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P57759

- ERP29_MOUSE

UniProt

P57759 - ERP29_MOUSE

Protein

Endoplasmic reticulum resident protein 29

Gene

Erp29

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.

    GO - Biological processi

    1. protein secretion Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum resident protein 29
    Short name:
    ERp29
    Gene namesi
    Name:Erp29
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1914647. Erp29.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434By similarityAdd
    BLAST
    Chaini35 – 262228Endoplasmic reticulum resident protein 29PRO_0000021198Add
    BLAST

    Proteomic databases

    MaxQBiP57759.
    PaxDbiP57759.
    PRIDEiP57759.

    2D gel databases

    COMPLUYEAST-2DPAGEP57759.
    REPRODUCTION-2DPAGEP57759.

    PTM databases

    PhosphoSiteiP57759.

    Expressioni

    Gene expression databases

    ArrayExpressiP57759.
    BgeeiP57759.
    CleanExiMM_ERP29.
    GenevestigatoriP57759.

    Interactioni

    Subunit structurei

    Homodimer. Part of a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX By similarity.By similarity

    Protein-protein interaction databases

    BioGridi212160. 1 interaction.
    IntActiP57759. 2 interactions.
    MINTiMINT-1765655.

    Structurei

    3D structure databases

    ProteinModelPortaliP57759.
    SMRiP57759. Positions 35-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi259 – 2624Prevents secretion from ERPROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG82861.
    GeneTreeiENSGT00390000018566.
    HOVERGENiHBG051508.
    InParanoidiP57759.
    KOiK09586.
    OMAiPYGEKHE.
    PhylomeDBiP57759.
    TreeFamiTF324701.

    Family and domain databases

    Gene3Di1.20.1150.12. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR016855. ER_p29.
    IPR011679. ER_p29_C.
    IPR012883. ERp29_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF07749. ERp29. 1 hit.
    PF07912. ERp29_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027352. ER_p29. 1 hit.
    SUPFAMiSSF47933. SSF47933. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P57759-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAAGVSGA ASLSPLLSVL LGLLLLFAPH GGSGLHTKGA LPLDTVTFYK    50
    VIPKSKFVLV KFDTQYPYGE KQDEFKRLAE NSASSEELLV AEVGISDYGD 100
    KLNMELSEKY KLDKESYPVF YLFRDGDLEN PVLYNGAVKV GAIQRWLKGQ 150
    GVYLGMPGCL PAYDALAGEF IKASSIEARQ AILKQGQDGL LSVKETEKKW 200
    ASQYLKIMGK ILDQGEDFPA SEMARIGKLI ENKMSDSKKE ELQKSLNILT 250
    AFRKKEAEKE EL 262
    Length:262
    Mass (Da):28,823
    Last modified:June 1, 2001 - v2
    Checksum:iCA4C83757CA8732B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004795 mRNA. Translation: BAB23570.1.
    AK009881 mRNA. Translation: BAB26559.1.
    AK154539 mRNA. Translation: BAE32664.1.
    AK168112 mRNA. Translation: BAE40083.1.
    BC017125 mRNA. Translation: AAH17125.1.
    CCDSiCCDS19634.1.
    RefSeqiNP_080405.1. NM_026129.2.
    UniGeneiMm.154570.

    Genome annotation databases

    EnsembliENSMUST00000130451; ENSMUSP00000117347; ENSMUSG00000029616.
    GeneIDi67397.
    KEGGimmu:67397.
    UCSCiuc008zjf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004795 mRNA. Translation: BAB23570.1 .
    AK009881 mRNA. Translation: BAB26559.1 .
    AK154539 mRNA. Translation: BAE32664.1 .
    AK168112 mRNA. Translation: BAE40083.1 .
    BC017125 mRNA. Translation: AAH17125.1 .
    CCDSi CCDS19634.1.
    RefSeqi NP_080405.1. NM_026129.2.
    UniGenei Mm.154570.

    3D structure databases

    ProteinModelPortali P57759.
    SMRi P57759. Positions 35-257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212160. 1 interaction.
    IntActi P57759. 2 interactions.
    MINTi MINT-1765655.

    PTM databases

    PhosphoSitei P57759.

    2D gel databases

    COMPLUYEAST-2DPAGE P57759.
    REPRODUCTION-2DPAGE P57759.

    Proteomic databases

    MaxQBi P57759.
    PaxDbi P57759.
    PRIDEi P57759.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000130451 ; ENSMUSP00000117347 ; ENSMUSG00000029616 .
    GeneIDi 67397.
    KEGGi mmu:67397.
    UCSCi uc008zjf.1. mouse.

    Organism-specific databases

    CTDi 10961.
    MGIi MGI:1914647. Erp29.

    Phylogenomic databases

    eggNOGi NOG82861.
    GeneTreei ENSGT00390000018566.
    HOVERGENi HBG051508.
    InParanoidi P57759.
    KOi K09586.
    OMAi PYGEKHE.
    PhylomeDBi P57759.
    TreeFami TF324701.

    Miscellaneous databases

    ChiTaRSi ERP29. mouse.
    NextBioi 324462.
    PROi P57759.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P57759.
    Bgeei P57759.
    CleanExi MM_ERP29.
    Genevestigatori P57759.

    Family and domain databases

    Gene3Di 1.20.1150.12. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR016855. ER_p29.
    IPR011679. ER_p29_C.
    IPR012883. ERp29_N.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF07749. ERp29. 1 hit.
    PF07912. ERp29_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027352. ER_p29. 1 hit.
    SUPFAMi SSF47933. SSF47933. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: BALB/c, C57BL/6J and NOD.
      Tissue: Lung and Tongue.
    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].
      Tissue: Eye.
    3. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 115-124, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    4. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
      Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
      Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF A CHAPERONE COMPLEX.

    Entry informationi

    Entry nameiERP29_MOUSE
    AccessioniPrimary (citable) accession number: P57759
    Secondary accession number(s): Q3THW3, Q9CQ42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3