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P30040

- ERP29_HUMAN

UniProt

P30040 - ERP29_HUMAN

Protein

Endoplasmic reticulum resident protein 29

Gene

ERP29

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 4 (15 Dec 1998)
      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 - Molecular functioni

    1. protein binding Source: IntAct
    2. protein disulfide isomerase activity Source: ProtInc

    GO - Biological processi

    1. intracellular protein transport Source: ProtInc
    2. protein folding Source: ProtInc
    3. protein secretion Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum resident protein 29
    Short name:
    ERp29
    Alternative name(s):
    Endoplasmic reticulum resident protein 28
    Short name:
    ERp28
    Endoplasmic reticulum resident protein 31
    Short name:
    ERp31
    Gene namesi
    Name:ERP29
    Synonyms:C12orf8, ERP28
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:13799. ERP29.

    Subcellular locationi

    Endoplasmic reticulum lumen. Melanosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. endoplasmic reticulum Source: ProtInc
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. melanosome Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25509.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32321 PublicationAdd
    BLAST
    Chaini33 – 261229Endoplasmic reticulum resident protein 29PRO_0000021197Add
    BLAST

    Proteomic databases

    MaxQBiP30040.
    PaxDbiP30040.
    PeptideAtlasiP30040.
    PRIDEiP30040.

    2D gel databases

    OGPiP30040.
    REPRODUCTION-2DPAGEIPI00024911.
    SWISS-2DPAGEP30040.

    PTM databases

    PhosphoSiteiP30040.

    Expressioni

    Tissue specificityi

    Ubiquitous. Mostly expressed in secretory tissues.

    Gene expression databases

    ArrayExpressiP30040.
    BgeeiP30040.
    CleanExiHS_ERP29.
    GenevestigatoriP30040.

    Organism-specific databases

    HPAiHPA039363.
    HPA039456.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Erp29P525552EBI-8762218,EBI-917740From a different organism.

    Protein-protein interaction databases

    BioGridi116160. 7 interactions.
    IntActiP30040. 6 interactions.
    MINTiMINT-5002525.
    STRINGi9606.ENSP00000261735.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 495
    Helixi50 – 523
    Beta strandi54 – 607
    Helixi68 – 8013
    Beta strandi86 – 916
    Beta strandi96 – 983
    Helixi102 – 1076
    Helixi112 – 1143
    Beta strandi116 – 1227
    Helixi138 – 14710
    Helixi159 – 17012
    Helixi174 – 1807
    Helixi183 – 1875
    Helixi193 – 21119
    Helixi217 – 23014
    Helixi235 – 24814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QC7X-ray2.90A/B34-261[»]
    ProteinModelPortaliP30040.
    SMRiP30040. Positions 33-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30040.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi258 – 2614Prevents secretion from ERPROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG82861.
    HOGENOMiHOG000046371.
    HOVERGENiHBG051508.
    InParanoidiP30040.
    KOiK09586.
    OMAiPYGEKHE.
    OrthoDBiEOG7XH6RH.
    PhylomeDBiP30040.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30040-1) [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

    MAAAVPRAAF LSPLLPLLLG FLLLSAPHGG SGLHTKGALP LDTVTFYKVI    50
    PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL 100
    NMELSEKYKL DKESYPVFYL FRDGDFENPV PYTGAVKVGA IQRWLKGQGV 150
    YLGMPGCLPV YDALAGEFIR ASGVEARQAL LKQGQDNLSS VKETQKKWAE 200
    QYLKIMGKIL DQGEDFPASE MTRIARLIEK NKMSDGKKEE LQKSLNILTA 250
    FQKKGAEKEE L 261
    Length:261
    Mass (Da):28,993
    Last modified:December 15, 1998 - v4
    Checksum:i76145006433A1983
    GO
    Isoform 2 (identifier: P30040-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         49-53: VIPKS → IMVTS
         54-261: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:53
    Mass (Da):5,477
    Checksum:i67DE41DE8CA1F165
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei49 – 535VIPKS → IMVTS in isoform 2. 1 PublicationVSP_045680
    Alternative sequencei54 – 261208Missing in isoform 2. 1 PublicationVSP_045681Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94910 mRNA. Translation: CAA64397.1.
    AA412124 mRNA. No translation available.
    CR541667 mRNA. Translation: CAG46468.1.
    AC073575 Genomic DNA. No translation available.
    BC101493 mRNA. Translation: AAI01494.1.
    BC101495 mRNA. Translation: AAI01496.1.
    CCDSiCCDS44977.1. [P30040-2]
    CCDS9158.1. [P30040-1]
    PIRiT09549.
    RefSeqiNP_001029197.1. NM_001034025.1. [P30040-2]
    NP_006808.1. NM_006817.3. [P30040-1]
    UniGeneiHs.75841.

    Genome annotation databases

    EnsembliENST00000261735; ENSP00000261735; ENSG00000089248. [P30040-1]
    ENST00000455836; ENSP00000412083; ENSG00000089248. [P30040-2]
    GeneIDi10961.
    KEGGihsa:10961.
    UCSCiuc001ttk.1. human. [P30040-1]

    Polymorphism databases

    DMDMi6015110.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94910 mRNA. Translation: CAA64397.1 .
    AA412124 mRNA. No translation available.
    CR541667 mRNA. Translation: CAG46468.1 .
    AC073575 Genomic DNA. No translation available.
    BC101493 mRNA. Translation: AAI01494.1 .
    BC101495 mRNA. Translation: AAI01496.1 .
    CCDSi CCDS44977.1. [P30040-2 ]
    CCDS9158.1. [P30040-1 ]
    PIRi T09549.
    RefSeqi NP_001029197.1. NM_001034025.1. [P30040-2 ]
    NP_006808.1. NM_006817.3. [P30040-1 ]
    UniGenei Hs.75841.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QC7 X-ray 2.90 A/B 34-261 [» ]
    ProteinModelPortali P30040.
    SMRi P30040. Positions 33-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116160. 7 interactions.
    IntActi P30040. 6 interactions.
    MINTi MINT-5002525.
    STRINGi 9606.ENSP00000261735.

    PTM databases

    PhosphoSitei P30040.

    Polymorphism databases

    DMDMi 6015110.

    2D gel databases

    OGPi P30040.
    REPRODUCTION-2DPAGE IPI00024911.
    SWISS-2DPAGE P30040.

    Proteomic databases

    MaxQBi P30040.
    PaxDbi P30040.
    PeptideAtlasi P30040.
    PRIDEi P30040.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261735 ; ENSP00000261735 ; ENSG00000089248 . [P30040-1 ]
    ENST00000455836 ; ENSP00000412083 ; ENSG00000089248 . [P30040-2 ]
    GeneIDi 10961.
    KEGGi hsa:10961.
    UCSCi uc001ttk.1. human. [P30040-1 ]

    Organism-specific databases

    CTDi 10961.
    GeneCardsi GC12P112451.
    HGNCi HGNC:13799. ERP29.
    HPAi HPA039363.
    HPA039456.
    MIMi 602287. gene.
    neXtProti NX_P30040.
    PharmGKBi PA25509.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82861.
    HOGENOMi HOG000046371.
    HOVERGENi HBG051508.
    InParanoidi P30040.
    KOi K09586.
    OMAi PYGEKHE.
    OrthoDBi EOG7XH6RH.
    PhylomeDBi P30040.
    TreeFami TF324701.

    Miscellaneous databases

    ChiTaRSi ERP29. human.
    EvolutionaryTracei P30040.
    GeneWikii ERP29.
    GenomeRNAii 10961.
    NextBioi 41652.
    PROi P30040.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30040.
    Bgeei P30040.
    CleanExi HS_ERP29.
    Genevestigatori P30040.

    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. "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif."
      Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling H.D.
      Eur. J. Biochem. 255:570-579(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    6. Cited for: PROTEIN SEQUENCE OF 33-52.
      Tissue: Liver.
    7. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 33-42.
      Tissue: Liver.
    8. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 113-122, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    9. Hubbard M.J.
      Submitted (DEC-1998) to UniProtKB
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    10. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
      Hubbard M.J., McHugh N.J.
      Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
      Tissue: Liver.
    11. "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.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiERP29_HUMAN
    AccessioniPrimary (citable) accession number: P30040
    Secondary accession number(s): C9J183, Q3MJC3, Q6FHT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 153 of the entry and version 4 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3