mscS

Functionⁱ

Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds.11 Publications

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular water homeostasis
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 10202137
ion transmembrane transport
Source: UniProtKB
Inferred from direct assayⁱ
- 12551944
protein homooligomerization
Source: UniProtKB
Inferred from direct assayⁱ
- 12551944

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ion channel
Biological process	Ion transport, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11160-MONOMER

BioCycⁱ

EcoCyc:EG11160-MONOMER

Protein family/group databases

TCDBⁱ	1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) family

TCDBⁱ

1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Small-conductance mechanosensitive channel
Gene namesⁱ	Name:mscS Synonyms:yggB Ordered Locus Names:b2924, JW2891
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11160 mscS

EcoGeneⁱ

EG11160 mscS

Subcellular locationⁱ

Cell inner membrane
7 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Pressure-sensitive ion channel in Escherichia coli."
  Martinac B., Buechner M., Delcour A.H., Adler J., Kung C.
  Proc. Natl. Acad. Sci. U.S.A. 84:2297-2301(1987) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Ref.5
  "Characterization of mechanosensitive channels in Escherichia coli cytoplasmic membrane by whole-cell patch clamp recording."
  Cui C., Smith D.O., Adler J.
  J. Membr. Biol. 144:31-42(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, SENSITIVITY TO OSMOTIC AND VOLTAGE DIFFERENCES ACROSS THE CYTOPLASMIC MEMBRANE.
- Ref.6
  "Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity."
  Levina N., Toetemeyer S., Stokes N.R., Louis P., Jones M.A., Booth I.R.
  EMBO J. 18:1730-1737(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, PHYSIOLOGICAL ROLE.
- Ref.9
  "C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening."
  Koprowski P., Kubalski A.
  J. Biol. Chem. 278:11237-11245(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: CROSS-LINKING OF THE C-TERMINI INHIBITS CHANNEL OPENING, DOMAIN, FUNCTION, SUBCELLULAR LOCATION.
- Ref.12
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
- Ref.16
  "Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy."
  Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.
  Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.17
  "Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance."
  Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J., Blount P., Li Y., Yang M.
  Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 272-286, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ALA-158.
; Multi-pass membrane protein
5 Publications
Manual assertion based on experiment inⁱ
- Ref.12
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
- Ref.15
  "Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel."
  Bass R.B., Strop P., Barclay M., Rees D.C.
  Science 298:1582-1587(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 27-280 PROBABLY IN THE OPEN STATE, SUBUNIT, FUNCTION, TOPOLOGY, DOMAIN.
- Ref.16
  "Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy."
  Pliotas C., Ward R., Branigan E., Rasmussen A., Hagelueken G., Huang H., Black S.S., Booth I.R., Schiemann O., Naismith J.H.
  Proc. Natl. Acad. Sci. U.S.A. 109:E2675-E2682(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.18
  "Open and shut: crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 A and 4.1 A resolutions."
  Lai J.Y., Poon Y.S., Kaiser J.T., Rees D.C.
  Protein Sci. 22:502-509(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (4.37 ANGSTROMS), SUBUNIT, TOPOLOGY.
- Ref.19
  "The role of lipids in mechanosensation."
  Pliotas C., Dahl A.C., Rasmussen T., Mahendran K.R., Smith T.K., Marius P., Gault J., Banda T., Rasmussen A., Miller S., Robinson C.V., Bayley H., Sansom M.S., Booth I.R., Naismith J.H.
  Nat. Struct. Mol. Biol. 22:991-998(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 30	Periplasmic1 PublicationAdd BLAST	30
Transmembraneⁱ	31 – 52	Helical2 PublicationsAdd BLAST	22
Topological domainⁱ	53 – 67	Cytoplasmic1 PublicationAdd BLAST	15
Transmembraneⁱ	68 – 88	Helical2 PublicationsAdd BLAST	21
Topological domainⁱ	89 – 90	Periplasmic1 Publication	2
Transmembraneⁱ	91 – 111	Helical2 PublicationsAdd BLAST	21
Topological domainⁱ	112 – 286	Cytoplasmic1 PublicationAdd BLAST	175

GO - Cellular componentⁱ

integral component of membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 12080120
- 2480919
integral component of plasma membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 12551944

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	40	V → C, G or N: No detectable phenotype. 1 Publication	1
Mutagenesisⁱ	40	V → D or K: Normal growth stops, without cell death, due to increased membrane permeability to potassium ions and protons (permeability tested only for D substitutions). 1 Publication	1
Mutagenesisⁱ	58	S → C: Readily forms disulfide bonds with cross-linkers, suggesting that individual S-58 are only 3 Angstroms apart in the closed state, versus 33 Angstroms apart in the open state crystal structure. 1 Publication	1
Mutagenesisⁱ	158	A → F: Decreased conductance, due to decreased diameter of the channel portal. 1 Publication	1
Mutagenesisⁱ	266 – 286	ISFPY…EDKAA → HHHHHHLE: Normal levels of channels are expressed; they recover more slowly than wild-type cells after desensitization. 1 PublicationAdd BLAST	21
Mutagenesisⁱ	266 – 286	ISFPY…EDKAA → LE: Fewer channels present in the membrane, they require slightly more pressure to open and do not recover after desensitization. 1 PublicationAdd BLAST	21
Mutagenesisⁱ	267	S → C: Provides biochemical evidence for heptameric structure upon cross-linking. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000110238	1 – 286	Small-conductance mechanosensitive channelAdd BLAST		286

Proteomic databases

PaxDbⁱ	P0C0S1
PRIDEⁱ	P0C0S1

Interactionⁱ

Subunit structureⁱ

Homoheptamer.7 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-554616,EBI-554616

With

Entry

#Exp.

IntAct

Notes

itself

5

EBI-554616,EBI-554616

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16079137
- 26551077

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259238, 255 interactors
Database of interacting proteins More...DIPⁱ	DIP-36192N
IntActⁱ	P0C0S1, 2 interactors
STRINGⁱ	316385.ECDH10B_3099

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	22 – 58	Combined sources	37
Helixⁱ	63 – 87	Combined sources	25
Turnⁱ	88 – 90	Combined sources	3
Helixⁱ	93 – 127	Combined sources	35
Beta strandⁱ	135 – 140	Combined sources	6
Beta strandⁱ	142 – 148	Combined sources	7
Beta strandⁱ	150 – 156	Combined sources	7
Beta strandⁱ	162 – 166	Combined sources	5
Helixⁱ	167 – 172	Combined sources	6
Beta strandⁱ	175 – 192	Combined sources	18
Helixⁱ	198 – 211	Combined sources	14
Beta strandⁱ	221 – 228	Combined sources	8
Beta strandⁱ	233 – 242	Combined sources	10
Turnⁱ	243 – 245	Combined sources	3
Helixⁱ	246 – 264	Combined sources	19
Beta strandⁱ	272 – 279	Combined sources	8

Show more details

3D structure databases

ProteinModelPortalⁱ	P0C0S1
SMRⁱ	P0C0S1
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0C0S1

Family & Domainsⁱ

Domainⁱ

The channel pore is formed by TM3 and the loop between TM2 and TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127) is oriented nearly parallel to the plane of the putative lipid bilayer. On the intracellular side of the channel, the permeation pathway of MscS does not connect directly to the cytoplasm but instead opens to a large chamber that is connected to the cytoplasm. This chamber resembles a molecular filter that could serve to prescreen large molecules before they are allowed passage to the transmembrane pore. The TM1 and TM2 helices appear to be likely candidates for mediating the tension and voltage sensitivities of MscS. Gating requires large rearrangements of at least the C-terminus, and is probably influenced by freely exchangeable membrane lipids that bind in grooves and pockets between the transmembrane helices and enhance the stability of the closed channel conformation. In a hypoosmotic environment the membrane is stretched, and lipids may be pulled into the lipid bilayer and away from the protein, which is predicted to destabilize the closed conformation and promote channel gating.5 Publications

Sequence similaritiesⁱ

Belongs to the MscS (TC 1.A.23) family. [View classification]Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105D64 Bacteria COG0668 LUCA
HOGENOMⁱ	HOG000110050
InParanoidⁱ	P0C0S1
KEGG Orthology (KO) More...KOⁱ	K03442
OMAⁱ	IEDGIFN
PhylomeDBⁱ	P0C0S1

Family and domain databases

Gene3Dⁱ	2.30.30.60, 1 hit
InterProⁱ	View protein in InterPro IPR010920 LSM_dom_sf IPR011066 MscC_channel_C IPR006685 MscS_channel IPR006686 MscS_channel_CS IPR011014 MscS_channel_TM-2 IPR023408 MscS_dom_sf IPR008910 TM_helix
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00924 MS_channel, 1 hit PF05552 TM_helix, 1 hit
SUPFAMⁱ	SSF50182 SSF50182, 1 hit SSF82689 SSF82689, 1 hit SSF82861 SSF82861, 1 hit
PROSITEⁱ	View protein in PROSITE PS01246 UPF0003, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0C0S1-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN 
        60         70         80         90        100
AVNRLMISRK IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL 
       110        120        130        140        150
GAAGLAVGLA LQGSLSNLAA GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI 
       160        170        180        190        200
FSTTMRTADG KIIVIPNGKI IAGNIINFSR EPVRRNEFII GVAYDSDIDQ 
       210        220        230        240        250
VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW SNSGDLQNVY 
       260        270        280 
WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA

Length:286

Mass (Da):30,896

Last modified:December 6, 2005 - v1

Checksum:ⁱFF00AD64F795E9FE

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X14436 Genomic DNA Translation: CAA32606.1 U28377 Genomic DNA Translation: AAA69091.1 U00096 Genomic DNA Translation: AAC75961.1 AP009048 Genomic DNA Translation: BAE76988.1
PIRⁱ	S04735 QQEC4A
NCBI Reference Sequences More...RefSeqⁱ	NP_417399.1, NC_000913.3 WP_000389818.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75961; AAC75961; b2924 BAE76988; BAE76988; BAE76988
GeneIDⁱ	947416
KEGGⁱ	ecj:JW2891 eco:b2924
PATRICⁱ	fig\|1411691.4.peg.3808

Protein	Similar proteins		Species	Score	Length	Source
P0C0S1	Small-conductance mechanosensitive channel		ECO57		286	UniRef100_P0C0S2
Small-conductance mechanosensitive channel		SHIFL		286
Mechanosensitive channel		Escherichia coli NCCP15648		286
Mechanosensitive channel MscS		KLEPN		286
Small-conductance mechanosensitive channel		Escherichia coli M8		286
+120

Protein	Similar proteins		Species	Score	Length	Source
P0C0S1	Small-conductance mechanosensitive channel		ECO57		286	UniRef90_P0C0S2
Small-conductance mechanosensitive channel		SHIFL		286
Mechanosensitive channel		Escherichia coli NCCP15648		286
Mechanosensitive channel MscS		KLEPN		286
Small-conductance mechanosensitive channel		Escherichia coli M8		286
+567

Protein	Similar proteins		Species	Score	Length	Source
P0C0S1	Small-conductance mechanosensitive channel		EDWI9		286	UniRef50_O52401
Uncharacterized MscS family protein BUsg_437		BUCAP		283
Uncharacterized MscS family protein BU452		BUCAI		305
Small-conductance mechanosensitive channel		ECO57		286
Small-conductance mechanosensitive channel		SHIFL		286
+1963

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X14436 Genomic DNA Translation: CAA32606.1 U28377 Genomic DNA Translation: AAA69091.1 U00096 Genomic DNA Translation: AAC75961.1 AP009048 Genomic DNA Translation: BAE76988.1
PIRⁱ	S04735 QQEC4A
RefSeqⁱ	NP_417399.1, NC_000913.3 WP_000389818.1, NZ_LN832404.1

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
	2OAU	X-ray	3.70	A/B/C/D/E/F/G	1-286	[»]
	2VV5	X-ray	3.45	A/B/C/D/E/F/G	1-286	[»]
	3UDC	X-ray	3.36	A/B/C/D/E/F/G	272-286	[»]
	4AGE	X-ray	4.84	A/B/C/D/E/F/G	1-286	[»]
	4AGF	X-ray	4.70	A/B/C/D/E/F/G	1-286	[»]
	4HWA	X-ray	4.37	A/B/C/D/E/F/G	1-286	[»]
	5AJI	X-ray	2.99	A/B/C/D/E/F/G	1-286	[»]
ProteinModelPortalⁱ	P0C0S1
SMRⁱ	P0C0S1
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259238, 255 interactors
DIPⁱ	DIP-36192N
IntActⁱ	P0C0S1, 2 interactors
STRINGⁱ	316385.ECDH10B_3099

Protein family/group databases

TCDBⁱ	1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) family

TCDBⁱ

1.A.23.2.1 the small conductance mechanosensitive ion channel (mscs) family

Proteomic databases

PaxDbⁱ	P0C0S1
PRIDEⁱ	P0C0S1

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75961; AAC75961; b2924 BAE76988; BAE76988; BAE76988
GeneIDⁱ	947416
KEGGⁱ	ecj:JW2891 eco:b2924
PATRICⁱ	fig\|1411691.4.peg.3808

Organism-specific databases

EchoBASEⁱ	EB1149
EcoGeneⁱ	EG11160 mscS

Phylogenomic databases

eggNOGⁱ	ENOG4105D64 Bacteria COG0668 LUCA
HOGENOMⁱ	HOG000110050
InParanoidⁱ	P0C0S1
KOⁱ	K03442
OMAⁱ	IEDGIFN
PhylomeDBⁱ	P0C0S1

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11160-MONOMER

BioCycⁱ

EcoCyc:EG11160-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0C0S1
Protein Ontology More...PROⁱ	PR:P0C0S1

Family and domain databases

Gene3Dⁱ	2.30.30.60, 1 hit
InterProⁱ	View protein in InterPro IPR010920 LSM_dom_sf IPR011066 MscC_channel_C IPR006685 MscS_channel IPR006686 MscS_channel_CS IPR011014 MscS_channel_TM-2 IPR023408 MscS_dom_sf IPR008910 TM_helix
Pfamⁱ	View protein in Pfam PF00924 MS_channel, 1 hit PF05552 TM_helix, 1 hit
SUPFAMⁱ	SSF50182 SSF50182, 1 hit SSF82689 SSF82689, 1 hit SSF82861 SSF82861, 1 hit
PROSITEⁱ	View protein in PROSITE PS01246 UPF0003, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MSCS_ECOLI
Accessionⁱ	P0C0S1Primary (citable) accession number: P0C0S1 Secondary accession number(s): P11666, Q2M9R8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
	Last sequence update:	December 6, 2005
	Last modified:	March 28, 2018
	This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P0C0S1 (MSCS_ECOLI)

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Small-conductance mechanosensitive channel

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<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

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GO - Biological processi

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<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

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<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

Topology

GO - Cellular componenti

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

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<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

Proteomic databases

<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

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<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

<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

Keywords - Domaini

Phylogenomic databases

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Sequence databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ