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Protein

E3 ubiquitin-protein ligase RNF133

Gene

Rnf133

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has E3 ubiquitin-protein ligase activity.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri256 – 29742RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • protein autoubiquitination Source: UniProtKB
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 RNF133 (EC:6.3.2.-)
Alternative name(s):
Goliath-related E3 ubiquitin-protein ligase 2
RING finger protein 133
Gene namesi
Name:Rnf133
Synonyms:Greul2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2677436. Rnf133.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei190 – 21021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382E3 ubiquitin-protein ligase RNF133PRO_0000380751Add
BLAST

Post-translational modificationi

Auto-ubiquitinated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PRIDEiQ14B02.

PTM databases

iPTMnetiQ14B02.
PhosphoSiteiQ14B02.

Expressioni

Tissue specificityi

Testis-specific.1 Publication

Developmental stagei

Expression begins in the testis at day 21 and increases dramatically from day 28 and thereafter.1 Publication

Gene expression databases

BgeeiQ14B02.
GenevisibleiQ14B02. MM.

Structurei

3D structure databases

ProteinModelPortaliQ14B02.
SMRiQ14B02. Positions 34-188, 245-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 167103PAAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri256 – 29742RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
InParanoidiQ14B02.
KOiK15702.
OMAiNCIDPWI.
OrthoDBiEOG7W41BX.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14B02-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNPLQTSTWQ NQAPSFWLLR FSFIWLVSQK CCTASAVWTA YMNISFHVGN
60 70 80 90 100
RMLSELGETG VFGRSSILKR VAGVVVPPEG KIQNACDPNT TFILPRNKEP
110 120 130 140 150
WIALIERGGC AFTQKIKVAS EHGARGVIIY NFPGTGNQVF PMSHQAFEDI
160 170 180 190 200
VVVMIGNIKG MEILHLIRKG VHVTVMVEVG RKHVIWLNHY FVSFMIVTTA
210 220 230 240 250
TLAYFTFYHI RRLWVARIEN RRWKRLTREL KKAFGQLQVR VLKEGDEEVN
260 270 280 290 300
PNADSCVICF EAYKPNEIVR ILTCKHFFHK NCIDPWILAH GTCPMCKCDI
310 320 330 340 350
LKALGIQMDI EDGTDSLQVL MSNELPGTLS PVEEETNYEL PPARTSSKVT
360 370 380
HVQEHPTSSA NAGSQPPEAE ETSHPSHGQQ VL
Length:382
Mass (Da):43,102
Last modified:August 22, 2006 - v1
Checksum:i3EC4A20E7B5CF4D0
GO
Isoform 2 (identifier: Q14B02-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-202: Missing.

Show »
Length:339
Mass (Da):38,143
Checksum:i5248DFA7C8EE1ABF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821K → E in AAN75222 (PubMed:12435366).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei160 – 20243Missing in isoform 2. 1 PublicationVSP_037829Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028082 mRNA. Translation: BAC25740.1.
CH466533 Genomic DNA. Translation: EDL13834.1.
BC116423 mRNA. Translation: AAI16424.1.
BC116424 mRNA. Translation: AAI16425.1.
AY155441 mRNA. Translation: AAN75222.1.
CCDSiCCDS19938.1. [Q14B02-2]
RefSeqiNP_937894.1. NM_198251.2. [Q14B02-2]
UniGeneiMm.436547.

Genome annotation databases

EnsembliENSMUST00000063548; ENSMUSP00000066906; ENSMUSG00000051956. [Q14B02-2]
ENSMUST00000115354; ENSMUSP00000111011; ENSMUSG00000051956. [Q14B02-1]
GeneIDi386611.
KEGGimmu:386611.
UCSCiuc009bbk.1. mouse. [Q14B02-2]
uc029vtq.1. mouse. [Q14B02-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028082 mRNA. Translation: BAC25740.1.
CH466533 Genomic DNA. Translation: EDL13834.1.
BC116423 mRNA. Translation: AAI16424.1.
BC116424 mRNA. Translation: AAI16425.1.
AY155441 mRNA. Translation: AAN75222.1.
CCDSiCCDS19938.1. [Q14B02-2]
RefSeqiNP_937894.1. NM_198251.2. [Q14B02-2]
UniGeneiMm.436547.

3D structure databases

ProteinModelPortaliQ14B02.
SMRiQ14B02. Positions 34-188, 245-297.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ14B02.
PhosphoSiteiQ14B02.

Proteomic databases

PRIDEiQ14B02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000063548; ENSMUSP00000066906; ENSMUSG00000051956. [Q14B02-2]
ENSMUST00000115354; ENSMUSP00000111011; ENSMUSG00000051956. [Q14B02-1]
GeneIDi386611.
KEGGimmu:386611.
UCSCiuc009bbk.1. mouse. [Q14B02-2]
uc029vtq.1. mouse. [Q14B02-1]

Organism-specific databases

CTDi168433.
MGIiMGI:2677436. Rnf133.

Phylogenomic databases

GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
InParanoidiQ14B02.
KOiK15702.
OMAiNCIDPWI.
OrthoDBiEOG7W41BX.
TreeFamiTF317486.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi405539.
PROiQ14B02.
SOURCEiSearch...

Gene expression databases

BgeeiQ14B02.
GenevisibleiQ14B02. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
  4. "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] OF 42-381 (ISOFORM 1).
    Strain: CD-1.
  5. "Mouse RING finger protein Rnf133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase."
    Nian H., Zhang W., Shi H., Zhao Q., Xie Q., Liao S., Zhang Y., Zhang Z., Wang C., Han C.
    Cell Res. 18:800-802(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiRN133_MOUSE
AccessioniPrimary (citable) accession number: Q14B02
Secondary accession number(s): Q8C1F1, Q8CGR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: August 22, 2006
Last modified: January 20, 2016
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.