UniProtKB - Q66H62 (CYLD_RAT)

BLAST

>sp|Q66H62|CYLD_RAT Ubiquitin carboxyl-terminal hydrolase CYLD OS=Rattus norvegicus OX=10116 GN=Cyld PE=1 SV=1
MSSGLWNQEKVTSPYWEERLFYLLLQECSVTDKQTQKLLRVPKGSIGQYIQDRSVGHSRV
PSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRIRLS
KGLQVDVGSPVRVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGV
YQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTVQVEPPPLEINSRVSLKV
GESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTVLLHIN
DIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSV
DSQQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSL
TKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPMPSSSGNAHGLEVGSLAEVKENPP
FYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDS
RFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYL
DSTLFCLFAFSSALDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLR
KILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNE
KVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLED
TPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHTYHPVSLPKD
LPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNI
PQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK

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History
Entry version 110 (10 Oct 2018)
Sequence version 1 (11 Oct 2004)
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Protein

Ubiquitin carboxyl-terminal hydrolase CYLD

Gene

Cyld

Organism

Rattus norvegicus (Rat)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Plays an important role in the regulation of pathways leading to NF-kappa-B activation. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (By similarity).By similarity

Catalytic activityⁱ

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	598	NucleophilePROSITE-ProRule annotation	1
Metal bindingⁱ	785	Zinc 1By similarity	1
Metal bindingⁱ	788	Zinc 1By similarity	1
Metal bindingⁱ	796	Zinc 2By similarity	1
Metal bindingⁱ	799	Zinc 2By similarity	1
Metal bindingⁱ	814	Zinc 1By similarity	1
Metal bindingⁱ	817	Zinc 1By similarity	1
Metal bindingⁱ	822	Zinc 2By similarity	1
Metal bindingⁱ	830	Zinc 2By similarity	1
Active siteⁱ	868	Proton acceptorPROSITE-ProRule annotation	1

GO - Molecular functionⁱ

Lys63-specific deubiquitinase activity Source: UniProtKB
thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
zinc ion binding Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

innate immune response Source: UniProtKB
necroptotic process Source: GO_Central
negative regulation of canonical Wnt signaling pathway Source: UniProtKB
negative regulation of JNK cascade Source: UniProtKB
negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
negative regulation of NIK/NF-kappaB signaling Source: UniProtKB
negative regulation of p38MAPK cascade Source: UniProtKB
positive regulation of extrinsic apoptotic signaling pathway Source: GO_Central
protein deubiquitination Source: UniProtKB
protein K63-linked deubiquitination Source: UniProtKB
protein linear deubiquitination Source: UniProtKB
regulation of cilium assembly Source: UniProtKB
regulation of intrinsic apoptotic signaling pathway Source: GO_Central
regulation of mitotic cell cycle Source: GO_Central
regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
ubiquitin-dependent protein catabolic process Source: InterPro
Wnt signaling pathway Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protease, Thiol protease
Biological process	Immunity, Innate immunity, Ubl conjugation pathway, Wnt signaling pathway
Ligand	Metal-binding, Zinc

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	C67.001

MEROPSⁱ

C67.001

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ubiquitin carboxyl-terminal hydrolase CYLD (EC:3.4.19.12By similarity) Alternative name(s): Deubiquitinating enzyme CYLD Ubiquitin thioesterase CYLD Ubiquitin-specific-processing protease CYLD
Gene namesⁱ	Name:Cyld Synonyms:Cyld1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [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 › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	1308346 Cyld

RGDⁱ

1308346 Cyld

Keywords - Cellular componentⁱ

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000326149	1 – 953	Ubiquitin carboxyl-terminal hydrolase CYLDAdd BLAST		953

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	384	PhosphoserineBy similarity	1
Modified residueⁱ	415	PhosphoserineCombined sources	1
Modified residueⁱ	419	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Phosphorylated on several serine residues by IKKA and/or IKKB in response to immune stimuli. Phosphorylation requires IKBKG. Phosphorylation abolishes TRAF2 deubiquitination, interferes with the activation of Jun kinases, and strongly reduces CD40-dependent gene activation by NF-kappa-B (By similarity).By similarity

Ubiquitinated. Polyubiquitinated in hepatocytes treated with palmitic acid. Ubiquitination is mediated by E3 ligase TRIM47 and leads to proteasomal degradation.By similarity

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	Q66H62
PRIDEⁱ	Q66H62

PTM databases

iPTMnetⁱ	Q66H62
PhosphoSitePlusⁱ	Q66H62

Interactionⁱ

Subunit structureⁱ

Interacts (via CAP-Gly domain) with IKBKG/NEMO (via proline-rich C-terminal region). Interacts with TRAF2 and TRIP. Interacts with PLK1, DVL1, DVL3, MAVS, TBK1, IKKE and DDX58. Interacts (via CAP-Gly domain) with microtubules. Interacts with HDAC6 and BCL3 (By similarity). Interacts with MAP3K7. Identified in a complex with TRAF6 and SQSTM1 (By similarity). Interacts with CEP350. Interacts with RNF31; the interaction is indirect and is mediated via SPATA2. Interacts with SPATA2 (via the PUB domain); the interaction is direct and recruits CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis (By similarity).By similarity

Protein-protein interaction databases

BioGridⁱ	260280, 2 interactors
STRINGⁱ	10116.ENSRNOP00000018888

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q66H62
SMRⁱ	Q66H62
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	153 – 198	CAP-Gly 1PROSITE-ProRule annotationAdd BLAST	46
Domainⁱ	253 – 286	CAP-Gly 2PROSITE-ProRule annotationAdd BLAST	34
Domainⁱ	489 – 532	CAP-Gly 3PROSITE-ProRule annotationAdd BLAST	44
Domainⁱ	589 – 947	USPAdd BLAST	359

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	106 – 590	Interaction with TRIPBy similarityAdd BLAST	485
Regionⁱ	391 – 466	Interaction with TRAF2By similarityAdd BLAST	76
Regionⁱ	467 – 681	Interaction with IKBKG/NEMOBy similarityAdd BLAST	215
Regionⁱ	778 – 830	B-boxBy similarityAdd BLAST	53

Sequence similaritiesⁱ

Belongs to the peptidase C19 family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG3556 Eukaryota ENOG410XP6I LUCA
HOGENOMⁱ	HOG000006796
HOVERGENⁱ	HBG051281
InParanoidⁱ	Q66H62
KEGG Orthology (KO) More...KOⁱ	K08601
PhylomeDBⁱ	Q66H62

Family and domain databases

Gene3Dⁱ	2.30.30.190, 3 hits
InterProⁱ	View protein in InterPro IPR036859 CAP-Gly_dom_sf IPR000938 CAP-Gly_domain IPR038765 Papain_like_cys_pep_sf IPR001394 Peptidase_C19_UCH IPR018200 USP_CS IPR028889 USP_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01302 CAP_GLY, 2 hits PF00443 UCH, 1 hit
SMARTⁱ	View protein in SMART SM01052 CAP_GLY, 3 hits
SUPFAMⁱ	SSF54001 SSF54001, 1 hit SSF74924 SSF74924, 3 hits
PROSITEⁱ	View protein in PROSITE PS00845 CAP_GLY_1, 1 hit PS50245 CAP_GLY_2, 2 hits PS00972 USP_1, 1 hit PS50235 USP_3, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

Q66H62-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSSGLWNQEK VTSPYWEERL FYLLLQECSV TDKQTQKLLR VPKGSIGQYI 
        60         70         80         90        100
QDRSVGHSRV PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL 
       110        120        130        140        150
LAITNCEERL SLFRNRIRLS KGLQVDVGSP VRVQLRSGEE KFPGVVRFRG 
       160        170        180        190        200
PLLAERTVSG IFFGVELLEE GRGQGFTDGV YQGKQLFQCD EDCGVFVALD 
       210        220        230        240        250
KLELIEDDDN GLESDFAGPG DTVQVEPPPL EINSRVSLKV GESTESGTVI 
       260        270        280        290        300
FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTVLLHIN 
       310        320        330        340        350
DIIPDSVTQE RRPPKLAFMS RGVGDKGSSS HNKPKVTGST SDPGSRNRSE 
       360        370        380        390        400
LFYTLNGSSV DSQQQSKSKN PWYIDEVAED PAKSLTEMSS DFGHSSPPPQ 
       410        420        430        440        450
PPSMNSLSSE NRFHSLPFSL TKMPNTNGSM AHSPLSLSVQ SVMGELNSTP 
       460        470        480        490        500
VQESPPMPSS SGNAHGLEVG SLAEVKENPP FYGVIRWIGQ PPGLSDVLAG 
       510        520        530        540        550
LELEDECAGC TDGTFRGTRY FTCALKKALF VKLKSCRPDS RFASLQPVSN 
       560        570        580        590        600
QIERCNSLAF GGYLSEVVEE NTPPKMEKEG LEIMIGKKKG IQGHYNSCYL 
       610        620        630        640        650
DSTLFCLFAF SSALDTVLLR PKEKNDVEYY SETQELLRTE IVNPLRIYGY 
       660        670        680        690        700
VCATKIMKLR KILEKVEAAS GFTSEEKDPE EFLNILFHDI LRVEPLLKIR 
       710        720        730        740        750
SAGQKVQDCN FYQIFMEKNE KVGVPTIQQL LEWSFINSNL KFAEAPSCLI 
       760        770        780        790        800
IQMPRFGKDF KLFKKIFPSL ELNITDLLED TPRQCRICGG LAMYECRECY 
       810        820        830        840        850
DDPDISAGKI KQFCKTCSTQ VHLHPRRLNH TYHPVSLPKD LPDWDWRHGC 
       860        870        880        890        900
IPCQKMELFA VLCIETSHYV AFVKYGKDDS AWLFFDSMAD RDGGQNGFNI 
       910        920        930        940        950
PQVTPCPEVG EYLKMSLEDL HSLDSRRIQG CARRLLCDAY MCMYQSPTMS 

LYK

Length:953

Mass (Da):106,713

Last modified:October 11, 2004 - v1

Checksum:ⁱ573B59E9BD795252

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F1LPJ6	F1LPJ6_RAT	Ubiquitin carboxyl-terminal hydrola... Ubiquitin carboxyl-terminal hydrolase CYLD	Cyld	950	Annotation score:
Q6TXJ6	Q6TXJ6_RAT	40S ribosomal protein S3a 40S ribosomal protein S3a	Cyld LOC100362727, RPS3A	454	Annotation score:

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC082001 mRNA Translation: AAH82001.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001017380.1, NM_001017380.1
UniGeneⁱ	Rn.128760 Rn.168938

Genome annotation databases

GeneIDⁱ	312937
KEGGⁱ	rno:312937

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q66H62	Ubiquitin carboxyl-terminal hydrolase CYLD	)	HUMAN		956	UniRef90_Q9NQC7
Ubiquitin carboxyl-terminal hydrolase CYLD		PONAB		956
Ubiquitin carboxyl-terminal hydrolase CYLD		BOVIN		953
Ubiquitin carboxyl-terminal hydrolase CYLD		MOUSE		952
CYLD isoform 1		PANTR		956
+230

Protein	Similar proteins		Species	Score	Length	Source
Q66H62	Ubiquitin carboxyl-terminal hydrolase CYLD	)	HUMAN		956	UniRef50_Q9NQC7
Ubiquitin carboxyl-terminal hydrolase CYLD		PONAB		956
Ubiquitin carboxyl-terminal hydrolase CYLD		BOVIN		953
Ubiquitin carboxyl-terminal hydrolase CYLD		MOUSE		952
CYLD isoform 1		PANTR		956
+606

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC082001 mRNA Translation: AAH82001.1
RefSeqⁱ	NP_001017380.1, NM_001017380.1
UniGeneⁱ	Rn.128760 Rn.168938

3D structure databases

ProteinModelPortalⁱ	Q66H62
SMRⁱ	Q66H62
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	260280, 2 interactors
STRINGⁱ	10116.ENSRNOP00000018888

Protein family/group databases

MEROPSⁱ	C67.001

MEROPSⁱ

C67.001

PTM databases

iPTMnetⁱ	Q66H62
PhosphoSitePlusⁱ	Q66H62

Proteomic databases

PaxDbⁱ	Q66H62
PRIDEⁱ	Q66H62

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	312937
KEGGⁱ	rno:312937

Organism-specific databases

CTDⁱ	1540
RGDⁱ	1308346 Cyld

Phylogenomic databases

eggNOGⁱ	KOG3556 Eukaryota ENOG410XP6I LUCA
HOGENOMⁱ	HOG000006796
HOVERGENⁱ	HBG051281
InParanoidⁱ	Q66H62
KOⁱ	K08601
PhylomeDBⁱ	Q66H62

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q66H62

PROⁱ

PR:Q66H62

Family and domain databases

Gene3Dⁱ	2.30.30.190, 3 hits
InterProⁱ	View protein in InterPro IPR036859 CAP-Gly_dom_sf IPR000938 CAP-Gly_domain IPR038765 Papain_like_cys_pep_sf IPR001394 Peptidase_C19_UCH IPR018200 USP_CS IPR028889 USP_dom
Pfamⁱ	View protein in Pfam PF01302 CAP_GLY, 2 hits PF00443 UCH, 1 hit
SMARTⁱ	View protein in SMART SM01052 CAP_GLY, 3 hits
SUPFAMⁱ	SSF54001 SSF54001, 1 hit SSF74924 SSF74924, 3 hits
PROSITEⁱ	View protein in PROSITE PS00845 CAP_GLY_1, 1 hit PS50245 CAP_GLY_2, 2 hits PS00972 USP_1, 1 hit PS50235 USP_3, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CYLD_RAT
Accessionⁱ	Q66H62Primary (citable) accession number: Q66H62
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
	Last sequence update:	October 11, 2004
	Last modified:	October 10, 2018
	This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

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Supporting data

UniProtKB - Q66H62 (CYLD_RAT)

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Ubiquitin carboxyl-terminal hydrolase CYLD

Cyld

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

<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

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

Cytoskeleton

Plasma membrane

Other locations

Cytoskeleton

Cytosol

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

PTM 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

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

<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

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ