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: 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 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)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi123 – 134121Add
BLAST
Calcium bindingi164 – 175122Add
BLAST

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

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

Organism-specific databases

HGNCiHGNC:17433. 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

  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi membrane Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • transport vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501D → A: Does not reduce calcium-binding, colocalization and interaction with SLC9A1. 1 Publication
Mutagenesisi134 – 1341E → 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 Publication
Mutagenesisi143 – 1431V → A: Inhibits translocation to the cytoplasm; when associated with A-145; A-147; A-183 and A-185. 1 Publication
Mutagenesisi145 – 1451V → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-147; A-183 and A-185. 1 Publication
Mutagenesisi147 – 1471I → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-183 and A-185. 1 Publication
Mutagenesisi175 – 1751E → 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 Publication
Mutagenesisi183 – 1831V → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-147 and A-185. 1 Publication
Mutagenesisi185 – 1851V → A: Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-147 and A-183. 1 Publication

Polymorphism and mutation databases

BioMutaiCHP1.
DMDMi3023439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 195194Calcineurin B homologous protein 1PRO_0000073843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication

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.
TopDownProteomicsiQ99653.

2D gel databases

OGPiQ99653.

PTM databases

iPTMnetiQ99653.
PhosphoSiteiQ99653.
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

BgeeiQ99653.
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

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

Protein-protein interaction databases

BioGridi116421. 13 interactions.
IntActiQ99653. 8 interactions.
MINTiMINT-1375478.
STRINGi9606.ENSP00000335632.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2212Combined sources
Helixi26 – 3712Combined sources
Turni38 – 414Combined sources
Helixi48 – 514Combined sources
Helixi57 – 593Combined sources
Helixi64 – 707Combined sources
Helixi80 – 889Combined sources
Beta strandi95 – 984Combined sources
Beta strandi107 – 1093Combined sources
Helixi111 – 12212Combined sources
Beta strandi127 – 1304Combined sources
Helixi132 – 14312Combined sources
Turni144 – 1463Combined sources
Helixi149 – 16315Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi171 – 1733Combined sources
Helixi174 – 1807Combined sources
Helixi185 – 1884Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E30NMR-A1-195[»]
ProteinModelPortaliQ99653.
SMRiQ99653. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6136EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini66 – 10136EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini110 – 14536EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 18636EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 18543Necessary for nuclear export signalAdd
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.
InParanoidiQ99653.
KOiK17610.
OMAiFQPISRV.
PhylomeDBiQ99653.
TreeFamiTF354284.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E30NMR-A1-195[»]
ProteinModelPortaliQ99653.
SMRiQ99653. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116421. 13 interactions.
IntActiQ99653. 8 interactions.
MINTiMINT-1375478.
STRINGi9606.ENSP00000335632.

PTM databases

iPTMnetiQ99653.
PhosphoSiteiQ99653.
SwissPalmiQ99653.

Polymorphism and mutation databases

BioMutaiCHP1.
DMDMi3023439.

2D gel databases

OGPiQ99653.

Proteomic databases

EPDiQ99653.
MaxQBiQ99653.
PaxDbiQ99653.
PeptideAtlasiQ99653.
PRIDEiQ99653.
TopDownProteomicsiQ99653.

Protocols and materials databases

DNASUi11261.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11261.
GeneCardsiCHP1.
HGNCiHGNC:17433. CHP1.
HPAiHPA006616.
MIMi606988. gene.
neXtProtiNX_Q99653.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119179.
HOGENOMiHOG000233019.
HOVERGENiHBG105307.
InParanoidiQ99653.
KOiK17610.
OMAiFQPISRV.
PhylomeDBiQ99653.
TreeFamiTF354284.

Enzyme and pathway databases

ReactomeiR-HSA-2160916. Hyaluronan uptake and degradation.

Miscellaneous databases

EvolutionaryTraceiQ99653.
GeneWikiiCHP_(gene).
GenomeRNAii11261.
PROiQ99653.
SOURCEiSearch...

Gene expression databases

BgeeiQ99653.
ExpressionAtlasiQ99653. baseline and differential.
GenevisibleiQ99653. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PH REGULATION, CALCIUM-BINDING, INTERACTION WITH SLC9A1, PHOSPHORYLATION, TISSUE SPECIFICITY.
    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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CALCINEURIN INHIBITOR, INTERACTION WITH PPP3CA.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC9A1, SUBCELLULAR LOCATION.
  8. "Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements."
    Pang T., Hisamitsu T., Mori H., Shigekawa M., Wakabayashi S.
    Biochemistry 43:3628-3636(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC9A1, SUBCELLULAR LOCATION, CALCIUM-BINDING, MUTAGENESIS OF ASP-50; GLU-134 AND GLU-175.
  9. "Nuclear-localized calcineurin homologous protein CHP1 interacts with upstream binding factor and inhibits ribosomal RNA synthesis."
    Jimenez-Vidal M., Srivastava J., Putney L.K., Barber D.L.
    J. Biol. Chem. 285:36260-36266(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-143; VAL-145; ILE-147; VAL-183 AND VAL-185.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-195 IN COMPLEX WITH CALCIUM IONS AND SLC9A1.

Entry informationi

Entry nameiCHP1_HUMAN
AccessioniPrimary (citable) accession number: Q99653
Secondary accession number(s): B2R6H9, Q6FHZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 162 of the entry and version 3 of the sequence. [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

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.