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Protein

Heat shock 70 kDa protein cognate 5

Gene

Hsc70-5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • mitochondrion morphogenesis Source: FlyBase
  • mitophagy Source: FlyBase
  • positive regulation of mitochondrial membrane potential Source: FlyBase
  • protein folding Source: FlyBase
  • response to heat Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein cognate 5
Gene namesi
Name:Hsc70-5
Synonyms:Hsc5
ORF Names:CG8542
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0001220. Hsc70-5.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 686686Heat shock 70 kDa protein cognate 5PRO_0000078342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP29845.
PRIDEiP29845.

PTM databases

iPTMnetiP29845.

Expressioni

Developmental stagei

Heat shock cognate proteins are expressed constitutively during normal development.

Gene expression databases

BgeeiP29845.
GenevisibleiP29845. DM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi62333. 14 interactions.
IntActiP29845. 1 interaction.
MINTiMINT-935704.
STRINGi7227.FBpp0086694.

Structurei

3D structure databases

ProteinModelPortaliP29845.
SMRiP29845. Positions 53-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
InParanoidiP29845.
KOiK04043.
OMAiEMMYKDA.
OrthoDBiEOG715Q3K.
PhylomeDBiP29845.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. 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.
TIGRFAMsiTIGR02350. prok_dnaK. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRVPKFLPR LARQAGVVPS HMSGASSMFR NLPGASNGIS SQLRYKSGEV
60 70 80 90 100
KGAVIGIDLG TTNSCLAVME GKQAKVIENA EGARTTPSHV AFTKDGERLV
110 120 130 140 150
GMPAKRQAVT NSANTFYATK RLIGRRFDDP EVKKDITNLS YKVVKASNGD
160 170 180 190 200
AWVSSTDGKV YSPSQIGAFI LMKMKETAEA YLNTPVKNAV VTVPAYFNDS
210 220 230 240 250
QRQATKDAGQ IAGLNVLRVI NEPTAAALAY GMDKTEDKII AVYDLGGGTF
260 270 280 290 300
DISILEIQKG VFEVKSTNGD TLLGGEDFDN HIVNFLVAEF KKDSGIDIRK
310 320 330 340 350
DNIAMQRLKE AAEKAKCELS SSQQTDINLP YLTMDAAGPQ HMNLKLTRSK
360 370 380 390 400
LESLVGDLIK RTIQPCQKAL SDAEVSKSEI GEVLLVGGMT RMPKVQSTVQ
410 420 430 440 450
ELFGRQPSRS VNPDEAVAVG AAVQGGVLAG DVTDVLLLDV TPLSLGIETL
460 470 480 490 500
GGVFTRLISR NTTIPTKKSQ VFSTASDGQT QVEIKVHQGE REMANDNKLL
510 520 530 540 550
GSFTLVGIPP APRGVPQIEV VFDIDANGIV HVSAKDKGTG KEQQIVIQSS
560 570 580 590 600
GGLSKDEIEN MIKKAEEYAT ADKQKRELIE IVNQGESIVH DTETKMEEFK
610 620 630 640 650
SQLPAEECEK LKKEIADLRT LLANKETADL EEVRKATSSL QQSSLKLFEL
660 670 680
AYKKMSAERE SNAGAGSSDS SSSSDTSGEA KKEEKN
Length:686
Mass (Da):74,066
Last modified:November 23, 2004 - v2
Checksum:i61A0C0EDA8E74B9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881A → V in AAA28628 (PubMed:8514184).Curated
Sequence conflicti661 – 6611S → T in AAA28628 (PubMed:8514184).Curated
Sequence conflicti678 – 6869GEAKKEEKN → ASQEGREELN (PubMed:8514184).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01502 mRNA. Translation: AAA28628.1.
AE013599 Genomic DNA. Translation: AAF58270.1.
AY118844 mRNA. Translation: AAM50704.1.
PIRiJN0667.
RefSeqiNP_001286414.1. NM_001299485.1.
NP_523741.2. NM_079017.2.
UniGeneiDm.7248.

Genome annotation databases

EnsemblMetazoaiFBtr0087568; FBpp0086694; FBgn0001220.
FBtr0339969; FBpp0308990; FBgn0001220.
GeneIDi36583.
KEGGidme:Dmel_CG8542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01502 mRNA. Translation: AAA28628.1.
AE013599 Genomic DNA. Translation: AAF58270.1.
AY118844 mRNA. Translation: AAM50704.1.
PIRiJN0667.
RefSeqiNP_001286414.1. NM_001299485.1.
NP_523741.2. NM_079017.2.
UniGeneiDm.7248.

3D structure databases

ProteinModelPortaliP29845.
SMRiP29845. Positions 53-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62333. 14 interactions.
IntActiP29845. 1 interaction.
MINTiMINT-935704.
STRINGi7227.FBpp0086694.

PTM databases

iPTMnetiP29845.

Proteomic databases

PaxDbiP29845.
PRIDEiP29845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087568; FBpp0086694; FBgn0001220.
FBtr0339969; FBpp0308990; FBgn0001220.
GeneIDi36583.
KEGGidme:Dmel_CG8542.

Organism-specific databases

CTDi36583.
FlyBaseiFBgn0001220. Hsc70-5.

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
InParanoidiP29845.
KOiK04043.
OMAiEMMYKDA.
OrthoDBiEOG715Q3K.
PhylomeDBiP29845.

Miscellaneous databases

ChiTaRSiHsc70-5. fly.
GenomeRNAii36583.
PROiP29845.

Gene expression databases

BgeeiP29845.
GenevisibleiP29845. DM.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. 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.
TIGRFAMsiTIGR02350. prok_dnaK. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
  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: Ovary.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiHSP7E_DROME
AccessioniPrimary (citable) accession number: P29845
Secondary accession number(s): Q9V6Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 23, 2004
Last modified: July 6, 2016
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.