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Protein

E3 ubiquitin-protein ligase RNF38

Gene

Rnf38

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

Functioni

Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme (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 fingeri466 – 50742RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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 RNF38 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 38
Gene namesi
Name:Rnf38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1920719. Rnf38.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518E3 ubiquitin-protein ligase RNF38PRO_0000056079Add
BLAST

Proteomic databases

PaxDbiQ8BI21.
PRIDEiQ8BI21.

PTM databases

iPTMnetiQ8BI21.
PhosphoSiteiQ8BI21.

Expressioni

Gene expression databases

BgeeiQ8BI21.
CleanExiMM_RNF38.
ExpressionAtlasiQ8BI21. baseline and differential.
GenevisibleiQ8BI21. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000095702.

Structurei

3D structure databases

ProteinModelPortaliQ8BI21.
SMRiQ8BI21. Positions 443-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi60 – 7415Bipartite nuclear localization signal 1By similarityAdd
BLAST
Motifi118 – 13316Bipartite nuclear localization signal 2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi242 – 407166Pro-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri466 – 50742RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00730000110459.
HOGENOMiHOG000231638.
HOVERGENiHBG059283.
InParanoidiQ8BI21.
KOiK19041.
OMAiIRPWESG.
OrthoDBiEOG74TWZV.
PhylomeDBiQ8BI21.
TreeFamiTF325756.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. 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: Q8BI21-1) [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
MAALMSEISP GANSAPLPGH PNKVICERVR LQSLFPLLPS DQNTTIQEDA
60 70 80 90 100
HFKAFFQSED SPSPKRQRLS HSVFDYTSAS PAPSPPMRPW EMTSNRQPPS
110 120 130 140 150
VRPNQHHFSG ERCNTPARNR RSPPVRRQRG RRERLSRHNS ISQDENYHHL
160 170 180 190 200
PYAQQQAIEE PRAFHPPNVS PRLLHPAAHP PQQNAVMVDI HDQLHQGTVP
210 220 230 240 250
VSYTVTTVAP HGLPLCTGQH IPACSTQQVP GCSVVFSGQH LPVCSVPPPM
260 270 280 290 300
LQACSVQHLP VPYAAFPPLI SSDPFLIHPP HLSPHHPPHL PPPGQFVPFQ
310 320 330 340 350
TQQSRSPLQR IENEVELLGE HLQVGSFTYP PSAHPPTLPP SAPLQFLTHD
360 370 380 390 400
PLHQEVSFGV PYPPFMPRRL TGRSRYRSQQ PMPPPPYHPS LLPYVLSMLP
410 420 430 440 450
VPPAVGPTFS FELDVEDGEV ENYEALLNLA ERLGEAKPRG LTKADIEQLP
460 470 480 490 500
SYRFNPSNHQ SEQTLCVVCM CDFESRQLLR VLPCNHEFHA KCVDKWLKGN
510
RTCPICRADA SEVHRDSE
Length:518
Mass (Da):57,999
Last modified:March 1, 2003 - v1
Checksum:i8BBA80CD6079F5E2
GO
Isoform 2 (identifier: Q8BI21-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MAALMSEISPGANSAPLPGHPNKVICERVRLQSLFPLLPSDQNTTIQEDAHFKAFFQ → MRE

Note: No experimental confirmation available.
Show »
Length:464
Mass (Da):52,168
Checksum:iA67EE0DCAC8101A2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757MAALM…KAFFQ → MRE in isoform 2. 1 PublicationVSP_012244Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029650 mRNA. Translation: BAC26547.1.
BC060730 mRNA. Translation: AAH60730.1.
BC062976 mRNA. Translation: AAH62976.1.
CCDSiCCDS18122.1. [Q8BI21-2]
RefSeqiNP_780410.2. NM_175201.5. [Q8BI21-2]
UniGeneiMm.262859.

Genome annotation databases

EnsembliENSMUST00000098098; ENSMUSP00000095702; ENSMUSG00000035696. [Q8BI21-2]
GeneIDi73469.
KEGGimmu:73469.
UCSCiuc008srq.2. mouse. [Q8BI21-2]
uc008srs.2. mouse. [Q8BI21-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029650 mRNA. Translation: BAC26547.1.
BC060730 mRNA. Translation: AAH60730.1.
BC062976 mRNA. Translation: AAH62976.1.
CCDSiCCDS18122.1. [Q8BI21-2]
RefSeqiNP_780410.2. NM_175201.5. [Q8BI21-2]
UniGeneiMm.262859.

3D structure databases

ProteinModelPortaliQ8BI21.
SMRiQ8BI21. Positions 443-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000095702.

PTM databases

iPTMnetiQ8BI21.
PhosphoSiteiQ8BI21.

Proteomic databases

PaxDbiQ8BI21.
PRIDEiQ8BI21.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098098; ENSMUSP00000095702; ENSMUSG00000035696. [Q8BI21-2]
GeneIDi73469.
KEGGimmu:73469.
UCSCiuc008srq.2. mouse. [Q8BI21-2]
uc008srs.2. mouse. [Q8BI21-1]

Organism-specific databases

CTDi152006.
MGIiMGI:1920719. Rnf38.

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00730000110459.
HOGENOMiHOG000231638.
HOVERGENiHBG059283.
InParanoidiQ8BI21.
KOiK19041.
OMAiIRPWESG.
OrthoDBiEOG74TWZV.
PhylomeDBiQ8BI21.
TreeFamiTF325756.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRnf38. mouse.
NextBioi338343.
PROiQ8BI21.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BI21.
CleanExiMM_RNF38.
ExpressionAtlasiQ8BI21. baseline and differential.
GenevisibleiQ8BI21. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. 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 1).
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "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).
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiRNF38_MOUSE
AccessioniPrimary (citable) accession number: Q8BI21
Secondary accession number(s): Q6P5B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 98 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.