Habp4
entrez
56541
canonical
uniprot
Q9JKS5
canonical
ensembl
ENSMUSG00000021476
resolver
ensp
ENSMUSP00000021929
resolver
enst
ENSMUST00000021929
resolver
genesymbol
Habp4
resolver
uniprot
E9QKB2
resolver
uniprot
Q3UJC1
resolver
uniprot
Q3UNH8
resolver
uniprot
Q9D450
resolver
uniprot_entry
E9QKB2_MOUSE
resolver
uniprot_entry
HABP4_MOUSE
resolver
uniprot_entry
Q3UJC1_MOUSE
resolver
uniprot_sec
Q3UNH8
resolver
uniprot_sec
Q9D450
resolver
amino_acid_sequence
MKGALGSPVAAAGAAMQETFGCVVANRFHQLLDDESDPFDILREAEHRRQQQLQRKRRDEAAAASGAGHRGGRSPAVASGHRPGAGGRRESQKERKSLAASGAQQPDSPGGPQPPGQKRTPRRGEQQGWNDNRGTDVVLERAERRSYREYRPYETERQADLPVEKFTDEKPVDRFDRDRPLRGRGGPRGGLRSRGRGGPGNRAFDSFDQRGKRDFERYSSNDKTNRMEDSMGGCGIRPWGSGKDTSDTEPPAPMEETSMMEECQGTLDEESAAKVPELEVEEENQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSRYRDDMVKEDYEDESHVFRKAANDITSQLEINFGNLPRPGRGARGSTRGGRGRMRRTENYGPRAEVVTQDVAPNPDDPEDFPALA
uniprot
proteins
function
FUNCTION: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature oocyte by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also binds RNA, regulating transcription and pre-mRNA splicing. Binds (via C-terminus) to poly(U) RNA. Seems to play a role in PML-nuclear bodies formation (By similarity). Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress (By similarity). {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0, ECO:0000250|UniProtKB:Q5XJA5}.
uniprot
proteins
mass_dalton
45924
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-352 and Thr-373. {ECO:0000250|UniProtKB:Q5JVS0}.; PTM: Methylated. Methylation is decreased by phorbol 12-myristate 13-acetate (PMA)-activated PKC, in vitro. {ECO:0000250|UniProtKB:Q5JVS0}.
uniprot
proteins
protein_family
SERBP1-HABP4 family
uniprot
proteins
pubmed
10887182
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
19523114
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23894536
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus speckle {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, gem {ECO:0000250|UniProtKB:Q5JVS0}. Note=Transported into the nuclear compartment in activated leukocytes. Inhibition of methylation alters its distribution between the nuclear and cytoplasmic compartments. Methylation may be required for its localization in subnuclear structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies (gems). Colocalizes with FMR1, FXR1 and FXR2 in cytoplasmic stress granules. In myocardial cells, localization at the sarcoplasm is reduced in response to mechanical stress. {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0}.
uniprot
proteins