Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00731
Entry Name
UniProt Accession
Theoretical PI
4.97
Molecular Weight
22432.12
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcineurin B homologous protein 1
Protein Synonyms/Alias
Calcineurin B-like protein; Calcium-binding protein CHP; Calcium-binding protein p22; EF-hand calcium-binding domain-containing protein p22;
Gene Name
Chp1
Gene Synonyms/Alias
Chp;
Created Date
26-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGSRASTLL
[1]
N-Myristoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Resh MD. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta. 1999 Aug12;1451(1):1-16. Review.[PMID:10446384]
Functional Description
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.
Sequence Annotation
Domain: 26 61 EF-hand 1.
Domain: 71 106 EF-hand 2.
Domain: 110 145 EF-hand 3.
Domain: 151 186 EF-hand 4.
Motif: 2 6 Necessary for association withmicrotubule and interaction with GAPDH.
Motif: 138 147 Nuclear export signal 1.
Motif: 176 185 Nuclear export signal 2.
Protein Length
195 AA.
Protein Sequence
(Canonical)
MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN  60
PLGDRIINAF FSEGEDQVNF RGFMRTLAHF RPIEDNEKSK DVNGPEPLNS RSNKLHFAFR  120
LYDLDKDDKI SRDELLQVLR MMVGVNISDE QLGSIADRTI QEADQDGDSA ISFTEFVKVL  180
EKVDVEQKMS IRFLH                                                   195
FASTA
(Canonical)
>LipidDB-10116-00731|P61023
MGSRASTLLRDEELEEIKKETGFSHSQITRLYSRFTSLDKGENGTLSREDFQRIPELAIN
PLGDRIINAFFSEGEDQVNFRGFMRTLAHFRPIEDNEKSKDVNGPEPLNSRSNKLHFAFR
LYDLDKDDKISRDELLQVLRMMVGVNISDEQLGSIADRTIQEADQDGDSAISFTEFVKVL
EKVDVEQKMSIRFLH
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; IDA:RGD
GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0000139; C:Golgi membrane; IDA:UniProtKB
GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0030133; C:transport vesicle; IDA:UniProtKB
GO:0005509; F:calcium ion binding; IDA:RGD
GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB
GO:0019900; F:kinase binding; IDA:UniProtKB
GO:0008017; F:microtubule binding; IDA:UniProtKB
GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW
GO:0005215; F:transporter activity; IDA:UniProtKB
GO:0017156; P:calcium ion-dependent exocytosis; IDA:RGD
GO:0019722; P:calcium-mediated signaling; TAS:RGD
GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB
GO:0031122; P:cytoplasmic microtubule organization; IDA:UniProtKB
GO:0022406; P:membrane docking; IDA:UniProtKB
GO:0061025; P:membrane fusion; IDA:UniProtKB
GO:0061024; P:membrane organization; IDA:UniProtKB
GO:0001578; P:microtubule bundle formation; IDA:UniProtKB
GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB
GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB
GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB
GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB
GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB
GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB
GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB
GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB
GO:0060050; P:positive regulation of protein glycosylation; IDA:UniProtKB
GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB
GO:0051222; P:positive regulation of protein transport; IDA:UniProtKB
GO:0032417; P:positive regulation of sodium:proton antiporter activity; ISS:UniProtKB
GO:0006611; P:protein export from nucleus; IDA:UniProtKB
GO:0051259; P:protein oligomerization; IDA:UniProtKB
GO:0050821; P:protein stabilization; IDA:UniProtKB
GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB
GO:0045056; P:transcytosis; IGI:RGD
Interpro
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR018247; EF_Hand_1_Ca_BS
InterPro; IPR002048; EF_hand_dom
Pfam
Pfam; PF13499; EF-hand_7;
SMART
SMART; SM00054; EFh;
PROSITE
PROSITE; PS00018; EF_HAND_1;
PROSITE; PS50222; EF_HAND_2;
PRINTS