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Q9D304

- RN128_MOUSE

UniProt

Q9D304 - RN128_MOUSE

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Protein

E3 ubiquitin-protein ligase RNF128

Gene

Rnf128

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri277 – 31842RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin-protein transferase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of cytokine biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF128 (EC:6.3.2.-)
Alternative name(s):
Gene related to anergy in lymphocytes protein
Goliath-related E3 ubiquitin-protein ligase 1
RING finger protein 128
Gene namesi
Name:Rnf128
Synonyms:Grail, Greul1
ORF Names:MNCb-3816
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1914139. Rnf128.

Subcellular locationi

Endomembrane system By similarity; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmperinuclear region By similarity
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 (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei208 – 22821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. endoplasmic reticulum Source: MGI
  3. Golgi apparatus Source: MGI
  4. integral component of membrane Source: UniProtKB-KW
  5. late endosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi277 – 2771C → G: Loss of ubiquitination activity. 1 Publication
Mutagenesisi280 – 2801C → G: Loss of ubiquitination activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence AnalysisAdd
BLAST
Chaini39 – 428390E3 ubiquitin-protein ligase RNF128PRO_0000261413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Auto-ubiquitinated. Controls the development of T-cell clonal anergy by ubiquitination (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9D304.
PRIDEiQ9D304.

PTM databases

PhosphoSiteiQ9D304.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Inductioni

Induced under anergic conditions. Up-regulated during T-cell anergy induction following signaling through the T-cell antigen receptor (By similarity).By similarity

Gene expression databases

BgeeiQ9D304.
CleanExiMM_RNF128.
ExpressionAtlasiQ9D304. baseline and differential.
GenevestigatoriQ9D304.

Interactioni

Protein-protein interaction databases

BioGridi211790. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9D304.
SMRiQ9D304. Positions 38-204, 277-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 183109PAAdd
BLAST

Domaini

Binding to E2 ubiquitin-conjugating enzyme requires an intact RING finger domain.By similarity

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri277 – 31842RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG271676.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
HOVERGENiHBG057659.
InParanoidiQ9D304.
KOiK10629.
PhylomeDBiQ9D304.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. Protease-assoc_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D304-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPPPGIGVY CRGGCGAARL LAWCFLLALS PHAPGSRGAE AVWTAYLNVS
60 70 80 90 100
WRVPHTGVNR TVWELSEEGV YGQDSPLEPV SGVLVPPDGP GALNACNPHT
110 120 130 140 150
NFTVPTVWGS TVQVSWLALI QRGGGCTFAD KIHLASERGA SGAVIFNFPG
160 170 180 190 200
TRNEVIPMSH PGAGDIVAIM IGNLKGTKIL QSIQRGIQVT MVIEVGKKHG
210 220 230 240 250
PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ SRKQRQLKAD
260 270 280 290 300
AKKAIGKLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
310 320 330 340 350
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEASNTA
360 370 380 390 400
SPHEEDSRSE TASSGYASVQ GADEPPLEEH AQSANENLQL VNHEANSVAV
410 420
DVVPHVDNPT FEEDETPDQE AAVREIKS
Length:428
Mass (Da):46,276
Last modified:June 1, 2001 - v1
Checksum:i480DCF46C75E238F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251G → S in BAB23613. (PubMed:16141072)Curated
Sequence conflicti131 – 1311K → N in BAB23613. (PubMed:16141072)Curated
Sequence conflicti132 – 1321I → V in BAA95033. 1 PublicationCurated
Sequence conflicti352 – 3521P → H in BAE27025. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY112656 mRNA. Translation: AAM51876.1.
AF426411 mRNA. Translation: AAL34514.1.
AB041548 mRNA. Translation: BAA95033.1.
AK004847 mRNA. Translation: BAB23613.1.
AK008312 mRNA. Translation: BAB25595.3.
AK018582 mRNA. Translation: BAB31291.1.
AK146266 mRNA. Translation: BAE27025.1.
AK167031 mRNA. Translation: BAE39203.1.
BC010477 mRNA. Translation: AAH10477.1.
CCDSiCCDS30435.1.
RefSeqiNP_001241690.1. NM_001254761.1.
NP_075759.3. NM_023270.5.
UniGeneiMm.27764.

Genome annotation databases

EnsembliENSMUST00000113026; ENSMUSP00000108649; ENSMUSG00000031438.
GeneIDi66889.
KEGGimmu:66889.
UCSCiuc009uki.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY112656 mRNA. Translation: AAM51876.1 .
AF426411 mRNA. Translation: AAL34514.1 .
AB041548 mRNA. Translation: BAA95033.1 .
AK004847 mRNA. Translation: BAB23613.1 .
AK008312 mRNA. Translation: BAB25595.3 .
AK018582 mRNA. Translation: BAB31291.1 .
AK146266 mRNA. Translation: BAE27025.1 .
AK167031 mRNA. Translation: BAE39203.1 .
BC010477 mRNA. Translation: AAH10477.1 .
CCDSi CCDS30435.1.
RefSeqi NP_001241690.1. NM_001254761.1.
NP_075759.3. NM_023270.5.
UniGenei Mm.27764.

3D structure databases

ProteinModelPortali Q9D304.
SMRi Q9D304. Positions 38-204, 277-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211790. 3 interactions.

PTM databases

PhosphoSitei Q9D304.

Proteomic databases

MaxQBi Q9D304.
PRIDEi Q9D304.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000113026 ; ENSMUSP00000108649 ; ENSMUSG00000031438 .
GeneIDi 66889.
KEGGi mmu:66889.
UCSCi uc009uki.2. mouse.

Organism-specific databases

CTDi 79589.
MGIi MGI:1914139. Rnf128.

Phylogenomic databases

eggNOGi NOG271676.
GeneTreei ENSGT00760000119057.
HOGENOMi HOG000231432.
HOVERGENi HBG057659.
InParanoidi Q9D304.
KOi K10629.
PhylomeDBi Q9D304.
TreeFami TF317486.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

NextBioi 322937.
PROi Q9D304.
SOURCEi Search...

Gene expression databases

Bgeei Q9D304.
CleanExi MM_RNF128.
ExpressionAtlasi Q9D304. baseline and differential.
Genevestigatori Q9D304.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR003137. Protease-assoc_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus development."
    Borchers A.G.M., Hufton A.L., Eldridge A.G., Jackson P.K., Harland R.M., Baker J.C.
    Dev. Biol. 251:395-408(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-277 AND CYS-280.
    Strain: CD-1.
  2. "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells."
    Anandasabapathy N., Ford G.S., Bloom D., Holness C., Paragas V., Seroogy C., Skrenta H., Hollenhorst M., Fathman C.G., Soares L.
    Immunity 18:535-547(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN UBIQUITINATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS.
  3. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum, Liver and Small intestine.
  5. "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].
    Strain: 129.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiRN128_MOUSE
AccessioniPrimary (citable) accession number: Q9D304
Secondary accession number(s): Q3UJY0
, Q9CVG1, Q9DBN3, Q9JJF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3