Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15084

- PDIA6_HUMAN

UniProt

Q15084 - PDIA6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein disulfide-isomerase A6

Gene

PDIA6

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (5)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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 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
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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: UniProtKB
  6. melanosome Source: UniProtKB-SubCell
  7. plasma membrane Source: UniProtKB-SubCell
  8. smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

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

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. 69 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 – 303Combined sources
Turni32 – 343Combined sources
Helixi35 – 384Combined sources
Turni39 – 413Combined sources
Beta strandi46 – 516Combined sources
Helixi56 – 7116Combined sources
Turni72 – 754Combined sources
Beta strandi76 – 827Combined sources
Turni83 – 853Combined sources
Helixi87 – 926Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi112 – 1143Combined sources
Helixi120 – 13920Combined sources
Beta strandi162 – 1643Combined sources
Turni167 – 1693Combined sources
Helixi170 – 1734Combined sources
Turni174 – 1763Combined sources
Beta strandi178 – 1869Combined sources
Helixi191 – 21121Combined sources
Beta strandi214 – 2218Combined sources
Helixi222 – 2243Combined sources
Helixi226 – 2316Combined sources
Beta strandi236 – 2438Combined sources
Beta strandi247 – 2526Combined sources
Helixi258 – 27114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000012631.
HOVERGENiHBG053548.
InParanoidiQ15084.
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

        10         20         30         40         50
MALLVLGLVS CTFFLAVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF 
        60         70         80         90        100
YAPWCGHCQR LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT 
       110        120        130        140        150
IKIFGSNKNR PEDYQGGRTG EAIVDAALSA LRQLVKDRLG GRSGGYSSGK 
       160        170        180        190        200
QGRSDSSSKK DVIELTDDSF DKNVLDSEDV WMVEFYAPWC GHCKNLEPEW 
       210        220        230        240        250
AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI KIFQKGESPV 
       260        270        280        290        300
DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKRT CEEHQLCVVA 
       310        320        330        340        350
VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG 
       360        370        380        390        400
IGGFGYPAMA AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG 
       410        420        430        440
GAFPTIVERE PWDGRDGELP VEDDIDLSDV ELDDLGKDEL
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:
EMBLi
GenBanki
DDBJi
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. [Q15084-5]
NP_001269635.1. NM_001282706.1. [Q15084-4]
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]
ENST00000617249; ENSP00000481892; ENSG00000143870. [Q15084-2]
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:
EMBLi
GenBanki
DDBJi
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. [Q15084-5 ]
NP_001269635.1. NM_001282706.1. [Q15084-4 ]
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:
PDBei
RCSB PDBi
PDBji
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. 69 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 ]
ENST00000617249 ; ENSP00000481892 ; ENSG00000143870 . [Q15084-2 ]
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.
GeneTreei ENSGT00730000110455.
HOGENOMi HOG000012631.
HOVERGENi HBG053548.
InParanoidi Q15084.
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

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

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 162 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

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.
© 2002– 2015 UniProt Consortium | License & Disclaimer