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Protein

Ribosome-associated molecular chaperone sks2

Gene

sks2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone pss1 and fes1 act as nucleotide exchange factors that cause substrate release.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73ATPBy similarity1
Binding sitei341ATP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 17ATPBy similarity3
Nucleotide bindingi204 – 206ATPBy similarity3
Nucleotide bindingi270 – 277ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Hydrolase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-associated molecular chaperone sks2Curated (EC:3.6.4.10)
Alternative name(s):
Heat shock cognate protein hsc11 Publication
Hsp70 chaperone Ssb
Suppressor of K-252a sensitivity protein 21 Publication
Gene namesi
Name:sks21 Publication
Synonyms:hsc11 Publication
ORF Names:SPBC1709.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1709.05
PomBaseiSPBC1709.05 sks2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000783811 – 613Ribosome-associated molecular chaperone sks2Add BLAST613

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40Phosphothreonine1 Publication1
Modified residuei151Phosphotyrosine1 Publication1
Modified residuei153Phosphoserine1 Publication1
Modified residuei155Phosphoserine1 Publication1
Modified residuei256Phosphoserine1 Publication1
Modified residuei353Phosphoserine1 Publication1
Modified residuei501Phosphoserine1 Publication1
Modified residuei514Phosphoserine1 Publication1
Modified residuei515Phosphoserine1 Publication1
Modified residuei516Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10284
PaxDbiQ10284
PRIDEiQ10284

PTM databases

iPTMnetiQ10284

Interactioni

Subunit structurei

Binds to ribosomes. Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins and rRNA. Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC) (By similarity). Interacts with pss1 (By similarity). Interacts with fes1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi276732, 8 interactors
IntActiQ10284, 2 interactors
STRINGi4896.SPBC1709.05.1

Structurei

3D structure databases

ProteinModelPortaliQ10284
SMRiQ10284
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 390Nucleotide binding domain (NBD)By similarityAdd BLAST390
Regioni391 – 401Inter-domain linkerBy similarityAdd BLAST11
Regioni402 – 612Substrate binding domain (SBD)By similarityAdd BLAST211
Regioni515 – 611Lid domain (SBDalpha)By similarityAdd BLAST97

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi573 – 581Nuclear export signalBy similarity9

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000228135
InParanoidiQ10284
KOiK03283
OMAiDFSARHE
OrthoDBiEOG092C1VPN
PhylomeDBiQ10284

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q10284-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEVYEGAIG IDLGTTYSCV AVWETANVEI IPNDQGARTT PSFVAFTETE
60 70 80 90 100
RLVGDAAKNQ AAMNPRNTVF DAKRLIGRRY EDPETQKDIK HWPFKVIDNN
110 120 130 140 150
GIPTIEVNYL GEKKQFTAQE ISAMVLTKMK EISEAKLNKR VEKAVITVPA
160 170 180 190 200
YFSDSQRAAT KDAGAIAGLN VLRIINEPTA AAIAYGLDAK SDKPKNVLIF
210 220 230 240 250
DLGGGTFDVS LLKIQGGVFE VLATAGDTHL GGEDFDNALV EHFIQEFKRK
260 270 280 290 300
QKIDISDDPR ALRRLRSACE RAKRALSSVT QTTVEVDSLS NGIDFSSSIT
310 320 330 340 350
RARFEDINAT TFKATIDPVA KVLKDSKVPK ADVHDIVLVG GSTRIPKVQR
360 370 380 390 400
LVSDFFDGRA LNKSINPDEA VAYGAAVQAA VLTNKADSDK TQDLLLLDVV
410 420 430 440 450
PLSLGVAMEG NVFGVVCPRN TPIPTIKKRT FTTVADNQTT VTFPVYQGER
460 470 480 490 500
VNCAENEPLG EFQLTGIPPM PRGQAELEAT FELDANGILK VTAVEKTTGR
510 520 530 540 550
SAHIEITNSV GHLSSTKIQE MIENADKFKQ QDKDFAKKLE AKSQLESYIS
560 570 580 590 600
NIETTISEPN VMMKLKRGDK SKIEAQLAEC MSQLELEDTN TDALRKAELR
610
LKRTVQKAFA SLR
Length:613
Mass (Da):67,205
Last modified:August 14, 2001 - v2
Checksum:iEE86C49DB1F59348
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti250 – 252KQK → TKR in BAA12279 (PubMed:8973306).Curated3
Sequence conflicti456N → T in BAA20093 (PubMed:9161410).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84218 Genomic DNA Translation: BAA12279.1
D63798 Genomic DNA Translation: BAA20093.1
CU329671 Genomic DNA Translation: CAA21244.1
PIRiJC5335
T39633
T43239
RefSeqiNP_595438.1, NM_001021346.2

Genome annotation databases

EnsemblFungiiSPBC1709.05.1; SPBC1709.05.1:pep; SPBC1709.05
GeneIDi2540199
KEGGispo:SPBC1709.05

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84218 Genomic DNA Translation: BAA12279.1
D63798 Genomic DNA Translation: BAA20093.1
CU329671 Genomic DNA Translation: CAA21244.1
PIRiJC5335
T39633
T43239
RefSeqiNP_595438.1, NM_001021346.2

3D structure databases

ProteinModelPortaliQ10284
SMRiQ10284
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276732, 8 interactors
IntActiQ10284, 2 interactors
STRINGi4896.SPBC1709.05.1

PTM databases

iPTMnetiQ10284

Proteomic databases

MaxQBiQ10284
PaxDbiQ10284
PRIDEiQ10284

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1709.05.1; SPBC1709.05.1:pep; SPBC1709.05
GeneIDi2540199
KEGGispo:SPBC1709.05

Organism-specific databases

EuPathDBiFungiDB:SPBC1709.05
PomBaseiSPBC1709.05 sks2

Phylogenomic databases

HOGENOMiHOG000228135
InParanoidiQ10284
KOiK03283
OMAiDFSARHE
OrthoDBiEOG092C1VPN
PhylomeDBiQ10284

Miscellaneous databases

PROiPR:Q10284

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSSB1_SCHPO
AccessioniPrimary (citable) accession number: Q10284
Secondary accession number(s): O74730, P87181
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: November 7, 2018
This is version 135 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
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Main funding by: National Institutes of Health

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