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Protein

Protein disulfide-isomerase A2

Gene

PDIA2

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

Functioni

Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711NucleophileBy similarity
Sitei72 – 721Contributes to redox potential valueBy similarity
Sitei73 – 731Contributes to redox potential valueBy similarity
Active sitei74 – 741NucleophileBy similarity
Sitei138 – 1381Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei418 – 4181NucleophileBy similarity
Sitei419 – 4191Contributes to redox potential valueBy similarity
Sitei420 – 4201Contributes to redox potential valueBy similarity
Active sitei421 – 4211NucleophileBy similarity
Sitei482 – 4821Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: ParkinsonsUK-UCL
  2. protein disulfide isomerase activity Source: GO_Central
  3. steroid binding Source: UniProtKB-KW

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. oxidation-reduction process Source: GOC
  3. peptidyl-proline hydroxylation Source: GOC
  4. protein folding Source: GO_Central
  5. protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
  6. protein retention in ER lumen Source: ProtInc
  7. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: GO_Central
  8. response to endoplasmic reticulum stress Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Keywords - Ligandi

Lipid-binding, Steroid-binding

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A2 (EC:5.3.4.1)
Alternative name(s):
Pancreas-specific protein disulfide isomerase
Short name:
PDIp
Gene namesi
Name:PDIA2
Synonyms:PDIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:14180. PDIA2.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181C → A: Impairs interchain disulfide bridge formation. 1 Publication
Mutagenesisi284 – 2841N → Q: Increases formation of a highly stable disulfide-bonded PDIA2 dimer. 1 Publication
Mutagenesisi364 – 3641C → A: No effect on interchain disulfide bridge formation. 1 Publication

Organism-specific databases

PharmGKBiPA33153.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 525504Protein disulfide-isomerase A2PRO_0000034222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 – 18Interchain1 Publication
Disulfide bondi71 ↔ 74Redox-activePROSITE-ProRule annotation
Glycosylationi127 – 1271N-linked (GlcNAc...)1 Publication
Glycosylationi284 – 2841N-linked (GlcNAc...)1 Publication
Disulfide bondi418 ↔ 421Redox-activePROSITE-ProRule annotation
Glycosylationi516 – 5161N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The disulfide-linked homodimer exhibits an enhanced chaperone activity.
Glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ13087.
PaxDbiQ13087.
PRIDEiQ13087.

PTM databases

PhosphoSiteiQ13087.

Expressioni

Tissue specificityi

Highly expressed in pancreas (at protein level).3 Publications

Gene expression databases

BgeeiQ13087.
CleanExiHS_PDIA2.
ExpressionAtlasiQ13087. baseline and differential.
GenevestigatoriQ13087.

Organism-specific databases

HPAiHPA051692.
HPA053492.

Interactioni

Subunit structurei

Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163333EBI-1752525,EBI-389883

Protein-protein interaction databases

BioGridi122240. 18 interactions.
IntActiQ13087. 10 interactions.
MINTiMINT-1513985.
STRINGi9606.ENSP00000219406.

Structurei

3D structure databases

ProteinModelPortaliQ13087.
SMRiQ13087. Positions 32-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 152126Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini367 – 496130Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi522 – 5254Prevents secretion from ERPROSITE-ProRule annotation

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.
HOVERGENiHBG005920.
InParanoidiQ13087.
KOiK09581.
OMAiQEVPPDW.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ13087.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. 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.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13087-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH
60 70 80 90 100
TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV
110 120 130 140 150
DGPAQRELAE EFGVTEYPTL KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR
160 170 180 190 200
VGPSAMRLED EAAAQALIGG RDLVVIGFFQ DLQDEDVATF LALAQDALDM
210 220 230 240 250
TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF
260 270 280 290 300
LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA
310 320 330 340 350
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV
360 370 380 390 400
DGGPVTAASI TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ
410 420 430 440 450
VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED IIIAELDATA
460 470 480 490 500
NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLETFSKF LDNGGVLPTE
510 520
EPPEEPAAPF PEPPANSTMG SKEEL
Length:525
Mass (Da):58,206
Last modified:May 26, 2002 - v2
Checksum:iB741851AA2C40540
GO
Isoform 2 (identifier: Q13087-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-183: Missing.

Show »
Length:522
Mass (Da):57,850
Checksum:i815CD5F3060B5747
GO

Sequence cautioni

The sequence AAC50401.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAH75029.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAG58339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961T → M in BAG58339 (PubMed:14702039).Curated
Sequence conflicti484 – 4841L → Q in BAG58339 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391P → S.
Corresponds to variant rs45455191 [ dbSNP | Ensembl ].
VAR_048087
Natural varianti119 – 1191T → R.
Corresponds to variant rs45614840 [ dbSNP | Ensembl ].
VAR_048088
Natural varianti185 – 1851E → K.
Corresponds to variant rs419949 [ dbSNP | Ensembl ].
VAR_048089
Natural varianti286 – 2861T → M.
Corresponds to variant rs2685127 [ dbSNP | Ensembl ].
VAR_048090
Natural varianti382 – 3821P → A.
Corresponds to variant rs45529833 [ dbSNP | Ensembl ].
VAR_048091
Natural varianti388 – 3881R → Q.
Corresponds to variant rs400037 [ dbSNP | Ensembl ].
VAR_048092
Natural varianti502 – 5021P → S.3 Publications
Corresponds to variant rs1048786 [ dbSNP | Ensembl ].
VAR_048093

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei181 – 1833Missing in isoform 2. CuratedVSP_039292

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB127078 mRNA. Translation: BAE48734.1.
AE006463 Genomic DNA. Translation: AAK61223.1.
Z69667 Genomic DNA. Translation: CAI95586.1.
Z69667 Genomic DNA. Translation: CAO78188.1.
CH471112 Genomic DNA. Translation: EAW85838.1.
BC000537 mRNA. Translation: AAH00537.2.
BC075029 mRNA. Translation: AAH75029.1. Sequence problems.
U19948 mRNA. Translation: AAC50401.1. Sequence problems.
AK295383 mRNA. Translation: BAG58339.1. Different initiation.
CCDSiCCDS42089.1. [Q13087-1]
RefSeqiNP_006840.2. NM_006849.2. [Q13087-1]
UniGeneiHs.66581.

Genome annotation databases

EnsembliENST00000219406; ENSP00000219406; ENSG00000185615. [Q13087-1]
ENST00000404312; ENSP00000384410; ENSG00000185615. [Q13087-2]
GeneIDi64714.
KEGGihsa:64714.
UCSCiuc002cgn.1. human. [Q13087-1]

Polymorphism databases

DMDMi21264492.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB127078 mRNA. Translation: BAE48734.1.
AE006463 Genomic DNA. Translation: AAK61223.1.
Z69667 Genomic DNA. Translation: CAI95586.1.
Z69667 Genomic DNA. Translation: CAO78188.1.
CH471112 Genomic DNA. Translation: EAW85838.1.
BC000537 mRNA. Translation: AAH00537.2.
BC075029 mRNA. Translation: AAH75029.1. Sequence problems.
U19948 mRNA. Translation: AAC50401.1. Sequence problems.
AK295383 mRNA. Translation: BAG58339.1. Different initiation.
CCDSiCCDS42089.1. [Q13087-1]
RefSeqiNP_006840.2. NM_006849.2. [Q13087-1]
UniGeneiHs.66581.

3D structure databases

ProteinModelPortaliQ13087.
SMRiQ13087. Positions 32-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122240. 18 interactions.
IntActiQ13087. 10 interactions.
MINTiMINT-1513985.
STRINGi9606.ENSP00000219406.

PTM databases

PhosphoSiteiQ13087.

Polymorphism databases

DMDMi21264492.

Proteomic databases

MaxQBiQ13087.
PaxDbiQ13087.
PRIDEiQ13087.

Protocols and materials databases

DNASUi64714.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219406; ENSP00000219406; ENSG00000185615. [Q13087-1]
ENST00000404312; ENSP00000384410; ENSG00000185615. [Q13087-2]
GeneIDi64714.
KEGGihsa:64714.
UCSCiuc002cgn.1. human. [Q13087-1]

Organism-specific databases

CTDi64714.
GeneCardsiGC16P000336.
H-InvDBHIX0202311.
HGNCiHGNC:14180. PDIA2.
HPAiHPA051692.
HPA053492.
MIMi608012. gene.
neXtProtiNX_Q13087.
PharmGKBiPA33153.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOVERGENiHBG005920.
InParanoidiQ13087.
KOiK09581.
OMAiQEVPPDW.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ13087.
TreeFamiTF106381.

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Miscellaneous databases

GenomeRNAii64714.
NextBioi66651.
PROiQ13087.
SOURCEiSearch...

Gene expression databases

BgeeiQ13087.
CleanExiHS_PDIA2.
ExpressionAtlasiQ13087. baseline and differential.
GenevestigatoriQ13087.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. 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.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human polycistronic mRNA composed of ARHGDIG and PDIP."
    Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T., Saito T.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-502.
  2. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525 (ISOFORM 1), VARIANT SER-502.
    Tissue: Brain.
  6. "Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas."
    Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L., Lan M.S.
    DNA Cell Biol. 15:9-16(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-525 (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-502.
    Tissue: Pancreas.
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-525 (ISOFORM 1).
    Tissue: Corpus callosum.
  8. "Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp."
    Desilva M.G., Notkins A.L., Lan M.S.
    DNA Cell Biol. 16:269-274(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, GLYCOSYLATION.
  9. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  10. "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond."
    Fu X., Zhu B.T.
    Arch. Biochem. Biophys. 485:1-9(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-18 AND CYS-364.
  11. "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an intracellular estrogen-binding protein that modulates estrogen levels and actions in target cells."
    Fu X.M., Zhu B.T.
    J. Steroid Biochem. Mol. Biol. 115:20-29(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  12. "N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2)."
    Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D.
    FEBS J. 280:233-243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-127; ASN-284 AND ASN-516, MUTAGENESIS OF ASN-284.

Entry informationi

Entry nameiPDIA2_HUMAN
AccessioniPrimary (citable) accession number: Q13087
Secondary accession number(s): A6ZJ64
, B4DI27, Q2WGM4, Q4TT67, Q6B010, Q96KJ6, Q9BW95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 14, 1998
Last sequence update: May 26, 2002
Last modified: March 31, 2015
This is version 151 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.