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Protein

E3 ubiquitin-protein ligase RNF180

Gene

Rnf180

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 promotes polyubiquitination and degradation by the proteasome pathway of ZIC2.1 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 fingeri432 – 47443RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • adult behavior Source: MGI
  • norepinephrine metabolic process Source: MGI
  • organic cyclic compound metabolic process Source: MGI
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • protein polyubiquitination Source: MGI
  • regulation of catalytic activity Source: MGI
  • serotonin metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.2.B10. 3474.
6.3.2.19. 3474.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF180 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 180
Gene namesi
Name:Rnf180
Synonyms:Rines
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1919066. Rnf180.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 564564CytoplasmicSequence analysisAdd
BLAST
Transmembranei565 – 58521HelicalSequence analysisAdd
BLAST
Topological domaini586 – 5927ExtracellularSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592E3 ubiquitin-protein ligase RNF180PRO_0000261618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3U827.
PaxDbiQ3U827.
PRIDEiQ3U827.

PTM databases

iPTMnetiQ3U827.
PhosphoSiteiQ3U827.

Expressioni

Tissue specificityi

brain, kidney, testis and uterus. membrane protein. Nucleus envelope.1 Publication

Developmental stagei

Detected in the ventricular zone of the lateral ventricle in brain from E13.5 and E17.5 embryos.1 Publication

Gene expression databases

BgeeiQ3U827.
CleanExiMM_RNF180.

Interactioni

Subunit structurei

Interacts with ZIC2.1 Publication

GO - Molecular functioni

  • ubiquitin conjugating enzyme binding Source: MGI

Protein-protein interaction databases

BioGridi214948. 1 interaction.
STRINGi10090.ENSMUSP00000064624.

Structurei

3D structure databases

ProteinModelPortaliQ3U827.
SMRiQ3U827. Positions 426-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 489208Interaction with ZIC2Add
BLAST

Domaini

The RING-type zinc finger domain mediates polyubiquitination of the interacting protein.1 Publication

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri432 – 47443RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IN5N. Eukaryota.
ENOG410ZJ1M. LUCA.
GeneTreeiENSGT00390000012786.
HOGENOMiHOG000154158.
HOVERGENiHBG093907.
InParanoidiQ3U827.
KOiK15708.
OMAiWHMNIEA.
OrthoDBiEOG790G06.
PhylomeDBiQ3U827.
TreeFamiTF328580.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033263. RNF180.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR23327:SF18. PTHR23327:SF18. 2 hits.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3U827-1) [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
MKRSEESTST QSPEEQTGTL HCWRCRKCIA SSGCFMTPLE TQVVEQDRHE
60 70 80 90 100
SVDAQNTCHL WHMNVDALPE WISCLLQKAQ WTVGKLNCPF CGARLGGFNF
110 120 130 140 150
VSTPKCSCGQ LAAVHLCKSR TDHQAAQGGR LMRPALKHLP HPGVPSGCDK
160 170 180 190 200
ETLLTGGGSK TRNHWLLSMA RNSNGLGRLT EALCLEVRAT YFEMKNEKLL
210 220 230 240 250
FKASDPKCQP FVPQPDTGRC PSRASHRKSH SLDLNISEKL ILLPTLYEIH
260 270 280 290 300
RKPTAYPRLN ETGPIDLSGL ALPCSNSSCS FQSPPSFDPN MLLHRLSVAP
310 320 330 340 350
HETQAQRGRE CQCGLEASSV YSDHANANSL PFLMDLPSAG RSVLEASDQE
360 370 380 390 400
EHLSQLDFLR SASFPLGTIN HRLNNRERSK LRTLRRQQRR ERWLQKQGKY
410 420 430 440 450
SGVGLLDHMT VSNEMSTDEE TEFPEEKDSY MCAVCLDVYF NPYMCYPCHH
460 470 480 490 500
IFCEPCLRTL AKDNPASTPC PLCRTIISRV FLQTELNNAT KTFFTKEYLK
510 520 530 540 550
IKQSFQKSSS AKWPLPSCRK GFHLFGGFHR RAAPVTRRQF PHGAHRMDYL
560 570 580 590
HFEDDSRGWW FDMDMVIIYI YSVNWVIGFV VFCFLCYFFF PF
Length:592
Mass (Da):67,371
Last modified:November 28, 2006 - v2
Checksum:i4121E22EC8C9D861
GO
Isoform 2 (identifier: Q3U827-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-46: Missing.

Show »
Length:591
Mass (Da):67,243
Checksum:i432E886013863862
GO
Isoform 3 (identifier: Q3U827-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     528-592: FHRRAAPVTR...CFLCYFFFPF → KPAQRLKPCR...FLSHSGHCLG

Note: No experimental confirmation available.
Show »
Length:575
Mass (Da):64,597
Checksum:iC8610CE34219E0B6
GO
Isoform 4 (identifier: Q3U827-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-46: Missing.
     485-592: ELNNATKTFF...CFLCYFFFPF → AQAGSCGRLIPIFQRKPPR

Note: No experimental confirmation available.
Show »
Length:502
Mass (Da):56,299
Checksum:iDF34039606B005FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661D → H in BAE31192 (PubMed:16141072).Curated
Sequence conflicti266 – 2661D → H in BAE30351 (PubMed:16141072).Curated
Sequence conflicti487 – 4871N → D in BAC27782 (PubMed:16141072).Curated
Sequence conflicti525 – 5251F → L in BAE31192 (PubMed:16141072).Curated
Sequence conflicti525 – 5251F → L in BAE30351 (PubMed:16141072).Curated
Sequence conflicti587 – 5871Y → F in BAE31192 (PubMed:16141072).Curated
Sequence conflicti587 – 5871Y → F in BAE30351 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 461Missing in isoform 2 and isoform 4. 2 PublicationsVSP_021741
Alternative sequencei485 – 592108ELNNA…FFFPF → AQAGSCGRLIPIFQRKPPR in isoform 4. 1 PublicationVSP_021742Add
BLAST
Alternative sequencei528 – 59265FHRRA…FFFPF → KPAQRLKPCRILDTGMRYEA MEGCCLLTCSHGWRAQPAFL SHSGHCLG in isoform 3. 1 PublicationVSP_021743Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013941 mRNA. Translation: BAB29072.1.
AK032259 mRNA. Translation: BAC27782.1.
AK136632 mRNA. Translation: BAE23080.1.
AK151379 mRNA. Translation: BAE30351.1.
AK152404 mRNA. Translation: BAE31192.1.
AK157911 mRNA. Translation: BAE34259.1.
BC046775 mRNA. Translation: AAH46775.1.
BC075700 mRNA. Translation: AAH75700.1.
CCDSiCCDS36775.1. [Q3U827-3]
RefSeqiNP_082210.1. NM_027934.2. [Q3U827-3]
XP_006517819.1. XM_006517756.2.
XP_006517820.1. XM_006517757.1. [Q3U827-1]
XP_006517822.1. XM_006517759.2. [Q3U827-1]
XP_006517823.1. XM_006517760.1. [Q3U827-1]
XP_006517825.1. XM_006517762.1. [Q3U827-2]
XP_011242998.1. XM_011244696.1. [Q3U827-2]
UniGeneiMm.317015.

Genome annotation databases

EnsembliENSMUST00000069686; ENSMUSP00000064624; ENSMUSG00000021720. [Q3U827-3]
GeneIDi71816.
KEGGimmu:71816.
UCSCiuc007rtr.1. mouse. [Q3U827-1]
uc007rts.1. mouse. [Q3U827-2]
uc007rtt.1. mouse. [Q3U827-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013941 mRNA. Translation: BAB29072.1.
AK032259 mRNA. Translation: BAC27782.1.
AK136632 mRNA. Translation: BAE23080.1.
AK151379 mRNA. Translation: BAE30351.1.
AK152404 mRNA. Translation: BAE31192.1.
AK157911 mRNA. Translation: BAE34259.1.
BC046775 mRNA. Translation: AAH46775.1.
BC075700 mRNA. Translation: AAH75700.1.
CCDSiCCDS36775.1. [Q3U827-3]
RefSeqiNP_082210.1. NM_027934.2. [Q3U827-3]
XP_006517819.1. XM_006517756.2.
XP_006517820.1. XM_006517757.1. [Q3U827-1]
XP_006517822.1. XM_006517759.2. [Q3U827-1]
XP_006517823.1. XM_006517760.1. [Q3U827-1]
XP_006517825.1. XM_006517762.1. [Q3U827-2]
XP_011242998.1. XM_011244696.1. [Q3U827-2]
UniGeneiMm.317015.

3D structure databases

ProteinModelPortaliQ3U827.
SMRiQ3U827. Positions 426-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214948. 1 interaction.
STRINGi10090.ENSMUSP00000064624.

PTM databases

iPTMnetiQ3U827.
PhosphoSiteiQ3U827.

Proteomic databases

MaxQBiQ3U827.
PaxDbiQ3U827.
PRIDEiQ3U827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069686; ENSMUSP00000064624; ENSMUSG00000021720. [Q3U827-3]
GeneIDi71816.
KEGGimmu:71816.
UCSCiuc007rtr.1. mouse. [Q3U827-1]
uc007rts.1. mouse. [Q3U827-2]
uc007rtt.1. mouse. [Q3U827-3]

Organism-specific databases

CTDi285671.
MGIiMGI:1919066. Rnf180.

Phylogenomic databases

eggNOGiENOG410IN5N. Eukaryota.
ENOG410ZJ1M. LUCA.
GeneTreeiENSGT00390000012786.
HOGENOMiHOG000154158.
HOVERGENiHBG093907.
InParanoidiQ3U827.
KOiK15708.
OMAiWHMNIEA.
OrthoDBiEOG790G06.
PhylomeDBiQ3U827.
TreeFamiTF328580.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 3474.
6.3.2.19. 3474.

Miscellaneous databases

PROiQ3U827.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U827.
CleanExiMM_RNF180.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033263. RNF180.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR23327:SF18. PTHR23327:SF18. 2 hits.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Epididymis, Head, Inner ear and Olfactory bulb.
  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.
  3. "Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-bound ubiquitin ligase."
    Ogawa M., Mizugishi K., Ishiguro A., Koyabu Y., Imai Y., Takahashi R., Mikoshiba K., Aruga J.
    Genes Cells 13:397-409(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TOPOLOGY, DOMAIN, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH ZIC2, SUBCELLULAR LOCATION.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRN180_MOUSE
AccessioniPrimary (citable) accession number: Q3U827
Secondary accession number(s): Q3UW39
, Q80ZX1, Q8CCR1, Q9CXV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: June 8, 2016
This is version 85 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.