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P27824 (CALX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calnexin
Alternative name(s):
IP90
Major histocompatibility complex class I antigen-binding protein p88
p90
Gene names
Name:CANX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.

Subunit structure

Interacts with MAPK3/ERK1. Interacts with KCNH2. Associates with ribosomes. Interacts with SGIP1; involved in negative regulation of endocytosis By similarity. The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins. Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Interacts with PPIB. Ref.13 Ref.22 Ref.25 Ref.27 Ref.28

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. The palmitoylated form preferentially localizes to the perinuclear rough ER. Ref.11 Ref.14 Ref.27 Ref.28

Post-translational modification

Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes By similarity.

Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins.

Sequence similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Lectin
Metal-binding
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

chaperone-mediated protein folding

Inferred from electronic annotation. Source: Ensembl

clathrin-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein folding

Traceable author statement. Source: Reactome

protein secretion

Traceable author statement Ref.3. Source: ProtInc

synaptic vesicle endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

dendrite cytoplasm

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay Ref.28. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from direct assay PubMed 19723497. Source: MGI

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

ribosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Traceable author statement Ref.2. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.28. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 592572Calnexin
PRO_0000004198

Regions

Topological domain21 – 481461Lumenal Potential
Transmembrane482 – 50221Helical; Potential
Topological domain503 – 59290Cytoplasmic Potential
Repeat278 – 290131-1
Repeat295 – 307131-2
Repeat314 – 326131-3
Repeat333 – 345131-4
Repeat348 – 358112-1
Repeat367 – 377112-2
Repeat381 – 391112-3
Repeat395 – 405112-4
Region276 – 409134P domain (Extended arm) By similarity
Region278 – 345684 X approximate repeats
Region326 – 35934Interaction with PPIB By similarity
Region348 – 405584 X approximate repeats
Region503 – 59290Sufficient to mediate interaction with SGIP1 By similarity

Sites

Metal binding741Calcium; via carbonyl oxygen By similarity
Metal binding1171Calcium; via carbonyl oxygen By similarity
Metal binding4361Calcium By similarity
Binding site1641Carbohydrate By similarity
Binding site1661Carbohydrate By similarity
Binding site1851Carbohydrate By similarity
Binding site2161Carbohydrate By similarity

Amino acid modifications

Modified residue1371N6-acetyllysine Ref.21
Modified residue5541Phosphoserine Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.23 Ref.26
Modified residue5621Phosphothreonine Ref.26
Modified residue5641Phosphoserine; by MAPK3 Ref.17 Ref.20 Ref.23 Ref.26
Modified residue5831Phosphoserine Ref.12 Ref.15 Ref.16 Ref.23 Ref.26
Lipidation5021S-palmitoyl cysteine Ref.27
Lipidation5031S-palmitoyl cysteine Ref.27
Disulfide bond160 ↔ 194 By similarity
Disulfide bond360 ↔ 366 By similarity

Experimental info

Sequence conflict1791F → L in AAA21749. Ref.2
Sequence conflict431 – 4333SDI → LTF in AAA35696. Ref.9
Sequence conflict4801R → L in AAA35696. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P27824 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: EDE094D9B82261EE

FASTA59267,568
        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 

« Hide

References

« Hide 'large scale' references
[1]"Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)."
David V., Hochstenbach F., Rajagopalan S., Brenner M.B.
J. Biol. Chem. 268:9585-9592(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5."
Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., Calderon J., Schreiber R.B., Gray P.W.
Biochemistry 33:3229-3236(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymph and Placenta.
[3]"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."
Honore B., Rasmussen H.H., Celis A., Leffers H., Madsen P., Celis J.E.
Electrophoresis 15:482-490(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Keratinocyte.
[4]Hansen J.J., Jorgensen M.M., Bolund L., Gregersen N.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Placenta.
[8]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 62-77; 171-193; 200-205; 221-227; 401-415; 517-525 AND 574-582, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]"The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene."
Galvin K., Krishna S., Ponchel F., Frohlich M., Cummings D.E., Carlson R., Wands J.R., Isselbacher K.J., Pillai S., Ozturk M.
Proc. Natl. Acad. Sci. U.S.A. 89:8452-8456(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 237-592.
[10]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523.
Tissue: Keratinocyte.
[11]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
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.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Mechanisms of pharmacological rescue of trafficking-defective hERG mutant channels in human long QT syndrome."
Gong Q., Jones M.A., Zhou Z.
J. Biol. Chem. 281:4069-4074(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNH2.
[14]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
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.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[15]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain."
Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.
J. Biol. Chem. 285:35551-35557(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIB.
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH DERL1; DERL2; DDOST; RPN1; RPN2; SELK; STT3A; VIMP AND VCP.
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562; SER-564 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Palmitoylated calnexin is a key component of the ribosome-translocon complex."
Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A., Dal Peraro M., van der Goot F.G.
EMBO J. 31:1823-1835(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-502 AND CYS-503 BY DHHC6, SUBCELLULAR LOCATION, INTERACTION WITH SSR1.
[28]"SERPINA2 is a novel gene with a divergent function from SERPINA1."
Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I., Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.
PLoS ONE 8:E66889-E66889(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SERPINA2P AND SERPINA1, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Wikipedia

Calnexin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10284 mRNA. Translation: AAA36125.1.
L18887 mRNA. Translation: AAA21013.1.
M94859 mRNA. Translation: AAA21749.1.
M98452 mRNA. Translation: AAA35696.1.
AK312334 mRNA. Translation: BAG35255.1.
CH471165 Genomic DNA. Translation: EAW53802.1.
CH471165 Genomic DNA. Translation: EAW53803.1.
CH471165 Genomic DNA. Translation: EAW53805.1.
BC003552 mRNA. Translation: AAH03552.1.
BC042843 mRNA. Translation: AAH42843.1.
AJ271880 mRNA. Translation: CAB72137.1.
CCDSCCDS4447.1.
PIRA46164.
A46673.
I53260.
RefSeqNP_001019820.1. NM_001024649.1.
NP_001737.1. NM_001746.3.
UniGeneHs.567968.

3D structure databases

ProteinModelPortalP27824.
SMRP27824. Positions 60-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107271. 78 interactions.
DIPDIP-457N.
IntActP27824. 63 interactions.
MINTMINT-5000964.
STRING9606.ENSP00000247461.

Chemistry

BindingDBP27824.
ChEMBLCHEMBL2719.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00025. Antihemophilic Factor.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP27824.

Polymorphism databases

DMDM543920.

Proteomic databases

MaxQBP27824.
PaxDbP27824.
PeptideAtlasP27824.
PRIDEP27824.

Protocols and materials databases

DNASU821.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247461; ENSP00000247461; ENSG00000127022.
ENST00000452673; ENSP00000391646; ENSG00000127022.
ENST00000504734; ENSP00000424063; ENSG00000127022.
GeneID821.
KEGGhsa:821.
UCSCuc003mkk.3. human.

Organism-specific databases

CTD821.
GeneCardsGC05P179105.
HGNCHGNC:1473. CANX.
HPACAB004738.
HPA009433.
HPA009696.
MIM114217. gene.
neXtProtNX_P27824.
PharmGKBPA26055.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305105.
HOGENOMHOG000192436.
HOVERGENHBG005407.
InParanoidP27824.
KOK08054.
OrthoDBEOG77126Z.
PhylomeDBP27824.
TreeFamTF300618.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP27824.
BgeeP27824.
CleanExHS_CANX.
GenevestigatorP27824.

Family and domain databases

Gene3D2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCANX. human.
GeneWikiCalnexin.
GenomeRNAi821.
NextBio3360.
PROP27824.
SOURCESearch...

Entry information

Entry nameCALX_HUMAN
AccessionPrimary (citable) accession number: P27824
Secondary accession number(s): B2R5V8, D3DWQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 165 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM