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Protein

Endoplasmic reticulum resident protein 27

Gene

ERP27

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum resident protein 27
Short name:
ER protein 27
Short name:
ERp27
Gene namesi
Name:ERP27
Synonyms:C12orf46
ORF Names:UNQ781/PRO1575
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:26495. ERP27.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681M → W: Decreases somatostatin-14 binding. 1 Publication
Mutagenesisi196 – 1961I → A, L or W: Decreases somatostatin-14 binding. 1 Publication
Mutagenesisi196 – 1961I → W: Conserved PDIA3 binding in vivo and in vitro. 1 Publication
Mutagenesisi231 – 2311E → K or A: Greatly reduces PDIA3 binding in vivo and in vitro. 1 Publication
Mutagenesisi232 – 2321W → A: Greatly reduces PDIA3 binding in vivo and in vitro. 1 Publication
Mutagenesisi233 – 2331D → G: Greatly reduces PDIA3 binding in vivo and in vitro. 1 Publication

Organism-specific databases

PharmGKBiPA162385401.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 273248Endoplasmic reticulum resident protein 27PRO_0000281118Add
BLAST

Proteomic databases

MaxQBiQ96DN0.
PaxDbiQ96DN0.
PRIDEiQ96DN0.

Expressioni

Gene expression databases

BgeeiQ96DN0.
CleanExiHS_ERP27.
ExpressionAtlasiQ96DN0. baseline and differential.
GenevestigatoriQ96DN0.

Organism-specific databases

HPAiHPA039636.
HPA052851.

Interactioni

Subunit structurei

Interacts with PDIA3. Binds somatostatin-14 via hydrophobic interactions.1 Publication

Protein-protein interaction databases

BioGridi125733. 4 interactions.
IntActiQ96DN0. 1 interaction.
MINTiMINT-2878436.
STRINGi9606.ENSP00000266397.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 549Combined sources
Beta strandi56 – 638Combined sources
Helixi71 – 788Combined sources
Turni79 – 813Combined sources
Beta strandi85 – 906Combined sources
Helixi93 – 986Combined sources
Beta strandi103 – 1108Combined sources
Turni111 – 1144Combined sources
Beta strandi115 – 1195Combined sources
Helixi121 – 1255Combined sources
Helixi129 – 13911Combined sources
Beta strandi143 – 1464Combined sources
Helixi149 – 1579Combined sources
Beta strandi162 – 1687Combined sources
Helixi175 – 18814Combined sources
Turni189 – 1924Combined sources
Beta strandi194 – 1996Combined sources
Helixi203 – 2053Combined sources
Helixi206 – 2116Combined sources
Helixi216 – 2183Combined sources
Beta strandi220 – 22910Combined sources
Beta strandi232 – 2354Combined sources
Helixi242 – 25312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L4CNMR-A26-141[»]
4F9ZX-ray2.20A/B/C/D/E30-256[»]
ProteinModelPortaliQ96DN0.
SMRiQ96DN0. Positions 38-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 152114ThioredoxinAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2334PDIA3-binding site

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi270 – 2734Prevents secretion from ER

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255456.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000112391.
HOVERGENiHBG081481.
InParanoidiQ96DN0.
OMAiEHVQNFC.
OrthoDBiEOG7P2XT5.
PhylomeDBiQ96DN0.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q96DN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAAPSRFMF LLFLLTCELA AEVAAEVEKS SDGPGAAQEP TWLTDVPAAM
60 70 80 90 100
EFIAATEVAV IGFFQDLEIP AVPILHSMVQ KFPGVSFGIS TDSEVLTHYN
110 120 130 140 150
ITGNTICLFR LVDNEQLNLE DEDIESIDAT KLSRFIEINS LHMVTEYNPV
160 170 180 190 200
TVIGLFNSVI QIHLLLIMNK ASPEYEENMH RYQKAAKLFQ GKILFILVDS
210 220 230 240 250
GMKENGKVIS FFKLKESQLP ALAIYQTLDD EWDTLPTAEV SVEHVQNFCD
260 270
GFLSGKLLKE NRESEGKTPK VEL
Length:273
Mass (Da):30,480
Last modified:December 1, 2001 - v1
Checksum:iD47280F6F6FDE419
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521F → L.
Corresponds to variant rs35030722 [ dbSNP | Ensembl ].
VAR_052582

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358536 mRNA. Translation: AAQ88900.1.
AK056677 mRNA. Translation: BAB71251.1.
BC030218 mRNA. Translation: AAH30218.1.
CCDSiCCDS8670.1.
RefSeqiNP_001287713.1. NM_001300784.1.
NP_689534.1. NM_152321.3.
UniGeneiHs.162143.

Genome annotation databases

EnsembliENST00000266397; ENSP00000266397; ENSG00000139055.
GeneIDi121506.
KEGGihsa:121506.
UCSCiuc001rco.3. human.

Polymorphism databases

DMDMi74731474.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358536 mRNA. Translation: AAQ88900.1.
AK056677 mRNA. Translation: BAB71251.1.
BC030218 mRNA. Translation: AAH30218.1.
CCDSiCCDS8670.1.
RefSeqiNP_001287713.1. NM_001300784.1.
NP_689534.1. NM_152321.3.
UniGeneiHs.162143.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L4CNMR-A26-141[»]
4F9ZX-ray2.20A/B/C/D/E30-256[»]
ProteinModelPortaliQ96DN0.
SMRiQ96DN0. Positions 38-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125733. 4 interactions.
IntActiQ96DN0. 1 interaction.
MINTiMINT-2878436.
STRINGi9606.ENSP00000266397.

Polymorphism databases

DMDMi74731474.

Proteomic databases

MaxQBiQ96DN0.
PaxDbiQ96DN0.
PRIDEiQ96DN0.

Protocols and materials databases

DNASUi121506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266397; ENSP00000266397; ENSG00000139055.
GeneIDi121506.
KEGGihsa:121506.
UCSCiuc001rco.3. human.

Organism-specific databases

CTDi121506.
GeneCardsiGC12M015066.
HGNCiHGNC:26495. ERP27.
HPAiHPA039636.
HPA052851.
MIMi610642. gene.
neXtProtiNX_Q96DN0.
PharmGKBiPA162385401.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255456.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000112391.
HOVERGENiHBG081481.
InParanoidiQ96DN0.
OMAiEHVQNFC.
OrthoDBiEOG7P2XT5.
PhylomeDBiQ96DN0.
TreeFamiTF106381.

Enzyme and pathway databases

BRENDAi5.3.4.1. 2681.

Miscellaneous databases

ChiTaRSiERP27. human.
GenomeRNAii121506.
NextBioi80755.
PROiQ96DN0.
SOURCEiSearch...

Gene expression databases

BgeeiQ96DN0.
CleanExiHS_ERP27.
ExpressionAtlasiQ96DN0. baseline and differential.
GenevestigatoriQ96DN0.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiERP27_HUMAN
AccessioniPrimary (citable) accession number: Q96DN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 1, 2001
Last modified: March 4, 2015
This is version 105 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.