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Q13087

- PDIA2_HUMAN

UniProt

Q13087 - PDIA2_HUMAN

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Protein
Protein disulfide-isomerase A2
Gene
PDIA2, PDIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Nucleophile By similarity
Sitei72 – 721Contributes to redox potential value By similarity
Sitei73 – 731Contributes to redox potential value By similarity
Active sitei74 – 741Nucleophile By similarity
Sitei138 – 1381Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei418 – 4181Nucleophile By similarity
Sitei419 – 4191Contributes to redox potential value By similarity
Sitei420 – 4201Contributes to redox potential value By similarity
Active sitei421 – 4211Nucleophile By similarity
Sitei482 – 4821Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein disulfide isomerase activity Source: RefGenome
  3. steroid binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Chaperone, Isomerase

Keywords - Ligandi

Lipid-binding, Steroid-binding

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A2 (EC:5.3.4.1)
Alternative name(s):
Pancreas-specific protein disulfide isomerase
Short name:
PDIp
Gene namesi
Name:PDIA2
Synonyms:PDIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:14180. PDIA2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181C → A: Impairs interchain disulfide bridge formation. 1 Publication
Mutagenesisi284 – 2841N → Q: Increases formation of a highly stable disulfide-bonded PDIA2 dimer. 1 Publication
Mutagenesisi364 – 3641C → A: No effect on interchain disulfide bridge formation. 1 Publication

Organism-specific databases

PharmGKBiPA33153.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 525504Protein disulfide-isomerase A2
PRO_0000034222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 – 18Interchain1 Publication
Disulfide bondi71 ↔ 74Redox-active By similarity
Glycosylationi127 – 1271N-linked (GlcNAc...)1 Publication
Glycosylationi284 – 2841N-linked (GlcNAc...)1 Publication
Disulfide bondi418 ↔ 421Redox-active By similarity
Glycosylationi516 – 5161N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The disulfide-linked homodimer exhibits an enhanced chaperone activity.
Glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ13087.
PaxDbiQ13087.
PRIDEiQ13087.

PTM databases

PhosphoSiteiQ13087.

Expressioni

Tissue specificityi

Highly expressed in pancreas (at protein level).3 Publications

Gene expression databases

ArrayExpressiQ13087.
BgeeiQ13087.
CleanExiHS_PDIA2.
GenevestigatoriQ13087.

Organism-specific databases

HPAiHPA051692.
HPA053492.

Interactioni

Subunit structurei

Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163333EBI-1752525,EBI-389883

Protein-protein interaction databases

BioGridi122240. 16 interactions.
IntActiQ13087. 10 interactions.
MINTiMINT-1513985.
STRINGi9606.ENSP00000219406.

Structurei

3D structure databases

ProteinModelPortaliQ13087.
SMRiQ13087. Positions 32-495.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 152126Thioredoxin 1
Add
BLAST
Domaini367 – 496130Thioredoxin 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi522 – 5254Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Contains 2 thioredoxin domains.

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
HOVERGENiHBG005920.
InParanoidiQ13087.
KOiK09581.
OMAiQEVPPDW.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ13087.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13087-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH    50
TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV 100
DGPAQRELAE EFGVTEYPTL KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR 150
VGPSAMRLED EAAAQALIGG RDLVVIGFFQ DLQDEDVATF LALAQDALDM 200
TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF 250
LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA 300
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV 350
DGGPVTAASI TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ 400
VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED IIIAELDATA 450
NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLETFSKF LDNGGVLPTE 500
EPPEEPAAPF PEPPANSTMG SKEEL 525
Length:525
Mass (Da):58,206
Last modified:May 27, 2002 - v2
Checksum:iB741851AA2C40540
GO
Isoform 2 (identifier: Q13087-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-183: Missing.

Show »
Length:522
Mass (Da):57,850
Checksum:i815CD5F3060B5747
GO

Sequence cautioni

The sequence AAC50401.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
The sequence AAH75029.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
The sequence BAG58339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391P → S.
Corresponds to variant rs45455191 [ dbSNP | Ensembl ].
VAR_048087
Natural varianti119 – 1191T → R.
Corresponds to variant rs45614840 [ dbSNP | Ensembl ].
VAR_048088
Natural varianti185 – 1851E → K.
Corresponds to variant rs419949 [ dbSNP | Ensembl ].
VAR_048089
Natural varianti286 – 2861T → M.
Corresponds to variant rs2685127 [ dbSNP | Ensembl ].
VAR_048090
Natural varianti382 – 3821P → A.
Corresponds to variant rs45529833 [ dbSNP | Ensembl ].
VAR_048091
Natural varianti388 – 3881R → Q.
Corresponds to variant rs400037 [ dbSNP | Ensembl ].
VAR_048092
Natural varianti502 – 5021P → S.3 Publications
Corresponds to variant rs1048786 [ dbSNP | Ensembl ].
VAR_048093

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei181 – 1833Missing in isoform 2.
VSP_039292

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961T → M in BAG58339. 1 Publication
Sequence conflicti484 – 4841L → Q in BAG58339. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB127078 mRNA. Translation: BAE48734.1.
AE006463 Genomic DNA. Translation: AAK61223.1.
Z69667 Genomic DNA. Translation: CAI95586.1.
Z69667 Genomic DNA. Translation: CAO78188.1.
CH471112 Genomic DNA. Translation: EAW85838.1.
BC000537 mRNA. Translation: AAH00537.2.
BC075029 mRNA. Translation: AAH75029.1. Sequence problems.
U19948 mRNA. Translation: AAC50401.1. Sequence problems.
AK295383 mRNA. Translation: BAG58339.1. Different initiation.
CCDSiCCDS42089.1. [Q13087-1]
RefSeqiNP_006840.2. NM_006849.2. [Q13087-1]
UniGeneiHs.66581.

Genome annotation databases

EnsembliENST00000219406; ENSP00000219406; ENSG00000185615. [Q13087-1]
ENST00000404312; ENSP00000384410; ENSG00000185615. [Q13087-2]
GeneIDi64714.
KEGGihsa:64714.
UCSCiuc002cgn.1. human. [Q13087-1]

Polymorphism databases

DMDMi21264492.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB127078 mRNA. Translation: BAE48734.1 .
AE006463 Genomic DNA. Translation: AAK61223.1 .
Z69667 Genomic DNA. Translation: CAI95586.1 .
Z69667 Genomic DNA. Translation: CAO78188.1 .
CH471112 Genomic DNA. Translation: EAW85838.1 .
BC000537 mRNA. Translation: AAH00537.2 .
BC075029 mRNA. Translation: AAH75029.1 . Sequence problems.
U19948 mRNA. Translation: AAC50401.1 . Sequence problems.
AK295383 mRNA. Translation: BAG58339.1 . Different initiation.
CCDSi CCDS42089.1. [Q13087-1 ]
RefSeqi NP_006840.2. NM_006849.2. [Q13087-1 ]
UniGenei Hs.66581.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei Q13087.

Polymorphism databases

DMDMi 21264492.

Proteomic databases

MaxQBi Q13087.
PaxDbi Q13087.
PRIDEi Q13087.

Protocols and materials databases

DNASUi 64714.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi 5.3.4.1. 2681.

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human polycistronic mRNA composed of ARHGDIG and PDIP."
    Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T., Saito T.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-502.
  2. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525 (ISOFORM 1), VARIANT SER-502.
    Tissue: Brain.
  6. "Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas."
    Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L., Lan M.S.
    DNA Cell Biol. 15:9-16(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-525 (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-502.
    Tissue: Pancreas.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-525 (ISOFORM 1).
    Tissue: Corpus callosum.
  8. "Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp."
    Desilva M.G., Notkins A.L., Lan M.S.
    DNA Cell Biol. 16:269-274(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, GLYCOSYLATION.
  9. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  10. "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond."
    Fu X., Zhu B.T.
    Arch. Biochem. Biophys. 485:1-9(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-18 AND CYS-364.
  11. "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an intracellular estrogen-binding protein that modulates estrogen levels and actions in target cells."
    Fu X.M., Zhu B.T.
    J. Steroid Biochem. Mol. Biol. 115:20-29(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  12. "N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2)."
    Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D.
    FEBS J. 280:233-243(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-127; ASN-284 AND ASN-516, MUTAGENESIS OF ASN-284.

Entry informationi

Entry nameiPDIA2_HUMAN
AccessioniPrimary (citable) accession number: Q13087
Secondary accession number(s): A6ZJ64
, B4DI27, Q2WGM4, Q4TT67, Q6B010, Q96KJ6, Q9BW95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 27, 2002
Last modified: September 3, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi