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P27824

- CALX_HUMAN

UniProt

P27824 - CALX_HUMAN

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Protein

Calnexin

Gene

CANX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Calcium; via carbonyl oxygenBy similarity
Metal bindingi117 – 1171Calcium; via carbonyl oxygenBy similarity
Binding sitei164 – 1641CarbohydrateBy similarity
Binding sitei166 – 1661CarbohydrateBy similarity
Binding sitei185 – 1851CarbohydrateBy similarity
Binding sitei216 – 2161CarbohydrateBy similarity
Metal bindingi436 – 4361CalciumBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. carbohydrate binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  4. cellular protein metabolic process Source: Reactome
  5. chaperone-mediated protein folding Source: Ensembl
  6. clathrin-mediated endocytosis Source: UniProtKB
  7. post-translational protein modification Source: Reactome
  8. protein folding Source: Reactome
  9. protein N-linked glycosylation via asparagine Source: Reactome
  10. protein secretion Source: ProtInc
  11. synaptic vesicle endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_23810. Calnexin/calreticulin cycle.
REACT_6277. Assembly of Viral Components at the Budding Site.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Calnexin
Alternative name(s):
IP90
Major histocompatibility complex class I antigen-binding protein p88
p90
Gene namesi
Name:CANX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1473. CANX.

Subcellular locationi

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.

GO - Cellular componenti

  1. axon Source: Ensembl
  2. dendrite cytoplasm Source: Ensembl
  3. dendritic spine Source: Ensembl
  4. endoplasmic reticulum Source: UniProtKB
  5. endoplasmic reticulum lumen Source: Reactome
  6. endoplasmic reticulum membrane Source: MGI
  7. ER-mitochondrion membrane contact site Source: MGI
  8. extracellular vesicular exosome Source: UniProtKB
  9. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  10. membrane Source: UniProtKB
  11. neuronal cell body Source: Ensembl
  12. protein complex Source: Ensembl
  13. ribosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 592572CalnexinPRO_0000004198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371N6-acetyllysine1 Publication
Disulfide bondi160 ↔ 194By similarity
Disulfide bondi360 ↔ 366By similarity
Lipidationi502 – 5021S-palmitoyl cysteine1 Publication
Lipidationi503 – 5031S-palmitoyl cysteine1 Publication
Modified residuei554 – 5541Phosphoserine8 Publications
Modified residuei562 – 5621Phosphothreonine1 Publication
Modified residuei564 – 5641Phosphoserine; by MAPK34 Publications
Modified residuei583 – 5831Phosphoserine5 Publications

Post-translational modificationi

Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes By similarity.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.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP27824.
PaxDbiP27824.
PeptideAtlasiP27824.
PRIDEiP27824.

PTM databases

PhosphoSiteiP27824.

Expressioni

Gene expression databases

BgeeiP27824.
CleanExiHS_CANX.
ExpressionAtlasiP27824. baseline and differential.
GenevestigatoriP27824.

Organism-specific databases

HPAiCAB004738.
HPA009433.
HPA009696.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP2A2P116072EBI-355947,EBI-8004986From a different organism.
CFTRP135693EBI-355947,EBI-349854
NDRG1Q925972EBI-355947,EBI-716486
OPRD1P411432EBI-355947,EBI-2624456
RPL12P300503EBI-355947,EBI-352743
SEC61A1P616193EBI-355947,EBI-358919
SSR1P433075EBI-355947,EBI-714168

Protein-protein interaction databases

BioGridi107271. 88 interactions.
DIPiDIP-457N.
IntActiP27824. 64 interactions.
MINTiMINT-5000964.
STRINGi9606.ENSP00000247461.

Structurei

3D structure databases

ProteinModelPortaliP27824.
SMRiP27824. Positions 60-457.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 481461LumenalSequence AnalysisAdd
BLAST
Topological domaini503 – 59290CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei482 – 50221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati278 – 290131-1Add
BLAST
Repeati295 – 307131-2Add
BLAST
Repeati314 – 326131-3Add
BLAST
Repeati333 – 345131-4Add
BLAST
Repeati348 – 358112-1Add
BLAST
Repeati367 – 377112-2Add
BLAST
Repeati381 – 391112-3Add
BLAST
Repeati395 – 405112-4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 409134P domain (Extended arm)By similarityAdd
BLAST
Regioni278 – 345684 X approximate repeatsAdd
BLAST
Regioni326 – 35934Interaction with PPIBBy similarityAdd
BLAST
Regioni348 – 405584 X approximate repeatsAdd
BLAST
Regioni503 – 59290Sufficient to mediate interaction with SGIP1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192436.
HOVERGENiHBG005407.
InParanoidiP27824.
KOiK08054.
OrthoDBiEOG77126Z.
PhylomeDBiP27824.
TreeFamiTF300618.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P27824-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT
60 70 80 90 100
APPSSPKVTY KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY
110 120 130 140 150
DGKWEVEEMK ESKLPGDKGL VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY
160 170 180 190 200
EVNFQNGIEC GGAYVKLLSK TPELNLDQFH DKTPYTIMFG PDKCGEDYKL
210 220 230 240 250
HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL ILNPDNSFEI
260 270 280 290 300
LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK
310 320 330 340 350
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW
360 370 380 390 400
EAPQIANPRC ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR
410 420 430 440 450
KIPNPDFFED LEPFRMTPFS AIGLELWSMT SDIFFDNFII CADRRIVDDW
460 470 480 490 500
ANDGWGLKKA ADGAAEPGVV GQMIEAAEER PWLWVVYILT VALPVFLVIL
510 520 530 540 550
FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE EEEGEEKLEE
560 570 580 590
KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE
Length:592
Mass (Da):67,568
Last modified:June 1, 1994 - v2
Checksum:iEDE094D9B82261EE
GO
Isoform 2 (identifier: P27824-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADRRTPTPFAGCRLPRQRRARDASQVSAPGTRRIM

Note: No experimental confirmation available.

Show »
Length:627
Mass (Da):71,503
Checksum:iE9AD69A866261080
GO
Isoform 3 (identifier: P27824-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: No experimental confirmation available.

Show »
Length:484
Mass (Da):55,598
Checksum:i61BB56B36E8C7A4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791F → L in AAA21749. (PubMed:8136357)Curated
Sequence conflicti431 – 4333SDI → LTF in AAA35696. (PubMed:1326756)Curated
Sequence conflicti480 – 4801R → L in AAA35696. (PubMed:1326756)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108Missing in isoform 3. 1 PublicationVSP_055515Add
BLAST
Alternative sequencei1 – 11M → MADRRTPTPFAGCRLPRQRR ARDASQVSAPGTRRIM in isoform 2. 1 PublicationVSP_055516

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10284 mRNA. Translation: AAA36125.1.
L18887 mRNA. Translation: AAA21013.1.
M94859 mRNA. Translation: AAA21749.1.
M98452 mRNA. Translation: AAA35696.1.
AK294702 mRNA. Translation: BAG57859.1.
AK304420 mRNA. Translation: BAG65250.1.
AK312334 mRNA. Translation: BAG35255.1.
AC113426 Genomic DNA. No translation available.
AC136604 Genomic DNA. No translation available.
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.
CCDSiCCDS4447.1. [P27824-1]
PIRiA46164.
A46673.
I53260.
RefSeqiNP_001019820.1. NM_001024649.1. [P27824-1]
NP_001737.1. NM_001746.3. [P27824-1]
UniGeneiHs.567968.

Genome annotation databases

EnsembliENST00000247461; ENSP00000247461; ENSG00000127022. [P27824-1]
ENST00000452673; ENSP00000391646; ENSG00000127022. [P27824-1]
ENST00000504734; ENSP00000424063; ENSG00000127022. [P27824-1]
GeneIDi821.
KEGGihsa:821.
UCSCiuc003mkk.3. human. [P27824-1]

Polymorphism databases

DMDMi543920.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Calnexin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10284 mRNA. Translation: AAA36125.1 .
L18887 mRNA. Translation: AAA21013.1 .
M94859 mRNA. Translation: AAA21749.1 .
M98452 mRNA. Translation: AAA35696.1 .
AK294702 mRNA. Translation: BAG57859.1 .
AK304420 mRNA. Translation: BAG65250.1 .
AK312334 mRNA. Translation: BAG35255.1 .
AC113426 Genomic DNA. No translation available.
AC136604 Genomic DNA. No translation available.
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 .
CCDSi CCDS4447.1. [P27824-1 ]
PIRi A46164.
A46673.
I53260.
RefSeqi NP_001019820.1. NM_001024649.1. [P27824-1 ]
NP_001737.1. NM_001746.3. [P27824-1 ]
UniGenei Hs.567968.

3D structure databases

ProteinModelPortali P27824.
SMRi P27824. Positions 60-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107271. 88 interactions.
DIPi DIP-457N.
IntActi P27824. 64 interactions.
MINTi MINT-5000964.
STRINGi 9606.ENSP00000247461.

Chemistry

BindingDBi P27824.
ChEMBLi CHEMBL2719.
DrugBanki DB00025. Antihemophilic Factor.
DB00031. Tenecteplase.

PTM databases

PhosphoSitei P27824.

Polymorphism databases

DMDMi 543920.

Proteomic databases

MaxQBi P27824.
PaxDbi P27824.
PeptideAtlasi P27824.
PRIDEi P27824.

Protocols and materials databases

DNASUi 821.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247461 ; ENSP00000247461 ; ENSG00000127022 . [P27824-1 ]
ENST00000452673 ; ENSP00000391646 ; ENSG00000127022 . [P27824-1 ]
ENST00000504734 ; ENSP00000424063 ; ENSG00000127022 . [P27824-1 ]
GeneIDi 821.
KEGGi hsa:821.
UCSCi uc003mkk.3. human. [P27824-1 ]

Organism-specific databases

CTDi 821.
GeneCardsi GC05P179105.
HGNCi HGNC:1473. CANX.
HPAi CAB004738.
HPA009433.
HPA009696.
MIMi 114217. gene.
neXtProti NX_P27824.
PharmGKBi PA26055.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG305105.
GeneTreei ENSGT00430000030841.
HOGENOMi HOG000192436.
HOVERGENi HBG005407.
InParanoidi P27824.
KOi K08054.
OrthoDBi EOG77126Z.
PhylomeDBi P27824.
TreeFami TF300618.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_23810. Calnexin/calreticulin cycle.
REACT_6277. Assembly of Viral Components at the Budding Site.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSi CANX. human.
GeneWikii Calnexin.
GenomeRNAii 821.
NextBioi 3360.
PROi P27824.
SOURCEi Search...

Gene expression databases

Bgeei P27824.
CleanExi HS_CANX.
ExpressionAtlasi P27824. baseline and differential.
Genevestigatori P27824.

Family and domain databases

Gene3Di 2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  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] (ISOFORM 1).
    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] (ISOFORM 1).
    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] (ISOFORM 1).
    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] (ISOFORMS 1; 2 AND 3).
    Tissue: Brain, Cerebellum and Trachea.
  6. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Placenta.
  9. 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.
  10. "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 (ISOFORM 1).
  11. "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.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  13. "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.
  14. "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.
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  17. "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.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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.
  22. "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].
  23. Cited for: INTERACTION WITH PPIB.
  24. "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.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.
  27. "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].
  28. "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.
  29. Cited for: INTERACTION WITH SERPINA2P AND SERPINA1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCALX_HUMAN
AccessioniPrimary (citable) accession number: P27824
Secondary accession number(s): B2R5V8
, B4DGP8, B4E2T8, D3DWQ3, D6R9K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 168 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3