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P35564

- CALX_MOUSE

UniProt

P35564 - CALX_MOUSE

Protein

Calnexin

Gene

Canx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi75 – 751Calcium; via carbonyl oxygenBy similarity
    Metal bindingi118 – 1181Calcium; via carbonyl oxygenBy similarity
    Binding sitei165 – 1651CarbohydrateBy similarity
    Binding sitei167 – 1671CarbohydrateBy similarity
    Binding sitei186 – 1861CarbohydrateBy similarity
    Binding sitei217 – 2171CarbohydrateBy similarity
    Metal bindingi437 – 4371CalciumBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. aging Source: Ensembl
    2. chaperone-mediated protein folding Source: Ensembl
    3. clathrin-mediated endocytosis Source: UniProtKB
    4. synaptic vesicle endocytosis Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    REACT_198616. Calnexin/calreticulin cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calnexin
    Gene namesi
    Name:Canx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:88261. Canx.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endoplasmic reticulum By similarity. Melanosome By similarity
    Note: The palmitoylated form preferentially localizes to the perinuclear rough ER By similarity. When bound to CD3 epsilon chains, calnexin's ER retention signal can be masked, permitting it to escape ER retention.By similarity

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. dendrite cytoplasm Source: Ensembl
    3. dendritic spine Source: Ensembl
    4. endoplasmic reticulum Source: MGI
    5. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    6. integral component of membrane Source: MGI
    7. melanosome Source: UniProtKB-SubCell
    8. membrane Source: MGI
    9. neuronal cell body Source: Ensembl
    10. protein complex Source: Ensembl
    11. ribosome Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 591571CalnexinPRO_0000004199Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei138 – 1381N6-acetyllysineBy similarity
    Disulfide bondi161 ↔ 195By similarity
    Disulfide bondi361 ↔ 367By similarity
    Lipidationi503 – 5031S-palmitoyl cysteineBy similarity
    Lipidationi504 – 5041S-palmitoyl cysteineBy similarity
    Modified residuei553 – 5531Phosphoserine2 Publications
    Modified residuei561 – 5611PhosphothreonineBy similarity
    Modified residuei563 – 5631Phosphoserine; by MAPK31 Publication
    Modified residuei582 – 5821Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated at Ser-563 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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP35564.
    PaxDbiP35564.
    PRIDEiP35564.

    PTM databases

    PhosphoSiteiP35564.

    Miscellaneous databases

    PMAP-CutDBP35564.

    Expressioni

    Gene expression databases

    ArrayExpressiP35564.
    BgeeiP35564.
    CleanExiMM_CANX.
    GenevestigatoriP35564.

    Interactioni

    Subunit structurei

    Interacts with MAPK3/ERK1 By similarity. Interacts with KCNH2 By similarity. Associates with ribosomes. The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins By similarity. Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1 By similarity. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP By similarity. Interacts with SGIP1; involved in negative regulation of endocytosis. Interacts with PPIB.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sgip1Q8VD373EBI-738422,EBI-776269

    Protein-protein interaction databases

    BioGridi198467. 8 interactions.
    IntActiP35564. 17 interactions.
    MINTiMINT-1862151.

    Structurei

    3D structure databases

    ProteinModelPortaliP35564.
    SMRiP35564. Positions 61-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 482462LumenalSequence AnalysisAdd
    BLAST
    Topological domaini504 – 59188CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei483 – 50321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati279 – 291131-1Add
    BLAST
    Repeati296 – 308131-2Add
    BLAST
    Repeati315 – 327131-3Add
    BLAST
    Repeati334 – 346131-4Add
    BLAST
    Repeati349 – 359112-1Add
    BLAST
    Repeati368 – 378112-2Add
    BLAST
    Repeati382 – 392112-3Add
    BLAST
    Repeati396 – 406112-4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni277 – 410134P domain (Extended arm)By similarityAdd
    BLAST
    Regioni279 – 346684 X approximate repeatsAdd
    BLAST
    Regioni327 – 36034Interaction with PPIBBy similarityAdd
    BLAST
    Regioni349 – 406584 X approximate repeatsAdd
    BLAST
    Regioni504 – 59188Sufficient to mediate interaction with SGIP1Add
    BLAST

    Sequence similaritiesi

    Belongs to the calreticulin family.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG305105.
    HOGENOMiHOG000192436.
    HOVERGENiHBG005407.
    InParanoidiP35564.
    KOiK08054.
    OMAiEAHDGHD.
    OrthoDBiEOG77126Z.
    PhylomeDBiP35564.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P35564-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD    50
    ASTPPSPKVT YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK 100
    YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ 150
    YEVNFQNGIE CGGAYVKLLS KTAELSLDQF HDKTPYTIMF GPDKCGEDYK 200
    LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE 250
    ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV 300
    KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE 350
    WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP 400
    RKIPNPDFFE DLEPFKMTPF SAIGLELWSM TSDIFFDNFI ISGDRRVVDD 450
    WANDGWGLKK AADGAAEPGV VLQMLEAAEE RPWLWVVYIL TVALPVFLVI 500
    LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE EEEEEKLEEK 550
    QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E 591
    Length:591
    Mass (Da):67,278
    Last modified:June 1, 1994 - v1
    Checksum:i0D9F8FE03434BADC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti416 – 4161K → R in AAA62450. (PubMed:8148318)Curated
    Sequence conflicti468 – 4681P → L in AAA62450. (PubMed:8148318)Curated
    Sequence conflicti472 – 4721L → G in AAA62450. (PubMed:8148318)Curated
    Sequence conflicti538 – 5381R → G in AAA62450. (PubMed:8148318)Curated
    Sequence conflicti560 – 5601V → G in AAA62450. (PubMed:8148318)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18888 mRNA. Translation: AAA21014.1.
    BC012408 mRNA. Translation: AAH12408.1.
    BC040244 mRNA. Translation: AAH40244.1.
    AK084175 mRNA. Translation: BAC39133.1.
    L23865 mRNA. Translation: AAA62450.1.
    CCDSiCCDS24633.1.
    PIRiB54354.
    RefSeqiNP_001103969.1. NM_001110499.1.
    NP_001103970.1. NM_001110500.1.
    NP_031623.1. NM_007597.3.
    UniGeneiMm.248827.

    Genome annotation databases

    EnsembliENSMUST00000020637; ENSMUSP00000020637; ENSMUSG00000020368.
    ENSMUST00000179865; ENSMUSP00000137440; ENSMUSG00000020368.
    GeneIDi12330.
    KEGGimmu:12330.
    UCSCiuc007isf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18888 mRNA. Translation: AAA21014.1 .
    BC012408 mRNA. Translation: AAH12408.1 .
    BC040244 mRNA. Translation: AAH40244.1 .
    AK084175 mRNA. Translation: BAC39133.1 .
    L23865 mRNA. Translation: AAA62450.1 .
    CCDSi CCDS24633.1.
    PIRi B54354.
    RefSeqi NP_001103969.1. NM_001110499.1.
    NP_001103970.1. NM_001110500.1.
    NP_031623.1. NM_007597.3.
    UniGenei Mm.248827.

    3D structure databases

    ProteinModelPortali P35564.
    SMRi P35564. Positions 61-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198467. 8 interactions.
    IntActi P35564. 17 interactions.
    MINTi MINT-1862151.

    PTM databases

    PhosphoSitei P35564.

    Proteomic databases

    MaxQBi P35564.
    PaxDbi P35564.
    PRIDEi P35564.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020637 ; ENSMUSP00000020637 ; ENSMUSG00000020368 .
    ENSMUST00000179865 ; ENSMUSP00000137440 ; ENSMUSG00000020368 .
    GeneIDi 12330.
    KEGGi mmu:12330.
    UCSCi uc007isf.2. mouse.

    Organism-specific databases

    CTDi 821.
    MGIi MGI:88261. Canx.

    Phylogenomic databases

    eggNOGi NOG305105.
    HOGENOMi HOG000192436.
    HOVERGENi HBG005407.
    InParanoidi P35564.
    KOi K08054.
    OMAi EAHDGHD.
    OrthoDBi EOG77126Z.
    PhylomeDBi P35564.
    TreeFami TF300618.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    REACT_198616. Calnexin/calreticulin cycle.

    Miscellaneous databases

    ChiTaRSi CANX. mouse.
    NextBioi 280926.
    PMAP-CutDB P35564.
    PROi P35564.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35564.
    Bgeei P35564.
    CleanExi MM_CANX.
    Genevestigatori P35564.

    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. "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].
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-155.
      Strain: C57BL/6J.
      Tissue: Eye.
    4. "Class II histocompatibility molecules associate with calnexin during assembly in the endoplasmic reticulum."
      Schreiber K.L., Bell M.P., Huntoon C.J., Rajagopalan S., Brenner M.B., McKean D.J.
      Int. Immunol. 6:101-111(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-591.
      Strain: BALB/c.
    5. "The molecular chaperone calnexin is expressed on the surface of immature thymocytes in association with clonotype-independent CD3 complexes."
      Wiest D.L., Burgess W.H., McKean D., Kearse K.P., Singer A.
      EMBO J. 14:3425-3433(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THYMOCYTE MATURATION, SUBCELLULAR LOCATION.
    6. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
      Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
      J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Teratocarcinoma.
    7. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "Enhanced clathrin-dependent endocytosis in the absence of calnexin."
      Li H.D., Liu W.X., Michalak M.
      PLoS ONE 6:E21678-E21678(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SGIP1.

    Entry informationi

    Entry nameiCALX_MOUSE
    AccessioniPrimary (citable) accession number: P35564
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3