Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase RNF14

Gene

Rnf14

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

Functioni

Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri221 – 27151RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri290 – 35162IBR-typeAdd
BLAST
Zinc fingeri405 – 43430RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF14 (EC:6.3.2.-)
Alternative name(s):
Androgen receptor-associated protein 54
Protein Triad2
RING finger protein 14
Gene namesi
Name:Rnf14
Synonyms:Ara54, Triad2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1929668. Rnf14.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485E3 ubiquitin-protein ligase RNF14PRO_0000056058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491PhosphoserineBy similarity

Post-translational modificationi

RING-type zinc finger-dependent and UBE2E2-dependent autoubiquitination.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9JI90.
MaxQBiQ9JI90.
PaxDbiQ9JI90.
PRIDEiQ9JI90.

PTM databases

iPTMnetiQ9JI90.
PhosphoSiteiQ9JI90.

Expressioni

Gene expression databases

BgeeiQ9JI90.
CleanExiMM_RNF14.
ExpressionAtlasiQ9JI90. baseline and differential.
GenevisibleiQ9JI90. MM.

Interactioni

Subunit structurei

Interacts with the ubiquitin-conjugating enzymes UBE2E1 and UBE2E2. Interacts with AR/androgen receptor; testosterone- and RNF6-regulated it promotes AR transcriptional activity.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208150. 9 interactions.
IntActiQ9JI90. 1 interaction.
STRINGi10090.ENSMUSP00000072212.

Structurei

3D structure databases

ProteinModelPortaliQ9JI90.
SMRiQ9JI90. Positions 237-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 137127RWDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459D-box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi173 – 1764Poly-Ala
Compositional biasi470 – 48516Asp/Glu-rich (acidic)Add
BLAST

Domaini

The N-terminal destruction box (D-box) could act as a recognition signal for degradation via the ubiquitin-proteasome pathway.By similarity
The RING-type zinc finger is essential for the interaction with UBE2E2.By similarity

Sequence similaritiesi

Belongs to the RBR family. RNF14 subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 RWD domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri221 – 27151RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri290 – 35162IBR-typeAdd
BLAST
Zinc fingeri405 – 43430RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1814. Eukaryota.
ENOG410Y5R1. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000237334.
HOVERGENiHBG057296.
InParanoidiQ9JI90.
KOiK11971.
OMAiFQIQIRD.
OrthoDBiEOG7BGHKF.
TreeFamiTF314401.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00591. RWD. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50908. RWD. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. 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: Q9JI90-1) [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
MSAEDLEAQE DELLALASIY DADEFRKAES VQGGETRIYL DLPQNFKIFV
60 70 80 90 100
SGNSNESLQN SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP
110 120 130 140 150
TQLSALCKHL DNLWEEHRGR VVLFAWMQFL KEETLTYLNI VSPFELKMGS
160 170 180 190 200
QKKVQRRATA QASSSTELGV GGAAAADVDQ EETVDERAVQ DVESLSSLIQ
210 220 230 240 250
EILDFNQARQ TKCFNSKLFL CSICFCEKLG SDCMYFLECK HVYCKACLKD
260 270 280 290 300
YFEIQIKDGQ VKCLNCPEPQ CPSVATPGQV KELVEADLFA RYDRLLLQST
310 320 330 340 350
LDLMADVVYC PRPCCQLPVM QEPGGTMAIC SSCNFAFCTL CRLTYHGLSP
360 370 380 390 400
CKVTAEKLID LRNEYLQADE ATKRFLEQRY GKRVIQKALE EMESKDWLEK
410 420 430 440 450
NSKSCPCCGT PIQKLDGCNK MTCTGCMQYF CWICMGSLSR ANPYRHFTDS
460 470 480
ESPCFNRLFH AVDINGDMWE DEIEEDDDDE DDDDD
Length:485
Mass (Da):54,926
Last modified:July 27, 2011 - v2
Checksum:i6228A9827F16FA47
GO
Isoform 2 (identifier: Q9JI90-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-79: GNSNESLQNSGFEYTICFLPPLVLNFEL → ALCSLQAPRQPVGRTPRQSGAVCLDAVS
     80-485: Missing.

Show »
Length:79
Mass (Da):8,631
Checksum:i5F0A682CF77C0EB9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → V in AAF74266 (Ref. 1) Curated
Sequence conflicti22 – 221A → V in AAF74267 (Ref. 1) Curated
Sequence conflicti62 – 621G → R in BAB26503 (PubMed:16141072).Curated
Sequence conflicti103 – 1064LSAL → GTLV in BAB26503 (PubMed:16141072).Curated
Sequence conflicti103 – 1064LSAL → GTLV in BAB26741 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei52 – 7928GNSNE…LNFEL → ALCSLQAPRQPVGRTPRQSG AVCLDAVS in isoform 2. 1 PublicationVSP_005751Add
BLAST
Alternative sequencei80 – 485406Missing in isoform 2. 1 PublicationVSP_005752Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249667 mRNA. Translation: AAF74266.1.
AF249668 mRNA. Translation: AAF74267.1.
AK011316 mRNA. Translation: BAB27541.1.
AK009783 mRNA. Translation: BAB26503.1.
AK010162 mRNA. Translation: BAB26741.1.
CH466528 Genomic DNA. Translation: EDL10081.1.
CH466528 Genomic DNA. Translation: EDL10082.1.
CH466528 Genomic DNA. Translation: EDL10083.1.
CH466528 Genomic DNA. Translation: EDL10084.1.
CH466528 Genomic DNA. Translation: EDL10087.1.
BC054841 mRNA. Translation: AAH54841.1.
BC094250 mRNA. Translation: AAH94250.1.
CCDSiCCDS29200.1. [Q9JI90-1]
RefSeqiNP_001158093.1. NM_001164621.1. [Q9JI90-1]
NP_001158094.1. NM_001164622.1.
NP_064396.2. NM_020012.2. [Q9JI90-1]
XP_006526184.1. XM_006526121.1. [Q9JI90-1]
XP_006526185.1. XM_006526122.1. [Q9JI90-1]
XP_006526186.1. XM_006526123.1. [Q9JI90-1]
XP_006526187.1. XM_006526124.1. [Q9JI90-1]
XP_006526188.1. XM_006526125.1. [Q9JI90-1]
XP_006526189.1. XM_006526126.1. [Q9JI90-1]
XP_006526190.1. XM_006526127.1. [Q9JI90-1]
UniGeneiMm.228903.

Genome annotation databases

EnsembliENSMUST00000072376; ENSMUSP00000072212; ENSMUSG00000060450. [Q9JI90-1]
ENSMUST00000171461; ENSMUSP00000126205; ENSMUSG00000060450. [Q9JI90-1]
GeneIDi56736.
KEGGimmu:56736.
UCSCiuc008ese.2. mouse. [Q9JI90-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249667 mRNA. Translation: AAF74266.1.
AF249668 mRNA. Translation: AAF74267.1.
AK011316 mRNA. Translation: BAB27541.1.
AK009783 mRNA. Translation: BAB26503.1.
AK010162 mRNA. Translation: BAB26741.1.
CH466528 Genomic DNA. Translation: EDL10081.1.
CH466528 Genomic DNA. Translation: EDL10082.1.
CH466528 Genomic DNA. Translation: EDL10083.1.
CH466528 Genomic DNA. Translation: EDL10084.1.
CH466528 Genomic DNA. Translation: EDL10087.1.
BC054841 mRNA. Translation: AAH54841.1.
BC094250 mRNA. Translation: AAH94250.1.
CCDSiCCDS29200.1. [Q9JI90-1]
RefSeqiNP_001158093.1. NM_001164621.1. [Q9JI90-1]
NP_001158094.1. NM_001164622.1.
NP_064396.2. NM_020012.2. [Q9JI90-1]
XP_006526184.1. XM_006526121.1. [Q9JI90-1]
XP_006526185.1. XM_006526122.1. [Q9JI90-1]
XP_006526186.1. XM_006526123.1. [Q9JI90-1]
XP_006526187.1. XM_006526124.1. [Q9JI90-1]
XP_006526188.1. XM_006526125.1. [Q9JI90-1]
XP_006526189.1. XM_006526126.1. [Q9JI90-1]
XP_006526190.1. XM_006526127.1. [Q9JI90-1]
UniGeneiMm.228903.

3D structure databases

ProteinModelPortaliQ9JI90.
SMRiQ9JI90. Positions 237-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208150. 9 interactions.
IntActiQ9JI90. 1 interaction.
STRINGi10090.ENSMUSP00000072212.

PTM databases

iPTMnetiQ9JI90.
PhosphoSiteiQ9JI90.

Proteomic databases

EPDiQ9JI90.
MaxQBiQ9JI90.
PaxDbiQ9JI90.
PRIDEiQ9JI90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072376; ENSMUSP00000072212; ENSMUSG00000060450. [Q9JI90-1]
ENSMUST00000171461; ENSMUSP00000126205; ENSMUSG00000060450. [Q9JI90-1]
GeneIDi56736.
KEGGimmu:56736.
UCSCiuc008ese.2. mouse. [Q9JI90-1]

Organism-specific databases

CTDi9604.
MGIiMGI:1929668. Rnf14.

Phylogenomic databases

eggNOGiKOG1814. Eukaryota.
ENOG410Y5R1. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000237334.
HOVERGENiHBG057296.
InParanoidiQ9JI90.
KOiK11971.
OMAiFQIQIRD.
OrthoDBiEOG7BGHKF.
TreeFamiTF314401.

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi313224.
PROiQ9JI90.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JI90.
CleanExiMM_RNF14.
ExpressionAtlasiQ9JI90. baseline and differential.
GenevisibleiQ9JI90. MM.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00591. RWD. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50908. RWD. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel TRIAD protein, TRIAD2."
    Van der Reijden B.A., Jansen J.H.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo and Tongue.
  3. 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].
  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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain and Eye.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRNF14_MOUSE
AccessioniPrimary (citable) accession number: Q9JI90
Secondary accession number(s): Q7TPR0
, Q9D0L2, Q9D6N2, Q9D6Z8, Q9JI89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.