P30101 (PDIA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PDIA3
Synonyms:	ERP57, ERP60, GRP58

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.16 Ref.23 Ref.24
Subcellular location	Endoplasmic reticulum lumen By similarity. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.15 Ref.17
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 component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine 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_component	cell surface Inferred from direct assay PubMed 19995400. Source: MGI endoplasmic reticulum lumen Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type endopeptidase activity Traceable author statement Ref.6. Source: ProtInc electron carrier activity Inferred from electronic annotation. Source: InterPro phospholipase C activity Traceable author statement PubMed 3398923. Source: ProtInc protein disulfide isomerase activity Traceable author statement Ref.4. Source: ProtInc protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	3	EBI-979862,EBI-77613
TAP1	Q03518	4	EBI-979862,EBI-747259

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.2 Ref.6 Ref.8 Ref.9 Ref.10

Chain

25 – 505

481

Protein disulfide-isomerase A3

PRO_0000034225

Regions

Domain

25 – 133

109

Thioredoxin 1

Domain

343 – 485

143

Thioredoxin 2

Motif

502 – 505

4

Prevents secretion from ER By similarity

Sites

Active site

57

1

Nucleophile By similarity

Active site

60

1

Nucleophile By similarity

Active site

406

1

Nucleophile By similarity

Active site

409

1

Nucleophile By similarity

Site

58

1

Contributes to redox potential value By similarity

Site

59

1

Contributes to redox potential value By similarity

Site

119

1

Lowers pKa of C-terminal Cys of first active site By similarity

Site

407

1

Contributes to redox potential value By similarity

Site

408

1

Contributes to redox potential value By similarity

Site

471

1

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond

57 ↔ 60

Redox-active; alternate By similarity

Disulfide bond

57

Interchain (with C-115 in TAPBP); alternate Ref.24

Disulfide bond

85 ↔ 92

Ref.24

Disulfide bond

406 ↔ 409

Redox-active By similarity

Natural variations

Natural variant

415

1

K → R.
Corresponds to variant rs6413485 [ dbSNP | Ensembl ].

VAR_020027

Experimental info

Mutagenesis

57

1

C → A: No loss of activity. No loss of activity; when associated with A-406. Ref.6

Mutagenesis

57

1

C → S: Activity changed to serine protease. Ref.6

Mutagenesis

60

1

C → S: Activity changed to serine protease; when associated with S-409. Ref.6

Mutagenesis

406

1

C → A: No loss of activity. No loss of activity; when associated with A-57. Ref.6

Mutagenesis

406

1

C → S: Activity changed to serine protease. Ref.6

Mutagenesis

409

1

C → S: Activity changed to serine protease; when associated with S-60. Ref.6

Sequence conflict

19

1

A → G in BAA11928. Ref.6

Sequence conflict

22

1

A → V in BAA11928. Ref.6

Sequence conflict

217

1

D → Y in BAA03759. Ref.1

Sequence conflict

225

1

Q → P in CAA89996. Ref.4

Sequence conflict

238

1

E → G in CAA89996. Ref.4

Sequence conflict

272

1

N → D in BAA03759. Ref.1

Sequence conflict

272

1

N → D in AAC51518. Ref.5

Sequence conflict

355

1

D → G in BAA03759. Ref.1

Sequence conflict

358

1

D → G in BAA03759. Ref.1

Sequence conflict

368

1

E → D in BAA03759. Ref.1

Secondary structure

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505

Helix Strand Turn

Details...

Beta strand

27 – 29

3

Turn

32 – 34

3

Helix

35 – 38

4

Helix

39 – 41

3

Beta strand

43 – 53

11

Helix

58 – 73

16

Turn

74 – 77

4

Beta strand

80 – 84

5

Turn

85 – 87

3

Helix

89 – 94

6

Beta strand

99 – 107

9

Beta strand

110 – 114

5

Helix

121 – 131

11

Beta strand

136 – 138

3

Helix

142 – 149

8

Beta strand

151 – 153

3

Beta strand

155 – 161

7

Helix

166 – 177

12

Turn

178 – 181

4

Beta strand

182 – 187

6

Helix

190 – 196

7

Beta strand

198 – 206

9

Helix

209 – 211

3

Beta strand

218 – 221

4

Helix

229 – 239

11

Turn

240 – 243

4

Turn

249 – 251

3

Helix

252 – 255

4

Beta strand

256 – 265

10

Turn

269 – 271

3

Helix

273 – 292

20

Beta strand

298 – 303

6

Turn

304 – 307

4

Helix

308 – 311

4

Helix

312 – 314

3

Beta strand

325 – 329

5

Beta strand

331 – 333

3

Beta strand

335 – 337

3

Helix

347 – 358

12

Beta strand

376 – 381

6

Turn

383 – 385

3

Helix

386 – 390

5

Beta strand

396 – 402

7

Helix

407 – 422

16

Turn

423 – 425

3

Beta strand

427 – 435

9

Turn

436 – 438

3

Beta strand

449 – 456

8

Helix

473 – 483

11

Sequences

	Sequence		Length	Mass (Da)
	P30101 [UniParc]. Last modified November 1, 1997. Version 4. Checksum: 529E5B6692D0D7E9	FASTA	505	56,782
	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

References

	« Hide 'large scale' referencesShow '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, 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], MASS SPECTROMETRY. 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], MASS SPECTROMETRY. 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]	"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.
[22]	"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.
[23]	"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.
[24]	"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 , 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.

IPI

IPI00025252.

PIR

JC5704.
S55507.
S63994.
S68363.

RefSeq

NP_005304.3. NM_005313.4.

UniGene

Hs.591095.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P30101.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29132N.

IntAct

P30101. 18 interactions.

MINT

MINT-5000005.

STRING

9606.ENSP00000300289.

PTM databases

PhosphoSite

P30101.

Polymorphism databases

DMDM

2507461.

2D gel databases

DOSAC-COBS-2DPAGE

P30101.

REPRODUCTION-2DPAGE

P30101.

SWISS-2DPAGE

P30101.

UCD-2DPAGE

P30101.

Proteomic databases

PaxDb

P30101.

PRIDE

P30101.

Protocols and materials databases

DNASU

2923.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300289; ENSP00000300289; ENSG00000167004.

GeneID

2923.

KEGG

hsa:2923.

UCSC

uc001zsu.3. human.

Organism-specific databases

CTD

2923.

GeneCards

GC15P044038.

HGNC

HGNC:4606. PDIA3.

HPA

CAB011199.
CAB015181.
HPA002645.
HPA003230.

MIM

602046. gene.

neXtProt

NX_P30101.

PharmGKB

PA29000.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000162459.

HOVERGEN

HBG005920.

InParanoid

P30101.

KO

K08056.

OMA

KNPKGTN.

OrthoDB

EOG42Z4PX.

PhylomeDB

P30101.

Enzyme and pathway databases

BRENDA

5.3.4.1. 2681.

Reactome

REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P30101.

Bgee

P30101.

CleanEx

HS_PDIA3.

Genevestigator

P30101.

GermOnline

ENSG00000167004. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 3 hits.

InterPro

IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF00085. Thioredoxin. 2 hits.
[Graphical view]

PRINTS

PR00421. THIOREDOXIN.

SUPFAM

SSF52833. Thiordxn-like_fd. 4 hits.

TIGRFAMs

TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.

PROSITE

PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PDIA3. human.

EvolutionaryTrace

P30101.

GenomeRNAi

2923.

NextBio

11593.

SOURCE

Search...

Entry information

Entry name

PDIA3_HUMAN

Accession

Primary (citable) accession number: P30101
Secondary accession number(s): Q13453 , Q14255, Q8IYF8, Q9UMU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 161 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.