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Protein

Heat shock protein 70 homolog lhs1

Gene

SPAC1F5.06

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Chaperone required for protein translocation and folding in the endoplasmic reticulum.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein 70 homolog lhs1 (EC:3.6.1.3)
Gene namesi
ORF Names:SPAC1F5.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1F5.06.
PomBaseiSPAC1F5.06.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum lumen Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 848827Heat shock protein 70 homolog lhs1PRO_0000013557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi488 – 4881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi678 – 6781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ10061.
PaxDbiQ10061.

Interactioni

Protein-protein interaction databases

MINTiMINT-4696646.

Structurei

3D structure databases

ProteinModelPortaliQ10061.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi845 – 8484Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
InParanoidiQ10061.
KOiK09486.
OMAiFITEART.
OrthoDBiEOG7DC2CX.
PhylomeDBiQ10061.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 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.

Q10061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSVLTIIL FFSCQFWHAF ASSVLAIDYG TEWTKAALIK PGIPLEIVLT
60 70 80 90 100
KDTRRKEQSA VAFKGNERIF GVDASNLATR FPAHSIRNVK ELLDTAGLES
110 120 130 140 150
VLVQKYQSSY PAIQLVENEE TTSGISFVIS DEENYSLEEI IAMTMEHYIS
160 170 180 190 200
LAEEMAHEKI TDLVLTVPPH FNELQRSILL EAARILNKHV LALIDDNVAV
210 220 230 240 250
AIEYSLSRSF STDPTYNIIY DSGSGSTSAT VISFDTVEGS SLGKKQNITR
260 270 280 290 300
IRALASGFTL KLSGNEINRK LIGFMKNSFY QKHGIDLSHN HRALARLEKE
310 320 330 340 350
ALRVKHILSA NSEAIASIEE LADGIDFRLK ITRSVLESLC KDMEDAAVEP
360 370 380 390 400
INKALKKANL TFSEINSIIL FGGASRIPFI QSTLADYVSS DKISKNVNAD
410 420 430 440 450
EASVKGAAFY GASLTKSFRV KPLIVQDIIN YPYLLSLGTS EYIVALPDST
460 470 480 490 500
PYGMQHNVTI HNVSTIGKHP SFPLSNNGEL IGEFTLSNIT DVEKVCACSN
510 520 530 540 550
KNIQISFSSD RTKGILVPLS AIMTCEHGEL SSKHKLGDRV KSLFGSHDES
560 570 580 590 600
GLRNNESYPI GFTYKKYGEM SDNALRLASA KLERRLQIDK SKAAHDNALN
610 620 630 640 650
ELETLLYRAQ AMVDDDEFLE FANPEETKIL KNDSVESYDW LIEYGSQSPT
660 670 680 690 700
SEVTDRYKKL DDTLKSISFR FDQAKQFNTS LENFKNALER AESLLTNFDV
710 720 730 740 750
PDYPLNVYDE KDVKRVNSLR GTSYKKLGNQ YYNDTQWLKD NLDSHLSHTL
760 770 780 790 800
SEDPLIKVEE LEEKAKRLQE LTYEYLRRSL QQPKLKAKKG ASSSSTAESK
810 820 830 840
VEDETFTNDI EPTTALNSTS TQETEKSRAS VTQRPSSLQQ EIDDSDEL
Length:848
Mass (Da):94,898
Last modified:February 1, 1996 - v1
Checksum:iA1983FD4253F38F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA92234.1.
PIRiT38089.
RefSeqiNP_592867.1. NM_001018267.2.

Genome annotation databases

EnsemblFungiiSPAC1F5.06.1; SPAC1F5.06.1:pep; SPAC1F5.06.
GeneIDi2541537.
KEGGispo:SPAC1F5.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA92234.1.
PIRiT38089.
RefSeqiNP_592867.1. NM_001018267.2.

3D structure databases

ProteinModelPortaliQ10061.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4696646.

Proteomic databases

MaxQBiQ10061.
PaxDbiQ10061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1F5.06.1; SPAC1F5.06.1:pep; SPAC1F5.06.
GeneIDi2541537.
KEGGispo:SPAC1F5.06.

Organism-specific databases

EuPathDBiFungiDB:SPAC1F5.06.
PomBaseiSPAC1F5.06.

Phylogenomic databases

eggNOGiCOG0443.
InParanoidiQ10061.
KOiK09486.
OMAiFITEART.
OrthoDBiEOG7DC2CX.
PhylomeDBiQ10061.

Miscellaneous databases

NextBioi20802634.
PROiQ10061.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLHS1_SCHPO
AccessioniPrimary (citable) accession number: Q10061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 22, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.