UniProtKB - P11484 (SSB1_YEAST)

BLAST

>sp|P11484|SSB1_YEAST Ribosome-associated molecular chaperone SSB1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SSB1 PE=1 SV=3
MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQ
AALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQE
ISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTA
AAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNL
LEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSL
TRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGK
QLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDMFGIVVPR
NTTVPTIKRRTFTTCADNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEA
IFEVDANGILKVTAVEKSTGKSSNITISNAVGRLSSEEIEKMVNQAEEFKAADEAFAKKH
EARQRLESYVASIEQTVTDPVLSSKLKRGSKSKIEAALSDALAALQIEDPSADELRKAEV
GLKRVVTKAMSSR

Align
Format
Add to basket Added to basket
History
Entry version 188 (10 Oct 2018)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

Ribosome-associated molecular chaperone SSB1

Gene

SSB1

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.8 Publications

Miscellaneous

Present with 170000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityⁱ

ATP + H₂O = ADP + phosphate.1 Publication

Kineticsⁱ

kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM potassium acetate) and 0.81 min(-1) with ATP as substrate (at 100 mM potassium acetate).1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	73	ATPBy similarity		1
Binding siteⁱ	342	ATP; via amide nitrogenBy similarity		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	16 – 18	ATPBy similarity	3
Nucleotide bindingⁱ	205 – 207	ATPBy similarity	3
Nucleotide bindingⁱ	271 – 278	ATPBy similarity	8

GO - Molecular functionⁱ

ATPase activity
Source: SGD
Inferred from direct assayⁱ
- 9860955
ATP binding Source: UniProtKB-KW
calmodulin binding
Source: SGD
Inferred from direct assayⁱ
- 17146552
unfolded protein binding
Source: SGD
Inferred from direct assayⁱ
- 9670014

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

'de novo' cotranslational protein folding
Source: SGD
Inferred from direct assayⁱ
- 9670014
cellular response to glucose starvation
Source: SGD
Inferred from genetic interactionⁱ
- 19723765
cytoplasmic translation
Source: SGD
Inferred from mutant phenotypeⁱ
- 1394434
regulation of translational fidelity
Source: SGD
Inferred from mutant phenotypeⁱ
- 15456889
ribosomal subunit export from nucleus
Source: SGD
Inferred from genetic interactionⁱ
- 20368619
rRNA processing
Source: SGD
Inferred from genetic interactionⁱ
- 20368619
translational frameshifting
Source: SGD
Inferred from mutant phenotypeⁱ
- 16607023
translational termination
Source: SGD
Inferred from mutant phenotypeⁱ
- 17483428

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone, Hydrolase
Biological process	Protein biosynthesis
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29608-MONOMER
Reactomeⁱ	R-SCE-3371453 Regulation of HSF1-mediated heat shock response

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ribosome-associated molecular chaperone SSB11 Publication (EC:3.6.4.101 Publication) Alternative name(s): Cold-inducible protein YG1011 Publication Heat shock protein SSB11 Publication Hsp70 chaperone Ssb1 Publication
Gene namesⁱ	Name:SSB11 Publication Synonyms:YG1011 Publication Ordered Locus Names:YDL229WImported
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome IV

Organism-specific databases

EuPathDBⁱ	FungiDB:YDL229W
Saccharomyces Genome Database More...SGDⁱ	S000002388 SSB1

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	73	K → A: Unable to hydrolyze ATP and moderately reduces ribosome binding. 1 Publication	1
Mutagenesisⁱ	567 – 568	KR → EE in SSB1-L(BC): Reduces ribosome-binding to less than 50%. 1 Publication	2
Mutagenesisⁱ	596 – 597	RK → DD in SSB1-D1: Reduces ribosome-binding to less than 50%. 1 Publication	2
Mutagenesisⁱ	603 – 604	KR → DD in SSB1-D2: Reduces ribosome-binding to less than 50%. 1 Publication	2

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000078389	2 – 613	Ribosome-associated molecular chaperone SSB1Add BLAST		612

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanine1 Publication	1
Modified residueⁱ	47	PhosphothreonineCombined sources	1
Modified residueⁱ	431	PhosphothreonineCombined sources	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P11484
PaxDbⁱ	P11484
PRIDEⁱ	P11484
TopDownProteomicsⁱ	P11484

2D gel databases

COMPLUYEAST-2DPAGEⁱ	P11484
SWISS-2DPAGEⁱ	P11484
UCD-2DPAGEⁱ	P11484

PTM databases

CarbonylDBⁱ	P11484
iPTMnetⁱ	P11484

Expressionⁱ

Inductionⁱ

Expression decreases after heat shock or during growth to stationary phase (PubMed:6761581, PubMed:2651414). Degraded during heat shock treatment (at protein level) (PubMed:7646503). Up-regulated upon carbon upshift and down-regulated upon amino acid limitation in an HSF1-dependent manner (PubMed:10322015).4 Publications

Interactionⁱ

Subunit structureⁱ

Binds to ribosomes (PubMed:9670014, PubMed:1394434, PubMed:27917864). Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins RPL35, RPL39 and RPL19, and rRNA (PubMed:27882919). Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC) (PubMed:11929994, PubMed:23332755). Interacts with SSE1 (PubMed:16219770, PubMed:16221677, PubMed:23332755). Interacts with FES1 (PubMed:17132105). Interacts with NAP1 (PubMed:18086883).10 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
BUD27	P43573	3	EBI-8627,EBI-22787
PFK26	P40433	2	EBI-8627,EBI-1956
SSE1	P32589	2	EBI-8627,EBI-8648
TOM71	P38825	2	EBI-8627,EBI-24694

GO - Molecular functionⁱ

calmodulin binding
Source: SGD
Inferred from direct assayⁱ
- 17146552
unfolded protein binding
Source: SGD
Inferred from direct assayⁱ
- 9670014

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	31882, 795 interactors
Database of interacting proteins More...DIPⁱ	DIP-2254N
IntActⁱ	P11484, 777 interactors
Molecular INTeraction database More...MINTⁱ	P11484
STRINGⁱ	4932.YDL229W

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	10 – 13	Combined sources	4
Beta strandⁱ	16 – 30	Combined sources	15
Beta strandⁱ	38 – 41	Combined sources	4
Beta strandⁱ	44 – 46	Combined sources	3
Beta strandⁱ	51 – 54	Combined sources	4
Helixⁱ	55 – 59	Combined sources	5
Helixⁱ	61 – 63	Combined sources	3
Helixⁱ	65 – 67	Combined sources	3
Helixⁱ	72 – 74	Combined sources	3
Turnⁱ	75 – 77	Combined sources	3
Helixⁱ	83 – 89	Combined sources	7
Beta strandⁱ	93 – 99	Combined sources	7
Beta strandⁱ	102 – 109	Combined sources	8
Beta strandⁱ	112 – 116	Combined sources	5
Helixⁱ	118 – 137	Combined sources	20
Beta strandⁱ	143 – 148	Combined sources	6
Helixⁱ	154 – 166	Combined sources	13
Beta strandⁱ	170 – 176	Combined sources	7
Helixⁱ	177 – 184	Combined sources	8
Turnⁱ	185 – 190	Combined sources	6
Beta strandⁱ	196 – 203	Combined sources	8
Beta strandⁱ	208 – 216	Combined sources	9
Beta strandⁱ	219 – 228	Combined sources	10
Helixⁱ	233 – 252	Combined sources	20
Helixⁱ	260 – 276	Combined sources	17
Turnⁱ	277 – 279	Combined sources	3
Beta strandⁱ	280 – 291	Combined sources	12
Beta strandⁱ	294 – 301	Combined sources	8
Helixⁱ	302 – 308	Combined sources	7
Helixⁱ	310 – 315	Combined sources	6
Helixⁱ	317 – 327	Combined sources	11
Helixⁱ	331 – 333	Combined sources	3
Beta strandⁱ	336 – 341	Combined sources	6
Helixⁱ	342 – 345	Combined sources	4
Helixⁱ	347 – 356	Combined sources	10
Turnⁱ	357 – 359	Combined sources	3
Turnⁱ	368 – 370	Combined sources	3
Helixⁱ	371 – 383	Combined sources	13

Show more details

3D structure databases

ProteinModelPortalⁱ	P11484
SMRⁱ	P11484
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P11484

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2 – 391	Nucleotide binding domain (NBD)By similarityAdd BLAST	390
Regionⁱ	392 – 402	Inter-domain linkerBy similarityAdd BLAST	11
Regionⁱ	403 – 613	Substrate binding domain (SBD)By similarityAdd BLAST	211
Regionⁱ	516 – 612	Lid domain (SBDalpha)By similarityAdd BLAST	97
Regionⁱ	601 – 613	Required for interaction with ribosomes1 PublicationAdd BLAST	13

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	428 – 430	Contributes to ribosome binding1 Publication		3
Motifⁱ	574 – 582	Nuclear export signal1 Publication		9

Sequence similaritiesⁱ

Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily.Curated

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00890000139503
HOGENOMⁱ	HOG000228135
InParanoidⁱ	P11484
OMAⁱ	FEEINST
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C1VPN

Family and domain databases

Gene3Dⁱ	1.20.1270.10, 1 hit 2.60.34.10, 1 hit
InterProⁱ	View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam
PANTHERⁱ	PTHR19375 PTHR19375, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00012 HSP70, 1 hit
PRINTSⁱ	PR00301 HEATSHOCK70
SUPFAMⁱ	SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit
PROSITEⁱ	View protein in PROSITE PS00297 HSP70_1, 1 hit PS00329 HSP70_2, 1 hit PS01036 HSP70_3, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P11484-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE 
        60         70         80         90        100
RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD 
       110        120        130        140        150
GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA 
       160        170        180        190        200
YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI 
       210        220        230        240        250
FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK 
       260        270        280        290        300
KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL 
       310        320        330        340        350
TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ 
       360        370        380        390        400
KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV 
       410        420        430        440        450
APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE 
       460        470        480        490        500
RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG 
       510        520        530        540        550
KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV 
       560        570        580        590        600
ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV 
       610 
GLKRVVTKAM SSR

Length:613

Mass (Da):66,602

Last modified:January 23, 2007 - v3

Checksum:ⁱF16FA7C25A40321A

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	180 – 184	AAAIA → VVVIV in AAA34692 (PubMed:6761581).Curated	5
Sequence conflictⁱ	189	A → V in AAA34692 (PubMed:6761581).Curated	1
Sequence conflictⁱ	192	S → F in AAA34692 (PubMed:6761581).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X13713 Genomic DNA Translation: CAA31995.1 M25395 mRNA Translation: AAA35099.1 Z74277 Genomic DNA Translation: CAA98807.1 M17585 Genomic DNA Translation: AAA34692.1 BK006938 Genomic DNA Translation: DAA11637.1
PIRⁱ	S20149
NCBI Reference Sequences More...RefSeqⁱ	NP_010052.1, NM_001180289.1

Genome annotation databases

EnsemblFungiⁱ	YDL229W; YDL229W; YDL229W
GeneIDⁱ	851369
KEGGⁱ	sce:YDL229W

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P11484	Heat shock protein SSB1		YEAS1		613	UniRef100_P11484
K7_Ssb1p		YEASK		613
Ssb1p		YEAS8		613
Ssb1p		YEASA		613
Ssb1p		SACCK		613
+7

Protein	Similar proteins		Species	Score	Length	Source
P11484	Ribosome-associated molecular chaperone SSB1		ASHGO		613	UniRef90_P11484
Ribosome-associated molecular chaperone SSB		CANGA		613
Ribosome-associated molecular chaperone SSB1		KLULA		613
Ribosome-associated molecular chaperone SSB1		KLUMA		613
Ribosome-associated molecular chaperone SSB2		YEAST		613
+40

Protein	Similar proteins		Species	Score	Length	Source
P11484	Ribosome-associated molecular chaperone SSB1		KLUMA		613	UniRef50_P11484
Ribosome-associated molecular chaperone SSB1		ASHGO		613
Ribosome-associated molecular chaperone SSB2		YEAST		613
Ribosome-associated molecular chaperone SSB1		KLULA		613
Ribosome-associated molecular chaperone SSB		CANGA		613
+152

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X13713 Genomic DNA Translation: CAA31995.1 M25395 mRNA Translation: AAA35099.1 Z74277 Genomic DNA Translation: CAA98807.1 M17585 Genomic DNA Translation: AAA34692.1 BK006938 Genomic DNA Translation: DAA11637.1
PIRⁱ	S20149
RefSeqⁱ	NP_010052.1, NM_001180289.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3GL1	X-ray	1.92	A/B	1-384	[»]
ProteinModelPortalⁱ	P11484
SMRⁱ	P11484
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	31882, 795 interactors
DIPⁱ	DIP-2254N
IntActⁱ	P11484, 777 interactors
MINTⁱ	P11484
STRINGⁱ	4932.YDL229W

PTM databases

CarbonylDBⁱ	P11484
iPTMnetⁱ	P11484

2D gel databases

COMPLUYEAST-2DPAGEⁱ	P11484
SWISS-2DPAGEⁱ	P11484
UCD-2DPAGEⁱ	P11484

Proteomic databases

MaxQBⁱ	P11484
PaxDbⁱ	P11484
PRIDEⁱ	P11484
TopDownProteomicsⁱ	P11484

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YDL229W; YDL229W; YDL229W
GeneIDⁱ	851369
KEGGⁱ	sce:YDL229W

Organism-specific databases

EuPathDBⁱ	FungiDB:YDL229W
SGDⁱ	S000002388 SSB1

Phylogenomic databases

GeneTreeⁱ	ENSGT00890000139503
HOGENOMⁱ	HOG000228135
InParanoidⁱ	P11484
OMAⁱ	FEEINST
OrthoDBⁱ	EOG092C1VPN

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29608-MONOMER
Reactomeⁱ	R-SCE-3371453 Regulation of HSF1-mediated heat shock response

Miscellaneous databases

EvolutionaryTraceⁱ	P11484
Protein Ontology More...PROⁱ	PR:P11484

Family and domain databases

Gene3Dⁱ	1.20.1270.10, 1 hit 2.60.34.10, 1 hit
InterProⁱ	View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam
PANTHERⁱ	PTHR19375 PTHR19375, 1 hit
Pfamⁱ	View protein in Pfam PF00012 HSP70, 1 hit
PRINTSⁱ	PR00301 HEATSHOCK70
SUPFAMⁱ	SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit
PROSITEⁱ	View protein in PROSITE PS00297 HSP70_1, 1 hit PS00329 HSP70_2, 1 hit PS01036 HSP70_3, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SSB1_YEAST
Accessionⁱ	P11484Primary (citable) accession number: P11484 Secondary accession number(s): D6VRC7, Q05834
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
	Last sequence update:	January 23, 2007
	Last modified:	October 10, 2018
	This is version 188 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
Yeast chromosome IV
Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P11484 (SSB1_YEAST)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Ribosome-associated molecular chaperone SSB1

SSB1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ