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Protein

E3 ubiquitin-protein ligase RNF19A

Gene

Rnf19a

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

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR.By similarity1 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 fingeri132 – 17948RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 26466IBR-typeAdd
BLAST
Zinc fingeri301 – 33232RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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 RNF19A (EC:6.3.2.-)
Alternative name(s):
Double ring-finger protein
Short name:
Dorfin
Gametogenesis-expressed protein GEG-154
RING finger protein 19A
UBCM4-interacting protein 117
Short name:
UIP117
XY body protein
Short name:
XYbp
Gene namesi
Name:Rnf19a
Synonyms:Geg-154, Rnf19, Xybp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1353623. Rnf19a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei368 – 38821HelicalSequence analysisAdd
BLAST
Transmembranei424 – 44421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840E3 ubiquitin-protein ligase RNF19APRO_0000056062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei631 – 6311PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP50636.
PRIDEiP50636.

PTM databases

iPTMnetiP50636.
PhosphoSiteiP50636.

Expressioni

Developmental stagei

Preferentially expressed in both sexes during gametogenesis.1 Publication

Gene expression databases

BgeeiP50636.
CleanExiMM_RNF19A.
GenevisibleiP50636. MM.

Interactioni

Subunit structurei

Interacts with UBE2L3 and UBE2L6. Also interacts with transcription factor Sp1. Interacts with SNCAIP and CASR (By similarity). Interacts with VCP.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SufuQ9Z0P73EBI-3508340,EBI-3508336

Protein-protein interaction databases

BioGridi206022. 5 interactions.
IntActiP50636. 4 interactions.
MINTiMINT-4996809.
STRINGi10090.ENSMUSP00000022890.

Structurei

3D structure databases

ProteinModelPortaliP50636.
SMRiP50636. Positions 132-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni660 – 840181Interaction with CASRBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the RBR family. RNF19 subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri132 – 17948RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 26466IBR-typeAdd
BLAST
Zinc fingeri301 – 33232RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000059258.
HOVERGENiHBG052073.
InParanoidiP50636.
KOiK11972.
OMAiSNMKINE.
OrthoDBiEOG7JDQXT.
PhylomeDBiP50636.
TreeFamiTF324777.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEQEISFIF KYNEGLCMNI DSDSILMSIL DMSLHQQMGS DRDLQSSTSS
60 70 80 90 100
VSLPSVKKAP KQRRISIGSL FRRKKDSKRK SRELNGGVDG IASIESIHSE
110 120 130 140 150
MCADKNSIFS TNTSSDNGLT SISKQIGDFI ECPLCLLRHS KDRFPDIMTC
160 170 180 190 200
HHRSCVDCLR QYLRIEISES RVNISCPECT ERFNPHDIRL ILSDDVLMEK
210 220 230 240 250
YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT CGREGCGTEF
260 270 280 290 300
CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP
310 320 330 340 350
CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW
360 370 380 390 400
GKKPWSRKKK ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN
410 420 430 440 450
RYEGKDVSKH KRNLAIAGGV TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV
460 470 480 490 500
PISLCRSGGC GVSAGNGKGV RIEFDDENDI NVGGTNAAID TTSVAEARHN
510 520 530 540 550
PSIGEGSVGG LTGSLSASGS HMDRIGTIRD NLSETASTMA LAGASITGSL
560 570 580 590 600
SGSAMVNCFN RLEVQADVQK ERCSLSGESG TVSLGTVSDN ASTKAMAGSI
610 620 630 640 650
LNSYIPLDRE GNSMEVQVDI ESKPFKFRHN SGSSSVDDSG ATRGHTGGAS
660 670 680 690 700
SGLPEGKSSA TKWSKEATGG KKSKSGKLRK KGNMKINETR EDMDAQLLEQ
710 720 730 740 750
QSTNSSEFEA PSLSDSMPSV ADSHSSHFSE FSCSDLESMR TSCSHGSSDC
760 770 780 790 800
HARFTAVNTL PEVENDRLEN SPHQCSSALL SKAASCSDVP QPSHAADEHG
810 820 830 840
TSRSGGKPMV DLCFGDALRE TNNNHSHQTA DLKVAVQTEI
Length:840
Mass (Da):90,632
Last modified:July 11, 2001 - v2
Checksum:iAC117A35849C023A
GO

Sequence cautioni

The sequence CAA50643.1 differs from that shown. Reason: Frameshift at position 778. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071R → G in BAE28125 (PubMed:16141072).Curated
Sequence conflicti466 – 4661N → D in BAE28125 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120206 mRNA. Translation: AAF18302.1.
AF120207 mRNA. Translation: AAF18303.1.
AK147768 mRNA. Translation: BAE28125.1.
BC040769 mRNA. Translation: AAH40769.1.
AF360999 mRNA. Translation: AAK51469.1.
AF071560 Genomic DNA. Translation: AAG37798.1.
X71642 mRNA. Translation: CAA50643.1. Frameshift.
CCDSiCCDS27427.1.
PIRiI48361.
RefSeqiNP_038951.1. NM_013923.2.
UniGeneiMm.5181.

Genome annotation databases

EnsembliENSMUST00000022890; ENSMUSP00000022890; ENSMUSG00000022280.
GeneIDi30945.
KEGGimmu:30945.
UCSCiuc007vmq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120206 mRNA. Translation: AAF18302.1.
AF120207 mRNA. Translation: AAF18303.1.
AK147768 mRNA. Translation: BAE28125.1.
BC040769 mRNA. Translation: AAH40769.1.
AF360999 mRNA. Translation: AAK51469.1.
AF071560 Genomic DNA. Translation: AAG37798.1.
X71642 mRNA. Translation: CAA50643.1. Frameshift.
CCDSiCCDS27427.1.
PIRiI48361.
RefSeqiNP_038951.1. NM_013923.2.
UniGeneiMm.5181.

3D structure databases

ProteinModelPortaliP50636.
SMRiP50636. Positions 132-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206022. 5 interactions.
IntActiP50636. 4 interactions.
MINTiMINT-4996809.
STRINGi10090.ENSMUSP00000022890.

PTM databases

iPTMnetiP50636.
PhosphoSiteiP50636.

Proteomic databases

PaxDbiP50636.
PRIDEiP50636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022890; ENSMUSP00000022890; ENSMUSG00000022280.
GeneIDi30945.
KEGGimmu:30945.
UCSCiuc007vmq.1. mouse.

Organism-specific databases

CTDi25897.
MGIiMGI:1353623. Rnf19a.

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000059258.
HOVERGENiHBG052073.
InParanoidiP50636.
KOiK11972.
OMAiSNMKINE.
OrthoDBiEOG7JDQXT.
PhylomeDBiP50636.
TreeFamiTF324777.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRnf19a. mouse.
NextBioi307398.
PROiP50636.
SOURCEiSearch...

Gene expression databases

BgeeiP50636.
CleanExiMM_RNF19A.
GenevisibleiP50636. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "XYbp, a novel RING-finger protein, is a component of the XY body of spermatocytes and centrosomes."
    Parraga M., del Mazo J.
    Mech. Dev. 90:95-101(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Strain: SWR/J.
    Tissue: Testis.
  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: Melanocyte.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4."
    Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.
    FEBS Lett. 454:257-261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-245, FUNCTION.
    Strain: CD-1.
  5. "Cloning and characterization of genes expressed during gametogenesis of female and male mice."
    Lopez-Alanon D.M., del Mazo J.
    J. Reprod. Fertil. 103:323-329(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 380-840, DEVELOPMENTAL STAGE.
    Strain: SWR/J.
    Tissue: Ovary.
  6. "Physical and functional interaction between dorfin and valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders."
    Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S., Kakizuka A., Tanaka K., Sobue G.
    J. Biol. Chem. 279:51376-51385(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCP.

Entry informationi

Entry nameiRN19A_MOUSE
AccessioniPrimary (citable) accession number: P50636
Secondary accession number(s): Q3UGT2, Q9QUJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 11, 2001
Last modified: May 11, 2016
This is version 131 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

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.