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P30101

- PDIA3_HUMAN

UniProt

P30101 - PDIA3_HUMAN

Protein

Protein disulfide-isomerase A3

Gene

PDIA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 4 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Catalyzes the rearrangement of -S-S- bonds in proteins.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei57 – 571NucleophileBy similarity
    Sitei58 – 581Contributes to redox potential valueBy similarity
    Sitei59 – 591Contributes to redox potential valueBy similarity
    Active sitei60 – 601NucleophileBy similarity
    Sitei119 – 1191Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei406 – 4061NucleophileBy similarity
    Sitei407 – 4071Contributes to redox potential valueBy similarity
    Sitei408 – 4081Contributes to redox potential valueBy similarity
    Active sitei409 – 4091NucleophileBy similarity
    Sitei471 – 4711Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: ProtInc
    2. phospholipase C activity Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    4. cell redox homeostasis Source: InterPro
    5. cellular protein metabolic process Source: Reactome
    6. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    7. post-translational protein modification Source: Reactome
    8. protein folding Source: RefGenome
    9. protein import into nucleus Source: ProtInc
    10. protein N-linked glycosylation via asparagine Source: Reactome
    11. protein retention in ER lumen Source: ProtInc
    12. proteolysis Source: GOC
    13. response to endoplasmic reticulum stress Source: RefGenome
    14. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BRENDAi5.3.4.1. 2681.
    ReactomeiREACT_111178. ER-Phagosome pathway.
    REACT_23810. Calnexin/calreticulin cycle.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A3 (EC:5.3.4.1)
    Alternative name(s):
    58 kDa glucose-regulated protein
    58 kDa microsomal protein
    Short name:
    p58
    Disulfide isomerase ER-60
    Endoplasmic reticulum resident protein 57
    Short name:
    ER protein 57
    Short name:
    ERp57
    Endoplasmic reticulum resident protein 60
    Short name:
    ER protein 60
    Short name:
    ERp60
    Gene namesi
    Name:PDIA3
    Synonyms:ERP57, ERP60, GRP58
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:4606. PDIA3.

    Subcellular locationi

    Endoplasmic reticulum. Endoplasmic reticulum lumen By similarity. 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: UniProtKB
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. melanosome Source: UniProtKB-SubCell
    6. nucleus Source: UniProt

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571C → A: No loss of activity. No loss of activity; when associated with A-406. 1 Publication
    Mutagenesisi57 – 571C → S: Activity changed to serine protease. 1 Publication
    Mutagenesisi60 – 601C → S: Activity changed to serine protease; when associated with S-409. 1 Publication
    Mutagenesisi406 – 4061C → A: No loss of activity. No loss of activity; when associated with A-57. 1 Publication
    Mutagenesisi406 – 4061C → S: Activity changed to serine protease. 1 Publication
    Mutagenesisi409 – 4091C → S: Activity changed to serine protease; when associated with S-60. 1 Publication

    Organism-specific databases

    PharmGKBiPA29000.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24245 PublicationsAdd
    BLAST
    Chaini25 – 505481Protein disulfide-isomerase A3PRO_0000034225Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi57 ↔ 60Redox-activePROSITE-ProRule annotation
    Disulfide bondi57 – 57Interchain (with C-115 in TAPBP); in linked form1 Publication
    Disulfide bondi85 ↔ 921 Publication
    Modified residuei129 – 1291N6-succinyllysineBy similarity
    Modified residuei152 – 1521N6-acetyllysineBy similarity
    Modified residuei218 – 2181N6-succinyllysineBy similarity
    Modified residuei252 – 2521N6-acetyllysineBy similarity
    Modified residuei362 – 3621N6-acetyllysineBy similarity
    Disulfide bondi406 ↔ 409Redox-activePROSITE-ProRule annotation
    Modified residuei494 – 4941N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP30101.
    PaxDbiP30101.
    PRIDEiP30101.

    2D gel databases

    DOSAC-COBS-2DPAGEP30101.
    REPRODUCTION-2DPAGEP30101.
    SWISS-2DPAGEP30101.
    UCD-2DPAGEP30101.

    PTM databases

    PhosphoSiteiP30101.

    Expressioni

    Tissue specificityi

    Detected in the flagellum and head region of spermatozoa (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP30101.
    BgeeiP30101.
    CleanExiHS_PDIA3.
    GenevestigatoriP30101.

    Organism-specific databases

    HPAiCAB011199.
    CAB015181.
    HPA002645.
    HPA003230.

    Interactioni

    Subunit structurei

    Subunit of the TAP complex, also known as the peptide loading complex (PLC). Can form disulfide-linked heterodimers with TAPBP. Interacts with ERP27 and CANX. Interacts with SERPINA2 and with the S and Z variants of SERPINA1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050673EBI-979862,EBI-77613
    CalrP184182EBI-979862,EBI-916742From a different organism.
    ERO1LQ96HE73EBI-979862,EBI-2564539
    ERO1LBQ86YB82EBI-979862,EBI-2806988
    PRDX4Q131622EBI-979862,EBI-2211957
    STIM1Q135863EBI-979862,EBI-448878
    TAP1Q035184EBI-979862,EBI-747259

    Protein-protein interaction databases

    BioGridi109180. 81 interactions.
    DIPiDIP-29132N.
    IntActiP30101. 53 interactions.
    MINTiMINT-5000005.
    STRINGi9606.ENSP00000300289.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 293
    Turni32 – 343
    Helixi35 – 384
    Helixi39 – 413
    Beta strandi43 – 5311
    Helixi58 – 7316
    Turni74 – 774
    Beta strandi80 – 845
    Turni85 – 873
    Helixi89 – 946
    Beta strandi99 – 1079
    Beta strandi110 – 1145
    Helixi121 – 13111
    Beta strandi136 – 1383
    Helixi142 – 1498
    Beta strandi151 – 1533
    Beta strandi155 – 1617
    Helixi166 – 17712
    Turni178 – 1814
    Beta strandi182 – 1876
    Helixi190 – 1967
    Beta strandi198 – 2069
    Helixi209 – 2113
    Beta strandi218 – 2214
    Helixi229 – 23911
    Turni240 – 2434
    Turni249 – 2513
    Helixi252 – 2554
    Beta strandi256 – 26510
    Turni269 – 2713
    Helixi273 – 29220
    Beta strandi298 – 3036
    Turni304 – 3074
    Helixi308 – 3114
    Helixi312 – 3143
    Beta strandi325 – 3295
    Beta strandi331 – 3333
    Beta strandi335 – 3373
    Helixi347 – 35812
    Beta strandi376 – 3816
    Turni383 – 3853
    Helixi386 – 3905
    Beta strandi396 – 4027
    Helixi407 – 42216
    Turni423 – 4253
    Beta strandi427 – 4359
    Turni436 – 4383
    Beta strandi449 – 4568
    Helixi473 – 48311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ALBNMR-A25-137[»]
    2DMMNMR-A357-485[»]
    2H8LX-ray2.00A/B/C134-376[»]
    3F8UX-ray2.60A/C25-505[»]
    ProteinModelPortaliP30101.
    SMRiP30101. Positions 25-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30101.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 133109Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini343 – 485143Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi502 – 5054Prevents secretion from ERBy similarity

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 2 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiP30101.
    KOiK08056.
    OMAiFEKFISD.
    OrthoDBiEOG7VHSX1.
    PhylomeDBiP30101.
    TreeFamiTF106382.

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEiPS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P30101-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLRRLALFP GVALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV    50
    EFFAPWCGHC KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY 100
    PTLKIFRDGE EAGAYDGPRT ADGIVSHLKK QAGPASVPLR TEEEFKKFIS 150
    DKDASIVGFF DDSFSEAHSE FLKAASNLRD NYRFAHTNVE SLVNEYDDNG 200
    EGIILFRPSH LTNKFEDKTV AYTEQKMTSG KIKKFIQENI FGICPHMTED 250
    NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA 300
    VASRKTFSHE LSDFGLESTA GEIPVVAIRT AKGEKFVMQE EFSRDGKALE 350
    RFLQDYFDGN LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE 400
    FYAPWCGHCK NLEPKYKELG EKLSKDPNIV IAKMDATAND VPSPYEVRGF 450
    PTIYFSPANK KLNPKKYEGG RELSDFISYL QREATNPPVI QEEKPKKKKK 500
    AQEDL 505
    Length:505
    Mass (Da):56,782
    Last modified:November 1, 1997 - v4
    Checksum:i529E5B6692D0D7E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191A → G in BAA11928. (PubMed:9399589)Curated
    Sequence conflicti22 – 221A → V in BAA11928. (PubMed:9399589)Curated
    Sequence conflicti217 – 2171D → Y in BAA03759. (PubMed:7945384)Curated
    Sequence conflicti225 – 2251Q → P in CAA89996. (PubMed:8624847)Curated
    Sequence conflicti238 – 2381E → G in CAA89996. (PubMed:8624847)Curated
    Sequence conflicti272 – 2721N → D in BAA03759. (PubMed:7945384)Curated
    Sequence conflicti272 – 2721N → D in AAC51518. (PubMed:9205111)Curated
    Sequence conflicti355 – 3551D → G in BAA03759. (PubMed:7945384)Curated
    Sequence conflicti358 – 3581D → G in BAA03759. (PubMed:7945384)Curated
    Sequence conflicti368 – 3681E → D in BAA03759. (PubMed:7945384)Curated

    Mass spectrometryi

    Molecular mass is 54265.22 Da from positions 25 - 505. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti415 – 4151K → R.
    Corresponds to variant rs6413485 [ dbSNP | Ensembl ].
    VAR_020027

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16234 mRNA. Translation: BAA03759.1.
    U42068 mRNA. Translation: AAC50331.1.
    Z49835 mRNA. Translation: CAA89996.1.
    U75885
    , U75875, U75876, U75877, U75878, U75879, U75880, U75881, U75882, U75883, U75884 Genomic DNA. Translation: AAC51518.1.
    D83485 mRNA. Translation: BAA11928.1.
    BC014433 mRNA. Translation: AAH14433.1.
    BC036000 mRNA. Translation: AAH36000.4.
    BC071878 mRNA. Translation: AAH71878.1.
    CCDSiCCDS10101.1.
    PIRiJC5704.
    S55507.
    S63994.
    S68363.
    RefSeqiNP_005304.3. NM_005313.4.
    UniGeneiHs.591095.

    Genome annotation databases

    EnsembliENST00000300289; ENSP00000300289; ENSG00000167004.
    GeneIDi2923.
    KEGGihsa:2923.
    UCSCiuc001zsu.3. human.

    Polymorphism databases

    DMDMi2507461.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16234 mRNA. Translation: BAA03759.1 .
    U42068 mRNA. Translation: AAC50331.1 .
    Z49835 mRNA. Translation: CAA89996.1 .
    U75885
    , U75875 , U75876 , U75877 , U75878 , U75879 , U75880 , U75881 , U75882 , U75883 , U75884 Genomic DNA. Translation: AAC51518.1 .
    D83485 mRNA. Translation: BAA11928.1 .
    BC014433 mRNA. Translation: AAH14433.1 .
    BC036000 mRNA. Translation: AAH36000.4 .
    BC071878 mRNA. Translation: AAH71878.1 .
    CCDSi CCDS10101.1.
    PIRi JC5704.
    S55507.
    S63994.
    S68363.
    RefSeqi NP_005304.3. NM_005313.4.
    UniGenei Hs.591095.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ALB NMR - A 25-137 [» ]
    2DMM NMR - A 357-485 [» ]
    2H8L X-ray 2.00 A/B/C 134-376 [» ]
    3F8U X-ray 2.60 A/C 25-505 [» ]
    ProteinModelPortali P30101.
    SMRi P30101. Positions 25-493.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109180. 81 interactions.
    DIPi DIP-29132N.
    IntActi P30101. 53 interactions.
    MINTi MINT-5000005.
    STRINGi 9606.ENSP00000300289.

    PTM databases

    PhosphoSitei P30101.

    Polymorphism databases

    DMDMi 2507461.

    2D gel databases

    DOSAC-COBS-2DPAGE P30101.
    REPRODUCTION-2DPAGE P30101.
    SWISS-2DPAGE P30101.
    UCD-2DPAGE P30101.

    Proteomic databases

    MaxQBi P30101.
    PaxDbi P30101.
    PRIDEi P30101.

    Protocols and materials databases

    DNASUi 2923.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300289 ; ENSP00000300289 ; ENSG00000167004 .
    GeneIDi 2923.
    KEGGi hsa:2923.
    UCSCi uc001zsu.3. human.

    Organism-specific databases

    CTDi 2923.
    GeneCardsi GC15P044038.
    HGNCi HGNC:4606. PDIA3.
    HPAi CAB011199.
    CAB015181.
    HPA002645.
    HPA003230.
    MIMi 602046. gene.
    neXtProti NX_P30101.
    PharmGKBi PA29000.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P30101.
    KOi K08056.
    OMAi FEKFISD.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi P30101.
    TreeFami TF106382.

    Enzyme and pathway databases

    BRENDAi 5.3.4.1. 2681.
    Reactomei REACT_111178. ER-Phagosome pathway.
    REACT_23810. Calnexin/calreticulin cycle.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Miscellaneous databases

    ChiTaRSi PDIA3. human.
    EvolutionaryTracei P30101.
    GenomeRNAii 2923.
    NextBioi 11593.
    PROi P30101.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30101.
    Bgeei P30101.
    CleanExi HS_PDIA3.
    Genevestigatori P30101.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEi PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a cDNA for bovine phospholipase C-alpha: proposal of redesignation of phospholipase C-alpha."
      Hirano N., Shibasaki F., Katoh H., Sakai R., Tanaka T., Nishida J., Yazaki Y., Takenawa T., Hirai H.
      Biochem. Biophys. Res. Commun. 204:375-382(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase."
      Bourdi M., Demady D., Martin J.L., Jabbour S.K., Martin B.M., George J.W., Pohl L.R.
      Arch. Biochem. Biophys. 323:397-403(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36 AND 130-144, CATALYTIC ACTIVITY.
      Tissue: Liver.
    3. "ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase."
      Koivunen P., Helaakoski T., Annunen P., Veijola J., Raeisaenen S., Pihlajaniemi T., Kivirikko K.I.
      Biochem. J. 316:599-605(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    4. "Cloning, expression and genomic organization of human placental protein disulfide isomerase (previously identified as phospholipase C alpha)."
      Charnock-Jones D.S., Day K., Smith S.K.
      Int. J. Biochem. Cell Biol. 28:81-89(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    5. "Structures of the human gene for the protein disulfide isomerase-related polypeptide ERp60 and a processed gene and assignment of these genes to 15q15 and 1q21."
      Koivunen P., Horelli-Kuitunen N., Helaakoski T., Karvonen P., Jaakkola M., Palotie A., Kivirikko K.I.
      Genomics 42:397-404(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease."
      Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.
      J. Biochem. 122:834-842(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-34 AND 504-505, MUTAGENESIS OF CYS-57; CYS-60; CYS-406 AND CYS-409.
      Tissue: Liver epithelium.
    7. "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: Liver, Lung and Lymph.
    8. "A two-dimensional gel database of human colon carcinoma proteins."
      Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
      Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-54; 62-75 AND 95-104.
      Tissue: Colon carcinoma.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-38.
      Tissue: Platelet.
    10. "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: PROTEIN SEQUENCE OF 25-33.
      Tissue: Liver.
    11. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
      Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
      Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-42.
      Tissue: Mammary carcinoma.
    12. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 63-73; 95-104; 108-129; 131-140; 259-271; 297-304; 306-329; 336-344; 352-362; 367-397; 434-460 AND 472-482, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    13. "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 95-104 AND 472-479.
      Tissue: Keratinocyte.
    14. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    16. "ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57."
      Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E.H., Kauppila A., Kellokumpu S., Ruddock L.W.
      J. Biol. Chem. 281:33727-33738(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERP27.
    17. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
      Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
      Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: INTERACTION WITH SERPINA1 AND SERPINA2, SUBCELLULAR LOCATION.
    22. "NMR assignment of the N-terminal domain a of the glycoprotein chaperone ERp57."
      Silvennoinen L., Koivunen P., Myllyharju J., Kilpelaeinen I., Permi P.
      J. Biomol. NMR 33:136-136(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 25-137.
    23. "The solution structure of the second thioredoxin domain of human protein disulfide-isomerase A3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 357-485.
    24. "Crystal structure of the bb' domains of the protein disulfide isomerase ERp57."
      Kozlov G., Maattanen P., Schrag J.D., Pollock S., Cygler M., Nagar B., Thomas D.Y., Gehring K.
      Structure 14:1331-1339(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-376, INTERACTION WITH CANX.
    25. "Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer."
      Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M.
      Immunity 30:21-32(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-505 IN COMPLEX WITH TAPBP, SUBUNIT, INTERACTION WITH TAPBP, DISULFIDE BONDS.

    Entry informationi

    Entry nameiPDIA3_HUMAN
    AccessioniPrimary (citable) accession number: P30101
    Secondary accession number(s): Q13453
    , Q14255, Q8IYF8, Q9UMU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 175 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

    Caution

    Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha).Curated

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3