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Q13087

- PDIA2_HUMAN

UniProt

Q13087 - PDIA2_HUMAN

Protein

Protein disulfide-isomerase A2

Gene

PDIA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (27 May 2002)
      Previous versions | rss
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    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. protein binding Source: IntAct
    2. protein disulfide isomerase activity Source: RefGenome
    3. steroid binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. peptidyl-proline hydroxylation Source: GOC
    3. protein folding Source: RefGenome
    4. protein retention in ER lumen Source: ProtInc
    5. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: RefGenome
    6. response to endoplasmic reticulum stress Source: RefGenome

    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: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:14180. PDIA2.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RefGenome
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    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...)2 Publications
    Glycosylationi284 – 2841N-linked (GlcNAc...)2 Publications
    Disulfide bondi418 ↔ 421Redox-activePROSITE-ProRule annotation
    Glycosylationi516 – 5161N-linked (GlcNAc...)2 Publications

    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

    ArrayExpressiQ13087.
    BgeeiQ13087.
    CleanExiHS_PDIA2.
    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. 16 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.
    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. Align

    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

    MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH    50
    TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV 100
    DGPAQRELAE EFGVTEYPTL KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR 150
    VGPSAMRLED EAAAQALIGG RDLVVIGFFQ DLQDEDVATF LALAQDALDM 200
    TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF 250
    LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA 300
    APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV 350
    DGGPVTAASI TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ 400
    VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED IIIAELDATA 450
    NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLETFSKF LDNGGVLPTE 500
    EPPEEPAAPF PEPPANSTMG SKEEL 525
    Length:525
    Mass (Da):58,206
    Last modified:May 27, 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. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAH75029.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence BAG58339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS42089.1. [Q13087-1 ]
    RefSeqi NP_006840.2. NM_006849.2. [Q13087-1 ]
    UniGenei Hs.66581.

    3D structure databases

    ProteinModelPortali Q13087.
    SMRi Q13087. Positions 32-495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122240. 16 interactions.
    IntActi Q13087. 10 interactions.
    MINTi MINT-1513985.
    STRINGi 9606.ENSP00000219406.

    PTM databases

    PhosphoSitei Q13087.

    Polymorphism databases

    DMDMi 21264492.

    Proteomic databases

    MaxQBi Q13087.
    PaxDbi Q13087.
    PRIDEi Q13087.

    Protocols and materials databases

    DNASUi 64714.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219406 ; ENSP00000219406 ; ENSG00000185615 . [Q13087-1 ]
    ENST00000404312 ; ENSP00000384410 ; ENSG00000185615 . [Q13087-2 ]
    GeneIDi 64714.
    KEGGi hsa:64714.
    UCSCi uc002cgn.1. human. [Q13087-1 ]

    Organism-specific databases

    CTDi 64714.
    GeneCardsi GC16P000336.
    H-InvDB HIX0202311.
    HGNCi HGNC:14180. PDIA2.
    HPAi HPA051692.
    HPA053492.
    MIMi 608012. gene.
    neXtProti NX_Q13087.
    PharmGKBi PA33153.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOVERGENi HBG005920.
    InParanoidi Q13087.
    KOi K09581.
    OMAi QEVPPDW.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi Q13087.
    TreeFami TF106381.

    Enzyme and pathway databases

    BRENDAi 5.3.4.1. 2681.

    Miscellaneous databases

    ChiTaRSi PDIA2. human.
    GenomeRNAii 64714.
    NextBioi 66651.
    PROi Q13087.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13087.
    Bgeei Q13087.
    CleanExi HS_PDIA2.
    Genevestigatori Q13087.

    Family and domain databases

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

    Publicationsi

    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 (NOV-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(2001) [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(2004) [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(2004) [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(1996) [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(2004) [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(1997) [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(2002) [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(2009) [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(2009) [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(2013) [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 15, 1998
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 145 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

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