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Q9HG01 (GRP78_PICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
78 kDa glucose-regulated protein homolog

Short name=GRP-78
Alternative name(s):
Immunoglobulin heavy chain-binding protein homolog
Short name=BiP
Gene names
Name:BiP
OrganismPichia angusta (Yeast) (Hansenula polymorpha)
Taxonomic identifier870730 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetales incertae sedisOgataea

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandATP-binding
Nucleotide-binding
Gene Ontology (GO)
   Biological_processresponse to unfolded protein

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 66563278 kDa glucose-regulated protein homolog
PRO_0000013584

Regions

Motif662 – 6654Prevents secretion from ER Potential

Sequences

Sequence LengthMass (Da)Tools
Q9HG01 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9A23F7BCCC0364B7

FASTA66573,222
        10         20         30         40         50         60 
MLTFNKSVVS CAAIIYALLL VVLPLTTQQF VKAESNENYG TVIGIDLGTT YSCVGVMKAG 

        70         80         90        100        110        120 
RVEIIPNDQG NRITPSYVAF TEDERLVGDA AKNQIASNPT NTIFDIKRLI GHRFDDKVIQ 

       130        140        150        160        170        180 
KEIKHLPYKV KDQDGRPVVE AKVNGELKTF TAEEISAMIL GKMKQIAEDY LGKKVTHAVV 

       190        200        210        220        230        240 
TVPAYFNDAQ RQATKDAGTI AGLEVLRIVN EPTAAAIAYG LDKTDEEKHI IVYDLGGGTF 

       250        260        270        280        290        300 
DVSLLTIAGG AFEVLATAGD THLGGEDFDY RVVRHFIKVF KKKHGIDISD NSKALAKLKR 

       310        320        330        340        350        360 
EVEKAKRTLS SQMSTRIEID SFVDGIDFSE SLSRAKFEEL NMDLFKKTLK PVQQVLDDAK 

       370        380        390        400        410        420 
MKPDEIDDVV FVGGSTRIPK VQELIENFFN GKKISKGINP DEAVAFGAAV QGGVLSGEEG 

       430        440        450        460        470        480 
VEDIVLIDVN PLTLGIETSG GVMTTLIKRN TPIPTQKSQI FSTAADNQPV VLIQVYEGER 

       490        500        510        520        530        540 
AMAKDNNLLG KFELTGIPPA PRGVPQIEVT FTLDSNGILK VSATDKGTGK SNSITITNDK 

       550        560        570        580        590        600 
GRLSKEEIEK KIEEAEKFAQ QDKELREKVE SRNALENYAH SLKNQANDEN GFGAKLEEDD 

       610        620        630        640        650        660 
KETLLDAINE ALEFLEDNFD TATKDEFDEQ KEKLSKVAYP ITSKLYDAPP TSDEEDEDDW 


DHDEL 

« Hide

References

[1]"Overproduction of BiP negatively affects the secretion of Aspergillus niger glucose oxidase by the yeast Hansenula polymorpha."
van der Heide M., Hollenberg C.P., van der Klei I.J., Veenhuis M.
Appl. Microbiol. Biotechnol. 58:487-494(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL Y-1798 / VKM Y-1397.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF245405 Genomic DNA. Translation: AAG09776.1.

3D structure databases

ProteinModelPortalQ9HG01.
SMRQ9HG01. Positions 40-579.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9HG01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGRP78_PICAN
AccessionPrimary (citable) accession number: Q9HG01
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families