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Q15084

- PDIA6_HUMAN

UniProt

Q15084 - PDIA6_HUMAN

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Protein

Protein disulfide-isomerase A6

Gene
PDIA6, ERP5, P5, TXNDC7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 551Nucleophile By similarity
Sitei56 – 561Contributes to redox potential value By similarity
Sitei57 – 571Contributes to redox potential value By similarity
Active sitei58 – 581Nucleophile By similarity
Sitei118 – 1181Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei190 – 1901Nucleophile By similarity
Sitei191 – 1911Contributes to redox potential value By similarity
Sitei192 – 1921Contributes to redox potential value By similarity
Active sitei193 – 1931Nucleophile By similarity
Sitei256 – 2561Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. isomerase activity Source: InterPro
  2. protein binding Source: UniProtKB
  3. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:30168. PDIA6.

Subcellular locationi

Endoplasmic reticulum lumen By similarity. Cell membrane. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.3 Publications

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
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-active By similarity
Disulfide bondi190 ↔ 193Redox-active By similarity
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.

Miscellaneous databases

EvolutionaryTraceiQ15084.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 133114Thioredoxin 1Add
BLAST
Domaini154 – 287134Thioredoxin 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi437 – 4404Prevents secretion from ER Reviewed prediction

Compositional bias

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

Sequence similaritiesi

Contains 2 thioredoxin domains.

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

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. VSP_021803
Alternative sequencei1 – 66MALLVL → MYPSTTMANAP in isoform 4. VSP_055173
Alternative sequencei1 – 66MALLVL → MRIITAPASKVSRGSNELMI LARRSDRGSPTSPAHSLSRK SPIMYPSTTMANAP in isoform 5. VSP_055174
Alternative sequencei1 – 55MALLV → MI in isoform 3. VSP_054370

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641E → K in BAH12614. 1 Publication
Sequence conflicti187 – 1871A → V in BAH12614. 1 Publication

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]
CCDS62854.1. [Q15084-2]
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.
ENST00000404371; ENSP00000385385; ENSG00000143870. [Q15084-2]
ENST00000404824; ENSP00000384459; ENSG00000143870.
ENST00000540494; ENSP00000438778; ENSG00000143870.
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 ]
CCDS62854.1. [Q15084-2 ]
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 .
ENST00000404371 ; ENSP00000385385 ; ENSG00000143870 . [Q15084-2 ]
ENST00000404824 ; ENSP00000384459 ; ENSG00000143870 .
ENST00000540494 ; ENSP00000438778 ; ENSG00000143870 .
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

« 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.

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: September 3, 2014
This is version 158 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

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