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P07237

- PDIA1_HUMAN

UniProt

P07237 - PDIA1_HUMAN

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Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531Nucleophile
Sitei54 – 541Contributes to redox potential value
Sitei55 – 551Contributes to redox potential value
Active sitei56 – 561Nucleophile
Sitei120 – 1201Lowers pKa of C-terminal Cys of first active site
Active sitei397 – 3971NucleophileBy similarity
Sitei398 – 3981Contributes to redox potential valueBy similarity
Sitei399 – 3991Contributes to redox potential valueBy similarity
Active sitei400 – 4001NucleophileBy similarity
Sitei461 – 4611Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. procollagen-proline 4-dioxygenase activity Source: ProtInc
  3. protein disulfide isomerase activity Source: RefGenome

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to hypoxia Source: BHF-UCL
  3. extracellular matrix organization Source: Reactome
  4. lipoprotein metabolic process Source: Reactome
  5. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
  6. protein folding Source: RefGenome
  7. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  8. response to endoplasmic reticulum stress Source: BHF-UCL
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.
ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_6841. Chylomicron-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
p55
Gene namesi
Name:P4HB
Synonyms:ERBA2L, PDI, PDIA1, PO4DB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:8548. P4HB.

Subcellular locationi

Endoplasmic reticulum lumen. Melanosome. Cell membrane Curated; Peripheral membrane protein Curated
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.Curated

GO - Cellular componenti

  1. endoplasmic reticulum Source: BHF-UCL
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular region Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. focal adhesion Source: UniProtKB
  7. plasma membrane Source: UniProtKB-KW
  8. procollagen-proline 4-dioxygenase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17174 PublicationsAdd
BLAST
Chaini18 – 508491Protein disulfide-isomerasePRO_0000034195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 56Redox-active1 PublicationPROSITE-ProRule annotation
Modified residuei200 – 2001N6-acetyllysineBy similarity
Modified residuei222 – 2221N6-succinyllysineBy similarity
Modified residuei271 – 2711N6-succinyllysineBy similarity
Disulfide bondi397 ↔ 400Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP07237.
PaxDbiP07237.
PeptideAtlasiP07237.
PRIDEiP07237.

2D gel databases

DOSAC-COBS-2DPAGEP07237.
OGPiP07237.
REPRODUCTION-2DPAGEIPI00010796.
P07237.
SWISS-2DPAGEP07237.

PTM databases

PhosphoSiteiP07237.

Miscellaneous databases

PMAP-CutDBP07237.

Expressioni

Gene expression databases

BgeeiP07237.
CleanExiHS_P4HB.
ExpressionAtlasiP07237. baseline and differential.
GenevestigatoriP07237.

Organism-specific databases

HPAiCAB012463.
HPA018884.

Interactioni

Subunit structurei

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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ERO1LQ96HE72EBI-395883,EBI-2564539
HM13Q8TCT93EBI-395883,EBI-347472
PRDX4Q131622EBI-395883,EBI-2211957
TAP1Q035184EBI-395883,EBI-747259

Protein-protein interaction databases

BioGridi111073. 80 interactions.
IntActiP07237. 34 interactions.
MINTiMINT-4999403.
STRINGi9606.ENSP00000327801.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 233
Beta strandi26 – 283
Turni31 – 333
Helixi34 – 407
Beta strandi42 – 498
Helixi54 – 7219
Beta strandi78 – 836
Turni84 – 863
Helixi88 – 936
Beta strandi101 – 1066
Beta strandi110 – 1123
Beta strandi114 – 1163
Helixi122 – 13211
Beta strandi137 – 1393
Helixi143 – 1519
Beta strandi153 – 1608
Turni162 – 1654
Helixi167 – 17812
Beta strandi180 – 1823
Beta strandi184 – 1874
Helixi190 – 1956
Beta strandi199 – 20911
Beta strandi212 – 2154
Helixi222 – 23211
Beta strandi237 – 2393
Turni242 – 2443
Helixi245 – 2495
Beta strandi250 – 2523
Beta strandi255 – 2606
Beta strandi265 – 2673
Helixi268 – 28013
Turni281 – 2855
Beta strandi287 – 2915
Helixi296 – 2983
Helixi299 – 3046
Helixi309 – 3113
Beta strandi313 – 3197
Beta strandi321 – 3233
Beta strandi325 – 3273
Beta strandi330 – 3323
Helixi336 – 34712
Beta strandi353 – 3553
Helixi362 – 3643
Beta strandi367 – 3726
Turni374 – 3763
Helixi377 – 3815
Beta strandi387 – 3937
Helixi398 – 41316
Turni414 – 4163
Beta strandi418 – 4269
Turni427 – 4293
Beta strandi439 – 4468
Beta strandi448 – 4514
Helixi463 – 4708
Turni471 – 4733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP07237.
SMRiP07237. Positions 17-478.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07237.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 134117Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini349 – 475127Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi505 – 5084Prevents secretion from ER

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP07237.
KOiK09580.
OMAiYRDHENI.
OrthoDBiEOG7VHSX1.
PhylomeDBiP07237.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 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.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. 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.

P07237-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA
60 70 80 90 100
PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP
110 120 130 140 150
TIKFFRNGDT ASPKEYTAGR EADDIVNWLK KRTGPAATTL PDGAAAESLV
160 170 180 190 200
ESSEVAVIGF FKDVESDSAK QFLQAAEAID DIPFGITSNS DVFSKYQLDK
210 220 230 240 250
DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF TEQTAPKIFG
260 270 280 290 300
GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR
310 320 330 340 350
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK
360 370 380 390 400
IKPHLMSQEL PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC
410 420 430 440 450
KQLAPIWDKL GETYKDHENI VIAKMDSTAN EVEAVKVHSF PTLKFFPASA
460 470 480 490 500
DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD DDDLEDLEEA EEPDMEEDDD

QKAVKDEL
Length:508
Mass (Da):57,116
Last modified:November 1, 1997 - v3
Checksum:i906CE6D9900B8FCE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 112AV → PW in CAA28775. (PubMed:3034602)Curated
Sequence conflicti21 – 211E → D AA sequence (PubMed:9399589)Curated
Sequence conflicti24 – 241D → V AA sequence (PubMed:9399589)Curated
Sequence conflicti44 – 452LL → PP in CAA28775. (PubMed:3034602)Curated
Sequence conflicti49 – 491Y → H in CAA28775. (PubMed:3034602)Curated
Sequence conflicti141 – 1411P → R in AAA61169. (PubMed:3611107)Curated
Sequence conflicti360 – 3623LPE → RAG in AAA61169. (PubMed:3611107)Curated
Sequence conflicti372 – 3721L → P in AAA61169. (PubMed:3611107)Curated
Sequence conflicti439 – 4391S → G in CAA28775. (PubMed:3034602)Curated
Sequence conflicti444 – 4441K → G in CAA28775. (PubMed:3034602)Curated
Sequence conflicti460 – 4601E → Q in CAA30112. (PubMed:3342239)Curated
Sequence conflicti481 – 4811D → V in CAA28775. (PubMed:3034602)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05130 mRNA. Translation: CAA28775.1.
J02783 mRNA. Translation: AAA61169.1.
M22806
, 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.
CCDSiCCDS11787.1.
PIRiA31913. ISHUSS.
RefSeqiNP_000909.2. NM_000918.3.
UniGeneiHs.464336.

Genome annotation databases

EnsembliENST00000331483; ENSP00000327801; ENSG00000185624.
GeneIDi5034.
KEGGihsa:5034.
UCSCiuc002kbn.1. human.

Polymorphism databases

DMDMi2507460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05130 mRNA. Translation: CAA28775.1 .
J02783 mRNA. Translation: AAA61169.1 .
M22806
, 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 .
CCDSi CCDS11787.1.
PIRi A31913. ISHUSS.
RefSeqi NP_000909.2. NM_000918.3.
UniGenei Hs.464336.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BJX NMR - A 136-245 [» ]
1MEK NMR - A 18-137 [» ]
1X5C NMR - A 368-475 [» ]
2BJX NMR - A 136-245 [» ]
2K18 NMR - A 135-357 [» ]
3BJ5 X-ray 2.20 A 230-368 [» ]
3UEM X-ray 2.29 A 137-479 [» ]
4EKZ X-ray 2.51 A 18-479 [» ]
4EL1 X-ray 2.88 A/B 18-479 [» ]
4JU5 X-ray 2.28 A/B 135-367 [» ]
ProteinModelPortali P07237.
SMRi P07237. Positions 17-478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111073. 80 interactions.
IntActi P07237. 34 interactions.
MINTi MINT-4999403.
STRINGi 9606.ENSP00000327801.

Chemistry

BindingDBi P07237.
ChEMBLi CHEMBL2364681.

PTM databases

PhosphoSitei P07237.

Polymorphism databases

DMDMi 2507460.

2D gel databases

DOSAC-COBS-2DPAGE P07237.
OGPi P07237.
REPRODUCTION-2DPAGE IPI00010796.
P07237.
SWISS-2DPAGE P07237.

Proteomic databases

MaxQBi P07237.
PaxDbi P07237.
PeptideAtlasi P07237.
PRIDEi P07237.

Protocols and materials databases

DNASUi 5034.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331483 ; ENSP00000327801 ; ENSG00000185624 .
GeneIDi 5034.
KEGGi hsa:5034.
UCSCi uc002kbn.1. human.

Organism-specific databases

CTDi 5034.
GeneCardsi GC17M079801.
HGNCi HGNC:8548. P4HB.
HPAi CAB012463.
HPA018884.
MIMi 176790. gene.
neXtProti NX_P07237.
PharmGKBi PA32876.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00760000119201.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi P07237.
KOi K09580.
OMAi YRDHENI.
OrthoDBi EOG7VHSX1.
PhylomeDBi P07237.
TreeFami TF106381.

Enzyme and pathway databases

BRENDAi 5.3.4.1. 2681.
Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_6841. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSi P4HB. human.
EvolutionaryTracei P07237.
GeneWikii P4HB.
GenomeRNAii 5034.
NextBioi 19398.
PMAP-CutDB P07237.
PROi P07237.
SOURCEi Search...

Gene expression databases

Bgeei P07237.
CleanExi HS_P4HB.
ExpressionAtlasi P07237. baseline and differential.
Genevestigatori P07237.

Family and domain databases

Gene3Di 3.40.30.10. 4 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 PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  24. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  28. 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.

Entry informationi

Entry nameiPDIA1_HUMAN
AccessioniPrimary (citable) accession number: P07237
Secondary accession number(s): B2RDQ2
, P30037, P32079, Q15205, Q6LDE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 196 of the entry and version 3 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

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3