RNF111

Functionⁱ

E3 ubiquitin-protein ligase (PubMed:26656854). Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019, PubMed:16601693). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (PubMed:14657019, PubMed:16601693). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (PubMed:17591695). Associates with UBE2D2 as an E2 enzyme (PubMed:22411132). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23751493). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (PubMed:23751493). Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity).By similarity6 Publications

Catalytic activityⁱ

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication

Activity regulationⁱ

Binds free ubiquitin non-covalently via its RING-type zinc finger. Ubiquitin-binding leads to enhance the E3 ubiquitin-protein ligase activity by stabilizing the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and activating ubiquitin transfer.By similarity

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.6 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	942	ZincBy similarity	1
Metal bindingⁱ	945	ZincBy similarity	1
Metal bindingⁱ	965	ZincBy similarity	1
Metal bindingⁱ	968	ZincBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	942 – 983	RING-type; atypicalPROSITE-ProRule annotationAdd BLAST		42

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
SMAD binding Source: Ensembl
SUMO polymer binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23086935
ubiquitin protein ligase activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 16601693

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

global genome nucleotide-excision repair Source: Reactome
pattern specification process Source: Ensembl
positive regulation of protein ubiquitination Source: Ensembl
positive regulation of transcription, DNA-templated
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 16601693
positive regulation of transcription by RNA polymerase II Source: Reactome
positive regulation of transforming growth factor beta receptor signaling pathway Source: GO_Central
proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
protein polyubiquitination Source: GO_Central
protein ubiquitination
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 16601693
ubiquitin-dependent SMAD protein catabolic process Source: GO_Central

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein, Transferase
Biological process	DNA damage, DNA repair, Ubl conjugation pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	6.3.2.19 2681
Reactomeⁱ	R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkⁱ	Q6ZNA4
SIGNORⁱ	Q6ZNA4
UniPathwayⁱ	UPA00143

Protein family/group databases

MoonDBⁱ	Q6ZNA4 Predicted

MoonDBⁱ

Q6ZNA4 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: E3 ubiquitin-protein ligase Arkadia1 Publication (EC:2.3.2.271 Publication) Alternative name(s): RING finger protein 111Imported Short name: hRNF1111 Publication RING-type E3 ubiquitin transferase ArkadiaCurated
Gene namesⁱ	Name:RNF111Imported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [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 › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000157450.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17384 RNF111
MIMⁱ	605840 gene
neXtProtⁱ	NX_Q6ZNA4

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	300 – 303	VVVI → AAAA or AVAA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 326-A--A-329 and 382-A--A-385. 1 Publication	4
Mutagenesisⁱ	326 – 329	VEIV → AAAA or AEAA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 300-A--A-303 and 382-A--A-385. 1 Publication	4
Mutagenesisⁱ	382 – 385	VVDL → AAAA or AADA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 300-A--A-303 and 326-A--A-329. 1 Publication	4
Mutagenesisⁱ	382	V → A: Abolishes SUMO binding. 1 Publication	1
Mutagenesisⁱ	382	V → L: Loss of affinity to SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	382	V → Y: No loss of affinity toward SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	383	V → A: Abolishes SUMO binding. 1 Publication	1
Mutagenesisⁱ	383	V → I: No loss of affinity toward SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	384	D → A: Abolishes SUMO binding. 1 Publication	1
Mutagenesisⁱ	384	D → E: Loss of affinity to SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	384	D → N: Loss of affinity to SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	385	L → A: Abolishes SUMO binding. 1 Publication	1
Mutagenesisⁱ	385	L → I: Loss of affinity to SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	386	T → A: Abolishes SUMO binding. 1 Publication	1
Mutagenesisⁱ	386	T → S: Loss of affinity to SUMO1 and SUMO2. 1 Publication	1
Mutagenesisⁱ	386	T → V: Loss of affinity to SUMO1 and SUMO2. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	54778
Open Targets More...OpenTargetsⁱ	ENSG00000157450
PharmGKBⁱ	PA134868772

Polymorphism and mutation databases

BioMutaⁱ	RNF111
DMDMⁱ	308153555

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000280690	1 – 994	E3 ubiquitin-protein ligase ArkadiaAdd BLAST		994

Amino acid modifications

Feature key	Position(s)	DescriptionActions
Cross-linkⁱ	19	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	28	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	34	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	47	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	59	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	73	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	87	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	96	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	110	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	173	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	198	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	218	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	923	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	927	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMⁱ

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q6ZNA4
PaxDbⁱ	Q6ZNA4
PeptideAtlas More...PeptideAtlasⁱ	Q6ZNA4
PRIDEⁱ	Q6ZNA4
ProteomicsDBⁱ	68002 68003 [Q6ZNA4-2] 68004 [Q6ZNA4-3]

PTM databases

iPTMnetⁱ	Q6ZNA4
PhosphoSitePlusⁱ	Q6ZNA4

Expressionⁱ

Tissue specificityⁱ

Broadly expressed.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000157450 Expressed in 224 organ(s), highest expression level in secondary oocyte
CleanExⁱ	HS_RNF111
ExpressionAtlasⁱ	Q6ZNA4 baseline and differential
Genevisibleⁱ	Q6ZNA4 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA038576 HPA038577

HPAⁱ

HPA038576
HPA038577

Interactionⁱ

Subunit structureⁱ

Monomer (PubMed:26656854). Interacts with SMAD6, SMAD7, AXIN1, AXIN2 and SKIL isoform SNON (PubMed:16601693, PubMed:17591695). Interacts with (phosphorylated) SMAD2 and SMAD3 (By similarity). Part of a complex containing RNF111, AXIN1 and SMAD7 (PubMed:16601693). Interacts (via SIM domains) with SUMO1 and SUMO2 (PubMed:23086935).By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
	B2R8Y4	3	EBI-2129175,EBI-10175581
AXIN1	O15169	2	EBI-2129175,EBI-710484
CSNK2A1	P68400	4	EBI-2129175,EBI-347804
EDARADD	Q8WWZ3	3	EBI-2129175,EBI-2949647
KRTAP5-9	P26371	4	EBI-2129175,EBI-3958099
LCE4A	Q5TA78	3	EBI-2129175,EBI-10246358
UBE2D1	P51668	5	EBI-2129175,EBI-743540
UBE2D3	P61077	5	EBI-2129175,EBI-348268
UBE2I	P63279	5	EBI-2129175,EBI-80168
UBE2V1	Q13404	2	EBI-2129175,EBI-1050671

GO - Molecular functionⁱ

SMAD binding Source: Ensembl
SUMO polymer binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23086935

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	120146, 71 interactors
IntActⁱ	Q6ZNA4, 38 interactors
Molecular INTeraction database More...MINTⁱ	Q6ZNA4
STRINGⁱ	9606.ENSP00000288199

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	938 – 942	Combined sources	5
Turnⁱ	943 – 946	Combined sources	4
Beta strandⁱ	951 – 953	Combined sources	3
Beta strandⁱ	955 – 957	Combined sources	3
Turnⁱ	959 – 961	Combined sources	3
Beta strandⁱ	963 – 965	Combined sources	3
Helixⁱ	966 – 975	Combined sources	10
Turnⁱ	980 – 982	Combined sources	3
Beta strandⁱ	984 – 986	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q6ZNA4
SMRⁱ	Q6ZNA4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	241 – 404	Interaction with AXIN11 PublicationAdd BLAST	164
Regionⁱ	907 – 909	Ubiquitin bindingBy similarity	3
Regionⁱ	957 – 961	Ubiquitin bindingBy similarity	5

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	300 – 304	SUMO interaction motif 1 (SIM)2 Publications	5
Motifⁱ	325 – 331	SUMO interaction motif 2 (SIM)2 Publications	7
Motifⁱ	382 – 386	SUMO interaction motif 3 (SIM)2 Publications	5

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	252 – 464	Ser-richAdd BLAST	213
Compositional biasⁱ	494 – 523	His-richAdd BLAST	30
Compositional biasⁱ	629 – 781	Pro-richAdd BLAST	153

Domainⁱ

The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate.2 Publications

The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity and binds directly to free ubiquitin (PubMed:26656854). Non-covalent ubiquitin-binding stabilizes the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and stimulates ubiquitin transfer (By similarity).By similarity1 Publication

Sequence similaritiesⁱ

Belongs to the Arkadia family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	942 – 983	RING-type; atypicalPROSITE-ProRule annotationAdd BLAST		42

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG0800 Eukaryota ENOG41121N2 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00730000110863
HOVERGENⁱ	HBG093884
InParanoidⁱ	Q6ZNA4
KEGG Orthology (KO) More...KOⁱ	K10635
OMAⁱ	QPLRQNA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0WPK
PhylomeDBⁱ	Q6ZNA4
TreeFamⁱ	TF331862

Family and domain databases

Gene3Dⁱ	3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR029306 RNF111_N IPR001841 Znf_RING IPR013083 Znf_RING/FYVE/PHD
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF15303 RNF111_N, 1 hit PF13639 zf-RING_2, 1 hit
SMARTⁱ	View protein in SMART SM00184 RING, 1 hit
PROSITEⁱ	View protein in PROSITE PS50089 ZF_RING_2, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q6ZNA4-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP 
        60         70         80         90        100
AGVEMINSKV GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA 
       110        120        130        140        150
GPSYVQNCVK ENQGILGLRQ HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS 
       160        170        180        190        200
DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR SHKWPRTETE SVSGLLMKRP 
       210        220        230        240        250
CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE VLARRKYALL 
       260        270        280        290        300
PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 
       310        320        330        340        350
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ 
       360        370        380        390        400
GSSSHASRPQ EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA 
       410        420        430        440        450
RMESQATSAS INNSNPSTSE QASDTASAVT SSQPSTVSET SATLTSNSTT 
       460        470        480        490        500
GTSIGDDSRR TTSSAVTETG PPAMPRLPSC CPQHSPCGGS SQNHHALGHP 
       510        520        530        540        550
HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE RPPQVQAPCG 
       560        570        580        590        600
ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 
       610        620        630        640        650
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY 
       660        670        680        690        700
ASLTRPLHHQ ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA 
       710        720        730        740        750
TSHPVAPPPP THLASTAAPI PQHLPPTHQP ISHHIPATAP PAQRLHPHEV 
       760        770        780        790        800
MQRMEVQRRR MMQHPTRAHE RPPPHPHRMH PNYGHGHHIH VPQTMSSHPR 
       810        820        830        840        850
QAPERSAWEL GIEAGVTAAT YTPGALHPHL AHYHAPPRLH HLQLGALPLM 
       860        870        880        890        900
VPDMAGYPHI RYISSGLDGT SFRGPFRGNF EELIHLEERL GNVNRGASQG 
       910        920        930        940        950
TIERCTYPHK YKKVTTDWFS QRKLHCKQDG EEGTEEDTEE KCTICLSILE 
       960        970        980        990 
EGEDVRRLPC MHLFHQVCVD QWLITNKKCP ICRVDIEAQL PSES

Length:994

Mass (Da):108,862

Last modified:October 5, 2010 - v3

Checksum:ⁱ7E387321E5F61FAB

GO

Isoform 2 (identifier: Q6ZNA4-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
914-921: Missing.

« Hide

        10         20         30         40         50
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP 
        60         70         80         90        100
AGVEMINSKV GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA 
       110        120        130        140        150
GPSYVQNCVK ENQGILGLRQ HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS 
       160        170        180        190        200
DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR SHKWPRTETE SVSGLLMKRP 
       210        220        230        240        250
CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE VLARRKYALL 
       260        270        280        290        300
PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 
       310        320        330        340        350
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ 
       360        370        380        390        400
GSSSHASRPQ EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA 
       410        420        430        440        450
RMESQATSAS INNSNPSTSE QASDTASAVT SSQPSTVSET SATLTSNSTT 
       460        470        480        490        500
GTSIGDDSRR TTSSAVTETG PPAMPRLPSC CPQHSPCGGS SQNHHALGHP 
       510        520        530        540        550
HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE RPPQVQAPCG 
       560        570        580        590        600
ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 
       610        620        630        640        650
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY 
       660        670        680        690        700
ASLTRPLHHQ ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA 
       710        720        730        740        750
TSHPVAPPPP THLASTAAPI PQHLPPTHQP ISHHIPATAP PAQRLHPHEV 
       760        770        780        790        800
MQRMEVQRRR MMQHPTRAHE RPPPHPHRMH PNYGHGHHIH VPQTMSSHPR 
       810        820        830        840        850
QAPERSAWEL GIEAGVTAAT YTPGALHPHL AHYHAPPRLH HLQLGALPLM 
       860        870        880        890        900
VPDMAGYPHI RYISSGLDGT SFRGPFRGNF EELIHLEERL GNVNRGASQG 
       910        920        930        940        950
TIERCTYPHK YKKRKLHCKQ DGEEGTEEDT EEKCTICLSI LEEGEDVRRL 
       960        970        980 
PCMHLFHQVC VDQWLITNKK CPICRVDIEA QLPSES

Show »

Length:986

Mass (Da):107,896

Checksum:ⁱBD07D5D2C2B6AEB4

GO

Isoform 3 (identifier: Q6ZNA4-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
766-766: T → TGLFVFCVSR

« Hide

        10         20         30         40         50
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP 
        60         70         80         90        100
AGVEMINSKV GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA 
       110        120        130        140        150
GPSYVQNCVK ENQGILGLRQ HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS 
       160        170        180        190        200
DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR SHKWPRTETE SVSGLLMKRP 
       210        220        230        240        250
CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE VLARRKYALL 
       260        270        280        290        300
PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 
       310        320        330        340        350
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ 
       360        370        380        390        400
GSSSHASRPQ EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA 
       410        420        430        440        450
RMESQATSAS INNSNPSTSE QASDTASAVT SSQPSTVSET SATLTSNSTT 
       460        470        480        490        500
GTSIGDDSRR TTSSAVTETG PPAMPRLPSC CPQHSPCGGS SQNHHALGHP 
       510        520        530        540        550
HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE RPPQVQAPCG 
       560        570        580        590        600
ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 
       610        620        630        640        650
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY 
       660        670        680        690        700
ASLTRPLHHQ ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA 
       710        720        730        740        750
TSHPVAPPPP THLASTAAPI PQHLPPTHQP ISHHIPATAP PAQRLHPHEV 
       760        770        780        790        800
MQRMEVQRRR MMQHPTGLFV FCVSRRAHER PPPHPHRMHP NYGHGHHIHV 
       810        820        830        840        850
PQTMSSHPRQ APERSAWELG IEAGVTAATY TPGALHPHLA HYHAPPRLHH 
       860        870        880        890        900
LQLGALPLMV PDMAGYPHIR YISSGLDGTS FRGPFRGNFE ELIHLEERLG 
       910        920        930        940        950
NVNRGASQGT IERCTYPHKY KKVTTDWFSQ RKLHCKQDGE EGTEEDTEEK 
       960        970        980        990       1000
CTICLSILEE GEDVRRLPCM HLFHQVCVDQ WLITNKKCPI CRVDIEAQLP 

SES

Note: No experimental confirmation available.

Show »

Length:1,003

Mass (Da):109,871

Checksum:ⁱ9F0D0B05B5EB39A8

GO

Isoform 4 (identifier: Q6ZNA4-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
766-766: T → TGLFVFCVSR
914-921: Missing.

« Hide

        10         20         30         40         50
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP 
        60         70         80         90        100
AGVEMINSKV GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA 
       110        120        130        140        150
GPSYVQNCVK ENQGILGLRQ HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS 
       160        170        180        190        200
DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR SHKWPRTETE SVSGLLMKRP 
       210        220        230        240        250
CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE VLARRKYALL 
       260        270        280        290        300
PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 
       310        320        330        340        350
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ 
       360        370        380        390        400
GSSSHASRPQ EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA 
       410        420        430        440        450
RMESQATSAS INNSNPSTSE QASDTASAVT SSQPSTVSET SATLTSNSTT 
       460        470        480        490        500
GTSIGDDSRR TTSSAVTETG PPAMPRLPSC CPQHSPCGGS SQNHHALGHP 
       510        520        530        540        550
HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE RPPQVQAPCG 
       560        570        580        590        600
ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 
       610        620        630        640        650
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY 
       660        670        680        690        700
ASLTRPLHHQ ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA 
       710        720        730        740        750
TSHPVAPPPP THLASTAAPI PQHLPPTHQP ISHHIPATAP PAQRLHPHEV 
       760        770        780        790        800
MQRMEVQRRR MMQHPTGLFV FCVSRRAHER PPPHPHRMHP NYGHGHHIHV 
       810        820        830        840        850
PQTMSSHPRQ APERSAWELG IEAGVTAATY TPGALHPHLA HYHAPPRLHH 
       860        870        880        890        900
LQLGALPLMV PDMAGYPHIR YISSGLDGTS FRGPFRGNFE ELIHLEERLG 
       910        920        930        940        950
NVNRGASQGT IERCTYPHKY KKRKLHCKQD GEEGTEEDTE EKCTICLSIL 
       960        970        980        990 
EEGEDVRRLP CMHLFHQVCV DQWLITNKKC PICRVDIEAQ LPSES

Note: No experimental confirmation available.

Show »

Length:995

Mass (Da):108,906

Checksum:ⁱA648717F19CFB655

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YKK5	H0YKK5_HUMAN	E3 ubiquitin-protein ligase Arkadia E3 ubiquitin-protein ligase Arkadia	RNF111	128	Annotation score:
H0YKS2	H0YKS2_HUMAN	E3 ubiquitin-protein ligase Arkadia E3 ubiquitin-protein ligase Arkadia	RNF111	131	Annotation score:
H0YLK9	H0YLK9_HUMAN	E3 ubiquitin-protein ligase Arkadia E3 ubiquitin-protein ligase Arkadia	RNF111	190	Annotation score:

Sequence cautionⁱ

The sequence AAH10369 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

The sequence BAC04531 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

The sequence BAD18633 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	165	H → R in BX647259 (PubMed:17974005).Curated	1
Sequence conflictⁱ	473	A → E in CAD98031 (PubMed:17974005).Curated	1
Sequence conflictⁱ	562	Missing in AAH60862 (PubMed:16572171).Curated	1
Sequence conflictⁱ	562	Missing in AAH20984 (PubMed:16572171).Curated	1
Sequence conflictⁱ	625	M → T in BX647259 (PubMed:17974005).Curated	1
Sequence conflictⁱ	738	T → I in BX647259 (PubMed:17974005).Curated	1
Sequence conflictⁱ	809	E → G in CAD98031 (PubMed:17974005).Curated	1
Sequence conflictⁱ	931	E → G in CAD98031 (PubMed:17974005).Curated	1
Sequence conflictⁱ	938	T → A in BX647259 (PubMed:17974005).Curated	1
Sequence conflictⁱ	974	I → V in BAD18471 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_031185	9	N → K3 PublicationsCorresponds to variant dbSNP:rs2899642Ensembl.		1
Natural variantⁱVAR_057216	718	A → T. Corresponds to variant dbSNP:rs34086812Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_023840	766	T → TGLFVFCVSR in isoform 3 and isoform 4. 2 Publications		1
Alternative sequenceⁱVSP_023841	914 – 921	Missing in isoform 2 and isoform 4. 2 Publications		8

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK095327 mRNA Translation: BAC04531.1 Different initiation. AK131304 mRNA Translation: BAD18471.1 AK131488 mRNA Translation: BAD18633.1 Different initiation. AL157474 mRNA Translation: CAB75669.2 BX538130 mRNA Translation: CAD98031.1 BX647259 mRNA No translation available. AC025918 Genomic DNA No translation available. AC090515 Genomic DNA No translation available. AC092757 Genomic DNA No translation available. CH471082 Genomic DNA Translation: EAW77561.1 BC010369 mRNA Translation: AAH10369.1 Different initiation. BC020984 mRNA Translation: AAH20984.1 BC060862 mRNA Translation: AAH60862.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10169.1 [Q6ZNA4-2] CCDS58365.1 [Q6ZNA4-4] CCDS58366.1 [Q6ZNA4-1] CCDS81888.1 [Q6ZNA4-3]
PIRⁱ	T46904
NCBI Reference Sequences More...RefSeqⁱ	NP_001257457.1, NM_001270528.1 [Q6ZNA4-4] NP_001257458.1, NM_001270529.1 NP_001257459.1, NM_001270530.1 [Q6ZNA4-1] NP_001317260.1, NM_001330331.1 [Q6ZNA4-3] NP_060080.6, NM_017610.7 [Q6ZNA4-2] XP_006720642.1, XM_006720579.3 [Q6ZNA4-3] XP_016877827.1, XM_017022338.1 [Q6ZNA4-1]
UniGeneⁱ	Hs.404423 Hs.603489 Hs.741727

Genome annotation databases

Ensemblⁱ	ENST00000348370; ENSP00000288199; ENSG00000157450 [Q6ZNA4-2] ENST00000557998; ENSP00000452732; ENSG00000157450 [Q6ZNA4-1] ENST00000559209; ENSP00000453872; ENSG00000157450 [Q6ZNA4-4] ENST00000561186; ENSP00000453015; ENSG00000157450 [Q6ZNA4-3]
GeneIDⁱ	54778
KEGGⁱ	hsa:54778
UCSC genome browser More...UCSCⁱ	uc002afs.5 human [Q6ZNA4-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q6ZNA4-2	Ring finger protein 111, isoform CRA_c		HUMAN		986	UniRef100_A0A024R5T5
UPI0007DC7289		HUMAN		1014
Q6ZNA4-3	E3 ubiquitin-protein ligase Arkadia (Fragment)		HUMAN		131	UniRef100_Q6ZNA4-3
UPI0007DC4E6A		HUMAN		1039

Protein	Similar proteins		Species	Score	Length	Source
Q6ZNA4	E3 ubiquitin-protein ligase Arkadia		PONAB		986	UniRef90_Q6ZNA4
E3 ubiquitin-protein ligase Arkadia isoform X1		DELLE		1028
E3 ubiquitin-protein ligase Arkadia isoform X1		PHYCD		1028
E3 ubiquitin-protein ligase Arkadia isoform X1		TURTR		1027
E3 ubiquitin-protein ligase Arkadia isoform X1		Enhydra lutris kenyoni		1009
+503

Protein	Similar proteins		Species	Score	Length	Source
Q6ZNA4	E3 ubiquitin-protein ligase Arkadia		PONAB		986	UniRef50_Q6ZNA4
E3 ubiquitin-protein ligase Arkadia		MOUSE		989
E3 ubiquitin-protein ligase Arkadia isoform X1		DELLE		1028
E3 ubiquitin-protein ligase Arkadia isoform X1		PHYCD		1028
E3 ubiquitin-protein ligase Arkadia isoform X1		TURTR		1027
+727

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK095327 mRNA Translation: BAC04531.1 Different initiation. AK131304 mRNA Translation: BAD18471.1 AK131488 mRNA Translation: BAD18633.1 Different initiation. AL157474 mRNA Translation: CAB75669.2 BX538130 mRNA Translation: CAD98031.1 BX647259 mRNA No translation available. AC025918 Genomic DNA No translation available. AC090515 Genomic DNA No translation available. AC092757 Genomic DNA No translation available. CH471082 Genomic DNA Translation: EAW77561.1 BC010369 mRNA Translation: AAH10369.1 Different initiation. BC020984 mRNA Translation: AAH20984.1 BC060862 mRNA Translation: AAH60862.1
CCDSⁱ	CCDS10169.1 [Q6ZNA4-2] CCDS58365.1 [Q6ZNA4-4] CCDS58366.1 [Q6ZNA4-1] CCDS81888.1 [Q6ZNA4-3]
PIRⁱ	T46904
RefSeqⁱ	NP_001257457.1, NM_001270528.1 [Q6ZNA4-4] NP_001257458.1, NM_001270529.1 NP_001257459.1, NM_001270530.1 [Q6ZNA4-1] NP_001317260.1, NM_001330331.1 [Q6ZNA4-3] NP_060080.6, NM_017610.7 [Q6ZNA4-2] XP_006720642.1, XM_006720579.3 [Q6ZNA4-3] XP_016877827.1, XM_017022338.1 [Q6ZNA4-1]
UniGeneⁱ	Hs.404423 Hs.603489 Hs.741727

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
	2KIZ	NMR	-	A	927-994	[»]
	5LG0	NMR	-	A	927-994	[»]
	5LG7	NMR	-	A	927-994	[»]
ProteinModelPortalⁱ	Q6ZNA4
SMRⁱ	Q6ZNA4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	120146, 71 interactors
IntActⁱ	Q6ZNA4, 38 interactors
MINTⁱ	Q6ZNA4
STRINGⁱ	9606.ENSP00000288199

Protein family/group databases

MoonDBⁱ	Q6ZNA4 Predicted

MoonDBⁱ

Q6ZNA4 Predicted

PTM databases

iPTMnetⁱ	Q6ZNA4
PhosphoSitePlusⁱ	Q6ZNA4

Polymorphism and mutation databases

BioMutaⁱ	RNF111
DMDMⁱ	308153555

Proteomic databases

MaxQBⁱ	Q6ZNA4
PaxDbⁱ	Q6ZNA4
PeptideAtlasⁱ	Q6ZNA4
PRIDEⁱ	Q6ZNA4
ProteomicsDBⁱ	68002 68003 [Q6ZNA4-2] 68004 [Q6ZNA4-3]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000348370; ENSP00000288199; ENSG00000157450 [Q6ZNA4-2] ENST00000557998; ENSP00000452732; ENSG00000157450 [Q6ZNA4-1] ENST00000559209; ENSP00000453872; ENSG00000157450 [Q6ZNA4-4] ENST00000561186; ENSP00000453015; ENSG00000157450 [Q6ZNA4-3]
GeneIDⁱ	54778
KEGGⁱ	hsa:54778
UCSCⁱ	uc002afs.5 human [Q6ZNA4-1]

Organism-specific databases

CTDⁱ	54778
DisGeNETⁱ	54778
EuPathDBⁱ	HostDB:ENSG00000157450.15
GeneCardsⁱ	RNF111
HGNCⁱ	HGNC:17384 RNF111
HPAⁱ	HPA038576 HPA038577
MIMⁱ	605840 gene
neXtProtⁱ	NX_Q6ZNA4
OpenTargetsⁱ	ENSG00000157450
PharmGKBⁱ	PA134868772
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0800 Eukaryota ENOG41121N2 LUCA
GeneTreeⁱ	ENSGT00730000110863
HOVERGENⁱ	HBG093884
InParanoidⁱ	Q6ZNA4
KOⁱ	K10635
OMAⁱ	QPLRQNA
OrthoDBⁱ	EOG091G0WPK
PhylomeDBⁱ	Q6ZNA4
TreeFamⁱ	TF331862

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
BRENDAⁱ	6.3.2.19 2681
Reactomeⁱ	R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkⁱ	Q6ZNA4
SIGNORⁱ	Q6ZNA4

Miscellaneous databases

ChiTaRSⁱ	RNF111 human
GeneWikiⁱ	RNF111
GenomeRNAiⁱ	54778
Protein Ontology More...PROⁱ	PR:Q6ZNA4
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000157450 Expressed in 224 organ(s), highest expression level in secondary oocyte
CleanExⁱ	HS_RNF111
ExpressionAtlasⁱ	Q6ZNA4 baseline and differential
Genevisibleⁱ	Q6ZNA4 HS

Family and domain databases

Gene3Dⁱ	3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR029306 RNF111_N IPR001841 Znf_RING IPR013083 Znf_RING/FYVE/PHD
Pfamⁱ	View protein in Pfam PF15303 RNF111_N, 1 hit PF13639 zf-RING_2, 1 hit
SMARTⁱ	View protein in SMART SM00184 RING, 1 hit
PROSITEⁱ	View protein in PROSITE PS50089 ZF_RING_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RN111_HUMAN
Accessionⁱ	Q6ZNA4Primary (citable) accession number: Q6ZNA4 Secondary accession number(s): C9JUS4 Q9NSR1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
	Last sequence update:	October 5, 2010
	Last modified:	September 12, 2018
	This is version 146 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q6ZNA4 (RN111_HUMAN)

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E3 ubiquitin-protein ligase Arkadia

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>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

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

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

Nucleus

Other locations

Cytosol

Nucleus

Other locations

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

Mutagenesis

Organism-specific databases

Polymorphism and mutation 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

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

Organism-specific 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

<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

Motif

Compositional bias

<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

Zinc finger

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

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

Polymorphism and mutation 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

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Functionⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ