Hspa2

Functionⁱ

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Plays a role in spermatogenesis (PubMed:24557841). In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841).By similarity1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	72	ATPBy similarity		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	13 – 16	ATPBy similarity	4
Nucleotide bindingⁱ	205 – 207	ATPBy similarity	3
Nucleotide bindingⁱ	271 – 278	ATPBy similarity	8
Nucleotide bindingⁱ	342 – 345	ATPBy similarity	4

GO - Molecular functionⁱ

ATPase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
ATPase activity, coupled
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
ATP binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chaperone binding Source: MGI
disordered domain specific binding Source: MGI
enzyme binding Source: MGI
glycolipid binding
Source: MGI
Inferred from direct assayⁱ
- 9337084
heat shock protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
misfolded protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein binding involved in protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
tau protein binding Source: MGI
unfolded protein binding Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to heat
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to unfolded protein
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chaperone cofactor-dependent protein refolding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
male meiosis I
Source: MGI
Inferred from mutant phenotypeⁱ
- 9409676
male meiotic nuclear division
Source: MGI
Inferred from mutant phenotypeⁱ
- 8622925
negative regulation of inclusion body assembly Source: MGI
positive regulation of ATPase activity
Source: CACAO
Inferred from mutant phenotypeⁱ
- 22495301
positive regulation of calcium-transporting ATPase activity
Source: CACAO
Inferred from mutant phenotypeⁱ
- 22495301
positive regulation of G2/M transition of mitotic cell cycle
Source: MGI
Inferred from mutant phenotypeⁱ
- 9247342
positive regulation of protein phosphorylation
Source: MGI
Inferred from mutant phenotypeⁱ
- 9247342
protein refolding Source: MGI
response to cold Source: AgBase
response to heat Source: AgBase
response to unfolded protein
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
spermatid development
Source: MGI
Inferred from mutant phenotypeⁱ
- 8622925
spermatogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 24557841
synaptonemal complex disassembly
Source: MGI
Inferred from mutant phenotypeⁱ
- 9409676
vesicle-mediated transport
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone
Biological process	Differentiation, Spermatogenesis, Stress response
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-3371453 Regulation of HSF1-mediated heat shock response R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-MMU-3371568 Attenuation phase

Reactomeⁱ

R-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-3371568 Attenuation phase

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Heat shock-related 70 kDa protein 2 Short name: Heat shock protein 70.2
Gene namesⁱ	Name:Hspa2 Synonyms:Hcp70.2, Hsp70-2
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 12

Organism-specific databases

MGIⁱ	MGI:96243 Hspa2

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000078259	1 – 633	Heat shock-related 70 kDa protein 2Add BLAST		633

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	403	PhosphoserineBy similarity	1
Modified residueⁱ	408	PhosphothreonineBy similarity	1
Modified residueⁱ	414	PhosphothreonineBy similarity	1
Modified residueⁱ	564	N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity	1

Keywords - PTMⁱ

Methylation, Phosphoprotein

Proteomic databases

EPDⁱ	P17156
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P17156
PaxDbⁱ	P17156
PeptideAtlas More...PeptideAtlasⁱ	P17156
PRIDEⁱ	P17156

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00331546 P17156
UCD-2DPAGEⁱ	P17156

PTM databases

iPTMnetⁱ	P17156
PhosphoSitePlusⁱ	P17156
SwissPalmⁱ	P17156

Expressionⁱ

Tissue specificityⁱ

Expressed in male germ cells (at protein level) (PubMed:24557841, PubMed:23055941, PubMed:3405224).3 Publications

Developmental stageⁱ

Specifically expressed in prophage stage of meiosis (PubMed:3405224).1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000059970 Expressed in 241 organ(s), highest expression level in testis
CleanExⁱ	MM_HSPA2
Genevisibleⁱ	P17156 MM

Interactionⁱ

Subunit structureⁱ

Interacts with FKBP6 (By similarity). Interacts with ZNF541 (PubMed:18849567). Component of the CatSper complex (PubMed:21224844). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (PubMed:23055941). Interacts with SHCBP1L; this interaction may promote the recruitment of HSPA2 to the spindle (PubMed:24557841). Interacts with MOV10L1 (PubMed:20547853).By similarity5 Publications

GO - Molecular functionⁱ

chaperone binding Source: MGI
disordered domain specific binding Source: MGI
enzyme binding Source: MGI
heat shock protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
misfolded protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein binding involved in protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
tau protein binding Source: MGI
unfolded protein binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	200453, 11 interactors
CORUMⁱ	P17156
Database of interacting proteins More...DIPⁱ	DIP-42071N
ELMⁱ	P17156
IntActⁱ	P17156, 8 interactors
Molecular INTeraction database More...MINTⁱ	P17156
STRINGⁱ	10090.ENSMUSP00000079306

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P17156
SMRⁱ	P17156
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	2 – 389	Nucleotide-binding domain (NBD)By similarityAdd BLAST		388
Regionⁱ	397 – 512	Substrate-binding domain (SBD)By similarityAdd BLAST		116

Domainⁱ

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.By similarity

Sequence similaritiesⁱ

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0101 Eukaryota COG0443 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000150862
HOGENOMⁱ	HOG000228135
HOVERGENⁱ	HBG051845
InParanoidⁱ	P17156
KEGG Orthology (KO) More...KOⁱ	K03283
OMAⁱ	QEVANPI
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03SF
TreeFamⁱ	TF105042

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.

P17156-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER 
        60         70         80         90        100
LIGDAAKNQV AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG 
       110        120        130        140        150
KPKVQVEYKG EMKTFFPEEI SSMVLTKMKE IAEAYLGGKV QSAVITVPAY 
       160        170        180        190        200
FNDSQRQATK DAGTITGLNV LRIINEPTAA AIAYGLDKKG CAGGEKNVLI 
       210        220        230        240        250
FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM VSHLAEEFKR 
       260        270        280        290        300
KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI 
       310        320        330        340        350
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ 
       360        370        380        390        400
KLLQDFFNGK ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT 
       410        420        430        440        450
PLSLGIETAG GVMTPLIKRN TTIPTKQTQT FTTYSDNQSS VLVQVYEGER 
       460        470        480        490        500
AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT FDIDANGILN VTAADKSTGK 
       510        520        530        540        550
ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA AKNAVESYTY 
       560        570        580        590        600
NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK 
       610        620        630 
ELERVCNPII SKLYQGGPGG GGSSGGPTIE EVD

Length:633

Mass (Da):69,642

Last modified:July 27, 2011 - v2

Checksum:ⁱ6F65773C7EFFA69F

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	71	A → R in AAA37859 (PubMed:3405224).Curated		1
Sequence conflictⁱ	222	V → L in AAA37859 (PubMed:3405224).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20567 Genomic DNA Translation: AAA37859.1 CH466526 Genomic DNA Translation: EDL36460.1 BC004714 mRNA Translation: AAH04714.1 BC052350 mRNA Translation: AAH52350.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS25993.1
PIRⁱ	S10859
NCBI Reference Sequences More...RefSeqⁱ	NP_001002012.1, NM_001002012.1 NP_032327.2, NM_008301.4 XP_006515547.1, XM_006515484.3
UniGeneⁱ	Mm.296181

Genome annotation databases

Ensemblⁱ	ENSMUST00000080449; ENSMUSP00000079306; ENSMUSG00000059970 ENSMUST00000219555; ENSMUSP00000151408; ENSMUSG00000059970
GeneIDⁱ	15512
KEGGⁱ	mmu:15512
UCSC genome browser More...UCSCⁱ	uc007nyf.1 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P17156	Heat shock-related 70 kDa protein 2		RAT		633	UniRef100_P17156
heat shock-related 70 kDa protein 2		MESAU		636

Protein	Similar proteins		Species	Score	Length	Source
P17156	Heat shock-related 70 kDa protein 2		RAT		633	UniRef90_P17156
Heat shock-related 70 kDa protein 2	)	HUMAN		639
Heat shock-related 70 kDa protein 2		BOVIN		636
Heat shock-related 70 kDa protein 2		CAPHI		636
Heat shock 70 kDa protein		CHICK		634
+232

Protein	Similar proteins		Species	Score	Length	Source
P17156	Heat shock protein SSA1	)	YEAST		642	UniRef50_P10591
Heat shock 70 kDa protein		SOYBN		645
Heat shock-related 70 kDa protein 2	)	HUMAN		639
Heat shock-related 70 kDa protein 2		BOVIN		636
Heat shock-related 70 kDa protein 2		CAPHI		636
+1224

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20567 Genomic DNA Translation: AAA37859.1 CH466526 Genomic DNA Translation: EDL36460.1 BC004714 mRNA Translation: AAH04714.1 BC052350 mRNA Translation: AAH52350.1
CCDSⁱ	CCDS25993.1
PIRⁱ	S10859
RefSeqⁱ	NP_001002012.1, NM_001002012.1 NP_032327.2, NM_008301.4 XP_006515547.1, XM_006515484.3
UniGeneⁱ	Mm.296181

3D structure databases

ProteinModelPortalⁱ	P17156
SMRⁱ	P17156
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	200453, 11 interactors
CORUMⁱ	P17156
DIPⁱ	DIP-42071N
ELMⁱ	P17156
IntActⁱ	P17156, 8 interactors
MINTⁱ	P17156
STRINGⁱ	10090.ENSMUSP00000079306

PTM databases

iPTMnetⁱ	P17156
PhosphoSitePlusⁱ	P17156
SwissPalmⁱ	P17156

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00331546 P17156
UCD-2DPAGEⁱ	P17156

Proteomic databases

EPDⁱ	P17156
MaxQBⁱ	P17156
PaxDbⁱ	P17156
PeptideAtlasⁱ	P17156
PRIDEⁱ	P17156

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000080449; ENSMUSP00000079306; ENSMUSG00000059970 ENSMUST00000219555; ENSMUSP00000151408; ENSMUSG00000059970
GeneIDⁱ	15512
KEGGⁱ	mmu:15512
UCSCⁱ	uc007nyf.1 mouse

Organism-specific databases

CTDⁱ	3306
MGIⁱ	MGI:96243 Hspa2

Phylogenomic databases

eggNOGⁱ	KOG0101 Eukaryota COG0443 LUCA
GeneTreeⁱ	ENSGT00930000150862
HOGENOMⁱ	HOG000228135
HOVERGENⁱ	HBG051845
InParanoidⁱ	P17156
KOⁱ	K03283
OMAⁱ	QEVANPI
OrthoDBⁱ	EOG091G03SF
TreeFamⁱ	TF105042

Enzyme and pathway databases

Reactomeⁱ	R-MMU-3371453 Regulation of HSF1-mediated heat shock response R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-MMU-3371568 Attenuation phase

Reactomeⁱ

R-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-3371568 Attenuation phase

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P17156
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000059970 Expressed in 241 organ(s), highest expression level in testis
CleanExⁱ	MM_HSPA2
Genevisibleⁱ	P17156 MM

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	HSP72_MOUSE
Accessionⁱ	P17156Primary (citable) accession number: P17156 Secondary accession number(s): Q99KD7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
	Last sequence update:	July 27, 2011
	Last modified:	November 7, 2018
	This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P17156 (HSP72_MOUSE)

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Heat shock-related 70 kDa protein 2

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

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

Cytoskeleton

Cytoskeleton

Cytosol

Mitochondrion

Nucleus

Plasma Membrane

Other locations

Keywords - 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

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

Gene expression 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

3D structure 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

<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

Gene expression 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ