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P29844

- HSP7C_DROME

UniProt

P29844 - HSP7C_DROME

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Protein
Heat shock 70 kDa protein cognate 3
Gene
Hsc70-3, Hsc3, CG4147
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. RNA interference Source: FlyBase
  2. centrosome duplication Source: FlyBase
  3. sleep Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_93794. ATF6-alpha activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein cognate 3
Alternative name(s):
78 kDa glucose-regulated protein homolog
GRP 78
Heat shock protein cognate 72
Gene namesi
Name:Hsc70-3
Synonyms:Hsc3
ORF Names:CG4147
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0001218. Hsc70-3.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: FlyBase
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. extracellular space Source: FlyBase
  4. lipid particle Source: FlyBase
  5. microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 656638Heat shock 70 kDa protein cognate 3
PRO_0000013546Add
BLAST

Proteomic databases

PaxDbiP29844.
PRIDEiP29844.

Expressioni

Gene expression databases

BgeeiP29844.

Interactioni

Protein-protein interaction databases

BioGridi58539. 17 interactions.
DIPiDIP-19696N.
IntActiP29844. 3 interactions.
MINTiMINT-1330773.

Structurei

3D structure databases

ProteinModelPortaliP29844.
SMRiP29844. Positions 27-598.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi653 – 6564Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
InParanoidiP29844.
KOiK09490.
OMAiDKRAVQK.
OrthoDBiEOG780RKX.
PhylomeDBiP29844.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29844-1 [UniParc]FASTAAdd to Basket

« Hide

MKLCILLAVV AFVGLSLGEE KKEKDKELGT VIGIDLGTTY SCVGVYKNGR    50
VEIIANDQGN RITPSYVAFT ADGERLIGDA AKNQLTTNPE NTVFDAKRLI 100
GREWSDTNVQ HDIKFFPFKV VEKNSKPHIS VDTSQGAKVF APEEISAMVL 150
GKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGVI AGLQVMRIIN 200
EPTAAAIAYG LDKKEGEKNV LVFDLGGGTF DVSLLTIDNG VFEVVATNGD 250
THLGGEDFDQ RVMDHFIKLY KKKKGKDIRK DNRAVQKLRR EVEKAKRALS 300
GSHQVRIEIE SFFEGDDFSE TLTRAKFEEL NLDLFRSTLK PVQKVLEDAD 350
MNKKDVHEIV LVGGSTRIPK VQQLVKDFFG GKEPSRGINP DEAVAYGAAV 400
QAGVLSGEQD TDAIVLLDVN PLTMGIETVG GVMTKLIPRN TVIPTKKSQV 450
FSTASDNQHT VTIQVYEGER PMTKDNHLLG KFDLTGIPPA PRGIPQIEVS 500
FEIDANGILQ VSAEDKGTGN KEKIVITNDQ NRLTPEDIDR MIRDAEKFAD 550
EDKKLKERVE SRNELESYAY SLKNQIGDKD KLGAKLSDDE KNKLESAIDE 600
SIKWLEQNPD ADPEEYKKQK KDLEAIVQPV IAKLYQGAGG APPPEGGDDA 650
DLKDEL 656
Length:656
Mass (Da):72,261
Last modified:July 5, 2004 - v2
Checksum:i06A68F839A06337D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131Missing in AAO45194. 1 Publication
Sequence conflicti507 – 5071G → A in AAA28626. 1 Publication
Sequence conflicti510 – 5101Q → T in AAA28626. 1 Publication
Sequence conflicti592 – 5921N → T in AAA28626. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01498 mRNA. Translation: AAA28626.1.
AE014298 Genomic DNA. Translation: AAF48095.1.
AE014298 Genomic DNA. Translation: AAN09299.1.
AE014298 Genomic DNA. Translation: AAN09300.1.
AE014298 Genomic DNA. Translation: AAN09301.1.
BT004838 mRNA. Translation: AAO45194.1.
PIRiJN0666.
RefSeqiNP_511132.2. NM_078577.2.
NP_727563.1. NM_167306.1.
NP_727564.1. NM_167307.1.
NP_727565.1. NM_167308.1.
UniGeneiDm.2924.

Genome annotation databases

EnsemblMetazoaiFBtr0073608; FBpp0073445; FBgn0001218.
FBtr0073609; FBpp0073446; FBgn0001218.
FBtr0073610; FBpp0073447; FBgn0001218.
FBtr0073611; FBpp0073448; FBgn0001218.
GeneIDi32133.
KEGGidme:Dmel_CG4147.
UCSCiCG4147-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01498 mRNA. Translation: AAA28626.1 .
AE014298 Genomic DNA. Translation: AAF48095.1 .
AE014298 Genomic DNA. Translation: AAN09299.1 .
AE014298 Genomic DNA. Translation: AAN09300.1 .
AE014298 Genomic DNA. Translation: AAN09301.1 .
BT004838 mRNA. Translation: AAO45194.1 .
PIRi JN0666.
RefSeqi NP_511132.2. NM_078577.2.
NP_727563.1. NM_167306.1.
NP_727564.1. NM_167307.1.
NP_727565.1. NM_167308.1.
UniGenei Dm.2924.

3D structure databases

ProteinModelPortali P29844.
SMRi P29844. Positions 27-598.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58539. 17 interactions.
DIPi DIP-19696N.
IntActi P29844. 3 interactions.
MINTi MINT-1330773.

Proteomic databases

PaxDbi P29844.
PRIDEi P29844.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0073608 ; FBpp0073445 ; FBgn0001218 .
FBtr0073609 ; FBpp0073446 ; FBgn0001218 .
FBtr0073610 ; FBpp0073447 ; FBgn0001218 .
FBtr0073611 ; FBpp0073448 ; FBgn0001218 .
GeneIDi 32133.
KEGGi dme:Dmel_CG4147.
UCSCi CG4147-RB. d. melanogaster.

Organism-specific databases

CTDi 32133.
FlyBasei FBgn0001218. Hsc70-3.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
InParanoidi P29844.
KOi K09490.
OMAi DKRAVQK.
OrthoDBi EOG780RKX.
PhylomeDBi P29844.

Enzyme and pathway databases

Reactomei REACT_93794. ATF6-alpha activates chaperone genes.

Miscellaneous databases

ChiTaRSi Hsc70-3. drosophila.
GenomeRNAii 32133.
NextBioi 777024.
PROi P29844.

Gene expression databases

Bgeei P29844.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure and sequence analysis of Drosophila melanogaster HSC70 genes."
    Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X.J., Wells Q., Palter K.B.
    Gene 128:155-163(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Larva.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiHSP7C_DROME
AccessioniPrimary (citable) accession number: P29844
Secondary accession number(s): A4V4C4
, Q86NM3, Q9VYU2, Q9VYU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi