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P08110

- ENPL_CHICK

UniProt

P08110 - ENPL_CHICK

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Protein

Endoplasmin

Gene

HSP90B1

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061ATPBy similarity
Binding sitei148 – 1481ATPBy similarity
Binding sitei161 – 1611ATPBy similarity
Binding sitei167 – 1671ATPBy similarity
Binding sitei198 – 1981ATP; via amide nitrogenBy similarity
Binding sitei447 – 4471ATPBy 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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 795774EndoplasminPRO_0000013601Add
BLAST

Amino acid modifications

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

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

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_C.
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

        10         20         30         40         50
MKSAWALALA CTLLLAASVT AEEVDVDATV EEDLGKSREG SRTDDEVVQR
60 70 80 90 100
EEEAIQLDGL NASQIKEIRE KSEKFAFQAE VNRMMKLIIN SLYKNKEIFL
110 120 130 140 150
RELISNASDA LDKIRLISLT DENALAGNEE LTVKIKCDKE KNMLHVTDTG
160 170 180 190 200
IGMTKEELIK NLGTIAKSGT SEFLNKMTEM QDDSQSTSEL IGQFGVGFYS
210 220 230 240 250
AFLVADRVIV TSKHNNDTQH IWESDSNEFS VIDDPRGNTL GRGTTITLVL
260 270 280 290 300
KEEASDYLEL DTVKNLVKKY SQFINFPIYV WSSKTETVEE PVEEEEAKEE
310 320 330 340 350
KEETDDNEAA VEEEEEEKKP KTKKVEKTVW DWELMNDIKP IWQRPSKEVE
360 370 380 390 400
EDEYKAFYKT FSKEHDDPMA YIHFTAEGEV TFKSILFVPN SAPRGLFDEY
410 420 430 440 450
GSKKSDFIKL YVRRVFITDD FHDMMPKYLN FVKGVVDSDD LPLNVSRETL
460 470 480 490 500
QQHKLLKVIR KKLVRKTLDM IKKIAEEKYN DTFWKEFGTN VKLGVIEDHS
510 520 530 540 550
NRTRLAKLLR FQSSHHESNL TSLDQYVERM KEKQDKIYFM AGASRKEAES
560 570 580 590 600
SPFVERLLKK GYEVIYLTEP VDEYCIQALP EFDGKRFQNV AKEGVKFEES
610 620 630 640 650
EKSKESREAL EKEFEPLLNW MKDKALKDKI EKAVLSQRLT QSPCALVASQ
660 670 680 690 700
YGWSGNMERI MKAQAYQTGK DISTNYYASQ KKTFEINPRH PLIKDMLRRV
710 720 730 740 750
KENEDDKTVS DLAVVLFETA TLRSGYMLPD TKEYGDRIER MLRLSLNIDL
760 770 780 790
DAKVEEEPEE PEDAAEEAEQ DEEEVDADAE DSETQKESTD VKDEL
Length:795
Mass (Da):91,555
Last modified:August 1, 1988 - v1
Checksum:iBE1B29E1DBEC5A9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061D → E in AAA48827. (PubMed:3027654)Curated
Sequence conflicti206 – 2061D → E in CAA28629. 1 PublicationCurated
Sequence conflicti267 – 2671V → L in AAA48827. (PubMed:3027654)Curated
Sequence conflicti303 – 3031E → Q in AAA48827. (PubMed:3027654)Curated
Sequence conflicti307 – 3071N → D in AAA48827. (PubMed:3027654)Curated
Sequence conflicti307 – 3071N → D in CAA28629. 1 PublicationCurated
Sequence conflicti317 – 3171E → H in AAA48827. (PubMed:3027654)Curated
Sequence conflicti378 – 3781G → A in AAA48827. (PubMed:3027654)Curated
Sequence conflicti593 – 5942EG → DR in AAA48827. (PubMed:3027654)Curated
Sequence conflicti653 – 6531W → C in AAA48827. (PubMed:3027654)Curated
Sequence conflicti669 – 6757GKDISTN → VFSS in CAA28629. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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_C.
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: November 26, 2014
This is version 126 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