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Protein

Calcineurin B homologous protein 1

Gene

Chp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi123 – 1341Add BLAST12
Calcium bindingi164 – 1752Add BLAST12

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • calcium ion binding Source: RGD
  • kinase binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein kinase inhibitor activity Source: UniProtKB-KW
  • transporter activity Source: UniProtKB

GO - Biological processi

  • calcium ion regulated exocytosis Source: RGD
  • calcium-mediated signaling Source: RGD
  • cellular response to acidic pH Source: UniProtKB
  • cytoplasmic microtubule organization Source: UniProtKB
  • membrane docking Source: UniProtKB
  • membrane fusion Source: UniProtKB
  • membrane organization Source: UniProtKB
  • microtubule bundle formation Source: UniProtKB
  • negative regulation of calcineurin-NFAT signaling cascade Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of phosphatase activity Source: UniProtKB
  • negative regulation of protein autophosphorylation Source: UniProtKB
  • negative regulation of protein import into nucleus Source: UniProtKB
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of protein ubiquitination Source: UniProtKB
  • positive regulation of protein glycosylation Source: UniProtKB
  • positive regulation of protein targeting to membrane Source: UniProtKB
  • positive regulation of protein transport Source: UniProtKB
  • positive regulation of sodium:proton antiporter activity Source: UniProtKB
  • protein complex oligomerization Source: UniProtKB
  • protein export from nucleus Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of intracellular pH Source: UniProtKB
  • regulation of neuron death Source: Ensembl

Keywordsi

Molecular functionProtein kinase inhibitor
Biological processProtein transport, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-2160916 Hyaluronan uptake and degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Calcineurin B homologous protein 1
Alternative name(s):
Calcineurin B-like protein
Calcium-binding protein CHP
Calcium-binding protein p22
EF-hand calcium-binding domain-containing protein p22
Gene namesi
Name:Chp1
Synonyms:Chp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi620447 Chp1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi134E → A: Inhibits calcium-mediated conformational changes. Loss of transcytotic targeting/fusion function. Reduces association with membranes. Does not affect microtubule formation. 2 Publications1
Mutagenesisi138V → 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. 1 Publication1
Mutagenesisi139L → 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. 1 Publication1
Mutagenesisi143V → 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. 2 Publications1
Mutagenesisi145V → 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. 2 Publications1
Mutagenesisi147I → 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. 2 Publications1
Mutagenesisi179V → 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. 1 Publication1
Mutagenesisi180L → 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. 1 Publication1
Mutagenesisi183V → 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. 2 Publications1
Mutagenesisi185V → 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. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000738462 – 195Calcineurin B homologous protein 1Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1

Post-translational modificationi

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).By similarity
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.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP61023
PRIDEiP61023

PTM databases

PhosphoSitePlusiP61023

Expressioni

Tissue specificityi

Expressed in liver and kidney (at protein level). Ubiquitously expressed. Expressed in the brain, lung, testes, kidney, spleen and heart.3 Publications

Gene expression databases

BgeeiENSRNOG00000004742
GenevisibleiP61023 RN

Interactioni

Subunit structurei

Interacts with PPP3CA. Interacts with SLC9A1/NHE1 (via the juxtamembrane region of the cytoplasmic C-terminal domain); the interaction occurs at the plasma membrane in a calcium-dependent manner and at a domain that is critical for growth factor stimulation of the exchanger (By similarity). Monomer. Interacts with STK17B; the interaction occurs in a calcium-independent manner and induces the translocation of CHP1 from the Golgi to the nucleus. Interacts with GAPDH; the interaction is direct, occurs in a N-myristoylation-dependent manner and facilitates the ability of CHP1 to bind microtubules. Interacts with KIF1B (via the C-terminal end of the kinesin-motor domain); the interaction occurs in a calcium-dependent manner. Associates (via C-terminal domain) with microtubules; the association occurs with polymerized microtubules during the cell cycle in a myristoylation- and calcium-independent manner and is enhanced by GAPDH.By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

IntActiP61023, 11 interactors
STRINGi10116.ENSRNOP00000053243

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Helixi11 – 21Combined sources11
Helixi25 – 38Combined sources14
Beta strandi43 – 46Combined sources4
Helixi49 – 53Combined sources5
Helixi55 – 58Combined sources4
Helixi63 – 68Combined sources6
Helixi80 – 88Combined sources9
Helixi111 – 122Combined sources12
Beta strandi127 – 130Combined sources4
Helixi132 – 142Combined sources11
Helixi149 – 163Combined sources15
Beta strandi165 – 172Combined sources8
Helixi173 – 178Combined sources6
Turni179 – 182Combined sources4
Helixi185 – 187Combined sources3
Helixi189 – 195Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CT9X-ray2.20A/B1-195[»]
ProteinModelPortaliP61023
SMRiP61023
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61023

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 61EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini71 – 106EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini110 – 145EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini151 – 186EF-hand 4PROSITE-ProRule annotationAdd BLAST36

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2 – 6Necessary for association with microtubule and interaction with GAPDH5
Motifi138 – 147Nuclear export signal 110
Motifi176 – 185Nuclear export signal 210

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0034 Eukaryota
COG5126 LUCA
GeneTreeiENSGT00860000133729
HOGENOMiHOG000233019
HOVERGENiHBG105307
InParanoidiP61023
KOiK17610
OMAiEFCRAME
OrthoDBiEOG091G0LZ1
PhylomeDBiP61023
TreeFamiTF354284

Family and domain databases

CDDicd00051 EFh, 1 hit
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
PfamiView protein in Pfam
PF13499 EF-hand_7, 1 hit
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 3 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED
60 70 80 90 100
FQRIPELAIN PLGDRIINAF FSEGEDQVNF RGFMRTLAHF RPIEDNEKSK
110 120 130 140 150
DVNGPEPLNS RSNKLHFAFR LYDLDKDDKI SRDELLQVLR MMVGVNISDE
160 170 180 190
QLGSIADRTI QEADQDGDSA ISFTEFVKVL EKVDVEQKMS IRFLH
Length:195
Mass (Da):22,432
Last modified:January 23, 2007 - v2
Checksum:i7B803EF0ABED829E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39875 mRNA Translation: AAB04146.1
AB070350 mRNA Translation: BAB63369.1
BC062029 mRNA Translation: AAH62029.1
RefSeqiNP_077053.1, NM_024139.2
UniGeneiRn.11041

Genome annotation databases

EnsembliENSRNOT00000056405; ENSRNOP00000053243; ENSRNOG00000004742
GeneIDi64152
KEGGirno:64152
UCSCiRGD:620447 rat

Similar proteinsi

Entry informationi

Entry nameiCHP1_RAT
AccessioniPrimary (citable) accession number: P61023
Secondary accession number(s): Q62877
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 122 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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