Q15084 (PDIA6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PDIA6
Synonyms:	ERP5, P5, TXNDC7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.10
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins. Ref.8 Ref.10
Subunit structure	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. Ref.8 Ref.16
Subcellular location	Endoplasmic reticulum lumen By similarity. Cell membrane. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.8 Ref.12 Ref.14
Tissue specificity	Expressed in platelets (at protein level). Ref.8
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Redox-active center Repeat Signal
Molecular function	Chaperone Isomerase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro oxidation-reduction process Inferred from electronic annotation. Source: GOC
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Traceable author statement. Source: Reactome endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay PubMed 15308636. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein disulfide isomerase activity Traceable author statement Ref.1. Source: ProtInc protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRDX4	Q13162	2	EBI-1043087,EBI-2211957

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15084-1)

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.

Isoform 2 (identifier: Q15084-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.7 Ref.8

Chain

20 – 440

421

Protein disulfide-isomerase A6

PRO_0000034236

Regions

Domain

20 – 133

114

Thioredoxin 1

Domain

154 – 287

134

Thioredoxin 2

Motif

437 – 440

4

Prevents secretion from ER Potential

Compositional bias

422 – 434

13

Asp/Glu-rich (acidic)

Sites

Active site

55

1

Nucleophile By similarity

Active site

58

1

Nucleophile By similarity

Active site

190

1

Nucleophile By similarity

Active site

193

1

Nucleophile By similarity

Site

56

1

Contributes to redox potential value By similarity

Site

57

1

Contributes to redox potential value By similarity

Site

118

1

Lowers pKa of C-terminal Cys of first active site By similarity

Site

191

1

Contributes to redox potential value By similarity

Site

192

1

Contributes to redox potential value By similarity

Site

256

1

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue

428

1

Phosphoserine Ref.13 Ref.15 Ref.18 Ref.20 Ref.21 Ref.23

Disulfide bond

55 ↔ 58

Redox-active By similarity

Disulfide bond

190 ↔ 193

Redox-active By similarity

Natural variations

Alternative sequence

1 – 6

6

MALLVL → MRRDLREKLVWVCRPLAPVE VPANISSDFQPCSPTSPAHS LSRKSPIMYPSTTMANAP in isoform 2.

VSP_021803

Natural variant

214

1

K → R. Ref.2 Ref.6
Corresponds to variant rs4807 [ dbSNP | Ensembl ].

VAR_022152

Experimental info

Mutagenesis

55

1

C → S: 50% decrease in enzyme activity; when associated with S-58. Abolishes enzyme activity; when associated with S-58; S-190 and S-193. Ref.10

Mutagenesis

58

1

C → 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. Ref.10

Mutagenesis

190

1

C → S: 25% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-58 and S-193. Ref.10

Mutagenesis

193

1

C → 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. Ref.10

Secondary structure

1

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440

Helix Strand Turn

Details...

Beta strand

28 – 30

3

Turn

32 – 34

3

Helix

35 – 38

4

Turn

39 – 41

3

Beta strand

46 – 51

6

Helix

56 – 71

16

Turn

72 – 75

4

Beta strand

76 – 82

7

Turn

83 – 85

3

Helix

87 – 92

6

Beta strand

100 – 104

5

Beta strand

112 – 114

3

Helix

120 – 139

20

Beta strand

162 – 164

3

Turn

167 – 169

3

Helix

170 – 173

4

Turn

174 – 176

3

Beta strand

178 – 186

9

Helix

191 – 211

21

Beta strand

214 – 221

8

Helix

222 – 224

3

Helix

226 – 231

6

Beta strand

236 – 243

8

Beta strand

247 – 252

6

Helix

258 – 271

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 06895409F0265D7C	FASTA	440	48,121
	10 20 30 40 50 60 MALLVLGLVS CTFFLAVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR 70 80 90 100 110 120 LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT IKIFGSNKNR PEDYQGGRTG 130 140 150 160 170 180 EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRSDSSSKK DVIELTDDSF DKNVLDSEDV 190 200 210 220 230 240 WMVEFYAPWC GHCKNLEPEW AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI 250 260 270 280 290 300 KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKRT CEEHQLCVVA 310 320 330 340 350 360 VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG IGGFGYPAMA 370 380 390 400 410 420 AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GAFPTIVERE PWDGRDGELP 430 440 VEDDIDLSDV ELDDLGKDEL
	Isoform 2 [UniParc]. Checksum: 987BB19EC01F116C	FASTA	492	53,901
	10 20 30 40 50 60 MRRDLREKLV WVCRPLAPVE VPANISSDFQ PCSPTSPAHS LSRKSPIMYP STTMANAPGL 70 80 90 100 110 120 VSCTFFLAVN GLYSSSDDVI ELTPSNFNRE VIQSDSLWLV EFYAPWCGHC QRLTPEWKKA 130 140 150 160 170 180 ATALKDVVKV GAVDADKHHS LGGQYGVQGF PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL 190 200 210 220 230 240 SALRQLVKDR LGGRSGGYSS GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP 250 260 270 280 290 300 WCGHCKNLEP EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES 310 320 330 340 350 360 PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV VAVLPHILDT 370 380 390 400 410 420 GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA LGIGGFGYPA MAAINARKMK 430 440 450 460 470 480 FALLKGSFSE QGINEFLREL SFGRGSTAPV GGGAFPTIVE REPWDGRDGE LPVEDDIDLS 490 DVELDDLGKD EL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 AND 2), VARIANT ARG-214. Tissue: 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]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D49489 mRNA. Translation: BAA08450.1.
AK127433 mRNA. Translation: BAC86977.1.
AK289428 mRNA. Translation: BAF82117.1.
AC092687 Genomic DNA. Translation: AAY24070.1.
CH471053 Genomic DNA. Translation: EAX00950.1.
BC001312 mRNA. Translation: AAH01312.1.
U79278 mRNA. Translation: AAB50217.1.

PIR

JC4369.

RefSeq

NP_001269633.1. NM_001282704.1.
NP_001269634.1. NM_001282705.1.
NP_001269635.1. NM_001282706.1.
NP_001269636.1. NM_001282707.1.
NP_005733.1. NM_005742.3.

UniGene

Hs.212102.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q15084.

SMR

Q15084. Positions 27-280.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

115434. 44 interactions.

IntAct

Q15084. 28 interactions.

MINT

MINT-3030897.

STRING

9606.ENSP00000272227.

Chemistry

ChEMBL

CHEMBL2146308.

PTM databases

PhosphoSite

Q15084.

Polymorphism databases

DMDM

2501205.

2D gel databases

OGP

Q15084.

REPRODUCTION-2DPAGE

IPI00644989.
Q15084.

Proteomic databases

PaxDb

Q15084.

PRIDE

Q15084.

Protocols and materials databases

DNASU

10130.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272227; ENSP00000272227; ENSG00000143870.
ENST00000404371; ENSP00000385385; ENSG00000143870.

GeneID

10130.

KEGG

hsa:10130.

UCSC

uc002rau.3. human.

Organism-specific databases

CTD

10130.

GeneCards

GC02M010923.

HGNC

HGNC:30168. PDIA6.

HPA

HPA034652.
HPA034653.

MIM

611099. gene.

neXtProt

NX_Q15084.

PharmGKB

PA134977905.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000012631.

HOVERGEN

HBG053548.

KO

K09584.

OMA

KNLEPEW.

OrthoDB

EOG7XDBFV.

PhylomeDB

Q15084.

TreeFam

TF315231.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpress

Q15084.

Bgee

Q15084.

CleanEx

HS_PDIA6.

Genevestigator

Q15084.

Family and domain databases

Gene3D

3.40.30.10. 2 hits.

InterPro

IPR005788. Disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF00085. Thioredoxin. 2 hits.
[Graphical view]

PRINTS

PR00421. THIOREDOXIN.

SUPFAM

SSF52833. SSF52833. 3 hits.

TIGRFAMs

TIGR01126. pdi_dom. 2 hits.

PROSITE

PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PDIA6. human.

EvolutionaryTrace

Q15084.

GenomeRNAi

10130.

NextBio

38319.

PRO

Q15084.

SOURCE

Search...

Entry information

Entry name

PDIA6_HUMAN

Accession

Primary (citable) accession number: Q15084
Secondary accession number(s): Q53RC7, Q6ZSH5, Q99778

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 19, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.