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P08110

- ENPL_CHICK

UniProt

P08110 - ENPL_CHICK

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Protein
Endoplasmin
Gene
HSP90B1, TRA1
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Molecular chaperone that functions in the processing and transport of secreted proteins. Has ATPase activity By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061ATP By similarity
Binding sitei148 – 1481ATP By similarity
Binding sitei161 – 1611ATP By similarity
Binding sitei167 – 1671ATP By similarity
Binding sitei198 – 1981ATP; via amide nitrogen By similarity
Binding sitei447 – 4471ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
  2. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmin
Alternative name(s):
Heat shock 108 kDa protein
Short name:
HSP 108
Short name:
HSP108
Heat shock protein 90 kDa beta member 1
Transferrin-binding protein
Gene namesi
Name:HSP90B1
Synonyms:TRA1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: AgBase
  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 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 795774EndoplasminUniRule annotation
PRO_0000013601Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi106 – 1061N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi137 – 137Interchain By similarity
Glycosylationi216 – 2161N-linked (GlcNAc...)1 Publication
Glycosylationi444 – 4441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi480 – 4801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi501 – 5011N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08110.
PRIDEiP08110.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

BioGridi675192. 1 interaction.
IntActiP08110. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP08110.
SMRiP08110. Positions 68-754.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi792 – 7954Prevents secretion from ERUniRule annotation

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0326.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP08110.
KOiK09487.
PhylomeDBiP08110.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08110-1 [UniParc]FASTAAdd to Basket

« Hide

MKSAWALALA CTLLLAASVT AEEVDVDATV EEDLGKSREG SRTDDEVVQR    50
EEEAIQLDGL NASQIKEIRE KSEKFAFQAE VNRMMKLIIN SLYKNKEIFL 100
RELISNASDA LDKIRLISLT DENALAGNEE LTVKIKCDKE KNMLHVTDTG 150
IGMTKEELIK NLGTIAKSGT SEFLNKMTEM QDDSQSTSEL IGQFGVGFYS 200
AFLVADRVIV TSKHNNDTQH IWESDSNEFS VIDDPRGNTL GRGTTITLVL 250
KEEASDYLEL DTVKNLVKKY SQFINFPIYV WSSKTETVEE PVEEEEAKEE 300
KEETDDNEAA VEEEEEEKKP KTKKVEKTVW DWELMNDIKP IWQRPSKEVE 350
EDEYKAFYKT FSKEHDDPMA YIHFTAEGEV TFKSILFVPN SAPRGLFDEY 400
GSKKSDFIKL YVRRVFITDD FHDMMPKYLN FVKGVVDSDD LPLNVSRETL 450
QQHKLLKVIR KKLVRKTLDM IKKIAEEKYN DTFWKEFGTN VKLGVIEDHS 500
NRTRLAKLLR FQSSHHESNL TSLDQYVERM KEKQDKIYFM AGASRKEAES 550
SPFVERLLKK GYEVIYLTEP VDEYCIQALP EFDGKRFQNV AKEGVKFEES 600
EKSKESREAL EKEFEPLLNW MKDKALKDKI EKAVLSQRLT QSPCALVASQ 650
YGWSGNMERI MKAQAYQTGK DISTNYYASQ KKTFEINPRH PLIKDMLRRV 700
KENEDDKTVS DLAVVLFETA TLRSGYMLPD TKEYGDRIER MLRLSLNIDL 750
DAKVEEEPEE PEDAAEEAEQ DEEEVDADAE DSETQKESTD VKDEL 795
Length:795
Mass (Da):91,555
Last modified:August 1, 1988 - v1
Checksum:iBE1B29E1DBEC5A9A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061D → E in AAA48827. 1 Publication
Sequence conflicti206 – 2061D → E in CAA28629. 1 Publication
Sequence conflicti267 – 2671V → L in AAA48827. 1 Publication
Sequence conflicti303 – 3031E → Q in AAA48827. 1 Publication
Sequence conflicti307 – 3071N → D in AAA48827. 1 Publication
Sequence conflicti307 – 3071N → D in CAA28629. 1 Publication
Sequence conflicti317 – 3171E → H in AAA48827. 1 Publication
Sequence conflicti378 – 3781G → A in AAA48827. 1 Publication
Sequence conflicti593 – 5942EG → DR in AAA48827. 1 Publication
Sequence conflicti653 – 6531W → C in AAA48827. 1 Publication
Sequence conflicti669 – 6757GKDISTN → VFSS in CAA28629. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14772 mRNA. Translation: AAA48826.1.
M31321 Genomic DNA. Translation: AAA48827.1.
X04961 Genomic DNA. Translation: CAA28629.1.
PIRiA24461. HHCH08.
I50255.
RefSeqiNP_989620.1. NM_204289.1.
UniGeneiGga.4724.

Genome annotation databases

GeneIDi374163.
KEGGigga:374163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14772 mRNA. Translation: AAA48826.1 .
M31321 Genomic DNA. Translation: AAA48827.1 .
X04961 Genomic DNA. Translation: CAA28629.1 .
PIRi A24461. HHCH08.
I50255.
RefSeqi NP_989620.1. NM_204289.1.
UniGenei Gga.4724.

3D structure databases

ProteinModelPortali P08110.
SMRi P08110. Positions 68-754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 675192. 1 interaction.
IntActi P08110. 1 interaction.

Proteomic databases

PaxDbi P08110.
PRIDEi P08110.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 374163.
KEGGi gga:374163.

Organism-specific databases

CTDi 7184.

Phylogenomic databases

eggNOGi COG0326.
HOGENOMi HOG000031988.
HOVERGENi HBG007374.
InParanoidi P08110.
KOi K09487.
PhylomeDBi P08110.

Miscellaneous databases

NextBioi 20813673.
PROi P08110.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Amino acid sequence of a chicken heat shock protein derived from the complementary DNA nucleotide sequence."
    Kulomaa M.S., Weigel N.L., Kleinsek D.A., Beattie W.G., Conneely O.M., March C., Zarucki-Schulz T., Schrader W.T., O'Malley B.W.
    Biochemistry 25:6244-6251(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of a steroid-regulated 108K heat shock protein gene from hen oviduct."
    Kleinsek D.A., Beattie W.G., Tsai M.J., O'Malley B.W.
    Nucleic Acids Res. 14:10053-10069(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Oviduct.
  3. Forsgren M.
    Submitted (SEP-1987) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Oviduct.
  4. "A chicken transferrin binding protein is heat shock protein 108."
    Hayes G.R., Himpler B.S., Weiner K.X.B., Lucas J.J.
    Biochem. Biophys. Res. Commun. 200:65-70(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-216.

Entry informationi

Entry nameiENPL_CHICK
AccessioniPrimary (citable) accession number: P08110
Secondary accession number(s): Q90869, Q90870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 11, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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