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Q9D8U3

- ERP27_MOUSE

UniProt

Q9D8U3 - ERP27_MOUSE

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Protein

Endoplasmic reticulum resident protein 27

Gene
Erp27
Organism
Mus musculus (Mouse)
Status
Reviewed - 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: Chromosome 6

Organism-specific databases

MGIiMGI:1916437. Erp27.

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9D8U3.
PaxDbiQ9D8U3.
PRIDEiQ9D8U3.

Expressioni

Gene expression databases

BgeeiQ9D8U3.
CleanExiMM_ERP27.
GenevestigatoriQ9D8U3.

Interactioni

Subunit structurei

Interacts with PDIA3 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9D8U3.
SMRiQ9D8U3. Positions 38-255.

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 By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi269 – 2724Prevents secretion from ER By similarity

Sequence similaritiesi

Contains 1 thioredoxin domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255456.
GeneTreeiENSGT00740000115202.
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

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MKITRSRCLI LSFVLVCGLV PEVTADVEEA TDGLSTTQEP IWLTDVPATV    50
ELIAAAEVAV IGFFQDLEIP IVSVFRSMAR QFQDVSFGIS NHSEVLTHYN 100
VTSNSICLFR LVDDQQLHLN AEDIENLDAA KLSRFIHVNN LHWVTEYSPM 150
IAAGLFNTMV QTHLLLMMKK TSPEYEESMR RYREAAKLFQ GQILFVLVDS 200
GKRENGKVMS YFKLKESQLP ALAIYESVDD KWDTLPIAEV TVEKVRGFCE 250
GFLKGLLQRD HEAEGDSGKE EL 272
Length:272
Mass (Da):30,693
Last modified:June 1, 2001 - v1
Checksum:iB4BC442A4C54E60C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041N → S in AAI04407. 1 Publication
Sequence conflicti104 – 1041N → S in AAI04408. 1 Publication
Sequence conflicti138 – 1381V → M in AAI04407. 1 Publication
Sequence conflicti138 – 1381V → M in AAI04408. 1 Publication
Sequence conflicti261 – 2611H → L in AAI04407. 1 Publication
Sequence conflicti261 – 2611H → L in AAI04408. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK007684 mRNA. Translation: BAB25188.1 .
AK131830 mRNA. Translation: BAE20822.1 .
BC104406 mRNA. Translation: AAI04407.1 .
BC104407 mRNA. Translation: AAI04408.1 .
CCDSi CCDS20660.1.
RefSeqi NP_081259.1. NM_026983.2.
UniGenei Mm.33692.

3D structure databases

ProteinModelPortali Q9D8U3.
SMRi Q9D8U3. Positions 38-255.
ModBasei Search...
MobiDBi Search...

Proteomic databases

MaxQBi Q9D8U3.
PaxDbi Q9D8U3.
PRIDEi Q9D8U3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032343 ; ENSMUSP00000032343 ; ENSMUSG00000030219 .
GeneIDi 69187.
KEGGi mmu:69187.
UCSCi uc009emm.1. mouse.

Organism-specific databases

CTDi 121506.
MGIi MGI:1916437. Erp27.

Phylogenomic databases

eggNOGi NOG255456.
GeneTreei ENSGT00740000115202.
HOGENOMi HOG000112391.
HOVERGENi HBG081481.
InParanoidi Q9D8U3.
OMAi EHVQNFC.
OrthoDBi EOG7P2XT5.
PhylomeDBi Q9D8U3.
TreeFami TF106381.

Miscellaneous databases

ChiTaRSi ERP27. mouse.
NextBioi 328798.
PROi Q9D8U3.
SOURCEi Search...

Gene expression databases

Bgeei Q9D8U3.
CleanExi MM_ERP27.
Genevestigatori Q9D8U3.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR012336. Thioredoxin-like_fold.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 100 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

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