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9  structures 270  species 0  interactions 773  sequences 11  architectures

Family: Caprin-1_dimer (PF18293)

Summary: Caprin-1 dimerization domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Caprin-1". More...

Caprin-1 Edit Wikipedia article

Available structures
PDB Ortholog search: PDBe RCSB
Aliases CAPRIN1, GPIAP1, GPIP137, GRIP137, M11S1, RNG105, p137GPI, cell cycle associated protein 1
External IDs MGI: 1858234 HomoloGene: 4310 GeneCards: CAPRIN1
Gene location (Human)
Chromosome 11 (human)
Chr. Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for CAPRIN1
Genomic location for CAPRIN1
Band 11p13 Start 34,051,683 bp[1]
End 34,101,156 bp[1]
RNA expression pattern
PBB GE GPIAP1 200723 s at fs.png

PBB GE GPIAP1 200722 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 11: 34.05 – 34.1 Mb Chr 11: 103.76 – 103.8 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Caprin-1 is a protein that in humans is encoded by the CAPRIN1 gene.[5][6][7][8][9][10] It is suggested that Caprin1 (a.k.a. RNG105) is essential for the formation of long-term memory.[11]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000135387 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027184 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Ellis JA, Luzio JP (Oct 1995). "Identification and characterization of a novel protein (p137) which transcytoses bidirectionally in Caco-2 cells". J Biol Chem. 270 (35): 20717–23. doi:10.1074/jbc.270.35.20717. PMID 7657653. 
  6. ^ Wang B, David MD, Schrader JW (Sep 2005). "Absence of caprin-1 results in defects in cellular proliferation". J Immunol. 175 (7): 4274–82. doi:10.4049/jimmunol.175.7.4274. PMID 16177067. 
  7. ^ Solomon S, Xu Y, Wang B, David MD, Schubert P, Kennedy D, Schrader JW (Feb 2007). "Distinct Structural Features ofCaprin-1 Mediate Its Interaction with G3BP-1 and Its Induction of Phosphorylation of Eukaryotic Translation Initiation Factor 2α, Entry to Cytoplasmic Stress Granules, and Selective Interaction with a Subset of mRNAs". Mol Cell Biol. 27 (6): 2324–42. doi:10.1128/MCB.02300-06. PMC 1820512Freely accessible. PMID 17210633. 
  8. ^ Grill B, Wilson GM, Zhang KX, Wang B, Doyonnas R, Quadroni M, Schrader JW (Feb 2004). "Activation/division of lymphocytes results in increased levels of cytoplasmic activation/proliferation-associated protein-1: prototype of a new family of proteins". J Immunol. 172 (4): 2389–400. doi:10.4049/jimmunol.172.4.2389. PMID 14764709. 
  9. ^ Katsafanas GC, Moss B (Dec 2004). "Vaccinia virus intermediate stage transcription is complemented by Ras-GTPase-activating protein SH3 domain-binding protein (G3BP) and cytoplasmic activation/proliferation-associated protein (p137) individually or as a heterodimer". J Biol Chem. 279 (50): 52210–7. doi:10.1074/jbc.M411033200. PMID 15471883. 
  10. ^ "Entrez Gene: GPIAP1 GPI-anchored membrane protein 1". 
  11. ^

Further reading

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.

Caprin-1 dimerization domain Provide feedback

This domain is found in human Caprin-1 protein. Caprin-1 plays a role in many important biological processes, including cellular proliferation, innate immune response and synaptic plasticity. This domain is found in the highly conserved homologous region 1(HR1) and is responsible for the tight homodimerization of Caprin-1 [1].

Literature references

  1. Wu Y, Zhu J, Huang X, Du Z;, Acta Crystallogr D Struct Biol. 2016;72:718-727.: Crystal structure of a dimerization domain of human Caprin-1: insights into the assembly of an evolutionarily conserved ribonucleoprotein complex consisting of Caprin-1, FMRP and G3BP1. PUBMED:27303792 EPMC:27303792

This tab holds annotation information from the InterPro database.

InterPro entry IPR041637

This domain is found in human Caprin-1 protein. Caprin-1 plays a role in many important biological processes, including cellular proliferation, innate immune response and synaptic plasticity. This domain is found in the highly conserved homologous region 1(HR1) and is responsible for the tight homodimerization of Caprin-1 [PUBMED:27303792].

Domain organisation

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

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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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, 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.

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

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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...


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.

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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: ECOD:EUF07081
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Smart A
Number in seed: 20
Number in full: 773
Average length of the domain: 114.50 aa
Average identity of full alignment: 47 %
Average coverage of the sequence by the domain: 14.68 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 28.2 27.5
Noise cut-off 26.5 26.2
Model length: 116
Family (HMM) version: 2
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 Caprin-1_dimer domain has been found. There are 9 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 sequence.

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