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Q99653 (CHP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-binding protein p22
Alternative name(s):
Calcineurin B homolog
Calcineurin homologous protein
Calcium-binding protein CHP
Gene names
Name:CHP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for constitutive membrane traffic. Inhibits GTPase-stimulated Na+/H+ exchange. Also inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1. Ref.7

Subunit structure

Monomer By similarity. Specifically binds to SLC9A1/NHE1 at a domain that is critical for growth factor stimulation of exchange activity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

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

Post-translational modification

Both N-myristoylation and calcium-mediated conformational changes are essential for its function in exocytic traffic By similarity.

Phosphorylated; decreased phosphorylation is associated with an increase in exchange activity. The phosphorylation state may regulate the binding to NHE1.

Sequence similarities

Contains 4 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 195194Calcium-binding protein p22
PRO_0000073843

Regions

Domain26 – 6136EF-hand 1
Domain66 – 10136EF-hand 2
Domain110 – 14536EF-hand 3
Domain151 – 18636EF-hand 4
Calcium binding123 – 134121
Calcium binding164 – 175122

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity

Secondary structure

.................................. 195
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99653 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8E82EEF0CA5E832F

FASTA19522,456
        10         20         30         40         50         60 
MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN 

        70         80         90        100        110        120 
PLGDRIINAF FPEGEDQVNF RGFMRTLAHF RPIEDNEKSK DVNGPEPLNS RSNKLHFAFR 

       130        140        150        160        170        180 
LYDLDKDEKI SRDELLQVLR MMVGVNISDE QLGSIADRTI QEADQDGDSA ISFTEFVKVL 

       190 
EKVDVEQKMS IRFLH 

« Hide

References

« Hide 'large scale' references
[1]"A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange."
Lin X., Barber D.L.
Proc. Natl. Acad. Sci. U.S.A. 93:12631-12636(1996) [PubMed: 8901634] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SLC9A1.
Tissue: B-cell.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[6]"Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein."
Lin X., Sikkink R.A., Rusnak F., Barber D.L.
J. Biol. Chem. 274:36125-36131(1999) [PubMed: 10593895] [Abstract]
Cited for: INHIBITION OF CALCINEURIN.
[7]"Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers."
Pang T., Su X., Wakabayashi S., Shigekawa M.
J. Biol. Chem. 276:17367-17372(2001) [PubMed: 11350981] [Abstract]
Cited for: FUNCTION.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1."
Mishima M., Wakabayashi S., Kojima C.
J. Biol. Chem. 282:2741-2751(2007) [PubMed: 17050540] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-195 IN COMPLEX WITH CALCIUM IONS AND SLC9A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00218924.
RefSeqNP_009167.1. NM_007236.4.
UniGeneHs.406234.
Hs.706184.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E30NMR-A1-195[»]
ProteinModelPortalQ99653.
SMRQ99653. Positions 1-195.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99653. 3 interactions.
MINTMINT-1375478.
STRINGQ99653.

PTM databases

PhosphoSiteQ99653.

Polymorphism databases

DMDM3023439.

2D gel databases

OGPQ99653.

Proteomic databases

PeptideAtlasQ99653.
PRIDEQ99653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334660; ENSP00000335632; ENSG00000187446.
GeneID11261.
KEGGhsa:11261.
UCSCuc001znl.1. human.

Organism-specific databases

CTD11261.
GeneCardsGC15P041523.
H-InvDBHIX0012148.
HPAHPA006616.
MIM606988. gene.
neXtProtNX_Q99653.

Phylogenomic databases

eggNOGprNOG07134.
GeneTreeENSGT00600000084053.
HOGENOMHBG746798.
HOVERGENHBG105307.
InParanoidQ99653.
OMAMYDLDDD.
OrthoDBEOG4PG61X.
PhylomeDBQ99653.

Enzyme and pathway databases

Pathway_Interaction_DBtcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Gene expression databases

ArrayExpressQ99653.
BgeeQ99653.
GenevestigatorQ99653.

Family and domain databases

InterProIPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
KOK06268.
PfamPF00036. efhand. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio42856.
SOURCESearch...

Entry information

Entry nameCHP1_HUMAN
AccessionPrimary (citable) accession number: Q99653
Secondary accession number(s): B2R6H9, Q6FHZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families