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P13667

- PDIA4_HUMAN

UniProt

P13667 - PDIA4_HUMAN

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Protein

Protein disulfide-isomerase A4

Gene

PDIA4

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

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein disulfide isomerase activity Source: UniProt

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. chaperone-mediated protein folding Source: UniProt
  3. protein folding Source: RefGenome
  4. protein secretion Source: ProtInc
  5. response to endoplasmic reticulum stress Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A4 (EC:5.3.4.1)
Alternative name(s):
Endoplasmic reticulum resident protein 70
Short name:
ER protein 70
Short name:
ERp70
Endoplasmic reticulum resident protein 72
Short name:
ER protein 72
Short name:
ERp-72
Short name:
ERp72
Gene namesi
Name:PDIA4
Synonyms:ERP70, ERP72
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:30167. PDIA4.

Subcellular locationi

Endoplasmic reticulum lumen. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: RefGenome
  3. endoplasmic reticulum lumen Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 645625Protein disulfide-isomerase A4PRO_0000034229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 94Redox-activePROSITE-ProRule annotation
Disulfide bondi206 ↔ 209Redox-activePROSITE-ProRule annotation
Modified residuei366 – 3661N6-acetyllysine1 Publication
Disulfide bondi555 ↔ 558Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP13667.
PaxDbiP13667.
PeptideAtlasiP13667.
PRIDEiP13667.

2D gel databases

OGPiP13667.
REPRODUCTION-2DPAGEIPI00009904.

PTM databases

PhosphoSiteiP13667.

Expressioni

Gene expression databases

BgeeiP13667.
CleanExiHS_PDIA4.
ExpressionAtlasiP13667. baseline and differential.
GenevestigatoriP13667.

Organism-specific databases

HPAiCAB017368.
HPA006139.
HPA006140.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
Q763533EBI-1054653,EBI-6248077From a different organism.
PPIBP232843EBI-1054653,EBI-8771982

Protein-protein interaction databases

BioGridi114966. 53 interactions.
IntActiP13667. 17 interactions.
MINTiMINT-4999858.
STRINGi9606.ENSP00000286091.

Structurei

Secondary structure

1
645
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 613
Beta strandi64 – 663
Turni69 – 713
Helixi72 – 765
Beta strandi80 – 878
Helixi92 – 10918
Beta strandi111 – 1133
Beta strandi117 – 1215
Turni122 – 1243
Helixi126 – 1316
Beta strandi136 – 1449
Beta strandi147 – 1504
Helixi157 – 16812
Beta strandi178 – 1814
Turni184 – 1863
Helixi187 – 1937
Beta strandi195 – 2028
Helixi208 – 2114
Helixi213 – 22412
Beta strandi226 – 2283
Beta strandi232 – 2365
Turni237 – 2393
Helixi241 – 2466
Beta strandi251 – 2599
Beta strandi262 – 2654
Helixi272 – 28211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDVX-ray1.95A53-284[»]
ProteinModelPortaliP13667.
SMRiP13667. Positions 54-645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13667.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 169149Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 301144Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini505 – 636132Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi642 – 6454Prevents secretion from ER

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 5517Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 3 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000162459.
HOVERGENiHBG005920.
InParanoidiP13667.
KOiK09582.
OMAiIIGVFKG.
OrthoDBiEOG7VHSX1.
PhylomeDBiP13667.
TreeFamiTF106382.

Family and domain databases

Gene3Di3.40.30.10. 4 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMiSSF52833. SSF52833. 5 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13667 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD
60 70 80 90 100
EEEDDLEVKE ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE
110 120 130 140 150
YEKIANILKD KDPPIPVAKI DATSASVLAS RFDVSGYPTI KILKKGQAVD
160 170 180 190 200
YEGSRTQEEI VAKVREVSQP DWTPPPEVTL VLTKENFDEV VNDADIILVE
210 220 230 240 250
FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE TDLAKRFDVS
260 270 280 290 300
GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
310 320 330 340 350
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV
360 370 380 390 400
SQGQLVVMQP EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR
410 420 430 440 450
KVSNDAKRYT RRPLVVVYYS VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF
460 470 480 490 500
AIADEEDYAG EVKDLGLSES GEDVNAAILD ESGKKFAMEP EEFDSDTLRE
510 520 530 540 550
FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM DPKKDVLIEF
560 570 580 590 600
YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
610 620 630 640
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL
Length:645
Mass (Da):72,932
Last modified:May 1, 1991 - v2
Checksum:i1919C2AE12CD2684
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021E → G in BAF83660. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731T → M.
Corresponds to variant rs2290971 [ dbSNP | Ensembl ].
VAR_052580

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05016 mRNA. Translation: AAA58460.1.
AK290971 mRNA. Translation: BAF83660.1.
AC093743 Genomic DNA. Translation: AAQ96863.1.
CH471146 Genomic DNA. Translation: EAW80065.1.
CH471146 Genomic DNA. Translation: EAW80066.1.
BC000425 mRNA. Translation: AAH00425.1.
BC001928 mRNA. Translation: AAH01928.1.
BC006344 mRNA. Translation: AAH06344.1.
BC011754 mRNA. Translation: AAH11754.1.
CCDSiCCDS5893.1.
PIRiA23723.
RefSeqiNP_004902.1. NM_004911.4.
UniGeneiHs.93659.

Genome annotation databases

EnsembliENST00000286091; ENSP00000286091; ENSG00000155660.
GeneIDi9601.
KEGGihsa:9601.
UCSCiuc003wff.2. human.

Polymorphism databases

DMDMi119530.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05016 mRNA. Translation: AAA58460.1 .
AK290971 mRNA. Translation: BAF83660.1 .
AC093743 Genomic DNA. Translation: AAQ96863.1 .
CH471146 Genomic DNA. Translation: EAW80065.1 .
CH471146 Genomic DNA. Translation: EAW80066.1 .
BC000425 mRNA. Translation: AAH00425.1 .
BC001928 mRNA. Translation: AAH01928.1 .
BC006344 mRNA. Translation: AAH06344.1 .
BC011754 mRNA. Translation: AAH11754.1 .
CCDSi CCDS5893.1.
PIRi A23723.
RefSeqi NP_004902.1. NM_004911.4.
UniGenei Hs.93659.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IDV X-ray 1.95 A 53-284 [» ]
ProteinModelPortali P13667.
SMRi P13667. Positions 54-645.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114966. 53 interactions.
IntActi P13667. 17 interactions.
MINTi MINT-4999858.
STRINGi 9606.ENSP00000286091.

PTM databases

PhosphoSitei P13667.

Polymorphism databases

DMDMi 119530.

2D gel databases

OGPi P13667.
REPRODUCTION-2DPAGE IPI00009904.

Proteomic databases

MaxQBi P13667.
PaxDbi P13667.
PeptideAtlasi P13667.
PRIDEi P13667.

Protocols and materials databases

DNASUi 9601.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286091 ; ENSP00000286091 ; ENSG00000155660 .
GeneIDi 9601.
KEGGi hsa:9601.
UCSCi uc003wff.2. human.

Organism-specific databases

CTDi 9601.
GeneCardsi GC07M148700.
HGNCi HGNC:30167. PDIA4.
HPAi CAB017368.
HPA006139.
HPA006140.
neXtProti NX_P13667.
PharmGKBi PA142671190.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00760000119201.
HOGENOMi HOG000162459.
HOVERGENi HBG005920.
InParanoidi P13667.
KOi K09582.
OMAi IIGVFKG.
OrthoDBi EOG7VHSX1.
PhylomeDBi P13667.
TreeFami TF106382.

Enzyme and pathway databases

BRENDAi 5.3.4.1. 2681.

Miscellaneous databases

ChiTaRSi PDIA4. human.
EvolutionaryTracei P13667.
GenomeRNAii 9601.
NextBioi 36019.
PROi P13667.

Gene expression databases

Bgeei P13667.
CleanExi HS_PDIA4.
ExpressionAtlasi P13667. baseline and differential.
Genevestigatori P13667.

Family and domain databases

Gene3Di 3.40.30.10. 4 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 3 hits.
[Graphical view ]
PIRSFi PIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMi SSF52833. SSF52833. 5 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of expression in cell lines with and without enzyme activity."
    Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
    J. Biol. Chem. 264:14762-14768(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. Erratum
    Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
    J. Biol. Chem. 266:5353-5353(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "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].
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Lung and Muscle.
  7. "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.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDIA4_HUMAN
AccessioniPrimary (citable) accession number: P13667
Secondary accession number(s): A8K4K6, Q549T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 1991
Last modified: October 29, 2014
This is version 167 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

Caution

Was originally thought to be a deoxycytidine kinase.1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3