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Q96DN0 (ERP27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmic reticulum resident protein 27

Short name=ER protein 27
Short name=ERp27
Gene names
Name:ERP27
Synonyms:C12orf46
ORF Names:UNQ781/PRO1575
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Interacts with PDIA3. Binds somatostatin-14 via hydrophobic interactions. Ref.4

Subcellular location

Endoplasmic reticulum lumen Ref.4.

Miscellaneous

Does not contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainSignal
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 273248Endoplasmic reticulum resident protein 27
PRO_0000281118

Regions

Domain39 – 152114Thioredoxin
Region230 – 2334PDIA3-binding site
Motif270 – 2734Prevents secretion from ER

Natural variations

Natural variant521F → L.
Corresponds to variant rs35030722 [ dbSNP | Ensembl ].
VAR_052582

Experimental info

Mutagenesis1681M → W: Decreases somatostatin-14 binding. Ref.4
Mutagenesis1961I → A, L or W: Decreases somatostatin-14 binding. Ref.4
Mutagenesis1961I → W: Conserved PDIA3 binding in vivo and in vitro. Ref.4
Mutagenesis2311E → K or A: Greatly reduces PDIA3 binding in vivo and in vitro. Ref.4
Mutagenesis2321W → A: Greatly reduces PDIA3 binding in vivo and in vitro. Ref.4
Mutagenesis2331D → G: Greatly reduces PDIA3 binding in vivo and in vitro. Ref.4

Secondary structure

.......................................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96DN0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D47280F6F6FDE419

FASTA27330,480
        10         20         30         40         50         60 
MEAAPSRFMF LLFLLTCELA AEVAAEVEKS SDGPGAAQEP TWLTDVPAAM EFIAATEVAV 

        70         80         90        100        110        120 
IGFFQDLEIP AVPILHSMVQ KFPGVSFGIS TDSEVLTHYN ITGNTICLFR LVDNEQLNLE 

       130        140        150        160        170        180 
DEDIESIDAT KLSRFIEINS LHMVTEYNPV TVIGLFNSVI QIHLLLIMNK ASPEYEENMH 

       190        200        210        220        230        240 
RYQKAAKLFQ GKILFILVDS GMKENGKVIS FFKLKESQLP ALAIYQTLDD EWDTLPTAEV 

       250        260        270 
SVEHVQNFCD GFLSGKLLKE NRESEGKTPK VEL 

« Hide

References

« Hide 'large scale' references
[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. expand/collapse author list , 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].
Tissue: Pancreas.
[3]"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.
[4]"ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57."
Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E.H., Kauppila A., Kellokumpu S., Ruddock L.W.
J. Biol. Chem. 281:33727-33738(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION, INTERACTION WITH PDIA3, MUTAGENESIS OF MET-168; ILE-196; GLU-231; TRP-232 AND ASP-233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY358536 mRNA. Translation: AAQ88900.1.
AK056677 mRNA. Translation: BAB71251.1.
BC030218 mRNA. Translation: AAH30218.1.
RefSeqNP_689534.1. NM_152321.2.
UniGeneHs.162143.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L4CNMR-A26-141[»]
4F9ZX-ray2.20A/B/C/D/E30-256[»]
ProteinModelPortalQ96DN0.
SMRQ96DN0. Positions 38-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125733. 1 interaction.
IntActQ96DN0. 1 interaction.
MINTMINT-2878436.
STRING9606.ENSP00000266397.

Polymorphism databases

DMDM74731474.

Proteomic databases

PaxDbQ96DN0.
PRIDEQ96DN0.

Protocols and materials databases

DNASU121506.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266397; ENSP00000266397; ENSG00000139055.
GeneID121506.
KEGGhsa:121506.
UCSCuc001rco.3. human.

Organism-specific databases

CTD121506.
GeneCardsGC12M015066.
HGNCHGNC:26495. ERP27.
HPAHPA039636.
MIM610642. gene.
neXtProtNX_Q96DN0.
PharmGKBPA162385401.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255456.
HOGENOMHOG000112391.
HOVERGENHBG081481.
InParanoidQ96DN0.
OMAEHVQNFC.
OrthoDBEOG7P2XT5.
PhylomeDBQ96DN0.
TreeFamTF106381.

Enzyme and pathway databases

BRENDA5.3.4.1. 2681.

Gene expression databases

ArrayExpressQ96DN0.
BgeeQ96DN0.
CleanExHS_ERP27.
GenevestigatorQ96DN0.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMSSF52833. SSF52833. 2 hits.
ProtoNetSearch...

Other

ChiTaRSERP27. human.
GenomeRNAi121506.
NextBio80755.
PROQ96DN0.
SOURCESearch...

Entry information

Entry nameERP27_HUMAN
AccessionPrimary (citable) accession number: Q96DN0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM