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Protein

E3 ubiquitin-protein ligase RNF13

Gene

Rnf13

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

Functioni

E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation.1 Publication

Pathway:iprotein 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 fingeri240 – 28243RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

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 RNF13 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 13
Gene namesi
Name:Rnf13
Synonyms:Rzf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1346341. Rnf13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 182148LumenalSequence AnalysisAdd
BLAST
Transmembranei183 – 20321HelicalSequence AnalysisAdd
BLAST
Topological domaini204 – 381178CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • late endosome membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • nuclear inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Lysosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi266 – 2661C → A: Loss of E3 ligase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 381347E3 ubiquitin-protein ligase RNF13PRO_0000056055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Auto-ubiquitinated.1 Publication
N-glycosylated and also modified with chondroitin sulfate.1 Publication

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiO54965.
PRIDEiO54965.

PTM databases

PhosphoSiteiO54965.

Expressioni

Tissue specificityi

Expressed in the brain, heart, kidney, liver and spleen. Higher expression in adult tissues compared to the embryonic counterparts.1 Publication

Gene expression databases

BgeeiO54965.
CleanExiMM_RNF13.
GenevisibleiO54965. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049331.

Structurei

3D structure databases

ProteinModelPortaliO54965.
SMRiO54965. Positions 240-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 16097PAAdd
BLAST

Domaini

The RING-type zinc finger domain is required for E3 ligase activity.

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri240 – 28243RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG260066.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000234362.
HOVERGENiHBG063762.
InParanoidiO54965.
KOiK15692.
OMAiNMTESSE.
OrthoDBiEOG7NW68S.
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]

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: O54965-1) [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
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFED
60 70 80 90 100
LPARFGYRLP AEGLKGFLIN SKPENACEPI VPPPLKDNSS GTFIVLIRRL
110 120 130 140 150
DCNFDIKVLN AQRAGYKAAI VHNVDSDDLI SMGSNDIDTL KKIDIPSVFI
160 170 180 190 200
GESSANSLKD EFTYEKGGHI ILVPELSLPL EYYLIPFLII VGICLILIVI
210 220 230 240 250
FMITKFVQDR HRNRRNRLRK DQLKKLPVHK FKKGDEYDVC AICLEEYEDG
260 270 280 290 300
DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
310 320 330 340 350
EENQVSEHTP LLPPSASART QSFGSLSESH SHHNMTESSD YEDDDNEETD
360 370 380
SSDADNEITD HSVVVQLQPN GEQDYNIANT V
Length:381
Mass (Da):42,732
Last modified:July 27, 2011 - v2
Checksum:i1E0EF4801A2C6FE8
GO
Isoform 2 (identifier: O54965-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     261-268: AYHCKCVD → GMSTHTVL
     269-381: Missing.

Show »
Length:268
Mass (Da):30,249
Checksum:iEB09D3ECF7660546
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti362 – 3621S → I in AAC03770 (Ref. 1) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei261 – 2688AYHCKCVD → GMSTHTVL in isoform 2. 1 PublicationVSP_005749
Alternative sequencei269 – 381113Missing in isoform 2. 1 PublicationVSP_005750Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037205 mRNA. Translation: AAC03770.1.
AF037206 mRNA. Translation: AAC03771.1.
AK158046 mRNA. Translation: BAE34334.1.
CH466530 Genomic DNA. Translation: EDL35322.1.
CH466530 Genomic DNA. Translation: EDL35326.1.
BC058182 mRNA. Translation: AAH58182.1.
CCDSiCCDS50913.1. [O54965-1]
RefSeqiNP_001106884.1. NM_001113413.2. [O54965-1]
NP_036013.1. NM_011883.4. [O54965-2]
XP_006501520.1. XM_006501457.2. [O54965-1]
UniGeneiMm.274360.
Mm.445604.

Genome annotation databases

EnsembliENSMUST00000041826; ENSMUSP00000049331; ENSMUSG00000036503. [O54965-1]
GeneIDi24017.
KEGGimmu:24017.
UCSCiuc008phj.3. mouse. [O54965-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037205 mRNA. Translation: AAC03770.1.
AF037206 mRNA. Translation: AAC03771.1.
AK158046 mRNA. Translation: BAE34334.1.
CH466530 Genomic DNA. Translation: EDL35322.1.
CH466530 Genomic DNA. Translation: EDL35326.1.
BC058182 mRNA. Translation: AAH58182.1.
CCDSiCCDS50913.1. [O54965-1]
RefSeqiNP_001106884.1. NM_001113413.2. [O54965-1]
NP_036013.1. NM_011883.4. [O54965-2]
XP_006501520.1. XM_006501457.2. [O54965-1]
UniGeneiMm.274360.
Mm.445604.

3D structure databases

ProteinModelPortaliO54965.
SMRiO54965. Positions 240-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049331.

PTM databases

PhosphoSiteiO54965.

Proteomic databases

MaxQBiO54965.
PRIDEiO54965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041826; ENSMUSP00000049331; ENSMUSG00000036503. [O54965-1]
GeneIDi24017.
KEGGimmu:24017.
UCSCiuc008phj.3. mouse. [O54965-1]

Organism-specific databases

CTDi11342.
MGIiMGI:1346341. Rnf13.

Phylogenomic databases

eggNOGiNOG260066.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000234362.
HOVERGENiHBG063762.
InParanoidiO54965.
KOiK15692.
OMAiNMTESSE.
OrthoDBiEOG7NW68S.
TreeFamiTF317486.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi303955.
PROiO54965.
SOURCEiSearch...

Gene expression databases

BgeeiO54965.
CleanExiMM_RNF13.
GenevisibleiO54965. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene for a RING zinc finger protein is expressed in the inner chick ear after noise exposure."
    Lomax M.I., Warner S.J., Bersirli C.G., Gong T.-W.L.
    Prim. Sens. Neuron 2:305-316(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "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: Inner ear.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: FVB/N.
    Tissue: Mammary tumor.
  5. "The PA-TM-RING protein RING finger protein 13 is an endosomal integral membrane E3 ubiquitin ligase whose RING finger domain is released to the cytoplasm by proteolysis."
    Bocock J.P., Carmicle S., Chhotani S., Ruffolo M.R., Chu H., Erickson A.H.
    FEBS J. 276:1860-1877(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOGRAPHY, TISSUE SPECIFICITY, AUTOUBIQUITINATION, GLYCOSYLATION, MUTAGENESIS OF CYS-266.
  6. "Nuclear targeting of an endosomal E3 ubiquitin ligase."
    Bocock J.P., Carmicle S., Madamba E., Erickson A.H.
    Traffic 11:756-766(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRNF13_MOUSE
AccessioniPrimary (citable) accession number: O54965
Secondary accession number(s): O54966, Q6PEA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 108 of the entry and version 2 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

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 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.