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7  structures 96  species 1  interaction 631  sequences 20  architectures

Family: PTB (PF08416)

Summary: Phosphotyrosine-binding domain

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This is the Wikipedia entry entitled "Phosphotyrosine-binding domain". More...

Phosphotyrosine-binding domain Edit Wikipedia article

Phosphotyrosine-binding domain
PDB 1wvh EBI.jpg
Structure of the PTB domain of tensin1.[1]
Identifiers
Symbol PTB
Pfam PF08416
InterPro IPR013625
CDD cd00934
PTB domain (IRS-1 type)
PDB 1irs EBI.jpg
irs-1 ptb domain complexed with a il-4 receptor phosphopeptide, nmr, minimized average structure
Identifiers
Symbol IRS
Pfam PF02174
InterPro IPR002404
SMART PTBI
SCOP 1cli
SUPERFAMILY 1cli
CDD cd01204

In molecular biology, Phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine.

The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (Pfam PF00017) domain and a region similar to the tumour suppressor PTEN.[2] The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.[3]

The phosphotyrosine-binding domain of insulin receptor substrate-1 is not related to the phosphotyrosine-binding domain of tensin. Insulin receptor substrate-1 proteins contain both a pleckstrin homology domain and a phosphotyrosine binding (PTB) domain. The PTB domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. The PTB domain is situated towards the N terminus. Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac-LYASSNPApY-NH2 peptide in the juxtamembrane region of the insulin receptor. Further interactions via "bridged" water molecules are coordinated by residues an Asn and a Ser residue.[4] The PTB domain has a compact, 7-stranded beta-sandwich structure, capped by a C-terminal helix. The substrate peptide fits into an L-shaped surface cleft formed from the C-terminal helix and strands 5 and 6.[5]

Human proteins containing these domains[edit]

APBA1; APBA2; APBA3; EPS8; EPS8L1; EPS8L2; EPS8L3; TENC1; TNS; TNS1; TNS3; TNS4; DOK1; DOK2; DOK3; DOK4; DOK5; DOK6; DOK7; FRS2; FRS3; IRS1; IRS2; IRS4; TLN1; TLN2

References[edit]

  1. ^ McCleverty CJ, Lin DC, Liddington RC (June 2007). "Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions". Protein Sci. 16 (6): 1223–9. doi:10.1110/ps.072798707. PMC 2206669. PMID 17473008. 
  2. ^ Chen H, Ishii A, Wong WK, Chen LB, Lo SH (October 2000). "Molecular characterization of human tensin". Biochem. J. 351 (2): 403–11. PMC 1221376. PMID 11023826. 
  3. ^ Lo SH (January 2004). "Tensin". Int. J. Biochem. Cell Biol. 36 (1): 31–4. doi:10.1016/S1357-2725(03)00171-7. PMID 14592531. 
  4. ^ Eck MJ, Dhe-Paganon S, Trub T, Nolte RT, Shoelson SE (May 1996). "Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor". Cell 85 (5): 695–705. doi:10.1016/S0092-8674(00)81236-2. PMID 8646778. 
  5. ^ Zhou MM, Huang B, Olejniczak ET, Meadows RP, Shuker SB, Miyazaki M, Trub T, Shoelson SE, Fesik SW (April 1996). "Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain". Nat. Struct. Biol. 3 (4): 388–93. doi:10.1038/nsb0496-388. PMID 8599766. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR013625

This article incorporates text from the public domain Pfam and InterPro IPR002404


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Phosphotyrosine-binding domain Provide feedback

The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (PF00017) domain and a region similar to the tumour suppressor PTEN [1]. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif [2].

Literature references

  1. Chen H, Ishii A, Wong WK, Chen LB, Lo SH; , Biochem J 2000;351:403-411.: Molecular characterization of human tensin. PUBMED:11023826 EPMC:11023826

  2. Lo SH; , Int J Biochem Cell Biol 2004;36:31-34.: Tensin. PUBMED:14592531 EPMC:14592531


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013625

The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) of tensin tends to be found at the C terminus of a protein. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (INTERPRO) domain and a region similar to the tumour suppressor PTEN [PUBMED:11023826]. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif [PUBMED:14592531].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan PH (CL0266), which has the following description:

Members of this clan share a PH-like fold. Many families in this clan bind to short peptide motifs in proteins and are involved in signalling.

The clan contains the following 33 members:

bPH_1 bPH_2 bPH_3 bPH_4 bPH_5 bPH_6 DCP1 DUF1448 FERM_C GRAM ICAP-1_inte_bdg Mcp5_PH PH PH_10 PH_11 PH_2 PH_3 PH_4 PH_5 PH_6 PH_7 PH_8 PH_9 PH_BEACH PID PID_2 PTB Ran_BP1 Rtt106 SSrecog Voldacs Vps36_ESCRT-II WH1

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(14)
Full
(631)
Representative proteomes NCBI
(1087)
Meta
(1)
RP15
(54)
RP35
(78)
RP55
(174)
RP75
(308)
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Format an alignment

  Seed
(14)
Full
(631)
Representative proteomes NCBI
(1087)
Meta
(1)
RP15
(54)
RP35
(78)
RP55
(174)
RP75
(308)
Alignment:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(14)
Full
(631)
Representative proteomes NCBI
(1087)
Meta
(1)
RP15
(54)
RP35
(78)
RP55
(174)
RP75
(308)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_3174 (release 18.0)
Previous IDs: none
Type: Family
Author: Wuster A
Number in seed: 14
Number in full: 631
Average length of the domain: 127.00 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 14.53 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.6 20.6
Trusted cut-off 20.6 20.6
Noise cut-off 20.5 20.5
Model length: 131
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

PTB

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PTB domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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