Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27824

- CALX_HUMAN

UniProt

P27824 - CALX_HUMAN

Protein

Calnexin

Gene

CANX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. poly(A) RNA binding Source: UniProtKB
    3. protein 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

    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. extracellular vesicular exosome Source: UniProt
    8. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    9. integral component of membrane Source: Ensembl
    10. melanosome Source: UniProtKB-SubCell
    11. membrane Source: UniProtKB
    12. neuronal cell body Source: Ensembl
    13. protein complex Source: Ensembl
    14. ribosome Source: Ensembl

    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

    ArrayExpressiP27824.
    BgeeiP27824.
    CleanExiHS_CANX.
    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. 79 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.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [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

    MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT    50
    APPSSPKVTY KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY 100
    DGKWEVEEMK ESKLPGDKGL VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY 150
    EVNFQNGIEC GGAYVKLLSK TPELNLDQFH DKTPYTIMFG PDKCGEDYKL 200
    HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL ILNPDNSFEI 250
    LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK 300
    PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW 350
    EAPQIANPRC ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR 400
    KIPNPDFFED LEPFRMTPFS AIGLELWSMT SDIFFDNFII CADRRIVDDW 450
    ANDGWGLKKA ADGAAEPGVV GQMIEAAEER PWLWVVYILT VALPVFLVIL 500
    FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE EEEGEEKLEE 550
    KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE 592
    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.
    PIRiA46164.
    A46673.
    I53260.
    RefSeqiNP_001019820.1. NM_001024649.1.
    NP_001737.1. NM_001746.3.
    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.

    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.
    PIRi A46164.
    A46673.
    I53260.
    RefSeqi NP_001019820.1. NM_001024649.1.
    NP_001737.1. NM_001746.3.
    UniGenei Hs.567968.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi 107271. 79 interactions.
    DIPi DIP-457N.
    IntActi P27824. 64 interactions.
    MINTi MINT-5000964.
    STRINGi 9606.ENSP00000247461.

    Chemistry

    BindingDBi P27824.
    ChEMBLi CHEMBL2719.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00025. Antihemophilic Factor.
    DB00015. Reteplase.
    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.

    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.
    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

    ArrayExpressi P27824.
    Bgeei P27824.
    CleanExi HS_CANX.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [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

    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 1, 2014
    This is version 167 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