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23  structures 341  species 2  interactions 4368  sequences 240  architectures

Family: HECT (PF00632)

Summary: HECT-domain (ubiquitin-transferase)

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This is the Wikipedia entry entitled "HECT domain". More...

HECT domain Edit Wikipedia article

HECT-domain (ubiquitin-transferase)
PDB 1d5f EBI.jpg
structure of an e6ap-ubch7 complex: insights into the ubiquitination pathway
Identifiers
Symbol HECT
Pfam PF00632
InterPro IPR000569
SCOP 1d5f
SUPERFAMILY 1d5f

In molecular biology, the HECT domain is a protein domain found in ubiquitin-protein ligases. The name HECT comes from 'Homologous to the E6-AP Carboxyl Terminus'.[1] Proteins containing this domain at the C terminus include ubiquitin-protein ligase, which regulates ubiquitination of CDC25. Ubiquitin-protein ligase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester, and then directly transfers the ubiquitin to targeted substrates. A cysteine residue is required for ubiquitin-thiolester formation. Human thyroid receptor interacting protein 12 (TRIP12), which also contains this domain, is a component of an ATP-dependent multisubunit protein that interacts with the ligand binding domain of the thyroid hormone receptor. It could be an E3 ubiquitin-protein ligase. Human ubiquitin-protein ligase E3A interacts with the E6 protein of the cancer-associated Human papillomavirus type 16 and Human papillomavirus type 18. The E6/E6-AP complex binds to and targets the P53 tumour-suppressor protein for ubiquitin-mediated proteolysis.


References[edit]

  1. ^ Huibregtse JM, Scheffner M, Beaudenon S, Howley PM (March 1995). "A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase". Proc. Natl. Acad. Sci. U.S.A. 92 (7): 2563–7. doi:10.1073/pnas.92.7.2563. PMC 42258. PMID 7708685. 

This article incorporates text from the public domain Pfam and InterPro IPR000569

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

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HECT-domain (ubiquitin-transferase) Provide feedback

The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.

Literature references

  1. Huibregtse JM, Scheffner M, Beaudenon S, Howley PM; , Proc Natl Acad Sci U S A 1995;92:2563-2567.: A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. PUBMED:7708685 EPMC:7708685


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000569

The name HECT comes from 'Homologous to the E6-AP Carboxyl Terminus' [PUBMED:7708685]. Proteins containing this domain at the C terminus include ubiquitin-protein ligase, which regulates ubiquitination of CDC25. Ubiquitin-protein ligase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester, and then directly transfers the ubiquitin to targeted substrates. A cysteine residue is required for ubiquitin-thiolester formation. Human thyroid receptor interacting protein 12, which also contains this domain, is a component of an ATP-dependent multisubunit protein that interacts with the ligand binding domain of the thyroid hormone receptor. It could be an E3 ubiquitin-protein ligase. Human ubiquitin-protein ligase E3A interacts with the E6 protein of the cancer-associated Human papillomavirus type 16 and Human papillomavirus type 18. The E6/E6-AP complex binds to and targets the P53 tumour-suppressor protein for ubiquitin-mediated proteolysis.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 Hect (CL0552), which has the following description:

This superfamily is characterised by fmailies with E3-ligase catalytic acitvity. The fold consists of two alpha+beta domains; where the N-terminal domain is an array of helices and beta-hairpins; the C-terminal domain is an a/b sandwich with one left-handed beta-alpha(n)-beta unit.

The clan contains the following 2 members:

HECT HECT_2

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
(133)
Full
(4368)
Representative proteomes NCBI
(4212)
Meta
(88)
RP15
(1023)
RP35
(1454)
RP55
(2163)
RP75
(2797)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(133)
Full
(4368)
Representative proteomes NCBI
(4212)
Meta
(88)
RP15
(1023)
RP35
(1454)
RP55
(2163)
RP75
(2797)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(133)
Full
(4368)
Representative proteomes NCBI
(4212)
Meta
(88)
RP15
(1023)
RP35
(1454)
RP55
(2163)
RP75
(2797)
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.

Pfam alignments:

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: Prosite
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 133
Number in full: 4368
Average length of the domain: 293.50 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 21.16 %

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 20.4 20.4
Trusted cut-off 20.4 20.6
Noise cut-off 20.3 20.2
Model length: 317
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

UQ_con HECT

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 HECT domain has been found. There are 23 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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