Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calcineurin B homologous protein 1

Gene

CHP1

Organism
Homo sapiens (Human)
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.4 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: UniProtKB
  • kinase binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • potassium channel regulator activity Source: ProtInc
  • protein kinase inhibitor activity Source: UniProtKB-KW
  • transporter activity Source: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-2160916 Hyaluronan uptake and degradation

Protein family/group databases

TCDBi8.A.82.1.6 the calmodulin calcium binding protein (calmodulin) family

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000187446.11
HGNCiHGNC:17433 CHP1
MIMi606988 gene
neXtProtiNX_Q99653

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
Mutagenesisi50D → A: Does not reduce calcium-binding, colocalization and interaction with SLC9A1. 1 Publication1
Mutagenesisi134E → A: Reduces calcium-binding and SLC9A1-dependent Na(+)/H(+) exchange activity. Does not reduce colocalization and interaction with SLC9A1. Reduces colocalization and interaction with SLC9A1; when associated with A-175. 1 Publication1
Mutagenesisi143V → A: Inhibits translocation to the cytoplasm; when associated with A-145; A-147; A-183 and A-185. 1 Publication1
Mutagenesisi145V → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-147; A-183 and A-185. 1 Publication1
Mutagenesisi147I → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-183 and A-185. 1 Publication1
Mutagenesisi175E → A: Reduces calcium-binding and SLC9A1-dependent Na(+)/H(+) exchange activity. Does not reduce colocalization and interaction with SLC9A1. Reduces colocalization and interaction with SLC9A1; when associated with A-134. 1 Publication1
Mutagenesisi183V → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-147 and A-185. 1 Publication1
Mutagenesisi185V → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-147 and A-183. 1 Publication1

Organism-specific databases

DisGeNETi11261
OpenTargetsiENSG00000187446

Polymorphism and mutation databases

BioMutaiCHP1
DMDMi3023439

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000738432 – 195Calcineurin B homologous protein 1Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1

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/NHE1.1 Publication
Both N-myristoylation and calcium-mediated conformational changes are essential for its function in exocytic traffic (By similarity). N-myristoylation is required for its association with microtubules and interaction with GAPDH, but not for the constitutive association to membranes.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ99653
MaxQBiQ99653
PaxDbiQ99653
PeptideAtlasiQ99653
PRIDEiQ99653
ProteomicsDBi78381
TopDownProteomicsiQ99653

2D gel databases

OGPiQ99653

PTM databases

iPTMnetiQ99653
PhosphoSitePlusiQ99653
SwissPalmiQ99653

Expressioni

Tissue specificityi

Ubiquitously expressed. Has been found in fetal eye, lung, liver, muscle, heart, kidney, thymus and spleen.1 Publication

Gene expression databases

BgeeiENSG00000187446 Expressed in 231 organ(s), highest expression level in colon
ExpressionAtlasiQ99653 baseline and differential
GenevisibleiQ99653 HS

Organism-specific databases

HPAiHPA006616

Interactioni

Subunit structurei

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 similarity). 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 similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116421, 17 interactors
IntActiQ99653, 19 interactors
MINTiQ99653
STRINGi9606.ENSP00000335632

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ99653
SMRiQ99653
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99653

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 61EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini66 – 101EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini110 – 145EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini151 – 186EF-hand 4PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni143 – 185Necessary for nuclear export signalAdd BLAST43

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2 – 6Necessary for association with microtubule and interaction with GAPDHBy similarity5
Motifi138 – 147Nuclear export signal 1By similarity10
Motifi176 – 185Nuclear export signal 2By similarity10

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0034 Eukaryota
COG5126 LUCA
GeneTreeiENSGT00860000133729
HOGENOMiHOG000233019
HOVERGENiHBG105307
InParanoidiQ99653
KOiK17610
OMAiEFCRAME
OrthoDBiEOG091G0LZ1
PhylomeDBiQ99653
TreeFamiTF354284

Family and domain databases

CDDicd00051 EFh, 1 hit
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
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
PS50222 EF_HAND_2, 3 hits

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.iShow all

Q99653-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED
60 70 80 90 100
FQRIPELAIN PLGDRIINAF FPEGEDQVNF RGFMRTLAHF RPIEDNEKSK
110 120 130 140 150
DVNGPEPLNS RSNKLHFAFR LYDLDKDEKI SRDELLQVLR MMVGVNISDE
160 170 180 190
QLGSIADRTI QEADQDGDSA ISFTEFVKVL EKVDVEQKMS IRFLH
Length:195
Mass (Da):22,456
Last modified:January 23, 2007 - v3
Checksum:i8E82EEF0CA5E832F
GO

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YKE7H0YKE7_HUMAN
Calcineurin B homologous protein 1
CHP1
123Annotation score:
H0YNG9H0YNG9_HUMAN
Calcineurin B homologous protein 1
CHP1
154Annotation score:
F5GX29F5GX29_HUMAN
Calcineurin B homologous protein 1
CHP1
128Annotation score:
H0YLY7H0YLY7_HUMAN
Calcineurin B homologous protein 1
CHP1
91Annotation score:
H0YLX1H0YLX1_HUMAN
Calcineurin B homologous protein 1
CHP1
53Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61538 mRNA Translation: AAB37770.1
CR536539 mRNA Translation: CAG38776.1
CR542085 mRNA Translation: CAG46882.1
AK312582 mRNA Translation: BAG35476.1
CH471125 Genomic DNA Translation: EAW92474.1
BC031293 mRNA Translation: AAH31293.1
BC051815 mRNA No translation available.
CCDSiCCDS10073.1
RefSeqiNP_009167.1, NM_007236.4
UniGeneiHs.406234
Hs.745372

Genome annotation databases

EnsembliENST00000334660; ENSP00000335632; ENSG00000187446
GeneIDi11261
KEGGihsa:11261
UCSCiuc001znl.4 human

Similar proteinsi

Entry informationi

Entry nameiCHP1_HUMAN
AccessioniPrimary (citable) accession number: Q99653
Secondary accession number(s): B2R6H9, Q6FHZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 181 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again