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E3 ubiquitin-protein ligase RNF128 (EC 2.3.2.27) (Gene related to anergy in lymphocytes protein) (Goliath-related E3 ubiquitin-protein ligase 1) (RING finger protein 128) (RING-type E3 ubiquitin transferase RNF128)

 RN128_MOUSE             Reviewed;         428 AA.
Q9D304; Q3UJY0; Q9CVG1; Q9DBN3; Q9JJF8;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
30-AUG-2017, entry version 125.
RecName: Full=E3 ubiquitin-protein ligase RNF128;
EC=2.3.2.27;
AltName: Full=Gene related to anergy in lymphocytes protein;
AltName: Full=Goliath-related E3 ubiquitin-protein ligase 1;
AltName: Full=RING finger protein 128;
AltName: Full=RING-type E3 ubiquitin transferase RNF128 {ECO:0000305};
Flags: Precursor;
Name=Rnf128; Synonyms=Grail, Greul1; ORFNames=MNCb-3816;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-277 AND
CYS-280.
STRAIN=CD-1;
PubMed=12435366; DOI=10.1006/dbio.2002.0814;
Borchers A.G.M., Hufton A.L., Eldridge A.G., Jackson P.K.,
Harland R.M., Baker J.C.;
"The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus
development.";
Dev. Biol. 251:395-408(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN UBIQUITINATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS.
PubMed=12705856; DOI=10.1016/S1074-7613(03)00084-0;
Anandasabapathy N., Ford G.S., Bloom D., Holness C., Paragas V.,
Seroogy C., Skrenta H., Hollenhorst M., Fathman C.G., Soares L.;
"GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene
transcription is expressed in anergic CD4+ T cells.";
Immunity 18:535-547(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
Hashimoto K.;
"Isolation of full-length cDNA clones from mouse brain cDNA library
made by oligo-capping method.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum, Liver, and Small intestine;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129; TISSUE=Mammary tumor;
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).
-!- FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and
'Lys-63'-linked polyubiquitin chains formation. Functions as an
inhibitor of cytokine gene transcription. Inhibits IL2 and IL4
transcription, thereby playing an important role in the induction
of the anergic phenotype, a long-term stable state of T-lymphocyte
unresponsiveness to antigenic stimulation associated with the
blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-
48' linkages and COR1A with 'Lys-63' linkages leading to their
degradation, down-regulation of these cytosleletal components
results in impaired lamellipodium formation and reduced
accumulation of F-actin at the immunological synapse. Functions in
the patterning of the dorsal ectoderm; sensitizes ectoderm to
respond to neural-inducing signals (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12435366, ECO:0000269|PubMed:12705856}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-
pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
Note=Localized in an asymmetric perinuclear punctate manner.
Localizes to the internal pool of the transferrin recycling
endosomal pathway. Partially colocalized with the endoplasmic
reticulum resident HSPA5, with Golgi resident STX5, and with the
late endosomal GTPase RAB7A. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain, kidney, heart, liver,
ovary, testis and thymus. Expression increased as early as 4 hours
by 5- to 7-fold in anergized cultures as compared to resting or
activated cells. {ECO:0000269|PubMed:12705856}.
-!- DEVELOPMENTAL STAGE: At E6.0, expressed in both the extraembryonic
endoderm and extraembryonic ectoderm. After the beginning of
gastrulation, expression remains extraembryonic, and is mostly
confined to the visceral endoderm. At E8.5, expression appears
within the mesodermally derived allantois, and is highly expressed
in the epithelial layer of the yolk sac. At E9.5, expressed in the
hindgut and adjoining yolk sac. At stage E10, appears to be widely
expressed throughout the embryo with higher expression within the
branchial arches and within intersomitic endothelial cells.
{ECO:0000269|PubMed:12705856}.
-!- INDUCTION: Induced under anergic conditions. Up-regulated during
T-cell anergy induction following signaling through the T-cell
antigen receptor. {ECO:0000250|UniProtKB:Q8TEB7}.
-!- DOMAIN: Binding to E2 ubiquitin-conjugating enzyme requires an
intact RING finger domain. {ECO:0000250|UniProtKB:Q8TEB7}.
-!- PTM: Auto-ubiquitinated. Controls the development of T-cell clonal
anergy by ubiquitination. {ECO:0000250|UniProtKB:Q8TEB7}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY112656; AAM51876.1; -; mRNA.
EMBL; AF426411; AAL34514.1; -; mRNA.
EMBL; AB041548; BAA95033.1; -; mRNA.
EMBL; AK004847; BAB23613.1; -; mRNA.
EMBL; AK008312; BAB25595.3; -; mRNA.
EMBL; AK018582; BAB31291.1; -; mRNA.
EMBL; AK146266; BAE27025.1; -; mRNA.
EMBL; AK167031; BAE39203.1; -; mRNA.
EMBL; BC010477; AAH10477.1; -; mRNA.
CCDS; CCDS30435.1; -.
RefSeq; NP_001241690.1; NM_001254761.1.
RefSeq; NP_075759.3; NM_023270.5.
UniGene; Mm.27764; -.
ProteinModelPortal; Q9D304; -.
SMR; Q9D304; -.
BioGrid; 211790; 5.
STRING; 10090.ENSMUSP00000108649; -.
iPTMnet; Q9D304; -.
PhosphoSitePlus; Q9D304; -.
MaxQB; Q9D304; -.
PaxDb; Q9D304; -.
PRIDE; Q9D304; -.
Ensembl; ENSMUST00000113026; ENSMUSP00000108649; ENSMUSG00000031438.
GeneID; 66889; -.
KEGG; mmu:66889; -.
UCSC; uc009uki.2; mouse.
CTD; 79589; -.
MGI; MGI:1914139; Rnf128.
eggNOG; KOG4628; Eukaryota.
eggNOG; ENOG410Z5DF; LUCA.
GeneTree; ENSGT00760000119057; -.
HOGENOM; HOG000231432; -.
HOVERGEN; HBG057659; -.
InParanoid; Q9D304; -.
KO; K10629; -.
OrthoDB; EOG091G08OR; -.
PhylomeDB; Q9D304; -.
TreeFam; TF317486; -.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
UniPathway; UPA00143; -.
PRO; PR:Q9D304; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031438; -.
CleanEx; MM_RNF128; -.
ExpressionAtlas; Q9D304; baseline and differential.
Genevisible; Q9D304; MM.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0042036; P:negative regulation of cytokine biosynthetic process; IDA:MGI.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF02225; PA; 1.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
Metal-binding; Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
SIGNAL 1 38 {ECO:0000255}.
CHAIN 39 428 E3 ubiquitin-protein ligase RNF128.
/FTId=PRO_0000261413.
TRANSMEM 208 228 Helical. {ECO:0000255}.
DOMAIN 75 183 PA.
ZN_FING 277 318 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 277 277 C->G: Loss of ubiquitination activity.
{ECO:0000269|PubMed:12435366}.
MUTAGEN 280 280 C->G: Loss of ubiquitination activity.
{ECO:0000269|PubMed:12435366}.
CONFLICT 125 125 G -> S (in Ref. 4; BAB23613).
{ECO:0000305}.
CONFLICT 131 131 K -> N (in Ref. 4; BAB23613).
{ECO:0000305}.
CONFLICT 132 132 I -> V (in Ref. 3; BAA95033).
{ECO:0000305}.
CONFLICT 352 352 P -> H (in Ref. 4; BAE27025).
{ECO:0000305}.
SEQUENCE 428 AA; 46276 MW; 480DCF46C75E238F CRC64;
MGPPPGIGVY CRGGCGAARL LAWCFLLALS PHAPGSRGAE AVWTAYLNVS WRVPHTGVNR
TVWELSEEGV YGQDSPLEPV SGVLVPPDGP GALNACNPHT NFTVPTVWGS TVQVSWLALI
QRGGGCTFAD KIHLASERGA SGAVIFNFPG TRNEVIPMSH PGAGDIVAIM IGNLKGTKIL
QSIQRGIQVT MVIEVGKKHG PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ
SRKQRQLKAD AKKAIGKLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEASNTA SPHEEDSRSE
TASSGYASVQ GADEPPLEEH AQSANENLQL VNHEANSVAV DVVPHVDNPT FEEDETPDQE
AAVREIKS


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