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RING finger protein 11

 RNF11_HUMAN             Reviewed;         154 AA.
Q9Y3C5; A8KAI2; Q5T7R8;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-APR-2018, entry version 148.
RecName: Full=RING finger protein 11;
Name=RNF11; ORFNames=CGI-123;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10673045; DOI=10.1016/S0167-4781(99)00190-6;
Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y.,
Sugano S., Muramatsu M., Saito T.;
"Cloning and expression profile of mouse and human genes, Rnf11/RNF11,
encoding a novel RING-H2 finger protein.";
Biochim. Biophys. Acta 1489:421-427(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 70-113 AND 132-154, PHOSPHORYLATION AT THR-135,
SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, AND MUTAGENESIS OF
THR-135.
PubMed=16123141; DOI=10.1158/1541-7786.MCR-04-0166;
Connor M.K., Azmi P.B., Subramaniam V., Li H., Seth A.K.;
"Molecular characterization of ring finger protein 11.";
Mol. Cancer Res. 3:453-461(2005).
[8]
INTERACTION WITH ITCH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF TYR-40.
PubMed=14559117; DOI=10.1016/j.bbadis.2003.07.001;
Kitching R., Wong M.J., Koehler D., Burger A.M., Landberg G., Gish G.,
Seth A.K.;
"The RING-H2 protein RNF11 is differentially expressed in breast
tumours and interacts with HECT-type E3 ligases.";
Biochim. Biophys. Acta 1639:104-112(2003).
[9]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SMURF2 AND
UBE2D1, UBIQUITINATION, AND MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
PubMed=14562029; DOI=10.1038/sj.bjc.6601301;
Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J.,
Zubovits J., Burger A.M., Seth A.K.;
"The RING-H2 protein RNF11 is overexpressed in breast cancer and is a
target of Smurf2 E3 ligase.";
Br. J. Cancer 89:1538-1544(2003).
[10]
FUNCTION, INTERACTION WITH ZNF350; EPS15 AND STAMBP, AND MUTAGENESIS
OF TYR-40; CYS-99 AND CYS-102.
PubMed=14755250; DOI=10.1038/sj.onc.1207319;
Li H., Seth A.K.;
"An RNF11: Smurf2 complex mediates ubiquitination of the AMSH
protein.";
Oncogene 23:1801-1808(2004).
[11]
TISSUE SPECIFICITY.
PubMed=17917589; DOI=10.1097/nen.0b013e3181567f17;
Anderson L.R., Betarbet R., Gearing M., Gulcher J., Hicks A.A.,
Stefansson K., Lah J.J., Levey A.I.;
"PARK10 candidate RNF11 is expressed by vulnerable neurons and
localizes to Lewy bodies in Parkinson disease brain.";
J. Neuropathol. Exp. Neurol. 66:955-964(2007).
[12]
INTERACTION WITH WWP1, AND MUTAGENESIS OF TYR-40.
PubMed=18724389; DOI=10.1038/onc.2008.288;
Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.;
"The WW domain containing E3 ubiquitin protein ligase 1 upregulates
ErbB2 and EGFR through RING finger protein 11.";
Oncogene 27:6845-6855(2008).
[13]
INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1, AND MUTAGENESIS OF TYR-40
AND CYS-99.
PubMed=19131965; DOI=10.1038/emboj.2008.285;
Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.;
"The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-
kappaB signalling.";
EMBO J. 28:513-522(2009).
[14]
INTERACTION WITH UBE2N, AND MUTAGENESIS OF MET-103; ASP-127 AND
ASP-128.
PubMed=18615712; DOI=10.1002/prot.22120;
Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.;
"Analysis of electrostatic contributions to the selectivity of
interactions between RING-finger domains and ubiquitin-conjugating
enzymes.";
Proteins 74:92-103(2009).
[15]
INTERACTION WITH GGA1, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT
CYS-4, UBIQUITINATION BY ITCH, AND MUTAGENESIS OF GLY-2; CYS-4;
ASP-12; LEU-15; LEU-16; CYS-99 AND CYS-102.
PubMed=20676133; DOI=10.1038/onc.2010.294;
Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G.,
Castagnoli L.;
"Multiple modification and protein interaction signals drive the Ring
finger protein 11 (RNF11) E3 ligase to the endosomal compartment.";
Oncogene 29:5604-5618(2010).
[16]
MYRISTOYLATION AT GLY-2.
PubMed=20213681; DOI=10.1002/pmic.200900783;
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
Tsunasawa S., Utsumi T.;
"Strategy for comprehensive identification of human N-myristoylated
proteins using an insect cell-free protein synthesis system.";
Proteomics 10:1780-1793(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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.
{ECO:0000269|PubMed:14755250}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:14559117, ECO:0000269|PubMed:14562029,
ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:16123141,
ECO:0000269|PubMed:18615712, ECO:0000269|PubMed:18724389,
ECO:0000269|PubMed:19131965, ECO:0000269|PubMed:20676133}.
-!- INTERACTION:
Q9UJY5:GGA1; NbExp=3; IntAct=EBI-396669, EBI-447141;
Q96J02:ITCH; NbExp=2; IntAct=EBI-396669, EBI-1564678;
P46934:NEDD4; NbExp=2; IntAct=EBI-396669, EBI-726944;
P47897:QARS; NbExp=4; IntAct=EBI-396669, EBI-347462;
Q9HAU4:SMURF2; NbExp=5; IntAct=EBI-396669, EBI-396727;
O95630:STAMBP; NbExp=2; IntAct=EBI-396669, EBI-396676;
Q86VP1:TAX1BP1; NbExp=2; IntAct=EBI-396669, EBI-529518;
P21580:TNFAIP3; NbExp=2; IntAct=EBI-396669, EBI-527670;
P0CG47:UBB; NbExp=2; IntAct=EBI-396669, EBI-413034;
P51668:UBE2D1; NbExp=6; IntAct=EBI-396669, EBI-743540;
P62837:UBE2D2; NbExp=7; IntAct=EBI-396669, EBI-347677;
P61077:UBE2D3; NbExp=3; IntAct=EBI-396669, EBI-348268;
Q9Y2X8:UBE2D4; NbExp=6; IntAct=EBI-396669, EBI-745527;
P51965:UBE2E1; NbExp=2; IntAct=EBI-396669, EBI-348546;
P61088:UBE2N; NbExp=4; IntAct=EBI-396669, EBI-1052908;
-!- SUBCELLULAR LOCATION: Early endosome. Recycling endosome.
Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, when
unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1.
{ECO:0000269|PubMed:16123141}.
-!- 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. {ECO:0000269|PubMed:14559117,
ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:17917589}.
-!- DOMAIN: The PPxY motif mediates interaction with NEDD4.
{ECO:0000250}.
-!- PTM: Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1,
as well as WWP1. {ECO:0000269|PubMed:14562029,
ECO:0000269|PubMed:20676133}.
-!- PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the
proteasome. {ECO:0000269|PubMed:16123141}.
-!- PTM: Acylation at both Gly-2 and Cys-4 is required for proper
localization to the endosomes. {ECO:0000269|PubMed:20676133}.
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EMBL; AB024703; BAA84683.1; -; mRNA.
EMBL; AF151881; AAD34118.1; -; mRNA.
EMBL; AK293047; BAF85736.1; -; mRNA.
EMBL; AK313140; BAG35959.1; -; mRNA.
EMBL; AL162430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06831.1; -; Genomic_DNA.
EMBL; BC020964; AAH20964.1; -; mRNA.
EMBL; BC047654; AAH47654.1; -; mRNA.
CCDS; CCDS556.1; -.
RefSeq; NP_055187.1; NM_014372.4.
UniGene; Hs.309641; -.
ProteinModelPortal; Q9Y3C5; -.
SMR; Q9Y3C5; -.
BioGrid; 117941; 107.
CORUM; Q9Y3C5; -.
IntAct; Q9Y3C5; 62.
MINT; Q9Y3C5; -.
STRING; 9606.ENSP00000242719; -.
iPTMnet; Q9Y3C5; -.
PhosphoSitePlus; Q9Y3C5; -.
SwissPalm; Q9Y3C5; -.
BioMuta; RNF11; -.
DMDM; 21362884; -.
EPD; Q9Y3C5; -.
MaxQB; Q9Y3C5; -.
PaxDb; Q9Y3C5; -.
PeptideAtlas; Q9Y3C5; -.
PRIDE; Q9Y3C5; -.
DNASU; 26994; -.
Ensembl; ENST00000242719; ENSP00000242719; ENSG00000123091.
GeneID; 26994; -.
KEGG; hsa:26994; -.
UCSC; uc001csi.5; human.
CTD; 26994; -.
DisGeNET; 26994; -.
EuPathDB; HostDB:ENSG00000123091.4; -.
GeneCards; RNF11; -.
HGNC; HGNC:10056; RNF11.
HPA; HPA045781; -.
MIM; 612598; gene.
neXtProt; NX_Q9Y3C5; -.
OpenTargets; ENSG00000123091; -.
PharmGKB; PA34420; -.
eggNOG; KOG0800; Eukaryota.
eggNOG; ENOG41121N2; LUCA.
GeneTree; ENSGT00730000110988; -.
HOGENOM; HOG000007448; -.
HOVERGEN; HBG058444; -.
InParanoid; Q9Y3C5; -.
KO; K11980; -.
OMA; HLDCIDN; -.
OrthoDB; EOG091G0T50; -.
PhylomeDB; Q9Y3C5; -.
TreeFam; TF318022; -.
SIGNOR; Q9Y3C5; -.
ChiTaRS; RNF11; human.
GeneWiki; RNF11; -.
GenomeRNAi; 26994; -.
PRO; PR:Q9Y3C5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000123091; -.
CleanEx; HS_RNF11; -.
Genevisible; Q9Y3C5; HS.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Endosome;
Lipoprotein; Metal-binding; Myristate; Nucleus; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed.
CHAIN 2 154 RING finger protein 11.
/FTId=PRO_0000056050.
ZN_FING 99 140 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
MOTIF 37 40 PPxY motif.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYK7}.
MOD_RES 135 135 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:16123141}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:20213681,
ECO:0000269|PubMed:20676133}.
LIPID 4 4 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20676133}.
VARIANT 11 11 D -> E (in dbSNP:rs12077069).
/FTId=VAR_058272.
MUTAGEN 2 2 G->A: Loss of myristoylation. Change in
subcellular location: Becomes diffused
throughout the cytosol. Strong reduction
of ubiquitination. Reduced efficiency of
ITCH-binding.
{ECO:0000269|PubMed:20676133}.
MUTAGEN 4 4 C->S: Change in subcellular location:
Becomes partially cytosolic and retained
in association with the Golgi apparatus.
Partial reduction of ubiquitination.
{ECO:0000269|PubMed:20676133}.
MUTAGEN 12 12 D->A: Loss of GGA1-binding.
{ECO:0000269|PubMed:20676133}.
MUTAGEN 15 15 L->A: Loss of GGA1-binding.
{ECO:0000269|PubMed:20676133}.
MUTAGEN 16 16 L->A: Loss of GGA1-binding.
{ECO:0000269|PubMed:20676133}.
MUTAGEN 40 40 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.
{ECO:0000269|PubMed:14559117,
ECO:0000269|PubMed:14562029,
ECO:0000269|PubMed:14755250,
ECO:0000269|PubMed:18724389,
ECO:0000269|PubMed:19131965}.
MUTAGEN 99 99 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.
{ECO:0000269|PubMed:14562029,
ECO:0000269|PubMed:14755250,
ECO:0000269|PubMed:19131965,
ECO:0000269|PubMed:20676133}.
MUTAGEN 102 102 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. {ECO:0000269|PubMed:14562029,
ECO:0000269|PubMed:14755250,
ECO:0000269|PubMed:20676133}.
MUTAGEN 103 103 M->A,G: Loss of UBE2N-binding. No gain of
UBE2L3-binding.
{ECO:0000269|PubMed:18615712}.
MUTAGEN 103 103 M->L: No effect on UBE2N-binding. No gain
of UBE2L3-binding; when associated with
L-127 and L-128.
{ECO:0000269|PubMed:18615712}.
MUTAGEN 103 103 M->V: No effect on UBE2N-binding. Gain of
UBE2L3-binding.
{ECO:0000269|PubMed:18615712}.
MUTAGEN 127 127 D->L: No effect on UBE2N-binding. No gain
of UBE2L3-binding; when associated with
L-128. {ECO:0000269|PubMed:18615712}.
MUTAGEN 128 128 D->L: No effect on UBE2N-binding. No gain
of UBE2L3-binding.
{ECO:0000269|PubMed:18615712}.
MUTAGEN 135 135 T->E: Loss of phosphorylation and of 14-
3-3-binding.
{ECO:0000269|PubMed:16123141}.
CONFLICT 124 124 D -> G (in Ref. 3; BAF85736).
{ECO:0000305}.
SEQUENCE 154 AA; 17444 MW; C368E38148FC1D0D CRC64;
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH PTPSQTRLAT
QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI
YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN


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