UniProtKB - P0A903 (BAMC_ECOLI)

BLAST

>sp|P0A903|BAMC_ECOLI Outer membrane protein assembly factor BamC OS=Escherichia coli (strain K12) OX=83333 GN=bamC PE=1 SV=1
MAYSVQKSRLAKVAGVSLVLLLAACSSDSRYKRQVSGDEAYLEAAPLAELHAPAGMILPV
TSGDYAIPVTNGSGAVGKALDIRPPAQPLALVSGARTQFTGDTASLLVENGRGNTLWPQV
VSVLQAKNYTITQRDDAGQTLTTDWVQWNRLDEDEQYRGRYQISVKPQGYQQAVTVKLLN
LEQAGKPVADAASMQRYSTEMMNVISAGLDKSATDAANAAQNRASTTMDVQSAADDTGLP
MLVVRGPFNVVWQRLPAALEKVGMKVTDSTRSQGNMAVTYKPLSDSDWQELGASDPGLAS
GDYKLQVGDLDNRSSLQFIDPKGHTLTQSQNDALVAVFQAAFSK

Align
Format
Add to basket Added to basket
History
Entry version 117 (07 Nov 2018)
Sequence version 1 (19 Jul 2005)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

Outer membrane protein assembly factor BamC

Gene

bamC

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).7 Publications

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 21586578

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

Gram-negative-bacterium-type cell outer membrane assembly
Source: EcoliWiki
Inferred from genetic interactionⁱ
- 15851030
protein insertion into membrane Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10658-MONOMER

BioCycⁱ

EcoCyc:EG10658-MONOMER

Protein family/group databases

TCDBⁱ	1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

TCDBⁱ

1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Outer membrane protein assembly factor BamCUniRule annotation
Gene namesⁱ	Name:bamCUniRule annotation Synonyms:dapX, nlpB Ordered Locus Names:b2477, JW2462
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	EG10658 bamC

EcoGeneⁱ

EG10658 bamC

Subcellular locationⁱ

Cell outer membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00924
3 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "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.19
  "Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins."
  Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y.
  Nat. Struct. Mol. Biol. 23:192-196(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 33-88 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.20
  "Structural basis of outer membrane protein insertion by the BAM complex."
  Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.
  Nature 531:64-69(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND LATERAL OPEN BAMACDE SUBCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
; Lipid-anchor
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00924
2 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "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.18
  "Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
  Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
  Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 25-189 IN LATERAL OPEN BAM COMPLEX, FUNCTION, REACTION MECHANISM, SUBUNIT, MASS SPECTROMETRY, LIPIDATION.

GO - Cellular componentⁱ

Bam protein complex
Source: EcoCyc
Inferred from direct assayⁱ
cell surface
Source: EcoCyc
Inferred from direct assayⁱ
- 22683355

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell outer membrane, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 24	Add BLAST		24
ChainⁱPRO_0000018027	25 – 344	Outer membrane protein assembly factor BamCAdd BLAST		320

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Lipidationⁱ	25	N-palmitoyl cysteineUniRule annotation1 Publication1 Publication		1
Lipidationⁱ	25	S-diacylglycerol cysteineUniRule annotation1 Publication1 Publication		1

Keywords - PTMⁱ

Lipoprotein, Palmitate

Proteomic databases

EPDⁱ	P0A903
PaxDbⁱ	P0A903
PRIDEⁱ	P0A903

2D gel databases

SWISS-2DPAGEⁱ	P0A903

SWISS-2DPAGEⁱ

P0A903

Interactionⁱ

Subunit structureⁱ

Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Forms a subcomplex with BamD and BamE. The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1129043,EBI-1129043
bamD	P0AC02	4	EBI-1129043,EBI-1128087

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 21586578

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4262898, 311 interactors
ComplexPortalⁱ	CPX-1923 Bam complex
Database of interacting proteins More...DIPⁱ	DIP-39898N
IntActⁱ	P0A903, 8 interactors
STRINGⁱ	316385.ECDH10B_2643

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	30 – 33	Combined sources	4
Turnⁱ	37 – 39	Combined sources	3
Helixⁱ	40 – 43	Combined sources	4
Helixⁱ	77 – 79	Combined sources	3
Beta strandⁱ	96 – 100	Combined sources	5
Beta strandⁱ	103 – 108	Combined sources	6
Helixⁱ	109 – 112	Combined sources	4
Helixⁱ	116 – 126	Combined sources	11
Beta strandⁱ	131 – 135	Combined sources	5
Helixⁱ	136 – 138	Combined sources	3
Beta strandⁱ	140 – 143	Combined sources	4
Beta strandⁱ	146 – 148	Combined sources	3
Helixⁱ	153 – 155	Combined sources	3
Beta strandⁱ	157 – 168	Combined sources	12
Beta strandⁱ	171 – 183	Combined sources	13
Beta strandⁱ	186 – 188	Combined sources	3
Helixⁱ	191 – 208	Combined sources	18
Beta strandⁱ	230 – 234	Combined sources	5
Turnⁱ	235 – 237	Combined sources	3
Beta strandⁱ	240 – 246	Combined sources	7
Helixⁱ	248 – 261	Combined sources	14
Beta strandⁱ	264 – 270	Combined sources	7
Helixⁱ	271 – 273	Combined sources	3
Beta strandⁱ	275 – 280	Combined sources	6
Helixⁱ	285 – 291	Combined sources	7
Beta strandⁱ	300 – 310	Combined sources	11
Beta strandⁱ	313 – 319	Combined sources	7
Beta strandⁱ	321 – 323	Combined sources	3
Helixⁱ	328 – 344	Combined sources	17

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A903
SMRⁱ	P0A903
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A903

Family & Domainsⁱ

Domainⁱ

Contains two well-defined domains connected by a flexible linker. The C-terminal domain may serve as an important protein-binding surface for interaction with other Bam components or substrates. In addition, contains a long unstructured N-terminal region, which is required to stabilize the BamCD complex. Only the N-terminus of this protein is observed in the Bam complex in X-ray or EM structures, most of the protein must be highly mobile (PubMed:26900875, PubMed:26901871, PubMed:27686148, PubMed:26744406).7 Publications

Sequence similaritiesⁱ

Belongs to the BamC family.UniRule annotation

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG4107EG0 Bacteria COG3317 LUCA
HOGENOMⁱ	HOG000123040
KEGG Orthology (KO) More...KOⁱ	K07287

Family and domain databases

HAMAPⁱ	MF_00924 OM_assembly_BamC, 1 hit
InterProⁱ	View protein in InterPro IPR014524 BamC IPR010653 NlpB/DapX
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06804 Lipoprotein_18, 1 hit
PIRSFⁱ	PIRSF026343 NlpB, 1 hit
PROSITEⁱ	View protein in PROSITE PS51257 PROKAR_LIPOPROTEIN, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P0A903-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL 
        60         70         80         90        100
HAPAGMILPV TSGDYAIPVT NGSGAVGKAL DIRPPAQPLA LVSGARTQFT 
       110        120        130        140        150
GDTASLLVEN GRGNTLWPQV VSVLQAKNYT ITQRDDAGQT LTTDWVQWNR 
       160        170        180        190        200
LDEDEQYRGR YQISVKPQGY QQAVTVKLLN LEQAGKPVAD AASMQRYSTE 
       210        220        230        240        250
MMNVISAGLD KSATDAANAA QNRASTTMDV QSAADDTGLP MLVVRGPFNV 
       260        270        280        290        300
VWQRLPAALE KVGMKVTDST RSQGNMAVTY KPLSDSDWQE LGASDPGLAS 
       310        320        330        340 
GDYKLQVGDL DNRSSLQFID PKGHTLTQSQ NDALVAVFQA AFSK

Length:344

Mass (Da):36,842

Last modified:July 19, 2005 - v1

Checksum:ⁱ49991F277D9D923C

Sequence cautionⁱ

The sequence M33928 differs from that shown. Reason: Frameshift at positions 50, 64, 81 and 134.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	219	A → R in M33928 (PubMed:2120198).Curated		1

Mass spectrometryⁱ

Molecular mass is 35163 Da from positions 25 - 344. Determined by ESI. With 3 palmitic acid (C16) acyl chains.1 Publication

Molecular mass is 35183 Da from positions 25 - 344. Determined by ESI. With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.1 Publication

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X57402 Genomic DNA Translation: CAA40661.1 M33928 Genomic DNA No translation available. U00096 Genomic DNA Translation: AAC75530.2 AP009048 Genomic DNA Translation: BAA16354.1
PIRⁱ	D65023
NCBI Reference Sequences More...RefSeqⁱ	NP_416972.4, NC_000913.3 WP_001297320.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75530; AAC75530; b2477 BAA16354; BAA16354; BAA16354
GeneIDⁱ	946954
KEGGⁱ	ecj:JW2462 eco:b2477
PATRICⁱ	fig\|1411691.4.peg.4262

Protein	Similar proteins		Species	Score	Length	Source
P0A903	Outer membrane protein assembly factor BamC		SHIFL		344	UniRef100_P0A903
Outer membrane protein assembly factor BamC		ECOLX		345
Outer membrane protein assembly factor BamC		SHIF2		345
Outer membrane protein assembly factor BamC		Escherichia coli chi7122		345
Outer membrane protein assembly factor BamC		SHISS		345
+117

Protein	Similar proteins		Species	Score	Length	Source
P0A903	Outer membrane protein assembly factor BamC		SHIFL		344	UniRef90_P0A903
Outer membrane protein assembly factor BamC		ECOLX		345
Outer membrane protein assembly factor BamC		SHIF2		345
Outer membrane protein assembly factor BamC		Escherichia coli chi7122		345
Outer membrane protein assembly factor BamC		SHISS		345
+764

Protein	Similar proteins		Species	Score	Length	Source
P0A903	Outer membrane protein assembly factor BamC		SHIFL		344	UniRef50_P0A903
Outer membrane protein assembly factor BamC		YERPE		352
Outer membrane protein assembly factor BamC		PHOAA		349
Outer membrane protein assembly factor BamC		RAHSY		359
Outer membrane protein assembly factor BamC		XENNA		348
+1769

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X57402 Genomic DNA Translation: CAA40661.1 M33928 Genomic DNA No translation available. U00096 Genomic DNA Translation: AAC75530.2 AP009048 Genomic DNA Translation: BAA16354.1
PIRⁱ	D65023
RefSeqⁱ	NP_416972.4, NC_000913.3 WP_001297320.1, 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
	2LAE	NMR	-	A	101-344	[»]
	2LAF	NMR	-	A	101-344	[»]
	2YH5	X-ray	1.25	A	226-344	[»]
	2YH6	X-ray	1.55	A/B/C/D	101-212	[»]
	3SNS	X-ray	1.50	A	224-343	[»]
	3TGO	X-ray	2.90	C/D	26-344	[»]
	5AYW	X-ray	3.56	C	33-88	[»]
	5D0O	X-ray	2.90	C	1-344	[»]
	5D0Q	X-ray	3.50	C/G	1-344	[»]
	5EKQ	X-ray	3.39	C	25-344	[»]
	5LJO	electron microscopy	4.90	C	25-189	[»]
ProteinModelPortalⁱ	P0A903
SMRⁱ	P0A903
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262898, 311 interactors
ComplexPortalⁱ	CPX-1923 Bam complex
DIPⁱ	DIP-39898N
IntActⁱ	P0A903, 8 interactors
STRINGⁱ	316385.ECDH10B_2643

Protein family/group databases

TCDBⁱ	1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

TCDBⁱ

1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

2D gel databases

SWISS-2DPAGEⁱ	P0A903

SWISS-2DPAGEⁱ

P0A903

Proteomic databases

EPDⁱ	P0A903
PaxDbⁱ	P0A903
PRIDEⁱ	P0A903

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	946954
Structural Biology Knowledgebase	Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75530; AAC75530; b2477 BAA16354; BAA16354; BAA16354
GeneIDⁱ	946954
KEGGⁱ	ecj:JW2462 eco:b2477
PATRICⁱ	fig\|1411691.4.peg.4262

Organism-specific databases

EchoBASEⁱ	EB0652
EcoGeneⁱ	EG10658 bamC

Phylogenomic databases

eggNOGⁱ	ENOG4107EG0 Bacteria COG3317 LUCA
HOGENOMⁱ	HOG000123040
KOⁱ	K07287

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10658-MONOMER

BioCycⁱ

EcoCyc:EG10658-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0A903
Protein Ontology More...PROⁱ	PR:P0A903

Family and domain databases

HAMAPⁱ	MF_00924 OM_assembly_BamC, 1 hit
InterProⁱ	View protein in InterPro IPR014524 BamC IPR010653 NlpB/DapX
Pfamⁱ	View protein in Pfam PF06804 Lipoprotein_18, 1 hit
PIRSFⁱ	PIRSF026343 NlpB, 1 hit
PROSITEⁱ	View protein in PROSITE PS51257 PROKAR_LIPOPROTEIN, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BAMC_ECOLI
Accessionⁱ	P0A903Primary (citable) accession number: P0A903 Secondary accession number(s): P21167, P76564
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
	Last sequence update:	July 19, 2005
	Last modified:	November 7, 2018
	This is version 117 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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0A903 (BAMC_ECOLI)

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>

Outer membrane protein assembly factor BamC

bamC

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

<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

Protein family/group 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

GO - Cellular componenti

<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

<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

<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

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

Protein family/group 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

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ