Nek2

Functionⁱ

Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (By similarity). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (By similarity). Phosphorylates and activates NEK11 in G1/S-arrested cells. Involved in the regulation of centrosome disjunction (By similarity).By similarity2 Publications

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.

Cofactorⁱ

Mg²⁺

Activity regulationⁱ

Its catalytic activity is inhibited by the inhibitor CCT241950. In the presence of this inhibitor, displays an autoinhibited conformation: Tyr-70 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	37	ATPPROSITE-ProRule annotation		1
Active siteⁱ	141	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	14 – 22	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
metal ion binding Source: UniProtKB-KW
protein kinase activity
Source: MGI
Inferred from direct assayⁱ
- 14668482
- 14697346
protein phosphatase binding Source: MGI
protein serine/threonine kinase activity Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

blastocyst development
Source: MGI
Inferred from mutant phenotypeⁱ
- 19117032
cell division Source: UniProtKB-KW
centrosome separation Source: MGI
chromosome segregation
Source: MGI
Inferred from mutant phenotypeⁱ
- 19117032
meiotic cell cycle Source: UniProtKB-KW
mitotic sister chromatid segregation
Source: MGI
Inferred from mutant phenotypeⁱ
- 15479717
mitotic spindle assembly
Source: MGI
Inferred from mutant phenotypeⁱ
- 19117032
negative regulation of centriole-centriole cohesion Source: MGI
negative regulation of DNA binding
Source: MGI
Inferred from direct assayⁱ
- 14668482
positive regulation of telomerase activity Source: MGI
positive regulation of telomere capping Source: MGI
positive regulation of telomere maintenance via telomerase Source: MGI
protein autophosphorylation Source: UniProtKB
protein phosphorylation
Source: MGI
Inferred from direct assayⁱ
- 14697346
regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
regulation of mitotic centrosome separation Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Serine/threonine-protein kinase, Transferase
Biological process	Cell cycle, Cell division, Chromosome partition, Meiosis, Mitosis
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition R-MMU-380259 Loss of Nlp from mitotic centrosomes R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes R-MMU-380320 Recruitment of NuMA to mitotic centrosomes R-MMU-5620912 Anchoring of the basal body to the plasma membrane R-MMU-8854518 AURKA Activation by TPX2

Reactomeⁱ

R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-380259 Loss of Nlp from mitotic centrosomes
R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-5620912 Anchoring of the basal body to the plasma membrane
R-MMU-8854518 AURKA Activation by TPX2

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Serine/threonine-protein kinase Nek2 (EC:2.7.11.1) Alternative name(s): Never in mitosis A-related kinase 2 Short name: NimA-related protein kinase 2
Gene namesⁱ	Name:Nek2
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 1

Organism-specific databases

MGIⁱ	MGI:109359 Nek2

Keywords - Cellular componentⁱ

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000086422	1 – 443	Serine/threonine-protein kinase Nek2Add BLAST		443

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	170	Phosphothreonine; by autocatalysisBy similarity	1
Modified residueⁱ	171	Phosphoserine; by autocatalysisBy similarity	1
Modified residueⁱ	175	Phosphothreonine; by autocatalysisBy similarity	1
Modified residueⁱ	179	Phosphothreonine; by autocatalysisBy similarity	1
Modified residueⁱ	184	PhosphoserineBy similarity	1
Modified residueⁱ	241	Phosphoserine; by autocatalysisBy similarity	1
Modified residueⁱ	300	PhosphoserineBy similarity	1
Modified residueⁱ	356	Phosphoserine; by STK3/MST2By similarity	1
Modified residueⁱ	389	PhosphoserineBy similarity	1
Modified residueⁱ	396	PhosphoserineBy similarity	1
Modified residueⁱ	401	PhosphoserineBy similarity	1
Modified residueⁱ	436	Phosphoserine; by STK3/MST2By similarity	1

Post-translational modificationⁱ

Activated by autophosphorylation. Protein phosphatase 1 represses autophosphorylation and activation of isoform 1 by dephosphorylation. Phosphorylation by STK3/MST2 is necessary for its localization to the centrosome.By similarity

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O35942
PaxDbⁱ	O35942
PRIDEⁱ	O35942

PTM databases

iPTMnetⁱ	O35942
PhosphoSitePlusⁱ	O35942

Expressionⁱ

Tissue specificityⁱ

Most abundantly expressed in testis. Low levels found in mid-gestation embryo, ovary, placenta, intestine, thymus and skin. Within the testis, expression restricted to germ cells with highest levels detected in spermatocytes at pachytene and diplotene stages. Also expressed in meiotic pachytene oocytes.2 Publications

Gene expression databases

Bgeeⁱ	ENSMUSG00000026622 Expressed in 195 organ(s), highest expression level in testis
Genevisibleⁱ	O35942 MM

Interactionⁱ

Subunit structureⁱ

Forms homodimers and heterodimers. Interacts with CDC20, CTNB1, MAD1L1, MAD2L1, MAPK, NEK11, NPM1, NDC80, PCNT, PPP1CA, PPP1CC and SGO1. Interacts with STK3/MST2 (via SARAH domain) and SAV1 (via SARAH domain) (By similarity). Interacts with NECAB3 and HMGA2 (PubMed:14697346, PubMed:14668482). Interacts with CEP68; the interaction leads to phosphorylation of CEP68. Interacts with CNTLN; the interaction leads to phosphorylation of CNTLN. Interacts with CEP85 (By similarity).By similarity2 Publications

GO - Molecular functionⁱ

protein phosphatase binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	201728, 38 interactors
IntActⁱ	O35942, 37 interactors
STRINGⁱ	10090.ENSMUSP00000027931

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	O35942
SMRⁱ	O35942
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	8 – 271	Protein kinasePROSITE-ProRule annotationAdd BLAST		264

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	264 – 443	Interaction with PCNTBy similarityAdd BLAST	180
Regionⁱ	301 – 443	Interaction with CEP85By similarityAdd BLAST	143
Regionⁱ	306 – 334	Leucine-zipperAdd BLAST	29
Regionⁱ	329 – 443	Necessary for interaction with MAD1L1By similarityAdd BLAST	115
Regionⁱ	333 – 370	Required for microtubule binding and for localization to the centrosomesBy similarityAdd BLAST	38
Regionⁱ	402 – 437	Interaction with SAV1 and STK3/MST2By similarityAdd BLAST	36

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	303 – 361	Sequence analysisAdd BLAST		59
Coiled coilⁱ	403 – 427	Sequence analysisAdd BLAST		25

Domainⁱ

The leucine-zipper domain is required for its dimerization and activation.By similarity

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.Curated

Keywords - Domainⁱ

Coiled coil

Phylogenomic databases

eggNOGⁱ	KOG0591 Eukaryota ENOG410XNQP LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118997
HOGENOMⁱ	HOG000233029
HOVERGENⁱ	HBG006461
InParanoidⁱ	O35942
KEGG Orthology (KO) More...KOⁱ	K20872
OMAⁱ	AYNQKEL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07PD
TreeFamⁱ	TF101184

Family and domain databases

InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

O35942-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPSRVEDYEV LHSIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEVEKQ 
        60         70         80         90        100
MLVSEVNLLR ELKHPNIVSY YDRIIDRTNT TLYIVMEYCE GGDLASVISK 
       110        120        130        140        150
GTKDRQYLEE EFVLRVMTQL TLALKECHRR SDGGHTVLHR DLKPANVFLD 
       160        170        180        190        200
SKHNVKLGDF GLARILNHDT SFAKTFVGTP YYMSPEQMSC LSYNEKSDIW 
       210        220        230        240        250
SLGCLLYELC ALMPPFTAFN QKELAGKIRE GRFRRIPYRY SDGLNDLITR 
       260        270        280        290        300
MLNLKDYHRP SVEEILESPL IADLVAEEQR RNLERRGRRS GEPSKLPDSS 
       310        320        330        340        350
PVLSELKLKE RQLQDREQAL RAREDILEQK ERELCIRERL AEDKLARAES 
       360        370        380        390        400
LMKNYSLLKE HRLLCLAGGP ELDLPSSAMK KKVHFHGESK ENTARSENSE 
       410        420        430        440 
SYLAKSKCRD LKKRLHAAQL RAQALADIEK NYQLKSRQIL GMR

Length:443

Mass (Da):51,243

Last modified:July 27, 2011 - v2

Checksum:ⁱ1EF2CA320F60FB5C

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	69	S → R in AAB67973 (PubMed:9187143).Curated	1
Sequence conflictⁱ	69	S → R in AAC35393 (PubMed:9583679).Curated	1
Sequence conflictⁱ	69	S → R in AAB70470 (PubMed:9434622).Curated	1
Sequence conflictⁱ	203	G → A in AAB67973 (PubMed:9187143).Curated	1
Sequence conflictⁱ	253	N → F in AAB67973 (PubMed:9187143).Curated	1
Sequence conflictⁱ	274	L → M in AAB67973 (PubMed:9187143).Curated	1
Sequence conflictⁱ	274	L → M in AAC35393 (PubMed:9583679).Curated	1
Sequence conflictⁱ	274	L → M in AAB70470 (PubMed:9434622).Curated	1
Sequence conflictⁱ	311	R → S in AAB67973 (PubMed:9187143).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U95610 mRNA Translation: AAB67973.1 AF013166 mRNA Translation: AAC35393.1 AF007247 mRNA Translation: AAB70470.1 AK147072 mRNA Translation: BAE27653.1 AK164467 mRNA Translation: BAE37799.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS15623.1
NCBI Reference Sequences More...RefSeqⁱ	NP_035022.2, NM_010892.3
UniGeneⁱ	Mm.33773 Mm.403999

Genome annotation databases

Ensemblⁱ	ENSMUST00000027931; ENSMUSP00000027931; ENSMUSG00000026622 ENSMUST00000213394; ENSMUSP00000149034; ENSMUSG00000110797
GeneIDⁱ	18005
KEGGⁱ	mmu:18005
UCSC genome browser More...UCSCⁱ	uc007ecx.2 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O35942	Uncharacterized protein		MOUSE		400	UniRef100_O35942

Protein	Similar proteins		Species	Score	Length	Source
O35942	Uncharacterized protein		MOUSE		400	UniRef90_O35942
NIMA (never in mitosis gene a)-related kinase 2-like 1		RAT		443
Uncharacterized protein		NEOLE		429
Serine/threonine-protein kinase Nek2		CRIGR		400
UPI000B4EDE37		MERUN		444
+13

Protein	Similar proteins		Species	Score	Length	Source
O35942	Serine/threonine-protein kinase Nek2	)	HUMAN		445	UniRef50_P51955
Uncharacterized protein		RHIBE		454
Serine/threonine-protein kinase Nek2		MYOBR		445
NEK2 isoform 2		PANTR		445
Uncharacterized protein		PANPA		445
+416

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U95610 mRNA Translation: AAB67973.1 AF013166 mRNA Translation: AAC35393.1 AF007247 mRNA Translation: AAB70470.1 AK147072 mRNA Translation: BAE27653.1 AK164467 mRNA Translation: BAE37799.1
CCDSⁱ	CCDS15623.1
RefSeqⁱ	NP_035022.2, NM_010892.3
UniGeneⁱ	Mm.33773 Mm.403999

3D structure databases

ProteinModelPortalⁱ	O35942
SMRⁱ	O35942
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	201728, 38 interactors
IntActⁱ	O35942, 37 interactors
STRINGⁱ	10090.ENSMUSP00000027931

PTM databases

iPTMnetⁱ	O35942
PhosphoSitePlusⁱ	O35942

Proteomic databases

MaxQBⁱ	O35942
PaxDbⁱ	O35942
PRIDEⁱ	O35942

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000027931; ENSMUSP00000027931; ENSMUSG00000026622 ENSMUST00000213394; ENSMUSP00000149034; ENSMUSG00000110797
GeneIDⁱ	18005
KEGGⁱ	mmu:18005
UCSCⁱ	uc007ecx.2 mouse

Organism-specific databases

CTDⁱ	4751
MGIⁱ	MGI:109359 Nek2

Phylogenomic databases

eggNOGⁱ	KOG0591 Eukaryota ENOG410XNQP LUCA
GeneTreeⁱ	ENSGT00760000118997
HOGENOMⁱ	HOG000233029
HOVERGENⁱ	HBG006461
InParanoidⁱ	O35942
KOⁱ	K20872
OMAⁱ	AYNQKEL
OrthoDBⁱ	EOG091G07PD
TreeFamⁱ	TF101184

Enzyme and pathway databases

Reactomeⁱ	R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition R-MMU-380259 Loss of Nlp from mitotic centrosomes R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes R-MMU-380320 Recruitment of NuMA to mitotic centrosomes R-MMU-5620912 Anchoring of the basal body to the plasma membrane R-MMU-8854518 AURKA Activation by TPX2

Reactomeⁱ

R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-380259 Loss of Nlp from mitotic centrosomes
R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-5620912 Anchoring of the basal body to the plasma membrane
R-MMU-8854518 AURKA Activation by TPX2

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:O35942
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000026622 Expressed in 195 organ(s), highest expression level in testis
Genevisibleⁱ	O35942 MM

Family and domain databases

InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR008271 Ser/Thr_kinase_AS
Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NEK2_MOUSE
Accessionⁱ	O35942Primary (citable) accession number: O35942 Secondary accession number(s): O35959, Q3TPD7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
	Last sequence update:	July 27, 2011
	Last modified:	September 12, 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
Human and mouse protein kinases
Human and mouse protein kinases: classification and index

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UniProtKB - O35942 (NEK2_MOUSE)

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Serine/threonine-protein kinase Nek2

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

Nucleus

Other locations

Cytoskeleton

Nucleus

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

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

Domains and Repeats

Region

Coiled coil

<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

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

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

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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

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ