Q9Y3C5 (RNF11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RING finger protein 11

Gene names

Name:	RNF11
ORF Names:	CGI-123

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. Ref.10
Subunit structure	Interacts (when phosphorylated) with 14-3-3. Interacts with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 By similarity. Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350, EPS15 and STAMBP. After TNF stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they are lost after 1 hour of stimulation with TNF By similarity. Interacts with GGA1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15
Subcellular location	Early endosome. Recycling endosome. Cytoplasm. Nucleus. Note: Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1 (Ref.7). Ref.7 Ref.8 Ref.9
Tissue specificity	Expressed at low levels in the lung, liver, kidney, pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and peripheral blood lymphocytes, and, at intermediate levels, in the testis, heart, brain and placenta. Highest expression in the skeletal muscle. In the brain, expressed at different levels in several regions: high levels in the amygdala, moderate in the hippocampus and thalamus, low in the caudate and extremely low levels in the corpus callosum (at protein level). Restricted to neurons, enriched in somatodendritic compartments and excluded from white matter (at protein level). In substantia nigra, present in cell bodies and processes of dopaminergic and nondopaminergic cells (at protein level). In Parkinson disease, sequestered in Lewy bodies and neurites. Overexpressed in breast cancer cells, but not detected in the surrounding stroma and weakly, if at all, in normal breast epithelial cells (at protein level). Also expressed in several tumor cell lines. Ref.8 Ref.9 Ref.11
Domain	The WW-binding motif mediates interaction with NEDD4 By similarity.
Post-translational modification	Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1. Ref.9 Ref.15 Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome. May be acylated at Cys-4, possibly palmitoylated. Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes.
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Endosome Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GGA1	Q9UJY5	2	EBI-396669,EBI-447141
ITCH	Q96J02	2	EBI-396669,EBI-1564678
SMURF2	Q9HAU4	3	EBI-396669,EBI-396727
STAMBP	O95630	2	EBI-396669,EBI-396676
UBB	P0CG47	2	EBI-396669,EBI-413034
UBE2D1	P51668	4	EBI-396669,EBI-743540
UBE2D2	P62837	4	EBI-396669,EBI-347677
UBE2D3	P61077	3	EBI-396669,EBI-348268
UBE2E1	P51965	2	EBI-396669,EBI-348546
UBE2N	P61088	3	EBI-396669,EBI-1052908

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 154	153	RING finger protein 11		PRO_0000056050
Regions
	Zinc finger	99 – 140	42	RING-type
	Motif	37 – 40	4	WW-binding
Amino acid modifications
	Modified residue	135	1	Phosphothreonine; by PKB/AKT1 Ref.7
	Lipidation	2	1	N-myristoyl glycine Ref.15 Ref.16
Natural variations
	Natural variant	11	1	D → E. Corresponds to variant rs12077069 [ dbSNP | Ensembl ].		VAR_058272
Experimental info
	Mutagenesis	2	1	G → A: Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding. Ref.15
	Mutagenesis	4	1	C → S: Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination. Ref.15
	Mutagenesis	12	1	D → A: Loss of GGA1-binding. Ref.15
	Mutagenesis	15	1	L → A: Loss of GGA1-binding. Ref.15
	Mutagenesis	16	1	L → A: Loss of GGA1-binding. Ref.15
	Mutagenesis	40	1	Y → A: Loss of ITCH-, SMURF2- and WWP1-binding. Partial loss of ubiquitination by ITCH. No effect on STAMBP-binding; when associated with S-99 and S-102. Persistent TNF-mediated NFKBIA phosphorylation. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
	Mutagenesis	99	1	C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-102. Persistent TNF-mediated NFKBIA phosphorylation. No effect on STAMBP-binding; when associated with A-40 and S-102. No effect on ubiquitination by ITCH; when associated with S-102. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. Ref.9 Ref.10 Ref.13 Ref.15
	Mutagenesis	102	1	C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-99. No effect on ubiquitination by ITCH; when associated with S-102. No effect on STAMBP-binding; when associated with A-40 and S-99. Ref.9 Ref.10 Ref.15
	Mutagenesis	103	1	M → A or G: Loss of UBE2N-binding. No gain of UBE2L3-binding. Ref.14
	Mutagenesis	103	1	M → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128. Ref.14
	Mutagenesis	103	1	M → V: No effect on UBE2N-binding. Gain of UBE2L3-binding. Ref.14
	Mutagenesis	127	1	D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128. Ref.14
	Mutagenesis	128	1	D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding. Ref.14
	Mutagenesis	135	1	T → E: Loss of phosphorylation and of 14-3-3-binding. Ref.7
	Sequence conflict	124	1	D → G in BAF85736. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y3C5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C368E38148FC1D0D	FASTA	154	17,444
	10 20 30 40 50 60 MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH PTPSQTRLAT 70 80 90 100 110 120 QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI 130 140 150 YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression profile of mouse and human genes, Rnf11/RNF11, encoding a novel RING-H2 finger protein." Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y., Sugano S., Muramatsu M., Saito T. Biochim. Biophys. Acta 1489:421-427(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Skin.
[7]	"Molecular characterization of ring finger protein 11." Connor M.K., Azmi P.B., Subramaniam V., Li H., Seth A.K. Mol. Cancer Res. 3:453-461(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 70-113 AND 132-154, PHOSPHORYLATION AT THR-135, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESIS OF THR-135.
[8]	"The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases." Kitching R., Wong M.J., Koehler D., Burger A.M., Landberg G., Gish G., Seth A.K. Biochim. Biophys. Acta 1639:104-112(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITCH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-40.
[9]	"The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase." Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K. Br. J. Cancer 89:1538-1544(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SMURF2 AND UBE2D1, UBIQUITINATION, MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
[10]	"An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein." Li H., Seth A.K. Oncogene 23:1801-1808(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZNF350; EPS15 AND STAMBP, MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
[11]	"PARK10 candidate RNF11 is expressed by vulnerable neurons and localizes to Lewy bodies in Parkinson disease brain." Anderson L.R., Betarbet R., Gearing M., Gulcher J., Hicks A.A., Stefansson K., Lah J.J., Levey A.I. J. Neuropathol. Exp. Neurol. 66:955-964(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11." Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K. Oncogene 27:6845-6855(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWP1, MUTAGENESIS OF TYR-40.
[13]	"The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling." Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W. EMBO J. 28:513-522(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1, MUTAGENESIS OF TYR-40 AND CYS-99.
[14]	"Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes." Scheper J., Oliva B., Villa-Freixa J., Thomson T.M. Proteins 74:92-103(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBE2N, MUTAGENESIS OF MET-103; ASP-127 AND ASP-128.
[15]	"Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment." Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G., Castagnoli L. Oncogene 29:5604-5618(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GGA1, MYRISTOYLATION AT GLY-2, POSSIBLE ACYLATION AT CYS-4, UBIQUITINATION BY ITCH, MUTAGENESIS OF GLY-2; CYS-4; ASP-12; LEU-15; LEU-16; CYS-99 AND CYS-102.
[16]	"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system." Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T. Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB024703 mRNA. Translation: BAA84683.1. AF151881 mRNA. Translation: AAD34118.1. AK293047 mRNA. Translation: BAF85736.1. AK313140 mRNA. Translation: BAG35959.1. AL162430 Genomic DNA. Translation: CAI13140.1. CH471059 Genomic DNA. Translation: EAX06831.1. BC020964 mRNA. Translation: AAH20964.1. BC047654 mRNA. Translation: AAH47654.1.
IPI	IPI00003894.
RefSeq	NP_055187.1. NM_014372.4.
UniGene	Hs.309641.
3D structure databases
ProteinModelPortal	Q9Y3C5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y3C5. 22 interactions.
MINT	MINT-1180165.
STRING	9606.ENSP00000242719.
PTM databases
PhosphoSite	Q9Y3C5.
Polymorphism databases
DMDM	21362884.
Proteomic databases
PaxDb	Q9Y3C5.
PRIDE	Q9Y3C5.
Protocols and materials databases
DNASU	26994.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000242719; ENSP00000242719; ENSG00000123091.
GeneID	26994.
KEGG	hsa:26994.
UCSC	uc001csi.4. human.
Organism-specific databases
CTD	26994.
GeneCards	GC01P051701.
HGNC	HGNC:10056. RNF11.
HPA	HPA045781.
MIM	612598. gene.
neXtProt	NX_Q9Y3C5.
PharmGKB	PA34420.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG265447.
HOGENOM	HOG000007448.
HOVERGEN	HBG058444.
InParanoid	Q9Y3C5.
KO	K11980.
OMA	DPDQEPP.
OrthoDB	EOG41VK45.
PhylomeDB	Q9Y3C5.
Gene expression databases
Bgee	Q9Y3C5.
CleanEx	HS_RNF11.
Genevestigator	Q9Y3C5.
GermOnline	ENSG00000123091. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF13639. zf-RING_2. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RNF11. human.
GenomeRNAi	26994.
NextBio	49462.
SOURCE	Search...

Entry information

Entry name

RNF11_HUMAN

Accession

Primary (citable) accession number: Q9Y3C5
Secondary accession number(s): A8KAI2, Q5T7R8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.