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Protein

E3 ubiquitin-protein ligase RNF125

Gene

Rnf125

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

E3 ubiquitin-protein ligase that acts as a positive regulator of T-cell activation. E3 ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).By similarity

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 fingeri37 – 7741RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Adaptive immunity, Immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF125 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 125
Gene namesi
Name:Rnf125
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1914914. Rnf125.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 233232E3 ubiquitin-protein ligase RNF125PRO_0000056092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiQ9D9R0.
PRIDEiQ9D9R0.

PTM databases

iPTMnetiQ9D9R0.
PhosphoSiteiQ9D9R0.

Expressioni

Gene expression databases

BgeeiQ9D9R0.
CleanExiMM_RNF125.
GenevisibleiQ9D9R0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000058251.

Structurei

3D structure databases

ProteinModelPortaliQ9D9R0.
SMRiQ9D9R0. Positions 37-81.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 7741RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IJHI. Eukaryota.
ENOG410YBNH. LUCA.
GeneTreeiENSGT00530000063064.
HOGENOMiHOG000230946.
HOVERGENiHBG098958.
InParanoidiQ9D9R0.
KOiK12170.
OMAiVPNENAN.
OrthoDBiEOG7SFHXF.
PhylomeDBiQ9D9R0.
TreeFamiTF331012.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR008598. Di19_Zn_binding_dom.
IPR027370. Znf-RING_LisH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF05605. zf-Di19. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q9D9R0-1) [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
MGSLLSSDSS KSAPASATPR TLERSGDSEL PITSFDCSVC LEVLHQPVRT
60 70 80 90 100
RCGHVFCRSC IATSIKNNNK WTCPYCRAYL PSEGVPATDI AKRMKSEYQN
110 120 130 140 150
CAECGTLVCL SDMRAHIRTC EKYIDKYGPL LELGDTTARC VCPFCQRELD
160 170 180 190 200
EDCLLDHCII HHRSERRPVF CPLCHSRPDE SPSTFNGSLI RHLQVSHTLF
210 220 230
YDDFIDFDII EEAIIRRVLD RSLLEYVNQS NTT
Length:233
Mass (Da):26,362
Last modified:January 23, 2007 - v3
Checksum:i1B92E1F4F6C0113A
GO
Isoform 2 (identifier: Q9D9R0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Show »
Length:140
Mass (Da):16,302
Checksum:i41DE755191A98B93
GO

Sequence cautioni

The sequence BAB24656.1 differs from that shown. Reason: Frameshift at position 72. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841G → R in BAC34234 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9393Missing in isoform 2. 2 PublicationsVSP_015216Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006569 mRNA. Translation: BAB24656.1. Frameshift.
AK050395 mRNA. Translation: BAC34234.1.
AC138611 Genomic DNA. No translation available.
BC094290 mRNA. Translation: AAH94290.1.
BC116883 mRNA. Translation: AAI16884.1.
BC116887 mRNA. Translation: AAI16888.1.
CCDSiCCDS29088.1. [Q9D9R0-2]
RefSeqiNP_080577.1. NM_026301.2. [Q9D9R0-2]
XP_006526251.1. XM_006526188.2. [Q9D9R0-1]
UniGeneiMm.45980.

Genome annotation databases

EnsembliENSMUST00000050004; ENSMUSP00000058251; ENSMUSG00000033107. [Q9D9R0-2]
GeneIDi67664.
KEGGimmu:67664.
UCSCiuc008eez.1. mouse. [Q9D9R0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006569 mRNA. Translation: BAB24656.1. Frameshift.
AK050395 mRNA. Translation: BAC34234.1.
AC138611 Genomic DNA. No translation available.
BC094290 mRNA. Translation: AAH94290.1.
BC116883 mRNA. Translation: AAI16884.1.
BC116887 mRNA. Translation: AAI16888.1.
CCDSiCCDS29088.1. [Q9D9R0-2]
RefSeqiNP_080577.1. NM_026301.2. [Q9D9R0-2]
XP_006526251.1. XM_006526188.2. [Q9D9R0-1]
UniGeneiMm.45980.

3D structure databases

ProteinModelPortaliQ9D9R0.
SMRiQ9D9R0. Positions 37-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000058251.

PTM databases

iPTMnetiQ9D9R0.
PhosphoSiteiQ9D9R0.

Proteomic databases

PaxDbiQ9D9R0.
PRIDEiQ9D9R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050004; ENSMUSP00000058251; ENSMUSG00000033107. [Q9D9R0-2]
GeneIDi67664.
KEGGimmu:67664.
UCSCiuc008eez.1. mouse. [Q9D9R0-1]

Organism-specific databases

CTDi54941.
MGIiMGI:1914914. Rnf125.

Phylogenomic databases

eggNOGiENOG410IJHI. Eukaryota.
ENOG410YBNH. LUCA.
GeneTreeiENSGT00530000063064.
HOGENOMiHOG000230946.
HOVERGENiHBG098958.
InParanoidiQ9D9R0.
KOiK12170.
OMAiVPNENAN.
OrthoDBiEOG7SFHXF.
PhylomeDBiQ9D9R0.
TreeFamiTF331012.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRnf125. mouse.
NextBioi325181.
PROiQ9D9R0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D9R0.
CleanExiMM_RNF125.
GenevisibleiQ9D9R0. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR008598. Di19_Zn_binding_dom.
IPR027370. Znf-RING_LisH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF05605. zf-Di19. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-233 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-233 (ISOFORM 1).
    Strain: 129.
    Tissue: Brain and Mammary tumor.

Entry informationi

Entry nameiRN125_MOUSE
AccessioniPrimary (citable) accession number: Q9D9R0
Secondary accession number(s): Q0VG32, Q52KL4, Q8C7F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 117 of the entry and version 3 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.