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Protein

Endoplasmic reticulum resident protein 27

Gene

Erp27

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum resident protein 27
Short name:
ER protein 27
Short name:
ERp27
Gene namesi
Name:Erp27
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1916437. Erp27.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 272247Endoplasmic reticulum resident protein 27PRO_0000281119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9D8U3.
PaxDbiQ9D8U3.
PRIDEiQ9D8U3.

Expressioni

Gene expression databases

BgeeiQ9D8U3.
CleanExiMM_ERP27.
GenevisibleiQ9D8U3. MM.

Interactioni

Subunit structurei

Interacts with PDIA3.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032343.

Structurei

3D structure databases

ProteinModelPortaliQ9D8U3.
SMRiQ9D8U3. Positions 38-255.
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 siteBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi269 – 2724Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255456.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000112391.
HOVERGENiHBG081481.
InParanoidiQ9D8U3.
OMAiEHVQNFC.
OrthoDBiEOG7P2XT5.
PhylomeDBiQ9D8U3.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9D8U3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKITRSRCLI LSFVLVCGLV PEVTADVEEA TDGLSTTQEP IWLTDVPATV
60 70 80 90 100
ELIAAAEVAV IGFFQDLEIP IVSVFRSMAR QFQDVSFGIS NHSEVLTHYN
110 120 130 140 150
VTSNSICLFR LVDDQQLHLN AEDIENLDAA KLSRFIHVNN LHWVTEYSPM
160 170 180 190 200
IAAGLFNTMV QTHLLLMMKK TSPEYEESMR RYREAAKLFQ GQILFVLVDS
210 220 230 240 250
GKRENGKVMS YFKLKESQLP ALAIYESVDD KWDTLPIAEV TVEKVRGFCE
260 270
GFLKGLLQRD HEAEGDSGKE EL
Length:272
Mass (Da):30,693
Last modified:June 1, 2001 - v1
Checksum:iB4BC442A4C54E60C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041N → S in AAI04407 (PubMed:15489334).Curated
Sequence conflicti104 – 1041N → S in AAI04408 (PubMed:15489334).Curated
Sequence conflicti138 – 1381V → M in AAI04407 (PubMed:15489334).Curated
Sequence conflicti138 – 1381V → M in AAI04408 (PubMed:15489334).Curated
Sequence conflicti261 – 2611H → L in AAI04407 (PubMed:15489334).Curated
Sequence conflicti261 – 2611H → L in AAI04408 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007684 mRNA. Translation: BAB25188.1.
AK131830 mRNA. Translation: BAE20822.1.
BC104406 mRNA. Translation: AAI04407.1.
BC104407 mRNA. Translation: AAI04408.1.
CCDSiCCDS20660.1.
RefSeqiNP_081259.1. NM_026983.2.
UniGeneiMm.33692.

Genome annotation databases

EnsembliENSMUST00000032343; ENSMUSP00000032343; ENSMUSG00000030219.
GeneIDi69187.
KEGGimmu:69187.
UCSCiuc009emm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007684 mRNA. Translation: BAB25188.1.
AK131830 mRNA. Translation: BAE20822.1.
BC104406 mRNA. Translation: AAI04407.1.
BC104407 mRNA. Translation: AAI04408.1.
CCDSiCCDS20660.1.
RefSeqiNP_081259.1. NM_026983.2.
UniGeneiMm.33692.

3D structure databases

ProteinModelPortaliQ9D8U3.
SMRiQ9D8U3. Positions 38-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032343.

Proteomic databases

MaxQBiQ9D8U3.
PaxDbiQ9D8U3.
PRIDEiQ9D8U3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032343; ENSMUSP00000032343; ENSMUSG00000030219.
GeneIDi69187.
KEGGimmu:69187.
UCSCiuc009emm.1. mouse.

Organism-specific databases

CTDi121506.
MGIiMGI:1916437. Erp27.

Phylogenomic databases

eggNOGiNOG255456.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000112391.
HOVERGENiHBG081481.
InParanoidiQ9D8U3.
OMAiEHVQNFC.
OrthoDBiEOG7P2XT5.
PhylomeDBiQ9D8U3.
TreeFamiTF106381.

Miscellaneous databases

ChiTaRSiErp27. mouse.
NextBioi328798.
PROiQ9D8U3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8U3.
CleanExiMM_ERP27.
GenevisibleiQ9D8U3. MM.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  2. "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].

Entry informationi

Entry nameiERP27_MOUSE
AccessioniPrimary (citable) accession number: Q9D8U3
Secondary accession number(s): Q3SX97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.