UniProtKB - P00782 (SUBT_BACAM)

BLAST

>sp|P00782|SUBT_BACAM Subtilisin BPN' OS=Bacillus amyloliquefaciens OX=1390 GN=apr PE=1 SV=1
MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVI
SEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKA
PALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVA
ALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSA
ALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVG
PELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT
TTKLGDSFYYGKGLINVQAAAQ

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History
Entry version 155 (12 Sep 2018)
Sequence version 1 (21 Jul 1986)
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Protein

Subtilisin BPN'

Gene

apr

Organism

Bacillus amyloliquefaciens (Bacillus velezensis)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.1 Publication

Miscellaneous

Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.

Catalytic activityⁱ

Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

Cofactorⁱ

Ca²⁺Note: Binds 2 calcium ions per subunit.

Activity regulationⁱ

Completely inhibited by phenylmethylsulfony fluoride (PMSF) and partially inhibited by benzamidine hydrochloride, leupeptin, and pepstatin A.1 Publication

pH dependenceⁱ

Optimum pH is 9.0.1 Publication

Temperature dependenceⁱ

Optimum temperature is 48 degrees Celsius.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	109	Calcium 1	1
Active siteⁱ	139	Charge relay system1 Publication	1
Metal bindingⁱ	148	Calcium 1	1
Active siteⁱ	171	Charge relay system1 Publication	1
Metal bindingⁱ	182	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	184	Calcium 1	1
Metal bindingⁱ	186	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	188	Calcium 1; via carbonyl oxygen	1
Metal bindingⁱ	276	Calcium 2; via carbonyl oxygen	1
Metal bindingⁱ	278	Calcium 2; via carbonyl oxygen	1
Metal bindingⁱ	281	Calcium 2; via carbonyl oxygen	1
Active siteⁱ	328	Charge relay system1 Publication	1

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
serine-type endopeptidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 12524032

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

fibrinolysis
Source: UniProtKB
Inferred from direct assayⁱ
- 12524032
proteolysis
Source: UniProtKB
Inferred from direct assayⁱ
- 12524032
sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protease, Serine protease
Biological process	Sporulation
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	3.4.21.62 630
SABIO-RKⁱ	P00782

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	I09.001

MEROPSⁱ

I09.001

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Subtilisin BPN' (EC:3.4.21.62) Alternative name(s): Alkaline protease Subtilisin DFE Subtilisin Novo
Gene namesⁱ	Name:apr
Organismⁱ	Bacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifierⁱ	1390 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus amyloliquefaciens group

Subcellular locationⁱ

Secreted

GO - Cellular componentⁱ

extracellular region Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Biotechnological useⁱ

Used as a detergent protease. Sold under the name Alcalase by Novozymes.

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03297 Benzylsulfinic Acid DB04491 Diisopropylphosphono Group DB02442 Dioxyselenocysteine DB02325 Isopropyl Alcohol DB01805 Monoisopropylphosphorylserine DB01915 S-Hydroxycysteine

DrugBankⁱ

DB03297 Benzylsulfinic Acid
DB04491 Diisopropylphosphono Group
DB02442 Dioxyselenocysteine
DB02325 Isopropyl Alcohol
DB01805 Monoisopropylphosphorylserine
DB01915 S-Hydroxycysteine

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 30	By similarityAdd BLAST	30
PropeptideⁱPRO_0000027177	31 – 107	2 PublicationsAdd BLAST	77
ChainⁱPRO_0000027178	108 – 382	Subtilisin BPN'Add BLAST	275

Keywords - PTMⁱ

Zymogen

Proteomic databases

PRIDEⁱ	P00782

PRIDEⁱ

P00782

Miscellaneous databases

PMAP-CutDBⁱ	P00782

PMAP-CutDBⁱ

P00782

Interactionⁱ

Subunit structureⁱ

Monomer.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Ica-2	Q40059	8	EBI-1033955,EBI-1040468	From Hordeum vulgare.

With

Entry

#Exp.

IntAct

Notes

Ica-2

Q40059

EBI-1033955,EBI-1040468

From Hordeum vulgare.

Protein-protein interaction databases

IntActⁱ	P00782, 2 interactors
Molecular INTeraction database More...MINTⁱ	P00782

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	39 – 44	Combined sources	6
Turnⁱ	46 – 49	Combined sources	4
Helixⁱ	53 – 61	Combined sources	9
Turnⁱ	62 – 64	Combined sources	3
Beta strandⁱ	66 – 70	Combined sources	5
Beta strandⁱ	72 – 80	Combined sources	9
Helixⁱ	83 – 90	Combined sources	8
Beta strandⁱ	95 – 100	Combined sources	6
Beta strandⁱ	103 – 106	Combined sources	4
Helixⁱ	113 – 117	Combined sources	5
Helixⁱ	120 – 126	Combined sources	7
Beta strandⁱ	134 – 140	Combined sources	7
Beta strandⁱ	146 – 148	Combined sources	3
Beta strandⁱ	151 – 156	Combined sources	6
Beta strandⁱ	158 – 160	Combined sources	3
Beta strandⁱ	168 – 170	Combined sources	3
Helixⁱ	171 – 180	Combined sources	10
Beta strandⁱ	183 – 188	Combined sources	6
Helixⁱ	189 – 191	Combined sources	3
Beta strandⁱ	195 – 201	Combined sources	7
Beta strandⁱ	207 – 209	Combined sources	3
Helixⁱ	211 – 223	Combined sources	13
Beta strandⁱ	227 – 231	Combined sources	5
Beta strandⁱ	233 – 236	Combined sources	4
Helixⁱ	240 – 251	Combined sources	12
Beta strandⁱ	255 – 259	Combined sources	5
Turnⁱ	275 – 277	Combined sources	3
Beta strandⁱ	281 – 287	Combined sources	7
Beta strandⁱ	289 – 291	Combined sources	3
Beta strandⁱ	305 – 308	Combined sources	4
Beta strandⁱ	310 – 316	Combined sources	7
Turnⁱ	317 – 319	Combined sources	3
Beta strandⁱ	320 – 324	Combined sources	5
Helixⁱ	327 – 344	Combined sources	18
Helixⁱ	350 – 358	Combined sources	9
Beta strandⁱ	360 – 362	Combined sources	3
Helixⁱ	367 – 370	Combined sources	4
Helixⁱ	377 – 380	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P00782
SMRⁱ	P00782
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P00782

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	134 – 380	Peptidase S8Add BLAST		247

Sequence similaritiesⁱ

Belongs to the peptidase S8 family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	COG1404 LUCA

eggNOGⁱ

COG1404 LUCA

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd07477 Peptidases_S8_Subtilisin_subse, 1 hit
Gene3Dⁱ	3.30.70.80, 1 hit 3.40.50.200, 1 hit
InterProⁱ	View protein in InterPro IPR000209 Peptidase_S8/S53_dom IPR036852 Peptidase_S8/S53_dom_sf IPR023827 Peptidase_S8_Asp-AS IPR022398 Peptidase_S8_His-AS IPR023828 Peptidase_S8_Ser-AS IPR015500 Peptidase_S8_subtilisin-rel IPR010259 S8pro/Inhibitor_I9 IPR037045 S8pro/Inhibitor_I9_sf IPR034202 Subtilisin_Carlsberg-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05922 Inhibitor_I9, 1 hit PF00082 Peptidase_S8, 1 hit
PRINTSⁱ	PR00723 SUBTILISIN
SUPFAMⁱ	SSF52743 SSF52743, 1 hit
PROSITEⁱ	View protein in PROSITE PS00136 SUBTILASE_ASP, 1 hit PS00137 SUBTILASE_HIS, 1 hit PS00138 SUBTILASE_SER, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P00782-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST 
        60         70         80         90        100
MSAAKKKDVI SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE 
       110        120        130        140        150
DHVAHAYAQS VPYGVSQIKA PALHSQGYTG SNVKVAVIDS GIDSSHPDLK 
       160        170        180        190        200
VAGGASMVPS ETNPFQDNNS HGTHVAGTVA ALNNSIGVLG VAPSASLYAV 
       210        220        230        240        250
KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA ALKAAVDKAV 
       260        270        280        290        300
ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG 
       310        320        330        340        350
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN 
       360        370        380 
TQVRSSLENT TTKLGDSFYY GKGLINVQAA AQ

Length:382

Mass (Da):39,181

Last modified:July 21, 1986 - v1

Checksum:ⁱED987DAFA37B8335

Sequence cautionⁱ

The sequence CAA24990 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	128	Y → F in strain: DC-4. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	K02496 Genomic DNA Translation: AAB05345.1 X00165 Genomic DNA Translation: CAA24990.1 Different initiation.
PIRⁱ	B25415 SUBSN
NCBI Reference Sequences More...RefSeqⁱ	WP_013351733.1, NZ_MOEA01000001.1

Genome annotation databases

GeneIDⁱ	9780852

GeneIDⁱ

9780852

Protein	Similar proteins		Species	Score	Length	Source
P00782	AprE		BACAM		382	UniRef100_P00782
Peptidase S8		BACIU		382
UPI000002CFD0		BACIU		275

Protein	Similar proteins		Species	Score	Length	Source
P00782	AprE		BACAM		382	UniRef90_P00782
Peptidase S8		BACIU		382
Subtilisin		Bacillus sp. VMFN-A1		382
Subtilisin (Fragment)		Bacillus sp. SJ		352
Extracellular alkaline serine protease		BRELA		382
+62

Protein	Similar proteins		Species	Score	Length	Source
P00782	Subtilisin Carlsberg	)	BACLI		379	UniRef50_P00782
Subtilisin E	)	BACSU		381
Subtilisin amylosacchariticus		BACSA		381
Subtilisin NAT	)	BACNA		381
Subtilisin J		GEOSE		381
+477

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	K02496 Genomic DNA Translation: AAB05345.1 X00165 Genomic DNA Translation: CAA24990.1 Different initiation.
PIRⁱ	B25415 SUBSN
RefSeqⁱ	WP_013351733.1, NZ_MOEA01000001.1

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
	1A2Q	X-ray	1.80	A	108-382	[»]
	1AK9	X-ray	1.80	A	108-382	[»]
	1AQN	X-ray	1.80	A	108-382	[»]
	1AU9	X-ray	1.80	A	108-382	[»]
	1DUI	X-ray	2.00	A	108-382	[»]
	1GNS	X-ray	1.80	A	112-382	[»]
	1GNV	X-ray	1.90	A	108-382	[»]
	1LW6	X-ray	1.50	E	108-382	[»]
	1S01	X-ray	1.70	A	108-382	[»]
	1S02	X-ray	1.90	A	108-382	[»]
	1SBH	X-ray	1.80	A	108-382	[»]
	1SBI	X-ray	2.20	A	108-382	[»]
	1SBN	X-ray	2.10	E	108-382	[»]
	1SBT	X-ray	2.50	A	108-382	[»]
	1SIB	X-ray	2.40	E	108-382	[»]
	1SPB	X-ray	2.00	P	37-107	[»]
				S	108-382	[»]
	1ST2	X-ray	2.00	A	108-382	[»]
	1SUA	X-ray	2.10	A	108-382	[»]
	1SUB	X-ray	1.75	A	108-382	[»]
	1SUC	X-ray	1.80	A	108-382	[»]
	1SUD	X-ray	1.90	A	108-382	[»]
	1SUE	X-ray	1.80	A	108-382	[»]
	1SUP	X-ray	1.60	A	108-382	[»]
	1TM1	X-ray	1.70	E	108-382	[»]
	1TM3	X-ray	1.57	E	108-382	[»]
	1TM4	X-ray	1.70	E	108-382	[»]
	1TM5	X-ray	1.45	E	108-382	[»]
	1TM7	X-ray	1.59	E	108-382	[»]
	1TMG	X-ray	1.67	E	108-382	[»]
	1TO1	X-ray	1.68	E	108-382	[»]
	1TO2	X-ray	1.30	E	108-382	[»]
	1UBN	X-ray	2.40	A	108-382	[»]
	1V5I	X-ray	1.50	A	108-382	[»]
	1Y1K	X-ray	1.56	E	108-382	[»]
	1Y33	X-ray	1.80	E	108-382	[»]
	1Y34	X-ray	1.55	E	108-382	[»]
	1Y3B	X-ray	1.80	E	108-382	[»]
	1Y3C	X-ray	1.69	E	108-382	[»]
	1Y3D	X-ray	1.80	E	108-382	[»]
	1Y3F	X-ray	1.72	E	108-382	[»]
	1Y48	X-ray	1.84	E	108-382	[»]
	1Y4A	X-ray	1.60	E	108-382	[»]
	1Y4D	X-ray	2.00	E	108-382	[»]
	1YJA	X-ray	1.80	A	108-382	[»]
	1YJB	X-ray	1.80	A	108-382	[»]
	1YJC	X-ray	1.80	A	108-382	[»]
	2SBT	X-ray	2.80	A	108-382	[»]
	2SIC	X-ray	1.80	E	108-382	[»]
	2SNI	X-ray	2.10	E	108-382	[»]
	2ST1	X-ray	1.80	A	108-382	[»]
	3BGO	X-ray	1.80	P	32-111	[»]
				S	108-382	[»]
	3CNQ	X-ray	1.71	P	32-111	[»]
				S	108-382	[»]
	3CO0	X-ray	1.93	P	32-111	[»]
				S	108-382	[»]
	3F49	X-ray	1.70	S	108-382	[»]
	3SIC	X-ray	1.80	E	108-382	[»]
	5OX2	X-ray	2.24	A	108-382	[»]
	5SIC	X-ray	2.20	E	108-382	[»]
ProteinModelPortalⁱ	P00782
SMRⁱ	P00782
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P00782, 2 interactors
MINTⁱ	P00782

Chemistry databases

DrugBankⁱ	DB03297 Benzylsulfinic Acid DB04491 Diisopropylphosphono Group DB02442 Dioxyselenocysteine DB02325 Isopropyl Alcohol DB01805 Monoisopropylphosphorylserine DB01915 S-Hydroxycysteine

DrugBankⁱ

DB03297 Benzylsulfinic Acid
DB04491 Diisopropylphosphono Group
DB02442 Dioxyselenocysteine
DB02325 Isopropyl Alcohol
DB01805 Monoisopropylphosphorylserine
DB01915 S-Hydroxycysteine

Protein family/group databases

MEROPSⁱ	I09.001

MEROPSⁱ

I09.001

Proteomic databases

PRIDEⁱ	P00782

PRIDEⁱ

P00782

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	9780852

GeneIDⁱ

9780852

Phylogenomic databases

eggNOGⁱ	COG1404 LUCA

eggNOGⁱ

COG1404 LUCA

Enzyme and pathway databases

BRENDAⁱ	3.4.21.62 630
SABIO-RKⁱ	P00782

Miscellaneous databases

EvolutionaryTraceⁱ	P00782
PMAP-CutDBⁱ	P00782

Family and domain databases

CDDⁱ	cd07477 Peptidases_S8_Subtilisin_subse, 1 hit
Gene3Dⁱ	3.30.70.80, 1 hit 3.40.50.200, 1 hit
InterProⁱ	View protein in InterPro IPR000209 Peptidase_S8/S53_dom IPR036852 Peptidase_S8/S53_dom_sf IPR023827 Peptidase_S8_Asp-AS IPR022398 Peptidase_S8_His-AS IPR023828 Peptidase_S8_Ser-AS IPR015500 Peptidase_S8_subtilisin-rel IPR010259 S8pro/Inhibitor_I9 IPR037045 S8pro/Inhibitor_I9_sf IPR034202 Subtilisin_Carlsberg-like
Pfamⁱ	View protein in Pfam PF05922 Inhibitor_I9, 1 hit PF00082 Peptidase_S8, 1 hit
PRINTSⁱ	PR00723 SUBTILISIN
SUPFAMⁱ	SSF52743 SSF52743, 1 hit
PROSITEⁱ	View protein in PROSITE PS00136 SUBTILASE_ASP, 1 hit PS00137 SUBTILASE_HIS, 1 hit PS00138 SUBTILASE_SER, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SUBT_BACAM
Accessionⁱ	P00782Primary (citable) accession number: P00782 Secondary accession number(s): P83945, Q44684
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	September 12, 2018
	This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

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Annotation systems

Supporting data

UniProtKB - P00782 (SUBT_BACAM)

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Subtilisin BPN'

apr

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>pH dependencei

Temperature dependencei

Sites

<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

<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

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Chemistry databases

<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

Keywords - PTMi

Proteomic databases

Miscellaneous 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

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

Domains and Repeats

<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

Natural variant

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

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation 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

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Functionⁱ

pH dependenceⁱ

Temperature dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Biotechnological useⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ