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P30101 (PDIA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PDIA3
Synonyms:ERP57, ERP60, GRP58
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins. Ref.2

Subunit structure

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. Ref.16 Ref.21 Ref.24 Ref.25

Subcellular location

Endoplasmic reticulum. Endoplasmic reticulum lumen By similarity. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.15 Ref.17 Ref.21

Tissue specificity

Detected in the flagellum and head region of spermatozoa (at protein level). Ref.19

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Caution

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

Mass spectrometry

Molecular mass is 54265.22 Da from positions 25 - 505. Determined by MALDI. Ref.14

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular protein metabolic process

Traceable author statement. Source: Reactome

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein folding

Traceable author statement. Source: Reactome

protein import into nucleus

Traceable author statement Ref.2. Source: ProtInc

protein retention in ER lumen

Traceable author statement Ref.6. Source: ProtInc

signal transduction

Traceable author statement PubMed 3398923. Source: ProtInc

   Cellular_componentcell surface

Inferred from direct assay PubMed 19995400. Source: MGI

endoplasmic reticulum

Inferred from direct assay Ref.21. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase activity

Traceable author statement Ref.6. Source: ProtInc

phospholipase C activity

Traceable author statement PubMed 3398923. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein disulfide isomerase activity

Traceable author statement. Source: ProtInc

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2 Ref.6 Ref.8 Ref.9 Ref.10
Chain25 – 505481Protein disulfide-isomerase A3
PRO_0000034225

Regions

Domain25 – 133109Thioredoxin 1
Domain343 – 485143Thioredoxin 2
Motif502 – 5054Prevents secretion from ER By similarity

Sites

Active site571Nucleophile By similarity
Active site601Nucleophile By similarity
Active site4061Nucleophile By similarity
Active site4091Nucleophile By similarity
Site581Contributes to redox potential value By similarity
Site591Contributes to redox potential value By similarity
Site1191Lowers pKa of C-terminal Cys of first active site By similarity
Site4071Contributes to redox potential value By similarity
Site4081Contributes to redox potential value By similarity
Site4711Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue1291N6-succinyllysine By similarity
Modified residue1521N6-acetyllysine By similarity
Modified residue2181N6-succinyllysine By similarity
Modified residue2521N6-acetyllysine By similarity
Modified residue3621N6-acetyllysine By similarity
Modified residue4941N6-acetyllysine By similarity
Disulfide bond57 ↔ 60Redox-active; alternate By similarity
Disulfide bond57Interchain (with C-115 in TAPBP); alternate Ref.25
Disulfide bond85 ↔ 92 Ref.25
Disulfide bond406 ↔ 409Redox-active By similarity

Natural variations

Natural variant4151K → R.
Corresponds to variant rs6413485 [ dbSNP | Ensembl ].
VAR_020027

Experimental info

Mutagenesis571C → A: No loss of activity. No loss of activity; when associated with A-406. Ref.6
Mutagenesis571C → S: Activity changed to serine protease. Ref.6
Mutagenesis601C → S: Activity changed to serine protease; when associated with S-409. Ref.6
Mutagenesis4061C → A: No loss of activity. No loss of activity; when associated with A-57. Ref.6
Mutagenesis4061C → S: Activity changed to serine protease. Ref.6
Mutagenesis4091C → S: Activity changed to serine protease; when associated with S-60. Ref.6
Sequence conflict191A → G in BAA11928. Ref.6
Sequence conflict221A → V in BAA11928. Ref.6
Sequence conflict2171D → Y in BAA03759. Ref.1
Sequence conflict2251Q → P in CAA89996. Ref.4
Sequence conflict2381E → G in CAA89996. Ref.4
Sequence conflict2721N → D in BAA03759. Ref.1
Sequence conflict2721N → D in AAC51518. Ref.5
Sequence conflict3551D → G in BAA03759. Ref.1
Sequence conflict3581D → G in BAA03759. Ref.1
Sequence conflict3681E → D in BAA03759. Ref.1

Secondary structure

.................................................................................... 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30101 [UniParc].

Last modified November 1, 1997. Version 4.
Checksum: 529E5B6692D0D7E9

FASTA50556,782
        10         20         30         40         50         60 
MRLRRLALFP GVALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV EFFAPWCGHC 

        70         80         90        100        110        120 
KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT 

       130        140        150        160        170        180 
ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASIVGFF DDSFSEAHSE FLKAASNLRD 

       190        200        210        220        230        240 
NYRFAHTNVE SLVNEYDDNG EGIILFRPSH LTNKFEDKTV AYTEQKMTSG KIKKFIQENI 

       250        260        270        280        290        300 
FGICPHMTED NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA 

       310        320        330        340        350        360 
VASRKTFSHE LSDFGLESTA GEIPVVAIRT AKGEKFVMQE EFSRDGKALE RFLQDYFDGN 

       370        380        390        400        410        420 
LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE FYAPWCGHCK NLEPKYKELG 

       430        440        450        460        470        480 
EKLSKDPNIV IAKMDATAND VPSPYEVRGF PTIYFSPANK KLNPKKYEGG RELSDFISYL 

       490        500 
QREATNPPVI QEEKPKKKKK AQEDL 

« Hide

References

« Hide 'large scale' references
[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]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"SERPINA2 is a novel gene with a divergent function from SERPINA1."
Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I., Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.
PLoS ONE 8:E66889-E66889(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16234 mRNA. Translation: BAA03759.1.
U42068 mRNA. Translation: AAC50331.1.
Z49835 mRNA. Translation: CAA89996.1.
U75885 expand/collapse EMBL AC list , 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.
PIRJC5704.
S55507.
S63994.
S68363.
RefSeqNP_005304.3. NM_005313.4.
UniGeneHs.591095.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ALBNMR-A25-137[»]
2DMMNMR-A357-485[»]
2H8LX-ray2.00A/B/C134-376[»]
3F8UX-ray2.60A/C25-505[»]
ProteinModelPortalP30101.
SMRP30101. Positions 25-493.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109180. 79 interactions.
DIPDIP-29132N.
IntActP30101. 53 interactions.
MINTMINT-5000005.
STRING9606.ENSP00000300289.

PTM databases

PhosphoSiteP30101.

Polymorphism databases

DMDM2507461.

2D gel databases

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

Proteomic databases

PaxDbP30101.
PRIDEP30101.

Protocols and materials databases

DNASU2923.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300289; ENSP00000300289; ENSG00000167004.
GeneID2923.
KEGGhsa:2923.
UCSCuc001zsu.3. human.

Organism-specific databases

CTD2923.
GeneCardsGC15P044038.
HGNCHGNC:4606. PDIA3.
HPACAB011199.
CAB015181.
HPA002645.
HPA003230.
MIM602046. gene.
neXtProtNX_P30101.
PharmGKBPA29000.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP30101.
KOK08056.
OMAFEKFISD.
OrthoDBEOG7VHSX1.
PhylomeDBP30101.
TreeFamTF106382.

Enzyme and pathway databases

BRENDA5.3.4.1. 2681.
ReactomeREACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP30101.
BgeeP30101.
CleanExHS_PDIA3.
GenevestigatorP30101.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDIA3. human.
EvolutionaryTraceP30101.
GenomeRNAi2923.
NextBio11593.
PROP30101.
SOURCESearch...

Entry information

Entry namePDIA3_HUMAN
AccessionPrimary (citable) accession number: P30101
Secondary accession number(s): Q13453 expand/collapse secondary AC list , Q14255, Q8IYF8, Q9UMU7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM