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Protein

Calcineurin B homologous protein 1

Gene

Chp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 membranes. 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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi123 – 134121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi164 – 175122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protein kinase inhibitor

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-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
Sid 470
p24
Gene namesi
Name:Chp1
Synonyms:Chp, Sid470
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1927185. Chp1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity
  • Endomembrane system By similarity
  • Endoplasmic reticulum-Golgi intermediate compartment By similarity
  • Endoplasmic reticulum By similarity
  • Cell membrane By similarity
  • Membrane By similarity; Lipid-anchor By similarity

  • 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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 195194Calcineurin B homologous protein 1PRO_0000073844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity

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

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiP61022.
MaxQBiP61022.
PaxDbiP61022.
PRIDEiP61022.

PTM databases

iPTMnetiP61022.
PhosphoSiteiP61022.

Expressioni

Gene expression databases

BgeeiP61022.
CleanExiMM_1500003O03RIK.
ExpressionAtlasiP61022. baseline and differential.
GenevisibleiP61022. MM.

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. 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). Interacts with SLC9A1/NHE1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP61022. 2 interactions.
MINTiMINT-1786124.
STRINGi10090.ENSMUSP00000014221.

Structurei

3D structure databases

ProteinModelPortaliP61022.
SMRiP61022. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6136EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini71 – 10636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini110 – 14536EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 18636EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2 – 65Necessary for association with microtubule and interaction with GAPDHBy similarity
Motifi138 – 14710Nuclear export signal 1By similarity
Motifi176 – 18510Nuclear export signal 2By similarity

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119179.
HOGENOMiHOG000233019.
HOVERGENiHBG105307.
InParanoidiP61022.
KOiK17610.
OMAiFQPISRV.
OrthoDBiEOG78M035.
PhylomeDBiP61022.
TreeFamiTF354284.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61022-1 [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
AB025217 mRNA. Translation: BAA84688.1.
AK005067 mRNA. Translation: BAB23791.1.
AK045920 mRNA. Translation: BAC32532.1.
AK156588 mRNA. Translation: BAE33769.1.
AK166219 mRNA. Translation: BAE38637.1.
AK167179 mRNA. Translation: BAE39314.1.
AK167720 mRNA. Translation: BAE39762.1.
AK168284 mRNA. Translation: BAE40230.1.
AK169146 mRNA. Translation: BAE40925.1.
BC054733 mRNA. Translation: AAH54733.1.
BC064784 mRNA. Translation: AAH64784.1.
CCDSiCCDS16604.1.
RefSeqiNP_062743.1. NM_019769.3.
UniGeneiMm.214765.

Genome annotation databases

EnsembliENSMUST00000014221; ENSMUSP00000014221; ENSMUSG00000014077.
GeneIDi56398.
KEGGimmu:56398.
UCSCiuc008ltw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025217 mRNA. Translation: BAA84688.1.
AK005067 mRNA. Translation: BAB23791.1.
AK045920 mRNA. Translation: BAC32532.1.
AK156588 mRNA. Translation: BAE33769.1.
AK166219 mRNA. Translation: BAE38637.1.
AK167179 mRNA. Translation: BAE39314.1.
AK167720 mRNA. Translation: BAE39762.1.
AK168284 mRNA. Translation: BAE40230.1.
AK169146 mRNA. Translation: BAE40925.1.
BC054733 mRNA. Translation: AAH54733.1.
BC064784 mRNA. Translation: AAH64784.1.
CCDSiCCDS16604.1.
RefSeqiNP_062743.1. NM_019769.3.
UniGeneiMm.214765.

3D structure databases

ProteinModelPortaliP61022.
SMRiP61022. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP61022. 2 interactions.
MINTiMINT-1786124.
STRINGi10090.ENSMUSP00000014221.

PTM databases

iPTMnetiP61022.
PhosphoSiteiP61022.

Proteomic databases

EPDiP61022.
MaxQBiP61022.
PaxDbiP61022.
PRIDEiP61022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014221; ENSMUSP00000014221; ENSMUSG00000014077.
GeneIDi56398.
KEGGimmu:56398.
UCSCiuc008ltw.1. mouse.

Organism-specific databases

CTDi11261.
MGIiMGI:1927185. Chp1.

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119179.
HOGENOMiHOG000233019.
HOVERGENiHBG105307.
InParanoidiP61022.
KOiK17610.
OMAiFQPISRV.
OrthoDBiEOG78M035.
PhylomeDBiP61022.
TreeFamiTF354284.

Enzyme and pathway databases

ReactomeiR-MMU-2160916. Hyaluronan uptake and degradation.

Miscellaneous databases

PROiP61022.
SOURCEiSearch...

Gene expression databases

BgeeiP61022.
CleanExiMM_1500003O03RIK.
ExpressionAtlasiP61022. baseline and differential.
GenevisibleiP61022. MM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse calcium binding protein p22."
    Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ, C57BL/6J and NOD.
    Tissue: Corpora quadrigemina, Liver, Mammary gland, Placenta and Spleen.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  4. "Coimmunoprecipitation of a 24-kDa protein with NHE1, the ubiquitous isoform of the Na+/H+ exchanger."
    Goss G., Orlowski J., Grinstein S.
    Am. J. Physiol. 270:C1493-C1502(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A1.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCHP1_MOUSE
AccessioniPrimary (citable) accession number: P61022
Secondary accession number(s): Q62877, Q6ZWQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.