Chp1
entrez
64152
canonical
uniprot
P61023
canonical
ensembl
ENSRNOG00000004742
resolver
ensembl
ENSRNOG00055003343
resolver
ensembl
ENSRNOG00055023007
resolver
ensembl
ENSRNOG00060026528
resolver
ensembl
ENSRNOG00060028723
resolver
ensembl
ENSRNOG00065004699
resolver
ensembl
ENSRNOG00065023898
resolver
ensp
ENSRNOP00000053243
resolver
ensp
ENSRNOP00055003848
resolver
ensp
ENSRNOP00055032109
resolver
ensp
ENSRNOP00060038146
resolver
ensp
ENSRNOP00060041618
resolver
ensp
ENSRNOP00065004680
resolver
ensp
ENSRNOP00065033477
resolver
enst
ENSRNOT00000056405
resolver
enst
ENSRNOT00055005196
resolver
enst
ENSRNOT00055039535
resolver
enst
ENSRNOT00060045953
resolver
enst
ENSRNOT00060049915
resolver
enst
ENSRNOT00065006805
resolver
enst
ENSRNOT00065040996
resolver
genesymbol
Chp1
resolver
genesymbol_syn
Chp
resolver
uniprot
Q62877
resolver
uniprot_entry
CHP1_RAT
resolver
uniprot_sec
Q62877
resolver
amino_acid_sequence
MGSRASTLLRDEELEEIKKETGFSHSQITRLYSRFTSLDKGENGTLSREDFQRIPELAINPLGDRIINAFFSEGEDQVNFRGFMRTLAHFRPIEDNEKSKDVNGPEPLNSRSNKLHFAFRLYDLDKDDKISRDELLQVLRMMVGVNISDEQLGSIADRTIQEADQDGDSAISFTEFVKVLEKVDVEQKMSIRFLH
uniprot
proteins
function
FUNCTION: Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner. {ECO:0000269|PubMed:12966074, ECO:0000269|PubMed:14657246, ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:20720019, ECO:0000269|PubMed:21543739, ECO:0000269|PubMed:8626580}.
uniprot
proteins
mass_dalton
22432
uniprot
proteins
mutagenesis
MUTAGEN 134; /note="E->A: Inhibits calcium-mediated conformational changes. Loss of transcytotic targeting/fusion function. Reduces association with membranes. Does not affect microtubule formation."; /evidence="ECO:0000269|PubMed:14657246, ECO:0000269|PubMed:8626580"; MUTAGEN 138; /note="V->A: Predominantly located in the cytoplasm; when associated with A-139. Predominantly located in the nucleus; when associated with A-139; A-179 and A-180."; /evidence="ECO:0000269|PubMed:14769882"; MUTAGEN 139; /note="L->A: Predominantly located in the cytoplasm; when associated with A-138. Predominantly located in the nucleus; when associated with A-138; A-179 and A-180."; /evidence="ECO:0000269|PubMed:14769882"; MUTAGEN 143; /note="V->A: Predominantly located in the cytoplasm; when associated with A-145 and A-147. Predominantly located in the nucleus; when associated with A-145; A-147; A-183 and A-185."; /evidence="ECO:0000269|PubMed:14769882, ECO:0000269|PubMed:20720019"; MUTAGEN 145; /note="V->A: Predominantly located in the cytoplasm; when associated with A-143 and A-147. Predominantly located in the nucleus; when associated with A-143; A-147; A-183 and A-185."; /evidence="ECO:0000269|PubMed:14769882, ECO:0000269|PubMed:20720019"; MUTAGEN 147; /note="I->A: Predominantly located in the cytoplasm; when associated with A-143 and A-145. Predominantly located in the nucleus; when associated with A-143; A-145; A-183 and A-185."; /evidence="ECO:0000269|PubMed:14769882, ECO:0000269|PubMed:20720019"; MUTAGEN 179; /note="V->A: Predominantly located in the cytoplasm; when associated with A-180. Predominantly located in the nucleus; when associated with A-138; A-139 and A-180."; /evidence="ECO:0000269|PubMed:14769882"; MUTAGEN 180; /note="L->A: Predominantly located in the cytoplasm; when associated with A-179. Predominantly located in the nucleus; when associated with A-138; A-139 and A-179."; /evidence="ECO:0000269|PubMed:14769882"; MUTAGEN 183; /note="V->A: Predominantly located in the cytoplasm; when associated with A-185. Predominantly located in the nucleus; when associated with A-143; A-145; A-147 and A-185."; /evidence="ECO:0000269|PubMed:14769882, ECO:0000269|PubMed:20720019"; MUTAGEN 185; /note="V->A: Predominantly located in the cytoplasm; when associated with A-183. Predominantly located in the nucleus; when associated with A-143; A-145; A-147 and A-183."; /evidence="ECO:0000269|PubMed:14769882, ECO:0000269|PubMed:20720019
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; decreased phosphorylation is associated with an increase in SLC9A1/NHE1 Na(+)/H(+) exchange activity. Phosphorylation occurs in serum-dependent manner. The phosphorylation state may regulate the binding to SLC9A1/NHE1 (By similarity). {ECO:0000250}.; PTM: N-myristoylation is required for its association with microtubules and interaction with GAPDH, but not for the constitutive association to membranes. Both N-myristoylation and calcium-mediated conformational changes are essential in exocytic traffic.
uniprot
proteins
protein_family
CHP subfamily
uniprot
proteins
protein_family
Calcineurin regulatory subunit family
uniprot
proteins
pubmed
10512881
uniprot
proteins
pubmed
11481038
uniprot
proteins
pubmed
12204119
uniprot
proteins
pubmed
12966074
uniprot
proteins
pubmed
14657246
uniprot
proteins
pubmed
14769882
uniprot
proteins
pubmed
15312048
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15987692
uniprot
proteins
pubmed
16511110
uniprot
proteins
pubmed
20720019
uniprot
proteins
pubmed
21543739
uniprot
proteins
pubmed
8626580
uniprot
proteins
sequence_length
195
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20720019}. Cytoplasm {ECO:0000269|PubMed:12204119, ECO:0000269|PubMed:14769882}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10512881, ECO:0000269|PubMed:15312048}. Endomembrane system {ECO:0000269|PubMed:15312048}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:14657246}. Cell membrane {ECO:0000269|PubMed:21543739}. Membrane {ECO:0000250|UniProtKB:Q99653}; Lipid-anchor {ECO:0000250|UniProtKB:Q99653}. Note=Localizes in cytoplasmic compartments in dividing cells. Localizes in the nucleus in quiescent cells. Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) and CRM1-dependent pathway. May shuttle between nucleus and cytoplasm. Localizes with the microtubule-organizing center (MTOC) and extends toward the periphery along microtubules. Associates with membranes of the early secretory pathway in a GAPDH-independent, N-myristoylation- and calcium-dependent manner. Colocalizes with the mitotic spindle microtubules. Colocalizes with GAPDH along microtubules. Colocalizes with SLC9A1 at the reticulum endoplasmic and plasma membrane. Colocalizes with STK17B at the plasma membrane. {ECO:0000269|PubMed:14657246, ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:20720019, ECO:0000269|PubMed:21543739}.
uniprot
proteins