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P30101

- PDIA3_HUMAN

UniProt

P30101 - PDIA3_HUMAN

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Protein
Protein disulfide-isomerase A3
Gene
PDIA3, ERP57, ERP60, GRP58
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

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

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 N-linked glycosylation via asparagine Source: Reactome
  9. protein folding Source: RefGenome
  10. protein import into nucleus Source: ProtInc
  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
Complete GO annotation...

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.3 Publications

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
Complete GO annotation...

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 Publications
Add
BLAST
Chaini25 – 505481Protein disulfide-isomerase A3
PRO_0000034225Add
BLAST

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP30101.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 133109Thioredoxin 1
Add
BLAST
Domaini343 – 485143Thioredoxin 2
Add
BLAST

Motif

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

Sequence similaritiesi

Contains 2 thioredoxin domains.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191A → G in BAA11928. 1 Publication
Sequence conflicti22 – 221A → V in BAA11928. 1 Publication
Sequence conflicti217 – 2171D → Y in BAA03759. 1 Publication
Sequence conflicti225 – 2251Q → P in CAA89996. 1 Publication
Sequence conflicti238 – 2381E → G in CAA89996. 1 Publication
Sequence conflicti272 – 2721N → D in BAA03759. 1 Publication
Sequence conflicti272 – 2721N → D in AAC51518. 1 Publication
Sequence conflicti355 – 3551D → G in BAA03759. 1 Publication
Sequence conflicti358 – 3581D → G in BAA03759. 1 Publication
Sequence conflicti368 – 3681E → D in BAA03759. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 174 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).

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

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