HABP4
entrez
22927
canonical
uniprot
Q5JVS0
canonical
ensembl
ENSG00000130956
resolver
ensp
ENSP00000364398
resolver
ensp
ENSP00000673523
resolver
genesymbol
HABP4
resolver
hgnc
HGNC:17062
resolver
uniprot
O75804
resolver
uniprot
Q8WV33
resolver
uniprot
Q9NYJ2
resolver
uniprot_entry
HABP4_HUMAN
resolver
uniprot_sec
O75804
resolver
uniprot_sec
Q8WV33
resolver
uniprot_sec
Q9NYJ2
resolver
amino_acid_sequence
MKGALGSPVAAAGAAMQESFGCVVANRFHQLLDDESDPFDILREAERRRQQQLQRKRRDEAAAAAGAGPRGGRSPAGASGHRAGAGGRRESQKERKSLPAPVAQRPDSPGGGLQAPGQKRTPRRGEQQGWNDSRGPEGMLERAERRSYREYRPYETERQADFTAEKFPDEKPGDRFDRDRPLRGRGGPRGGMRGRGRGGPGNRVFDAFDQRGKREFERYGGNDKIAVRTEDNMGGCGVRTWGSGKDTSDVEPTAPMEEPTVVEESQGTPEEESPAKVPELEVEEETQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSKYRDDMVKDDYEDDSHVFRKPANDITSQLEINFGNLPRPGRGARGGTRGGRGRIRRAENYGPRAEVVMQDVAPNPDDPEDFPALS
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 (PubMed:14699138, PubMed:16455055, PubMed:19523114, PubMed:21771594). Binds (via C-terminus) to poly(U) RNA (PubMed:19523114). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). 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:Q5XJA5, ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:21771594, ECO:0000269|PubMed:28695742}.
uniprot
proteins
mass_dalton
45785
uniprot
proteins
mutagenesis
MUTAGEN 213; /note="K->R: Decreases sumoylation; when associated with R-336. Abolishes sumoylation; when associated with R-276 and R-336."; /evidence="ECO:0000269|PubMed:28695742"; MUTAGEN 276; /note="K->R: Decreases sumoylation; when associated with R-336. Abolishes sumoylation; when associated with R-213 and R-336."; /evidence="ECO:0000269|PubMed:28695742"; MUTAGEN 336; /note="K->R: Decreases sumoylation; when associated with R-213 or R-276. Abolishes sumoylation; when associated with R-213 and R-276."; /evidence="ECO:0000269|PubMed:28695742
uniprot
proteins
post_translational_modification
PTM: Methylated (PubMed:16879614). Methylation is decreased by phorbol 12-myristate 13-acetate (PMA)-activated PKC, in vitro (PubMed:16879614). {ECO:0000269|PubMed:16879614}.; PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-354 and Thr-375. {ECO:0000269|PubMed:14699138}.
uniprot
proteins
protein_family
SERBP1-HABP4 family
uniprot
proteins
pubmed
10887182
uniprot
proteins
pubmed
12505151
uniprot
proteins
pubmed
14699138
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15862299
uniprot
proteins
pubmed
16455055
uniprot
proteins
pubmed
16879614
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19523114
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21771594
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28695742
uniprot
proteins
pubmed
9523163
uniprot
proteins
sequence_length
413
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:9523163}. Cytoplasm {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:9523163}. Cytoplasm, Stress granule {ECO:0000269|PubMed:21771594}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body {ECO:0000269|PubMed:19523114}. Nucleus, nucleolus {ECO:0000269|PubMed:19523114}. Nucleus speckle {ECO:0000269|PubMed:19523114}. Nucleus, Cajal body {ECO:0000269|PubMed:19523114}. Nucleus, gem {ECO:0000269|PubMed:19523114}. Note=Transported into the nuclear compartment in activated leukocytes (PubMed:9523163). Inhibition of methylation alters its distribution between the nuclear and cytoplasmic compartments (PubMed:16879614, PubMed:19523114). Methylation may be required for its localization in subnuclear structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies (gems) (PubMed:19523114). Colocalizes with FMR1, FXR1 and FXR2 in cytoplasmic stress granules (PubMed:21771594). In myocardial cells, localization at the sarcoplasm is reduced in response to mechanical stress (By similarity). {ECO:0000250|UniProtKB:A1L1K8, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:21771594, ECO:0000269|PubMed:9523163}.
uniprot
proteins