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UniProtKB/Swiss-Prot entry P27824


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CALX_HUMAN
Primary accession number P27824
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 102)
Name and origin of the protein
Protein name Calnexin [Precursor]
Synonyms Major histocompatibility complex class I antigen-binding protein p88
p90
IP90
Gene name
Name: CANX
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8486646 [NCBI, ExPASy, EBI, Israel, Japan]
David V., Hochstenbach F., Rajagopalan S., Brenner M.B.;
"Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin).";
J. Biol. Chem. 268:9585-9592(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymph, and Placenta;
DOI=10.1021/bi00177a013; PubMed=8136357 [NCBI, ExPASy, EBI, Israel, Japan]
Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., Calderon J., Schreiber R.B., Gray P.W.;
"Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5.";
Biochemistry 33:3229-3236(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Keratinocyte;
PubMed=8055875 [NCBI, ExPASy, EBI, Israel, Japan]
Honore B., Rasmussen H.H., Celis A., Leffers H., Madsen P., Celis J.E.;
"The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin.";
Electrophoresis 15:482-490(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
Hansen J.J., Jorgensen M.M., Bolund L., Gregersen N.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 62-77; 171-193; 200-205; 221-227; 401-415; 517-525 AND 574-582, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 237-592.
PubMed=1326756 [NCBI, ExPASy, EBI, Israel, Japan]
Galvin K., Krishna S., Ponchel F., Frohlich M., Cummings D.E., Carlson R., Wands J.R., Isselbacher K.J., Pillai S., Ozturk M.;
"The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:8452-8456(1992).
[8]
PARTIAL PROTEIN SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr025562r; PubMed=12643545 [NCBI, ExPASy, EBI, Israel, Japan]
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562 AND SER-583, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
Comments
  • FUNCTION: Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins.
  • INTERACTION:
    Q92597:NDRG1; NbExp=2; IntAct=EBI-355947, EBI-716486;
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
  • SIMILARITY: Belongs to the calreticulin family.
  • WEB RESOURCE: Name=Wikipedia; Note=Calnexin entry; URL="http://en.wikipedia.org/wiki/Calnexin";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L10284; AAA36125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L18887; AAA21013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M94859; AAA21749.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M98452; AAA35696.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003552; AAH03552.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042843; AAH42843.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271880; CAB72137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A46164; A46164.
A46673; A46673.
I53260; I53260.
RefSeq NP_001019820.1; -.
NP_001737.1; -.
UniGene Hs.699155
3D structure databases
HSSP P24643; 1JHN. [HSSP ENTRY / PDB]
ModBase P27824.
Protein-protein interaction databases
DIP DIP:457N; -.
IntAct P27824; -.
PTM databases
PhosphoSite P27824; -.
2D gel databases
Aarhus/Ghent-2DPAGE 9702; IEF.
Organism-specific databases
H-InvDB HIX0005484; -.
HGNC HGNC:1473; CANX.
GenAtlas CANX.
HPA CAB004738; -.
HPA009433; -.
HPA009696; -.
MIM 114217; gene. [NCBI / EBI]
PharmGKB PA26055; -.
GeneCards P27824.
Gene expression databases
ArrayExpress P27824; -.
CleanEx HS_CANX; -.
GermOnline ENSG00000127022; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509; Molecular function: calcium ion binding (traceable author statement from ProtInc).
GO:0005529; Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (non-traceable author statement from UniProtKB).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from InterPro).
GO:0009306; Biological process: protein secretion (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001580; Calret/calnex.
IPR009033; Calreticulin/calnexin_P.
IPR013320; ConA_like_subgrp.
Graphical view of domain structure.
Gene3D G3DSA:2.10.250.10; Calreticulin/calnexin_P; 1.
G3DSA:2.60.120.200; ConA_like_subgrp; 1.
PANTHER PTHR11073; Calret/calnex; 1.
Pfam PF00262; Calreticulin; 1.
Pfam graphical view of domain structure.
PRINTS PR00626; CALRETICULIN.
ProDom PD001866; Calret/calnex; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00803; CALRETICULIN_1; 1.
PS00804; CALRETICULIN_2; 1.
PS00805; CALRETICULIN_REPEAT; 3.
BLOCKS P27824.
ProtoNet P27824.
Proteomic databases
PeptideAtlas P27824; -.
Genome annotation databases
Ensembl ENSG00000127022; Homo sapiens. [Contig view]
GeneID 821; -.
KEGG hsa:821; -.
Phylogenomic databases
HOGENOM P27824; -.
HOVERGEN P27824; -.
Other
DrugBank DB00009; Alteplase.
DB00029; Anistreplase.
DB00025; Antihemophilic Factor.
DB00015; Reteplase.
DB00031; Tenecteplase.
NextBio 3360; -.
SOURCE CANX; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Chaperone; Direct protein sequencing; Endoplasmic reticulum; Lectin; Membrane; Phosphoprotein; Repeat; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
CHAIN   21   592  572     Calnexin. PRO_0000004198
TOPO_DOM   21   481  461     Lumenal (Potential). 
TRANSMEM   482   502  21     Potential. 
TOPO_DOM   503   592  90     Cytoplasmic (Potential). 
REPEAT   278   290  13     1-1. 
REPEAT   295   307  13     1-2. 
REPEAT   314   326  13     1-3. 
REPEAT   333   345  13     1-4. 
REPEAT   348   358  11     2-1. 
REPEAT   367   377  11     2-2. 
REPEAT   381   391  11     2-3. 
REPEAT   395   405  11     2-4. 
REGION   278   345  68     4 X approximate repeats. 
REGION   348   405  58     4 X approximate repeats. 
MOD_RES   554   554        Phosphoserine. 
MOD_RES   562   562        Phosphothreonine. 
MOD_RES   564   564        Phosphoserine. 
MOD_RES   583   583        Phosphoserine. 
CONFLICT   179   179        F -> L (in Ref. 2; AAA21749). 
CONFLICT   431   433        SDI -> LTF (in Ref. 7; AAA35696). 
CONFLICT   480   480        R -> L (in Ref. 4; AAA35696). 
Sequence information
Length: 592 AA [This is the length of the unprocessed precursor] Molecular weight: 67568 Da [This is the MW of the unprocessed precursor] CRC64: EDE094D9B82261EE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY 

        70         80         90        100        110        120 
KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVEEMK ESKLPGDKGL 

       130        140        150        160        170        180 
VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH 

       190        200        210        220        230        240 
DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL 

       250        260        270        280        290        300 
ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK 

       310        320        330        340        350        360 
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPRC 

       370        380        390        400        410        420 
ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS 

       430        440        450        460        470        480 
AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER 

       490        500        510        520        530        540 
PWLWVVYILT VALPVFLVIL FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE 

       550        560        570        580        590 
EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE 

P27824 in FASTA format

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