

2018-04-04T20:40:21Z

Tanner Young: