Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07237 (PDIA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 190. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Short name=PDI
EC=5.3.4.1
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
p55
Gene names
Name:P4HB
Synonyms:ERBA2L, PDI, PDIA1, PO4DB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Ref.17 Ref.19

Catalytic activity

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

Subunit structure

Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity By similarity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Ref.20

Subcellular location

Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources Probable. Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.17 Ref.18 Ref.23 Ref.27

Miscellaneous

Reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   DomainRedox-active center
Repeat
Signal
   Molecular functionChaperone
Isomerase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular response to hypoxia

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

lipoprotein metabolic process

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay PubMed 7753822. Source: GOC

peptidyl-proline hydroxylation to 4-hydroxy-L-proline

Inferred from direct assay PubMed 7753822. Source: MGI

regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

response to endoplasmic reticulum stress

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.20. Source: BHF-UCL

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 15308636. Source: UniProtKB

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

procollagen-proline 4-dioxygenase complex

Inferred from direct assay PubMed 7753822. Source: MGI

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

procollagen-proline 4-dioxygenase activity

Traceable author statement Ref.3. Source: ProtInc

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 – 1717 Ref.8 Ref.9 Ref.10 Ref.11
Chain18 – 508491Protein disulfide-isomerase
PRO_0000034195

Regions

Domain18 – 134117Thioredoxin 1
Domain349 – 475127Thioredoxin 2
Motif505 – 5084Prevents secretion from ER

Sites

Active site531Nucleophile
Active site561Nucleophile
Active site3971Nucleophile By similarity
Active site4001Nucleophile By similarity
Site541Contributes to redox potential value
Site551Contributes to redox potential value
Site1201Lowers pKa of C-terminal Cys of first active site
Site3981Contributes to redox potential value By similarity
Site3991Contributes to redox potential value By similarity
Site4611Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2001N6-acetyllysine By similarity
Modified residue2221N6-succinyllysine By similarity
Modified residue2711N6-succinyllysine By similarity
Disulfide bond53 ↔ 56Redox-active Ref.30
Disulfide bond397 ↔ 400Redox-active By similarity

Experimental info

Sequence conflict10 – 112AV → PW in CAA28775. Ref.1
Sequence conflict211E → D AA sequence Ref.13
Sequence conflict241D → V AA sequence Ref.13
Sequence conflict44 – 452LL → PP in CAA28775. Ref.1
Sequence conflict491Y → H in CAA28775. Ref.1
Sequence conflict1411P → R in AAA61169. Ref.2
Sequence conflict360 – 3623LPE → RAG in AAA61169. Ref.2
Sequence conflict3721L → P in AAA61169. Ref.2
Sequence conflict4391S → G in CAA28775. Ref.1
Sequence conflict4441K → G in CAA28775. Ref.1
Sequence conflict4601E → Q in CAA30112. Ref.15
Sequence conflict4811D → V in CAA28775. Ref.1

Secondary structure

.................................................................................................... 508
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07237 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 906CE6D9900B8FCE

FASTA50857,116
        10         20         30         40         50         60 
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA 

        70         80         90        100        110        120 
PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTAGR 

       130        140        150        160        170        180 
EADDIVNWLK KRTGPAATTL PDGAAAESLV ESSEVAVIGF FKDVESDSAK QFLQAAEAID 

       190        200        210        220        230        240 
DIPFGITSNS DVFSKYQLDK DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF 

       250        260        270        280        290        300 
TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR 

       310        320        330        340        350        360 
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL 

       370        380        390        400        410        420 
PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI 

       430        440        450        460        470        480 
VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD 

       490        500 
DDDLEDLEEA EEPDMEEDDD QKAVKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene."
Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R., Huhtala M.-L., Koivu J., Kivirikko K.I.
EMBO J. 6:643-649(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum."
Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E., Merlino G.T., Pastan I.
J. Biol. Chem. 262:11221-11227(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase."
Tasanen K., Parkkonen T., Chow L.T., Kivirikko K.I., Pihlajaniemi T.
J. Biol. Chem. 263:16218-16224(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Synovium.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Colon, Lung and Skin.
[7]"Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements."
Tasanen K., Oikarinen J., Kivirikko K.I., Pihlajaniemi T.
J. Biol. Chem. 267:11513-11519(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[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 18-41.
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 18-30.
Tissue: Platelet.
[10]Frutiger S., Hughes G.J.
Submitted (FEB-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 18-29.
Tissue: Liver.
[11]"Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis."
Ward L.D., Hong J., Whitehead R.H., Simpson R.J.
Electrophoresis 11:883-891(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-26.
[12]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-28.
Tissue: Liver.
[13]"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: PROTEIN SEQUENCE OF 19-28.
[14]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 201-207; 223-230; 286-308 AND 402-409, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[15]"Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)."
Morris J.I., Varandani P.T.
Biochim. Biophys. Acta 949:169-180(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 293-508.
[16]"Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 317-325; 350-369 AND 401-419.
[17]"Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes."
Mezghrani A., Courageot J., Mani J.-C., Pugniere M., Bastiani P., Miquelis R.
J. Biol. Chem. 275:1920-1929(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding."
Fenouillet E., Barbouche R., Courageot J., Miquelis R.
J. Infect. Dis. 183:744-752(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS, SUBCELLULAR LOCATION.
[19]"Is protein disulfide isomerase a redox-dependent molecular chaperone?"
Lumb R.A., Bulleid N.J.
EMBO J. 21:6763-6770(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death."
Ko H.S., Uehara T., Nomura Y.
J. Biol. Chem. 277:35386-35392(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBQLN1.
[21]"Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry."
Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A., Ryser H.J.
J. Biol. Chem. 277:50579-50588(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[22]"Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion."
Barbouche R., Miquelis R., Jones I.M., Fenouillet E.
J. Biol. Chem. 278:3131-3136(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[23]"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.
[24]"Protein disulfide isomerase."
Wilkinson B., Gilbert H.F.
Biochim. Biophys. Acta 1699:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[25]"Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry."
Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M., Weiss C.D., Broder C.C., Strebel K., Clouse K.A.
Blood 103:1586-1594(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[26]"Glycosaminoglycans and protein disulfide isomerase-mediated reduction of HIV Env."
Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.
Mol. Pharmacol. 67:1111-1118(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[27]"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.
[28]"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].
[29]"Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase."
Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., Creighton T.E.
Protein Sci. 4:2587-2593(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 18-137.
[30]"Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy."
Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E.
Biochemistry 35:7684-7691(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 18-137, DISULFIDE BOND.
[31]"The structure in solution of the B domain of protein disulfide isomerase."
Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M., Darby N.J.
J. Biomol. NMR 13:357-368(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 136-245.
[32]"The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 368-477.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05130 mRNA. Translation: CAA28775.1.
J02783 mRNA. Translation: AAA61169.1.
M22806 expand/collapse EMBL AC list , M22803, M22804, M22805 Genomic DNA. Translation: AAC13652.1.
AK315631 mRNA. Translation: BAG37999.1.
CH471099 Genomic DNA. Translation: EAW89690.1.
BC010859 mRNA. Translation: AAH10859.1.
BC029617 mRNA. Translation: AAH29617.1.
BC071892 mRNA. Translation: AAH71892.1.
S37207 Genomic DNA. Translation: AAB22262.2.
X07077 mRNA. Translation: CAA30112.1.
PIRISHUSS. A31913.
RefSeqNP_000909.2. NM_000918.3.
UniGeneHs.464336.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJXNMR-A136-245[»]
1MEKNMR-A18-137[»]
1X5CNMR-A368-475[»]
2BJXNMR-A136-245[»]
2K18NMR-A135-357[»]
3BJ5X-ray2.20A230-368[»]
3UEMX-ray2.29A137-479[»]
4EKZX-ray2.51A18-479[»]
4EL1X-ray2.88A/B18-479[»]
4JU5X-ray2.28A/B135-367[»]
ProteinModelPortalP07237.
SMRP07237. Positions 17-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111073. 70 interactions.
IntActP07237. 33 interactions.
MINTMINT-4999403.
STRING9606.ENSP00000327801.

Chemistry

BindingDBP07237.
ChEMBLCHEMBL2364681.

PTM databases

PhosphoSiteP07237.

Polymorphism databases

DMDM2507460.

2D gel databases

DOSAC-COBS-2DPAGEP07237.
OGPP07237.
REPRODUCTION-2DPAGEIPI00010796.
P07237.
SWISS-2DPAGEP07237.

Proteomic databases

PaxDbP07237.
PeptideAtlasP07237.
PRIDEP07237.

Protocols and materials databases

DNASU5034.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331483; ENSP00000327801; ENSG00000185624.
GeneID5034.
KEGGhsa:5034.
UCSCuc002kbn.1. human.

Organism-specific databases

CTD5034.
GeneCardsGC17M079801.
HGNCHGNC:8548. P4HB.
HPACAB012463.
HPA018884.
MIM176790. gene.
neXtProtNX_P07237.
PharmGKBPA32876.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP07237.
KOK09580.
OMAKSHILMF.
OrthoDBEOG7VHSX1.
PhylomeDBP07237.
TreeFamTF106381.

Enzyme and pathway databases

BRENDA5.3.4.1. 2681.
ReactomeREACT_111217. Metabolism.
REACT_118779. Extracellular matrix organization.
REACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP07237.
BgeeP07237.
CleanExHS_P4HB.
GenevestigatorP07237.

Family and domain databases

Gene3D3.40.30.10. 4 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.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSP4HB. human.
EvolutionaryTraceP07237.
GeneWikiP4HB.
GenomeRNAi5034.
NextBio19398.
PMAP-CutDBP07237.
PROP07237.
SOURCESearch...

Entry information

Entry namePDIA1_HUMAN
AccessionPrimary (citable) accession number: P07237
Secondary accession number(s): B2RDQ2 expand/collapse secondary AC list , P30037, P32079, Q15205, Q6LDE5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 190 of the entry and version 3 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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM