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Q9D304 (RN128_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Rnf128
Synonyms:Grail, Greul1
ORF Names:MNCb-3816
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Endomembrane system; 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.

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. Ref.2

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. Ref.2

Induction

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

Domain

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

Post-translational modification

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

Sequence similarities

Contains 1 PA (protease associated) domain.

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 428390E3 ubiquitin-protein ligase RNF128
PRO_0000261413

Regions

Transmembrane208 – 22821Helical; Potential
Domain75 – 183109PA
Zinc finger277 – 31842RING-type; atypical

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis2771C → G: Loss of ubiquitination activity. Ref.1
Mutagenesis2801C → G: Loss of ubiquitination activity. Ref.1
Sequence conflict1251G → S in BAB23613. Ref.4
Sequence conflict1311K → N in BAB23613. Ref.4
Sequence conflict1321I → V in BAA95033. Ref.3
Sequence conflict3521P → H in BAE27025. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9D304 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 480DCF46C75E238F

FASTA42846,276
        10         20         30         40         50         60 
MGPPPGIGVY CRGGCGAARL LAWCFLLALS PHAPGSRGAE AVWTAYLNVS WRVPHTGVNR 

        70         80         90        100        110        120 
TVWELSEEGV YGQDSPLEPV SGVLVPPDGP GALNACNPHT NFTVPTVWGS TVQVSWLALI 

       130        140        150        160        170        180 
QRGGGCTFAD KIHLASERGA SGAVIFNFPG TRNEVIPMSH PGAGDIVAIM IGNLKGTKIL 

       190        200        210        220        230        240 
QSIQRGIQVT MVIEVGKKHG PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ 

       250        260        270        280        290        300 
SRKQRQLKAD AKKAIGKLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH 

       310        320        330        340        350        360 
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEASNTA SPHEEDSRSE 

       370        380        390        400        410        420 
TASSGYASVQ GADEPPLEEH AQSANENLQL VNHEANSVAV DVVPHVDNPT FEEDETPDQE 


AAVREIKS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS30435.1.
RefSeqNP_001241690.1. NM_001254761.1.
NP_075759.3. NM_023270.5.
UniGeneMm.27764.

3D structure databases

ProteinModelPortalQ9D304.
SMRQ9D304. Positions 38-204, 277-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211790. 2 interactions.

PTM databases

PhosphoSiteQ9D304.

Proteomic databases

PRIDEQ9D304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113026; ENSMUSP00000108649; ENSMUSG00000031438.
GeneID66889.
KEGGmmu:66889.
UCSCuc009uki.2. mouse.

Organism-specific databases

CTD79589.
MGIMGI:1914139. Rnf128.

Phylogenomic databases

eggNOGNOG271676.
GeneTreeENSGT00730000110457.
HOGENOMHOG000231432.
HOVERGENHBG057659.
InParanoidQ9D304.
KOK10629.
PhylomeDBQ9D304.
TreeFamTF317486.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9D304.
BgeeQ9D304.
CleanExMM_RNF128.
GenevestigatorQ9D304.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR003137. Protease-assoc_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio322937.
PROQ9D304.
SOURCESearch...

Entry information

Entry nameRN128_MOUSE
AccessionPrimary (citable) accession number: Q9D304
Secondary accession number(s): Q3UJY0 expand/collapse secondary AC list , Q9CVG1, Q9DBN3, Q9JJF8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot