ID RNF11_HUMAN Reviewed; 154 AA.
AC Q9Y3C5; A8KAI2; Q5T7R8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 178.
DE RecName: Full=RING finger protein 11;
GN Name=RNF11; ORFNames=CGI-123;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10673045; DOI=10.1016/s0167-4781(99)00190-6;
RA Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y.,
RA Sugano S., Muramatsu M., Saito T.;
RT "Cloning and expression profile of mouse and human genes, Rnf11/RNF11,
RT encoding a novel RING-H2 finger protein.";
RL Biochim. Biophys. Acta 1489:421-427(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 70-113 AND 132-154, PHOSPHORYLATION AT THR-135,
RP SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, AND MUTAGENESIS OF THR-135.
RX PubMed=16123141; DOI=10.1158/1541-7786.mcr-04-0166;
RA Connor M.K., Azmi P.B., Subramaniam V., Li H., Seth A.K.;
RT "Molecular characterization of ring finger protein 11.";
RL Mol. Cancer Res. 3:453-461(2005).
RN [8]
RP INTERACTION WITH ITCH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF TYR-40.
RX PubMed=14559117; DOI=10.1016/j.bbadis.2003.07.001;
RA Kitching R., Wong M.J., Koehler D., Burger A.M., Landberg G., Gish G.,
RA Seth A.K.;
RT "The RING-H2 protein RNF11 is differentially expressed in breast tumours
RT and interacts with HECT-type E3 ligases.";
RL Biochim. Biophys. Acta 1639:104-112(2003).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SMURF2 AND
RP UBE2D1, UBIQUITINATION, AND MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
RX PubMed=14562029; DOI=10.1038/sj.bjc.6601301;
RA Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J.,
RA Zubovits J., Burger A.M., Seth A.K.;
RT "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a
RT target of Smurf2 E3 ligase.";
RL Br. J. Cancer 89:1538-1544(2003).
RN [10]
RP FUNCTION, INTERACTION WITH ZNF350; EPS15 AND STAMBP, AND MUTAGENESIS OF
RP TYR-40; CYS-99 AND CYS-102.
RX PubMed=14755250; DOI=10.1038/sj.onc.1207319;
RA Li H., Seth A.K.;
RT "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein.";
RL Oncogene 23:1801-1808(2004).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=17917589; DOI=10.1097/nen.0b013e3181567f17;
RA Anderson L.R., Betarbet R., Gearing M., Gulcher J., Hicks A.A.,
RA Stefansson K., Lah J.J., Levey A.I.;
RT "PARK10 candidate RNF11 is expressed by vulnerable neurons and localizes to
RT Lewy bodies in Parkinson disease brain.";
RL J. Neuropathol. Exp. Neurol. 66:955-964(2007).
RN [12]
RP INTERACTION WITH WWP1, AND MUTAGENESIS OF TYR-40.
RX PubMed=18724389; DOI=10.1038/onc.2008.288;
RA Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.;
RT "The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2
RT and EGFR through RING finger protein 11.";
RL Oncogene 27:6845-6855(2008).
RN [13]
RP INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1, AND MUTAGENESIS OF TYR-40 AND
RP CYS-99.
RX PubMed=19131965; DOI=10.1038/emboj.2008.285;
RA Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.;
RT "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB
RT signalling.";
RL EMBO J. 28:513-522(2009).
RN [14]
RP INTERACTION WITH UBE2N, AND MUTAGENESIS OF MET-103; ASP-127 AND ASP-128.
RX PubMed=18615712; DOI=10.1002/prot.22120;
RA Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.;
RT "Analysis of electrostatic contributions to the selectivity of interactions
RT between RING-finger domains and ubiquitin-conjugating enzymes.";
RL Proteins 74:92-103(2009).
RN [15]
RP INTERACTION WITH GGA1, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4,
RP UBIQUITINATION BY ITCH, AND MUTAGENESIS OF GLY-2; CYS-4; ASP-12; LEU-15;
RP LEU-16; CYS-99 AND CYS-102.
RX PubMed=20676133; DOI=10.1038/onc.2010.294;
RA Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G.,
RA Castagnoli L.;
RT "Multiple modification and protein interaction signals drive the Ring
RT finger protein 11 (RNF11) E3 ligase to the endosomal compartment.";
RL Oncogene 29:5604-5618(2010).
RN [16]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Essential component of a ubiquitin-editing protein complex,
CC comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient
CC nature of inflammatory signaling pathways. Promotes the association of
CC TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-
CC 63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-
CC 48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation
CC and consequently termination of the TNF- or LPS-mediated activation of
CC NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for
CC ubiquitination, leading to its degradation by the 26S proteasome.
CC {ECO:0000269|PubMed:14755250}.
CC -!- SUBUNIT: Interacts (when phosphorylated) with 14-3-3. Interacts with
CC the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity).
CC Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and
CC UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350,
CC EPS15 and STAMBP. After TNF stimulation, interacts with TAX1BP1,
CC TNFAIP3 and RIPK1; these interactions are transient and they are lost
CC after 1 hour of stimulation with TNF (By similarity). Interacts with
CC GGA1. {ECO:0000250, ECO:0000269|PubMed:14559117,
CC ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:14755250,
CC ECO:0000269|PubMed:16123141, ECO:0000269|PubMed:18615712,
CC ECO:0000269|PubMed:18724389, ECO:0000269|PubMed:19131965,
CC ECO:0000269|PubMed:20676133}.
CC -!- INTERACTION:
CC Q9Y3C5; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-396669, EBI-10173507;
CC Q9Y3C5; Q6ZTN6-2: ANKRD13D; NbExp=3; IntAct=EBI-396669, EBI-25840993;
CC Q9Y3C5; Q8N8A2-2: ANKRD44; NbExp=3; IntAct=EBI-396669, EBI-21636328;
CC Q9Y3C5; Q86WR3: ANUBL1; NbExp=3; IntAct=EBI-396669, EBI-25880850;
CC Q9Y3C5; P13928: ANXA8; NbExp=3; IntAct=EBI-396669, EBI-2556915;
CC Q9Y3C5; D3DTF8: APLN; NbExp=3; IntAct=EBI-396669, EBI-22002556;
CC Q9Y3C5; P05067: APP; NbExp=3; IntAct=EBI-396669, EBI-77613;
CC Q9Y3C5; O94778: AQP8; NbExp=3; IntAct=EBI-396669, EBI-19124986;
CC Q9Y3C5; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-396669, EBI-2875816;
CC Q9Y3C5; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-396669, EBI-25844820;
CC Q9Y3C5; Q8WXK3: ASB13; NbExp=3; IntAct=EBI-396669, EBI-707573;
CC Q9Y3C5; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-396669, EBI-14199987;
CC Q9Y3C5; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-396669, EBI-10254793;
CC Q9Y3C5; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-396669, EBI-9089489;
CC Q9Y3C5; Q9H0Y0: ATG10; NbExp=3; IntAct=EBI-396669, EBI-1048913;
CC Q9Y3C5; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-396669, EBI-2891281;
CC Q9Y3C5; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-396669, EBI-4290814;
CC Q9Y3C5; P46379-2: BAG6; NbExp=3; IntAct=EBI-396669, EBI-10988864;
CC Q9Y3C5; Q16611: BAK1; NbExp=3; IntAct=EBI-396669, EBI-519866;
CC Q9Y3C5; Q8IXM2: BAP18; NbExp=3; IntAct=EBI-396669, EBI-4280811;
CC Q9Y3C5; Q14457: BECN1; NbExp=3; IntAct=EBI-396669, EBI-949378;
CC Q9Y3C5; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-396669, EBI-2837444;
CC Q9Y3C5; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-396669, EBI-10693038;
CC Q9Y3C5; Q8WZ55: BSND; NbExp=3; IntAct=EBI-396669, EBI-7996695;
CC Q9Y3C5; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-396669, EBI-751596;
CC Q9Y3C5; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-396669, EBI-25850646;
CC Q9Y3C5; Q96DZ5: CLIP3; NbExp=3; IntAct=EBI-396669, EBI-12823145;
CC Q9Y3C5; Q9BT09: CNPY3; NbExp=3; IntAct=EBI-396669, EBI-2835965;
CC Q9Y3C5; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-396669, EBI-25836090;
CC Q9Y3C5; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-396669, EBI-350590;
CC Q9Y3C5; P01040: CSTA; NbExp=3; IntAct=EBI-396669, EBI-724303;
CC Q9Y3C5; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-396669, EBI-12024320;
CC Q9Y3C5; P00167: CYB5A; NbExp=3; IntAct=EBI-396669, EBI-1047284;
CC Q9Y3C5; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-396669, EBI-25842815;
CC Q9Y3C5; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-396669, EBI-25842538;
CC Q9Y3C5; Q5VZB9: DMRTA1; NbExp=3; IntAct=EBI-396669, EBI-3939812;
CC Q9Y3C5; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-396669, EBI-10694655;
CC Q9Y3C5; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-396669, EBI-25847826;
CC Q9Y3C5; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-396669, EBI-724653;
CC Q9Y3C5; O75530-2: EED; NbExp=3; IntAct=EBI-396669, EBI-11132357;
CC Q9Y3C5; I6L9I8: EPN3; NbExp=3; IntAct=EBI-396669, EBI-12866582;
CC Q9Y3C5; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-396669, EBI-12260294;
CC Q9Y3C5; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-396669, EBI-10213520;
CC Q9Y3C5; Q99504: EYA3; NbExp=3; IntAct=EBI-396669, EBI-9089567;
CC Q9Y3C5; O15540: FABP7; NbExp=3; IntAct=EBI-396669, EBI-10697159;
CC Q9Y3C5; Q6P587-2: FAHD1; NbExp=3; IntAct=EBI-396669, EBI-12902289;
CC Q9Y3C5; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-396669, EBI-3893327;
CC Q9Y3C5; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-396669, EBI-11793142;
CC Q9Y3C5; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-396669, EBI-5461838;
CC Q9Y3C5; Q9NW38: FANCL; NbExp=3; IntAct=EBI-396669, EBI-2339898;
CC Q9Y3C5; P15407: FOSL1; NbExp=3; IntAct=EBI-396669, EBI-744510;
CC Q9Y3C5; P35575: G6PC1; NbExp=3; IntAct=EBI-396669, EBI-3906612;
CC Q9Y3C5; P15976-2: GATA1; NbExp=3; IntAct=EBI-396669, EBI-9090198;
CC Q9Y3C5; P23769-2: GATA2; NbExp=3; IntAct=EBI-396669, EBI-21856389;
CC Q9Y3C5; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-396669, EBI-8799578;
CC Q9Y3C5; Q9UJY5: GGA1; NbExp=7; IntAct=EBI-396669, EBI-447141;
CC Q9Y3C5; P62879: GNB2; NbExp=3; IntAct=EBI-396669, EBI-356942;
CC Q9Y3C5; Q9HBQ8: GOLGA2P5; NbExp=3; IntAct=EBI-396669, EBI-22000587;
CC Q9Y3C5; O95872: GPANK1; NbExp=3; IntAct=EBI-396669, EBI-751540;
CC Q9Y3C5; Q7Z602: GPR141; NbExp=3; IntAct=EBI-396669, EBI-21649723;
CC Q9Y3C5; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-396669, EBI-347538;
CC Q9Y3C5; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-396669, EBI-2868501;
CC Q9Y3C5; P68431: H3C12; NbExp=3; IntAct=EBI-396669, EBI-79722;
CC Q9Y3C5; A0A024R1L7: hCG_41307; NbExp=3; IntAct=EBI-396669, EBI-25849938;
CC Q9Y3C5; P52790: HK3; NbExp=3; IntAct=EBI-396669, EBI-2965780;
CC Q9Y3C5; P09017: HOXC4; NbExp=3; IntAct=EBI-396669, EBI-3923226;
CC Q9Y3C5; Q14005-2: IL16; NbExp=3; IntAct=EBI-396669, EBI-17178971;
CC Q9Y3C5; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-396669, EBI-743980;
CC Q9Y3C5; Q9UNL4: ING4; NbExp=3; IntAct=EBI-396669, EBI-2866661;
CC Q9Y3C5; Q8IXL9: IQCF2; NbExp=3; IntAct=EBI-396669, EBI-10238842;
CC Q9Y3C5; Q8NA54: IQUB; NbExp=3; IntAct=EBI-396669, EBI-10220600;
CC Q9Y3C5; Q96J02: ITCH; NbExp=2; IntAct=EBI-396669, EBI-1564678;
CC Q9Y3C5; Q9NVX7-2: KBTBD4; NbExp=3; IntAct=EBI-396669, EBI-25871195;
CC Q9Y3C5; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-396669, EBI-742916;
CC Q9Y3C5; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-396669, EBI-2796400;
CC Q9Y3C5; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-396669, EBI-714379;
CC Q9Y3C5; Q14525: KRT33B; NbExp=3; IntAct=EBI-396669, EBI-1049638;
CC Q9Y3C5; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-396669, EBI-10241353;
CC Q9Y3C5; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-396669, EBI-10261141;
CC Q9Y3C5; Q14847-2: LASP1; NbExp=3; IntAct=EBI-396669, EBI-9088686;
CC Q9Y3C5; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-396669, EBI-10245913;
CC Q9Y3C5; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-396669, EBI-10258746;
CC Q9Y3C5; Q68G74: LHX8; NbExp=3; IntAct=EBI-396669, EBI-8474075;
CC Q9Y3C5; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-396669, EBI-739832;
CC Q9Y3C5; A2RU56: LOC401296; NbExp=3; IntAct=EBI-396669, EBI-9088215;
CC Q9Y3C5; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-396669, EBI-749562;
CC Q9Y3C5; Q14693: LPIN1; NbExp=3; IntAct=EBI-396669, EBI-5278370;
CC Q9Y3C5; P61244-4: MAX; NbExp=3; IntAct=EBI-396669, EBI-25848049;
CC Q9Y3C5; Q03112-9: MECOM; NbExp=3; IntAct=EBI-396669, EBI-23820194;
CC Q9Y3C5; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-396669, EBI-8487781;
CC Q9Y3C5; Q15049: MLC1; NbExp=3; IntAct=EBI-396669, EBI-8475277;
CC Q9Y3C5; P51948: MNAT1; NbExp=3; IntAct=EBI-396669, EBI-716139;
CC Q9Y3C5; Q8N594: MPND; NbExp=3; IntAct=EBI-396669, EBI-2512452;
CC Q9Y3C5; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-396669, EBI-10699187;
CC Q9Y3C5; P46934: NEDD4; NbExp=7; IntAct=EBI-396669, EBI-726944;
CC Q9Y3C5; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-396669, EBI-718372;
CC Q9Y3C5; Q8NBF2-2: NHLRC2; NbExp=3; IntAct=EBI-396669, EBI-10697320;
CC Q9Y3C5; Q14995: NR1D2; NbExp=3; IntAct=EBI-396669, EBI-6144053;
CC Q9Y3C5; Q6X4W1-6: NSMF; NbExp=3; IntAct=EBI-396669, EBI-25842707;
CC Q9Y3C5; P36639-4: NUDT1; NbExp=3; IntAct=EBI-396669, EBI-25834643;
CC Q9Y3C5; O15381-5: NVL; NbExp=3; IntAct=EBI-396669, EBI-18577082;
CC Q9Y3C5; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-396669, EBI-9090919;
CC Q9Y3C5; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-396669, EBI-1058491;
CC Q9Y3C5; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-396669, EBI-25830200;
CC Q9Y3C5; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-396669, EBI-17159452;
CC Q9Y3C5; Q9NV79: PCMTD2; NbExp=3; IntAct=EBI-396669, EBI-6309018;
CC Q9Y3C5; Q9UF11-2: PLEKHB1; NbExp=3; IntAct=EBI-396669, EBI-12832742;
CC Q9Y3C5; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-396669, EBI-12891828;
CC Q9Y3C5; Q8NA72-3: POC5; NbExp=3; IntAct=EBI-396669, EBI-11751537;
CC Q9Y3C5; P54646: PRKAA2; NbExp=3; IntAct=EBI-396669, EBI-1383852;
CC Q9Y3C5; O43741: PRKAB2; NbExp=3; IntAct=EBI-396669, EBI-1053424;
CC Q9Y3C5; O60260-5: PRKN; NbExp=3; IntAct=EBI-396669, EBI-21251460;
CC Q9Y3C5; P11908: PRPS2; NbExp=3; IntAct=EBI-396669, EBI-4290895;
CC Q9Y3C5; P40306: PSMB10; NbExp=3; IntAct=EBI-396669, EBI-603329;
CC Q9Y3C5; P28070: PSMB4; NbExp=3; IntAct=EBI-396669, EBI-603350;
CC Q9Y3C5; P28062-2: PSMB8; NbExp=3; IntAct=EBI-396669, EBI-372312;
CC Q9Y3C5; P47897: QARS1; NbExp=10; IntAct=EBI-396669, EBI-347462;
CC Q9Y3C5; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-396669, EBI-14093916;
CC Q9Y3C5; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-396669, EBI-746228;
CC Q9Y3C5; Q96PK6: RBM14; NbExp=3; IntAct=EBI-396669, EBI-954272;
CC Q9Y3C5; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-396669, EBI-17589229;
CC Q9Y3C5; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-396669, EBI-714023;
CC Q9Y3C5; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-396669, EBI-25829984;
CC Q9Y3C5; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-396669, EBI-749039;
CC Q9Y3C5; Q9UBS8: RNF14; NbExp=3; IntAct=EBI-396669, EBI-2130308;
CC Q9Y3C5; Q8IYW5: RNF168; NbExp=4; IntAct=EBI-396669, EBI-914207;
CC Q9Y3C5; Q96D59: RNF183; NbExp=3; IntAct=EBI-396669, EBI-743938;
CC Q9Y3C5; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-396669, EBI-751555;
CC Q9Y3C5; P62244: RPS15A; NbExp=3; IntAct=EBI-396669, EBI-347895;
CC Q9Y3C5; P62979: RPS27A; NbExp=4; IntAct=EBI-396669, EBI-357375;
CC Q9Y3C5; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-396669, EBI-10248967;
CC Q9Y3C5; Q8N488: RYBP; NbExp=3; IntAct=EBI-396669, EBI-752324;
CC Q9Y3C5; Q7Z3H4: SAMD7; NbExp=3; IntAct=EBI-396669, EBI-12148649;
CC Q9Y3C5; P34741: SDC2; NbExp=3; IntAct=EBI-396669, EBI-1172957;
CC Q9Y3C5; O00560: SDCBP; NbExp=3; IntAct=EBI-396669, EBI-727004;
CC Q9Y3C5; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-396669, EBI-9089805;
CC Q9Y3C5; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-396669, EBI-346595;
CC Q9Y3C5; Q9NUL5-3: SHFL; NbExp=3; IntAct=EBI-396669, EBI-22000547;
CC Q9Y3C5; O60902-3: SHOX2; NbExp=3; IntAct=EBI-396669, EBI-9092164;
CC Q9Y3C5; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-396669, EBI-358545;
CC Q9Y3C5; Q9NSD5-3: SLC6A13; NbExp=3; IntAct=EBI-396669, EBI-25831241;
CC Q9Y3C5; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-396669, EBI-9845742;
CC Q9Y3C5; Q9HAU4: SMURF2; NbExp=5; IntAct=EBI-396669, EBI-396727;
CC Q9Y3C5; Q92966: SNAPC3; NbExp=3; IntAct=EBI-396669, EBI-1760638;
CC Q9Y3C5; Q13573: SNW1; NbExp=3; IntAct=EBI-396669, EBI-632715;
CC Q9Y3C5; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-396669, EBI-11959123;
CC Q9Y3C5; A0A024R4B0: SPATA3; NbExp=3; IntAct=EBI-396669, EBI-14123856;
CC Q9Y3C5; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-396669, EBI-8635958;
CC Q9Y3C5; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-396669, EBI-10174456;
CC Q9Y3C5; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-396669, EBI-8345366;
CC Q9Y3C5; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-396669, EBI-7082156;
CC Q9Y3C5; Q9C004: SPRY4; NbExp=3; IntAct=EBI-396669, EBI-354861;
CC Q9Y3C5; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-396669, EBI-2659201;
CC Q9Y3C5; Q99619: SPSB2; NbExp=3; IntAct=EBI-396669, EBI-2323209;
CC Q9Y3C5; Q92783-2: STAM; NbExp=3; IntAct=EBI-396669, EBI-12025738;
CC Q9Y3C5; O75886: STAM2; NbExp=4; IntAct=EBI-396669, EBI-373258;
CC Q9Y3C5; O95630: STAMBP; NbExp=5; IntAct=EBI-396669, EBI-396676;
CC Q9Y3C5; Q17RD7-3: SYT16; NbExp=3; IntAct=EBI-396669, EBI-25861603;
CC Q9Y3C5; Q9BQG1: SYT3; NbExp=3; IntAct=EBI-396669, EBI-17284568;
CC Q9Y3C5; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-396669, EBI-745958;
CC Q9Y3C5; Q86VP1: TAX1BP1; NbExp=2; IntAct=EBI-396669, EBI-529518;
CC Q9Y3C5; P62380: TBPL1; NbExp=3; IntAct=EBI-396669, EBI-716225;
CC Q9Y3C5; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-396669, EBI-2116184;
CC Q9Y3C5; Q13569: TDG; NbExp=3; IntAct=EBI-396669, EBI-348333;
CC Q9Y3C5; P28347-2: TEAD1; NbExp=3; IntAct=EBI-396669, EBI-12151837;
CC Q9Y3C5; Q96A09: TENT5B; NbExp=3; IntAct=EBI-396669, EBI-752030;
CC Q9Y3C5; Q8NA77: TEX19; NbExp=3; IntAct=EBI-396669, EBI-13323487;
CC Q9Y3C5; O60830: TIMM17B; NbExp=3; IntAct=EBI-396669, EBI-2372529;
CC Q9Y3C5; Q04724: TLE1; NbExp=3; IntAct=EBI-396669, EBI-711424;
CC Q9Y3C5; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-396669, EBI-25830583;
CC Q9Y3C5; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-396669, EBI-10242677;
CC Q9Y3C5; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-396669, EBI-25831574;
CC Q9Y3C5; P21580: TNFAIP3; NbExp=2; IntAct=EBI-396669, EBI-527670;
CC Q9Y3C5; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-396669, EBI-74615;
CC Q9Y3C5; P19474: TRIM21; NbExp=3; IntAct=EBI-396669, EBI-81290;
CC Q9Y3C5; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-396669, EBI-17716262;
CC Q9Y3C5; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-396669, EBI-11523450;
CC Q9Y3C5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-396669, EBI-12806590;
CC Q9Y3C5; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-396669, EBI-739485;
CC Q9Y3C5; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-396669, EBI-10964469;
CC Q9Y3C5; P62987: UBA52; NbExp=4; IntAct=EBI-396669, EBI-357304;
CC Q9Y3C5; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-396669, EBI-749370;
CC Q9Y3C5; Q8NBM4-4: UBAC2; NbExp=3; IntAct=EBI-396669, EBI-25840976;
CC Q9Y3C5; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-396669, EBI-7353612;
CC Q9Y3C5; P0CG47: UBB; NbExp=3; IntAct=EBI-396669, EBI-413034;
CC Q9Y3C5; P51668: UBE2D1; NbExp=9; IntAct=EBI-396669, EBI-743540;
CC Q9Y3C5; P62837: UBE2D2; NbExp=10; IntAct=EBI-396669, EBI-347677;
CC Q9Y3C5; P61077: UBE2D3; NbExp=3; IntAct=EBI-396669, EBI-348268;
CC Q9Y3C5; Q9Y2X8: UBE2D4; NbExp=10; IntAct=EBI-396669, EBI-745527;
CC Q9Y3C5; P51965: UBE2E1; NbExp=2; IntAct=EBI-396669, EBI-348546;
CC Q9Y3C5; Q969T4: UBE2E3; NbExp=4; IntAct=EBI-396669, EBI-348496;
CC Q9Y3C5; P61088: UBE2N; NbExp=4; IntAct=EBI-396669, EBI-1052908;
CC Q9Y3C5; Q13404: UBE2V1; NbExp=4; IntAct=EBI-396669, EBI-1050671;
CC Q9Y3C5; Q9UHD9: UBQLN2; NbExp=4; IntAct=EBI-396669, EBI-947187;
CC Q9Y3C5; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-396669, EBI-11530712;
CC Q9Y3C5; Q96RL1-2: UIMC1; NbExp=3; IntAct=EBI-396669, EBI-17761788;
CC Q9Y3C5; O75604-3: USP2; NbExp=3; IntAct=EBI-396669, EBI-10696113;
CC Q9Y3C5; P45880: VDAC2; NbExp=3; IntAct=EBI-396669, EBI-354022;
CC Q9Y3C5; P40337-2: VHL; NbExp=3; IntAct=EBI-396669, EBI-12157263;
CC Q9Y3C5; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-396669, EBI-2850578;
CC Q9Y3C5; P58304: VSX2; NbExp=3; IntAct=EBI-396669, EBI-6427899;
CC Q9Y3C5; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-396669, EBI-1237307;
CC Q9Y3C5; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-396669, EBI-7705033;
CC Q9Y3C5; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-396669, EBI-12040603;
CC Q9Y3C5; O00308: WWP2; NbExp=7; IntAct=EBI-396669, EBI-743923;
CC Q9Y3C5; P12956: XRCC6; NbExp=3; IntAct=EBI-396669, EBI-353208;
CC Q9Y3C5; O43167-2: ZBTB24; NbExp=3; IntAct=EBI-396669, EBI-25842419;
CC Q9Y3C5; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-396669, EBI-14104088;
CC Q9Y3C5; Q5W0Z9-4: ZDHHC20; NbExp=3; IntAct=EBI-396669, EBI-25840130;
CC Q9Y3C5; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-396669, EBI-2602314;
CC Q9Y3C5; Q9UJW8-4: ZNF180; NbExp=3; IntAct=EBI-396669, EBI-12055755;
CC Q9Y3C5; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-396669, EBI-8834821;
CC Q9Y3C5; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-396669, EBI-12988373;
CC Q9Y3C5; Q8N895: ZNF366; NbExp=3; IntAct=EBI-396669, EBI-2813661;
CC Q9Y3C5; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-396669, EBI-12010736;
CC Q9Y3C5; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-396669, EBI-25831733;
CC Q9Y3C5; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-396669, EBI-10486136;
CC Q9Y3C5; Q96C55: ZNF524; NbExp=3; IntAct=EBI-396669, EBI-10283126;
CC Q9Y3C5; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-396669, EBI-8490788;
CC Q9Y3C5; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-396669, EBI-12939666;
CC Q9Y3C5; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-396669, EBI-745276;
CC Q9Y3C5; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-396669, EBI-1538838;
CC Q9Y3C5; A0A384ME25; NbExp=3; IntAct=EBI-396669, EBI-10211777;
CC Q9Y3C5; B7Z3E8; NbExp=3; IntAct=EBI-396669, EBI-25831617;
CC Q9Y3C5; Q7L8T7; NbExp=3; IntAct=EBI-396669, EBI-25831943;
CC -!- SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cytoplasm.
CC Nucleus. Note=Predominantly cytoplasmic, when unphosphorylated, and
CC nuclear, when phosphorylated by PKB/AKT1.
CC {ECO:0000269|PubMed:16123141}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in the lung, liver, kidney,
CC pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and
CC peripheral blood lymphocytes, and, at intermediate levels, in the
CC testis, heart, brain and placenta. Highest expression in the skeletal
CC muscle. In the brain, expressed at different levels in several regions:
CC high levels in the amygdala, moderate in the hippocampus and thalamus,
CC low in the caudate and extremely low levels in the corpus callosum (at
CC protein level). Restricted to neurons, enriched in somatodendritic
CC compartments and excluded from white matter (at protein level). In
CC substantia nigra, present in cell bodies and processes of dopaminergic
CC and nondopaminergic cells (at protein level). In Parkinson disease,
CC sequestered in Lewy bodies and neurites. Overexpressed in breast cancer
CC cells, but not detected in the surrounding stroma and weakly, if at
CC all, in normal breast epithelial cells (at protein level). Also
CC expressed in several tumor cell lines. {ECO:0000269|PubMed:14559117,
CC ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:17917589}.
CC -!- DOMAIN: The PPxY motif mediates interaction with NEDD4. {ECO:0000250}.
CC -!- PTM: Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as
CC well as WWP1. {ECO:0000269|PubMed:14562029,
CC ECO:0000269|PubMed:20676133}.
CC -!- PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the
CC proteasome. {ECO:0000269|PubMed:16123141}.
CC -!- PTM: Acylation at both Gly-2 and Cys-4 is required for proper
CC localization to the endosomes. {ECO:0000269|PubMed:20676133}.
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DR EMBL; AB024703; BAA84683.1; -; mRNA.
DR EMBL; AF151881; AAD34118.1; -; mRNA.
DR EMBL; AK293047; BAF85736.1; -; mRNA.
DR EMBL; AK313140; BAG35959.1; -; mRNA.
DR EMBL; AL162430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06831.1; -; Genomic_DNA.
DR EMBL; BC020964; AAH20964.1; -; mRNA.
DR EMBL; BC047654; AAH47654.1; -; mRNA.
DR CCDS; CCDS556.1; -.
DR RefSeq; NP_055187.1; NM_014372.4.
DR AlphaFoldDB; Q9Y3C5; -.
DR SMR; Q9Y3C5; -.
DR BioGRID; 117941; 162.
DR CORUM; Q9Y3C5; -.
DR IntAct; Q9Y3C5; 272.
DR MINT; Q9Y3C5; -.
DR STRING; 9606.ENSP00000242719; -.
DR iPTMnet; Q9Y3C5; -.
DR PhosphoSitePlus; Q9Y3C5; -.
DR SwissPalm; Q9Y3C5; -.
DR BioMuta; RNF11; -.
DR DMDM; 21362884; -.
DR EPD; Q9Y3C5; -.
DR jPOST; Q9Y3C5; -.
DR MassIVE; Q9Y3C5; -.
DR MaxQB; Q9Y3C5; -.
DR PaxDb; 9606-ENSP00000242719; -.
DR PeptideAtlas; Q9Y3C5; -.
DR ProteomicsDB; 86014; -.
DR Pumba; Q9Y3C5; -.
DR Antibodypedia; 32937; 214 antibodies from 24 providers.
DR DNASU; 26994; -.
DR Ensembl; ENST00000242719.4; ENSP00000242719.3; ENSG00000123091.5.
DR GeneID; 26994; -.
DR KEGG; hsa:26994; -.
DR MANE-Select; ENST00000242719.4; ENSP00000242719.3; NM_014372.5; NP_055187.1.
DR UCSC; uc001csi.5; human.
DR AGR; HGNC:10056; -.
DR CTD; 26994; -.
DR DisGeNET; 26994; -.
DR GeneCards; RNF11; -.
DR HGNC; HGNC:10056; RNF11.
DR HPA; ENSG00000123091; Low tissue specificity.
DR MIM; 612598; gene.
DR neXtProt; NX_Q9Y3C5; -.
DR OpenTargets; ENSG00000123091; -.
DR PharmGKB; PA34420; -.
DR VEuPathDB; HostDB:ENSG00000123091; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00730000110988; -.
DR HOGENOM; CLU_123539_1_0_1; -.
DR InParanoid; Q9Y3C5; -.
DR OMA; HLDCIDN; -.
DR OrthoDB; 5474929at2759; -.
DR PhylomeDB; Q9Y3C5; -.
DR TreeFam; TF318022; -.
DR PathwayCommons; Q9Y3C5; -.
DR SignaLink; Q9Y3C5; -.
DR SIGNOR; Q9Y3C5; -.
DR BioGRID-ORCS; 26994; 45 hits in 1199 CRISPR screens.
DR ChiTaRS; RNF11; human.
DR GeneWiki; RNF11; -.
DR GenomeRNAi; 26994; -.
DR Pharos; Q9Y3C5; Tbio.
DR PRO; PR:Q9Y3C5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y3C5; Protein.
DR Bgee; ENSG00000123091; Expressed in lateral nuclear group of thalamus and 213 other cell types or tissues.
DR Genevisible; Q9Y3C5; HS.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd16468; RING-H2_RNF11; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042981; RNF11_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46359; GEO07743P1; 1.
DR PANTHER; PTHR46359:SF1; RING FINGER PROTEIN 11; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endosome; Lipoprotein; Metal-binding;
KW Myristate; Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..154
FT /note="RING finger protein 11"
FT /id="PRO_0000056050"
FT ZN_FING 99..140
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..40
FT /note="PPxY motif"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYK7"
FT MOD_RES 135
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:16123141"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681,
FT ECO:0000269|PubMed:20676133"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:20676133"
FT VARIANT 11
FT /note="D -> E (in dbSNP:rs12077069)"
FT /id="VAR_058272"
FT MUTAGEN 2
FT /note="G->A: Loss of myristoylation. Change in subcellular
FT location: Becomes diffused throughout the cytosol. Strong
FT reduction of ubiquitination. Reduced efficiency of ITCH-
FT binding."
FT /evidence="ECO:0000269|PubMed:20676133"
FT MUTAGEN 4
FT /note="C->S: Change in subcellular location: Becomes
FT partially cytosolic and retained in association with the
FT Golgi apparatus. Partial reduction of ubiquitination."
FT /evidence="ECO:0000269|PubMed:20676133"
FT MUTAGEN 12
FT /note="D->A: Loss of GGA1-binding."
FT /evidence="ECO:0000269|PubMed:20676133"
FT MUTAGEN 15
FT /note="L->A: Loss of GGA1-binding."
FT /evidence="ECO:0000269|PubMed:20676133"
FT MUTAGEN 16
FT /note="L->A: Loss of GGA1-binding."
FT /evidence="ECO:0000269|PubMed:20676133"
FT MUTAGEN 40
FT /note="Y->A: Loss of ITCH-, SMURF2- and WWP1-binding.
FT Partial loss of ubiquitination by ITCH. No effect on
FT STAMBP-binding; when associated with S-99 and S-102.
FT Persistent TNF-mediated NFKBIA phosphorylation. Loss of
FT stimulus-dependent complex formation with TAX1BP1, TNFAIP3
FT and RIPK1."
FT /evidence="ECO:0000269|PubMed:14559117,
FT ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:14755250,
FT ECO:0000269|PubMed:18724389, ECO:0000269|PubMed:19131965"
FT MUTAGEN 99
FT /note="C->S: No effect on STAMBP- and SMURF2-binding; when
FT associated with S-102. Persistent TNF-mediated NFKBIA
FT phosphorylation. No effect on STAMBP-binding; when
FT associated with A-40 and S-102. No effect on ubiquitination
FT by ITCH; when associated with S-102. Loss of stimulus-
FT dependent complex formation with TAX1BP1, TNFAIP3 and
FT RIPK1."
FT /evidence="ECO:0000269|PubMed:14562029,
FT ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:19131965,
FT ECO:0000269|PubMed:20676133"
FT MUTAGEN 102
FT /note="C->S: No effect on STAMBP- and SMURF2-binding; when
FT associated with S-99. No effect on ubiquitination by ITCH;
FT when associated with S-102. No effect on STAMBP-binding;
FT when associated with A-40 and S-99."
FT /evidence="ECO:0000269|PubMed:14562029,
FT ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:20676133"
FT MUTAGEN 103
FT /note="M->A,G: Loss of UBE2N-binding. No gain of UBE2L3-
FT binding."
FT /evidence="ECO:0000269|PubMed:18615712"
FT MUTAGEN 103
FT /note="M->L: No effect on UBE2N-binding. No gain of UBE2L3-
FT binding; when associated with L-127 and L-128."
FT /evidence="ECO:0000269|PubMed:18615712"
FT MUTAGEN 103
FT /note="M->V: No effect on UBE2N-binding. Gain of UBE2L3-
FT binding."
FT /evidence="ECO:0000269|PubMed:18615712"
FT MUTAGEN 127
FT /note="D->L: No effect on UBE2N-binding. No gain of UBE2L3-
FT binding; when associated with L-128."
FT /evidence="ECO:0000269|PubMed:18615712"
FT MUTAGEN 128
FT /note="D->L: No effect on UBE2N-binding. No gain of UBE2L3-
FT binding."
FT /evidence="ECO:0000269|PubMed:18615712"
FT MUTAGEN 135
FT /note="T->E: Loss of phosphorylation and of 14-3-3-
FT binding."
FT /evidence="ECO:0000269|PubMed:16123141"
FT CONFLICT 124
FT /note="D -> G (in Ref. 3; BAF85736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17444 MW; C368E38148FC1D0D CRC64;
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH PTPSQTRLAT
QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI
YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN
//
