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Q15084

- PDIA6_HUMAN

UniProt

Q15084 - PDIA6_HUMAN

Protein

Protein disulfide-isomerase A6

Gene

PDIA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.2 Publications

    Catalytic activityi

    Catalyzes the rearrangement of -S-S- bonds in proteins.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei55 – 551NucleophileBy similarity
    Sitei56 – 561Contributes to redox potential valueBy similarity
    Sitei57 – 571Contributes to redox potential valueBy similarity
    Active sitei58 – 581NucleophileBy similarity
    Sitei118 – 1181Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei190 – 1901NucleophileBy similarity
    Sitei191 – 1911Contributes to redox potential valueBy similarity
    Sitei192 – 1921Contributes to redox potential valueBy similarity
    Active sitei193 – 1931NucleophileBy similarity
    Sitei256 – 2561Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. apoptotic cell clearance Source: RefGenome
    3. cell redox homeostasis Source: InterPro
    4. cellular protein metabolic process Source: Reactome
    5. endoplasmic reticulum unfolded protein response Source: Reactome
    6. protein folding Source: RefGenome
    7. response to endoplasmic reticulum stress Source: RefGenome

    Keywords - Molecular functioni

    Chaperone, Isomerase

    Enzyme and pathway databases

    ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A6 (EC:5.3.4.1)
    Alternative name(s):
    Endoplasmic reticulum protein 5
    Short name:
    ER protein 5
    Short name:
    ERp5
    Protein disulfide isomerase P5
    Thioredoxin domain-containing protein 7
    Gene namesi
    Name:PDIA6
    Synonyms:ERP5, P5, TXNDC7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:30168. PDIA6.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Cell membrane. Melanosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. endoplasmic reticulum membrane Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. melanosome Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551C → S: 50% decrease in enzyme activity; when associated with S-58. Abolishes enzyme activity; when associated with S-58; S-190 and S-193. 1 Publication
    Mutagenesisi58 – 581C → S: 50% decrease in enzyme activity; when associated with S-55. 90% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-190 and S-193. 1 Publication
    Mutagenesisi190 – 1901C → S: 25% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-58 and S-193. 1 Publication
    Mutagenesisi193 – 1931C → S: 90% decrease in enzyme activity; when associated with S-58. 25% decrease in enzyme activity; when associated with S-190. Abolishes enzyme activity; when associated with S-55; S-58 and S-190. 1 Publication

    Organism-specific databases

    PharmGKBiPA134977905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19192 PublicationsAdd
    BLAST
    Chaini20 – 440421Protein disulfide-isomerase A6PRO_0000034236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
    Disulfide bondi190 ↔ 193Redox-activePROSITE-ProRule annotation
    Modified residuei428 – 4281Phosphoserine6 Publications

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ15084.
    PaxDbiQ15084.
    PRIDEiQ15084.

    2D gel databases

    OGPiQ15084.
    REPRODUCTION-2DPAGEIPI00644989.
    Q15084.

    PTM databases

    PhosphoSiteiQ15084.

    Expressioni

    Tissue specificityi

    Expressed in platelets (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ15084.
    BgeeiQ15084.
    CleanExiHS_PDIA6.
    GenevestigatoriQ15084.

    Organism-specific databases

    HPAiHPA034652.
    HPA034653.

    Interactioni

    Subunit structurei

    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. Interacts with MICA on the surface of tumor cells, leading to MICA disulfide bond reduction which is required for its release from tumor cells. Interacts with ITGB3 following platelet stimulation.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRDX4Q131622EBI-1043087,EBI-2211957

    Protein-protein interaction databases

    BioGridi115434. 58 interactions.
    IntActiQ15084. 29 interactions.
    MINTiMINT-3030897.
    STRINGi9606.ENSP00000272227.

    Structurei

    Secondary structure

    1
    440
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 303
    Turni32 – 343
    Helixi35 – 384
    Turni39 – 413
    Beta strandi46 – 516
    Helixi56 – 7116
    Turni72 – 754
    Beta strandi76 – 827
    Turni83 – 853
    Helixi87 – 926
    Beta strandi100 – 1045
    Beta strandi112 – 1143
    Helixi120 – 13920
    Beta strandi162 – 1643
    Turni167 – 1693
    Helixi170 – 1734
    Turni174 – 1763
    Beta strandi178 – 1869
    Helixi191 – 21121
    Beta strandi214 – 2218
    Helixi222 – 2243
    Helixi226 – 2316
    Beta strandi236 – 2438
    Beta strandi247 – 2526
    Helixi258 – 27114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X5DNMR-A161-280[»]
    3VWWX-ray1.93A/B25-140[»]
    3W8JX-ray2.10A/B20-140[»]
    4EF0X-ray1.50A/B27-140[»]
    4GWRX-ray1.81A/B160-274[»]
    ProteinModelPortaliQ15084.
    SMRiQ15084. Positions 27-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15084.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 133114Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini154 – 287134Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi437 – 4404Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi422 – 43413Asp/Glu-rich (acidic)Add
    BLAST

    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.
    HOGENOMiHOG000012631.
    HOVERGENiHBG053548.
    KOiK09584.
    OMAiKNLEPEW.
    OrthoDBiEOG7XDBFV.
    PhylomeDBiQ15084.
    TreeFamiTF315231.

    Family and domain databases

    Gene3Di3.40.30.10. 2 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 3 hits.
    TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15084-1) [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

    MALLVLGLVS CTFFLAVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF    50
    YAPWCGHCQR LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT 100
    IKIFGSNKNR PEDYQGGRTG EAIVDAALSA LRQLVKDRLG GRSGGYSSGK 150
    QGRSDSSSKK DVIELTDDSF DKNVLDSEDV WMVEFYAPWC GHCKNLEPEW 200
    AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI KIFQKGESPV 250
    DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKRT CEEHQLCVVA 300
    VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG 350
    IGGFGYPAMA AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG 400
    GAFPTIVERE PWDGRDGELP VEDDIDLSDV ELDDLGKDEL 440
    Length:440
    Mass (Da):48,121
    Last modified:November 1, 1997 - v1
    Checksum:i06895409F0265D7C
    GO
    Isoform 2 (identifier: Q15084-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MALLVL → MRRDLREKLVWVCRPLAPVEVPANISSDFQPCSPTSPAHSLSRKSPIMYPSTTMANAP

    Show »
    Length:492
    Mass (Da):53,901
    Checksum:i987BB19EC01F116C
    GO
    Isoform 3 (identifier: Q15084-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MALLV → MI

    Note: No experimental confirmation available.

    Show »
    Length:437
    Mass (Da):47,838
    Checksum:i80571DED0FA33DB3
    GO
    Isoform 4 (identifier: Q15084-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MALLVL → MYPSTTMANAP

    Note: No experimental confirmation available.

    Show »
    Length:445
    Mass (Da):48,646
    Checksum:i1C9AE81DD2216FFD
    GO
    Isoform 5 (identifier: Q15084-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MALLVL → MRIITAPASKVSRGSNELMILARRSDRGSPTSPAHSLSRKSPIMYPSTTMANAP

    Note: No experimental confirmation available.

    Show »
    Length:488
    Mass (Da):53,261
    Checksum:i79DDA7AC1EF6C39D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641E → K in BAH12614. (PubMed:14702039)Curated
    Sequence conflicti187 – 1871A → V in BAH12614. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141K → R.2 Publications
    Corresponds to variant rs4807 [ dbSNP | Ensembl ].
    VAR_022152

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MALLVL → MRRDLREKLVWVCRPLAPVE VPANISSDFQPCSPTSPAHS LSRKSPIMYPSTTMANAP in isoform 2. 1 PublicationVSP_021803
    Alternative sequencei1 – 66MALLVL → MYPSTTMANAP in isoform 4. 1 PublicationVSP_055173
    Alternative sequencei1 – 66MALLVL → MRIITAPASKVSRGSNELMI LARRSDRGSPTSPAHSLSRK SPIMYPSTTMANAP in isoform 5. 1 PublicationVSP_055174
    Alternative sequencei1 – 55MALLV → MI in isoform 3. 1 PublicationVSP_054370

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49489 mRNA. Translation: BAA08450.1.
    AK127433 mRNA. Translation: BAC86977.1.
    AK131234 mRNA. Translation: BAG54757.1.
    AK289428 mRNA. Translation: BAF82117.1.
    AK294347 mRNA. Translation: BAH11740.1.
    AK297547 mRNA. Translation: BAH12614.1.
    AC092687 Genomic DNA. Translation: AAY24070.1.
    CH471053 Genomic DNA. Translation: EAX00950.1.
    BC001312 mRNA. Translation: AAH01312.1.
    U79278 mRNA. Translation: AAB50217.1.
    CCDSiCCDS1675.1. [Q15084-1]
    CCDS62852.1. [Q15084-3]
    CCDS62853.1. [Q15084-4]
    CCDS62854.1. [Q15084-2]
    CCDS62855.1. [Q15084-5]
    PIRiJC4369.
    RefSeqiNP_001269633.1. NM_001282704.1. [Q15084-2]
    NP_001269634.1. NM_001282705.1.
    NP_001269635.1. NM_001282706.1.
    NP_001269636.1. NM_001282707.1. [Q15084-3]
    NP_005733.1. NM_005742.3. [Q15084-1]
    UniGeneiHs.212102.
    Hs.580464.

    Genome annotation databases

    EnsembliENST00000272227; ENSP00000272227; ENSG00000143870. [Q15084-1]
    ENST00000381611; ENSP00000371024; ENSG00000143870. [Q15084-4]
    ENST00000404371; ENSP00000385385; ENSG00000143870. [Q15084-2]
    ENST00000404824; ENSP00000384459; ENSG00000143870. [Q15084-5]
    ENST00000540494; ENSP00000438778; ENSG00000143870. [Q15084-3]
    GeneIDi10130.
    KEGGihsa:10130.
    UCSCiuc002rau.3. human. [Q15084-1]
    uc002rav.3. human. [Q15084-2]

    Polymorphism databases

    DMDMi2501205.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49489 mRNA. Translation: BAA08450.1 .
    AK127433 mRNA. Translation: BAC86977.1 .
    AK131234 mRNA. Translation: BAG54757.1 .
    AK289428 mRNA. Translation: BAF82117.1 .
    AK294347 mRNA. Translation: BAH11740.1 .
    AK297547 mRNA. Translation: BAH12614.1 .
    AC092687 Genomic DNA. Translation: AAY24070.1 .
    CH471053 Genomic DNA. Translation: EAX00950.1 .
    BC001312 mRNA. Translation: AAH01312.1 .
    U79278 mRNA. Translation: AAB50217.1 .
    CCDSi CCDS1675.1. [Q15084-1 ]
    CCDS62852.1. [Q15084-3 ]
    CCDS62853.1. [Q15084-4 ]
    CCDS62854.1. [Q15084-2 ]
    CCDS62855.1. [Q15084-5 ]
    PIRi JC4369.
    RefSeqi NP_001269633.1. NM_001282704.1. [Q15084-2 ]
    NP_001269634.1. NM_001282705.1.
    NP_001269635.1. NM_001282706.1.
    NP_001269636.1. NM_001282707.1. [Q15084-3 ]
    NP_005733.1. NM_005742.3. [Q15084-1 ]
    UniGenei Hs.212102.
    Hs.580464.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X5D NMR - A 161-280 [» ]
    3VWW X-ray 1.93 A/B 25-140 [» ]
    3W8J X-ray 2.10 A/B 20-140 [» ]
    4EF0 X-ray 1.50 A/B 27-140 [» ]
    4GWR X-ray 1.81 A/B 160-274 [» ]
    ProteinModelPortali Q15084.
    SMRi Q15084. Positions 27-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115434. 58 interactions.
    IntActi Q15084. 29 interactions.
    MINTi MINT-3030897.
    STRINGi 9606.ENSP00000272227.

    Chemistry

    ChEMBLi CHEMBL2146308.

    PTM databases

    PhosphoSitei Q15084.

    Polymorphism databases

    DMDMi 2501205.

    2D gel databases

    OGPi Q15084.
    REPRODUCTION-2DPAGE IPI00644989.
    Q15084.

    Proteomic databases

    MaxQBi Q15084.
    PaxDbi Q15084.
    PRIDEi Q15084.

    Protocols and materials databases

    DNASUi 10130.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272227 ; ENSP00000272227 ; ENSG00000143870 . [Q15084-1 ]
    ENST00000381611 ; ENSP00000371024 ; ENSG00000143870 . [Q15084-4 ]
    ENST00000404371 ; ENSP00000385385 ; ENSG00000143870 . [Q15084-2 ]
    ENST00000404824 ; ENSP00000384459 ; ENSG00000143870 . [Q15084-5 ]
    ENST00000540494 ; ENSP00000438778 ; ENSG00000143870 . [Q15084-3 ]
    GeneIDi 10130.
    KEGGi hsa:10130.
    UCSCi uc002rau.3. human. [Q15084-1 ]
    uc002rav.3. human. [Q15084-2 ]

    Organism-specific databases

    CTDi 10130.
    GeneCardsi GC02M010923.
    HGNCi HGNC:30168. PDIA6.
    HPAi HPA034652.
    HPA034653.
    MIMi 611099. gene.
    neXtProti NX_Q15084.
    PharmGKBi PA134977905.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000012631.
    HOVERGENi HBG053548.
    KOi K09584.
    OMAi KNLEPEW.
    OrthoDBi EOG7XDBFV.
    PhylomeDBi Q15084.
    TreeFami TF315231.

    Enzyme and pathway databases

    Reactomei REACT_18273. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi PDIA6. human.
    EvolutionaryTracei Q15084.
    GenomeRNAii 10130.
    NextBioi 35470712.
    PROi Q15084.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15084.
    Bgeei Q15084.
    CleanExi HS_PDIA6.
    Genevestigatori Q15084.

    Family and domain databases

    Gene3Di 3.40.30.10. 2 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 3 hits.
    TIGRFAMsi 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

    1. "Cloning and sequencing of the cDNA encoding human P5."
      Hayano T., Kikuchi M.
      Gene 164:377-378(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "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] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANT ARG-214.
      Tissue: Amygdala and Thalamus.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORM 1).
      Tissue: Placenta.
    6. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-440 (ISOFORM 1), VARIANT ARG-214.
      Tissue: Brain.
    7. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 20-38.
      Tissue: Leukemic T-cell.
    8. "A role for the thiol isomerase protein ERP5 in platelet function."
      Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
      Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 103-138; 195-212; 217-231; 242-289; 314-328 AND 374-386.
      Tissue: B-cell lymphoma.
    10. "Functional analysis of human P5, a protein disulfide isomerase homologue."
      Kikuchi M., Doi E., Tsujimoto I., Horibe T., Tsujimoto Y.
      J. Biochem. 132:451-455(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF CYS-55; CYS-58; CYS-190 AND CYS-193.
    11. "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.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands."
      Kaiser B.K., Yim D., Chow I.-T., Gonzalez S., Dai Z., Mann H.H., Strong R.K., Groh V., Spies T.
      Nature 447:482-486(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICA.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase A6."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 161-280.

    Entry informationi

    Entry nameiPDIA6_HUMAN
    AccessioniPrimary (citable) accession number: Q15084
    Secondary accession number(s): B3KY95
    , B5MCQ5, B7Z254, B7Z4M8, F8WA83, Q53RC7, Q6ZSH5, Q99778
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 159 of the entry and version 1 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

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

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3