P27824 (CALX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calnexin

Alternative name(s):
IP90
Major histocompatibility complex class I antigen-binding protein p88
p90

Gene names

Name:

CANX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.13 Ref.25
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. The palmitoylated form preferentially localizes to the perinuclear rough ER. Ref.11 Ref.14 Ref.25
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 component	Endoplasmic reticulum Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Lectin Metal-binding
Molecular function	Chaperone
PTM	Acetylation Disulfide bond Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara 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 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_component	axon Inferred from electronic annotation. Source: Compara dendrite cytoplasm Inferred from electronic annotation. Source: Compara dendritic spine Inferred from electronic annotation. Source: Compara endoplasmic reticulum lumen Traceable author statement. Source: Reactome integral to 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: Compara ribosome Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Traceable author statement Ref.2. Source: ProtInc unfolded protein binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDRG1	Q92597	2	EBI-355947,EBI-716486

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 592	572	Calnexin		PRO_0000004198
Regions
	Topological domain	21 – 481	461	Lumenal Potential
	Transmembrane	482 – 502	21	Helical; Potential
	Topological domain	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	276 – 409	134	P domain (Extended arm) By similarity
	Region	278 – 345	68	4 X approximate repeats
	Region	348 – 405	58	4 X approximate repeats
	Region	503 – 592	90	Sufficient to mediate interaction with SGIP1 By similarity
Sites
	Metal binding	74	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	117	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	436	1	Calcium By similarity
	Binding site	164	1	Carbohydrate By similarity
	Binding site	166	1	Carbohydrate By similarity
	Binding site	185	1	Carbohydrate By similarity
	Binding site	216	1	Carbohydrate By similarity
Amino acid modifications
	Modified residue	137	1	N6-acetyllysine Ref.21
	Modified residue	554	1	Phosphoserine Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.24
	Modified residue	562	1	Phosphothreonine Ref.24
	Modified residue	564	1	Phosphoserine; by MAPK3 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	583	1	Phosphoserine Ref.12 Ref.15 Ref.16 Ref.22 Ref.24
	Lipidation	502	1	S-palmitoyl cysteine Ref.25
	Lipidation	503	1	S-palmitoyl cysteine Ref.25
	Disulfide bond	160 ↔ 194		By similarity
	Disulfide bond	360 ↔ 366		By similarity
Experimental info
	Sequence conflict	179	1	F → L in AAA21749. Ref.2
	Sequence conflict	431 – 433	3	SDI → LTF in AAA35696. Ref.9
	Sequence conflict	480	1	R → L in AAA35696. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P27824 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: EDE094D9B82261EE	FASTA	592	67,568
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[22]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.
+	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.
IPI	IPI00941747.
PIR	A46164. A46673. I53260.
RefSeq	NP_001019820.1. NM_001024649.1. NP_001737.1. NM_001746.3.
UniGene	Hs.567968.
3D structure databases
ProteinModelPortal	P27824.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-457N.
IntAct	P27824. 20 interactions.
MINT	MINT-5000964.
STRING	9606.ENSP00000247461.
PTM databases
PhosphoSite	P27824.
Polymorphism databases
DMDM	543920.
Proteomic databases
PaxDb	P27824.
PeptideAtlas	P27824.
PRIDE	P27824.
Protocols and materials databases
DNASU	821.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000247461; ENSP00000247461; ENSG00000127022. ENST00000452673; ENSP00000391646; ENSG00000127022. ENST00000504734; ENSP00000424063; ENSG00000127022.
GeneID	821.
KEGG	hsa:821.
UCSC	uc003mkk.3. human.
Organism-specific databases
CTD	821.
GeneCards	GC05P179105.
HGNC	HGNC:1473. CANX.
HPA	CAB004738. HPA009433. HPA009696.
MIM	114217. gene.
neXtProt	NX_P27824.
PharmGKB	PA26055.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG305105.
HOGENOM	HOG000192436.
HOVERGEN	HBG005407.
InParanoid	P27824.
KO	K08054.
PhylomeDB	P27824.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P27824.
Bgee	P27824.
CleanEx	HS_CANX.
Genevestigator	P27824.
GermOnline	ENSG00000127022. Homo sapiens.
Family and domain databases
Gene3D	2.10.250.10. 1 hit. 2.60.120.200. 1 hit.
InterPro	IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009033. Calreticulin/calnexin_P_dom. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. [Graphical view]
PANTHER	PTHR11073. PTHR11073. 1 hit.
Pfam	PF00262. Calreticulin. 1 hit. [Graphical view]
PRINTS	PR00626. CALRETICULIN.
SUPFAM	SSF63887. Calret_calnex_P. 1 hit. SSF49899. ConA_like_lec_gl. 2 hits.
PROSITE	PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 3 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P27824.
ChEMBL	CHEMBL2719.
ChiTaRS	CANX. human.
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00025. Antihemophilic Factor. DB00015. Reteplase. DB00031. Tenecteplase.
GenomeRNAi	821.
NextBio	3360.
SOURCE	Search...

Entry information

Entry name

CALX_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.