Reviewed, UniProtKB/Swiss-Prot P27824 (CALX_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

CANX

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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. Ref.9 Ref.12
Sequence similarities	Belongs to the calreticulin family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Repeat Signal Transmembrane
Ligand	Calcium Lectin
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: InterPro protein secretion Ref.3 Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Ref.2 Traceable author statement. Source: ProtInc sugar binding Inferred from electronic annotation. Source: UniProtKB-KW 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	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	278 – 345	68	4 X approximate repeats
	Region	348 – 405	58	4 X approximate repeats
Amino acid modifications
	Modified residue	554	1	Phosphoserine Ref.11 Ref.15 Ref.16 Ref.17 Ref.18
	Modified residue	562	1	Phosphothreonine Ref.13
	Modified residue	564	1	Phosphoserine Ref.11 Ref.15 Ref.17 Ref.18
	Modified residue	583	1	Phosphoserine Ref.11 Ref.15 Ref.16 Ref.17 Ref.13 Ref.10 Ref.14
Experimental info
	Sequence conflict	179	1	F → L in AAA21749. Ref.2
	Sequence conflict	431 – 433	3	SDI → LTF in AAA35696. Ref.7
	Sequence conflict	480	1	R → L in AAA35696. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P27824-1 [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: 8486646] [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: 8136357] [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: 8055875] [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]	"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: Placenta.
[6]	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.
[7]	"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: 1326756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 237-592.
[8]	"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: 1286667] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523. Tissue: Keratinocyte.
[9]	"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: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, MASS SPECTROMETRY.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562 AND SER-583, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, MASS SPECTROMETRY.
[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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, MASS SPECTROMETRY. Tissue: Liver.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Wikipedia

Calnexin entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	L10284 mRNA. Translation: AAA36125.1. L18887 mRNA. Translation: AAA21013.1. M94859 mRNA. Translation: AAA21749.1. M98452 mRNA. Translation: AAA35696.1. BC003552 mRNA. Translation: AAH03552.1. BC042843 mRNA. Translation: AAH42843.1. AJ271880 mRNA. Translation: CAB72137.1.
IPI	IPI00020984.
PIR	A46164. A46673. I53260.
RefSeq	NP_001019820.1. NP_001737.1.
UniGene	Hs.699155
3D structure databases
HSSP	HSSP built from PDB template 1JHN based on UniProtKB P24643.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:457N.
IntAct	P27824. 12 interactions.
PTM databases
PhosphoSite	P27824.
2-D gel databases
Aarhus/Ghent-2DPAGE	9702. IEF.
Proteomic databases
PeptideAtlas	P27824.
PRIDE	P27824.
Genome annotation databases
Ensembl	ENSG00000127022. Homo sapiens. [Contig view]
GeneID	821.
KEGG	hsa:821.
UCSC	uc003mkk.1. human.
Organism-specific databases
GeneCards	GC05P179058.
H-InvDB	HIX0005484.
HGNC	HGNC:1473. CANX.
HPA	CAB004738. HPA009433. HPA009696.
MIM	114217. gene.
PharmGKB	PA26055.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P27824.
HOVERGEN	P27824.
OMA	P27824. FDNFIIS.
Gene expression databases
ArrayExpress	P27824.
Bgee	P27824.
CleanEx	HS_CANX.
GermOnline	ENSG00000127022. Homo sapiens.
Family and domain databases
InterPro	IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009033. Calreticulin/calnexin_P. IPR013320. ConA-like_subgrp. [Graphical view]
Gene3D	G3DSA:2.10.250.10. Calreticulin/calnexin_P. 1 hit. G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PANTHER	PTHR11073. Calret/calnex. 1 hit.
Pfam	PF00262. Calreticulin. 1 hit. [Graphical view]
PRINTS	PR00626. CALRETICULIN.
ProDom	PD001866. Calret/calnex. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00025. Antihemophilic Factor. DB00015. Reteplase. DB00031. Tenecteplase.
NextBio	3360.
SOURCE	Search...

Entry information

Entry name

CALX_HUMAN

Accession

Primary (citable) accession number: P27824

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	June 1, 1994
Last modified:	July 7, 2009
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)