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Protein

E3 ubiquitin-protein ligase listerin

Gene

Ltn1

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

Functioni

E3 ubiquitin-protein ligase (PubMed:19196968). Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (By similarity). Ubiquitination leads to Vcp/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity).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 fingeri1716 – 176348RING-typePROSITE-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 listerin (EC:6.3.2.-)
Alternative name(s):
RING finger protein 160
Zinc finger protein 294
Short name:
Zfp-294
Gene namesi
Name:Ltn1
Synonyms:Kiaa0714, Lister, Rnf160, Zfp294, Znf294
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1926163. Ltn1.

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality. Mice with a milder mutant caused by an internal in-frame deletion of exon 11, producing a 14-amino acid deletion prior to the RING-type zinc finger, display profound early-onset and progressive neurological and motor dysfunction.1 Publication

Keywords - Diseasei

Neurodegeneration

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17671767E3 ubiquitin-protein ligase listerinPRO_0000056305Add
BLAST

Post-translational modificationi

Autoubiquitinated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ6A009.
MaxQBiQ6A009.
PaxDbiQ6A009.
PeptideAtlasiQ6A009.
PRIDEiQ6A009.

PTM databases

iPTMnetiQ6A009.
PhosphoSiteiQ6A009.

Expressioni

Tissue specificityi

Widely expressed, including in the brain and spinal cord.1 Publication

Gene expression databases

BgeeiQ6A009.
CleanExiMM_ZFP294.
GenevisibleiQ6A009. MM.

Interactioni

Subunit structurei

Component of the ribosome quality control complex (RQC), composed of at least the E3 ubiquitin ligase Ltn1 and Nemf. The complex probably also contains Tcf25 as well as Vcp/p97 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits.By similarity

Protein-protein interaction databases

BioGridi219701. 1 interaction.
DIPiDIP-48713N.
STRINGi10090.ENSMUSP00000038775.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati59 – 9638HEAT 1Sequence analysisAdd
BLAST
Repeati100 – 13839HEAT 2Sequence analysisAdd
BLAST
Repeati273 – 31442HEAT 3Sequence analysisAdd
BLAST
Repeati335 – 37238HEAT 4Sequence analysisAdd
BLAST
Repeati380 – 41839HEAT 5Sequence analysisAdd
BLAST
Repeati433 – 47341HEAT 6Sequence analysisAdd
BLAST
Repeati509 – 54739HEAT 7Sequence analysisAdd
BLAST
Repeati621 – 65838HEAT 8Sequence analysisAdd
BLAST
Repeati676 – 71439HEAT 9Sequence analysisAdd
BLAST
Repeati1067 – 110438HEAT 10Sequence analysisAdd
BLAST
Repeati1183 – 122644HEAT 11Sequence analysisAdd
BLAST
Repeati1315 – 135339HEAT 12Sequence analysisAdd
BLAST
Repeati1378 – 141538HEAT 13Sequence analysisAdd
BLAST
Repeati1476 – 151338HEAT 14Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the LTN1 family.Curated
Contains 14 HEAT repeats.Sequence analysis
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1716 – 176348RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0803. Eukaryota.
COG5219. LUCA.
GeneTreeiENSGT00390000016055.
InParanoidiQ6A009.
OMAiNSCLQTK.
OrthoDBiEOG7BZVRF.
TreeFamiTF314286.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001841. Znf_RING.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6A009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGKNKQRTK GNLRPSNSGR AAELLAKEQG TVPGFIGFGT SHSDLGYVPA
60 70 80 90 100
VQGAEDIDSL VDSDFRMVLR KLSKKDVTTK LKAMQEFGIM CTERDTEAVK
110 120 130 140 150
GVLPYWPRIF CKISLDHDRR VREATQQAFE KLILKVKKHL APYLKSVMGY
160 170 180 190 200
WLMAQCDTYP PAALAAKDAF EAAFPPSKQP EAIAFCKEEI TTVLQDHLLK
210 220 230 240 250
ETPDTLSDPQ TVPEEEREAK FHRVVTCSLL ALKRLLCFLP NNELDSLEEK
260 270 280 290 300
FKSLLSQNKF WKYGKHSVPQ VRSAYFELVS ALCQHVPQVM KEEAAKVSPS
310 320 330 340 350
VLLSIDDSDP VVCPALWEAV LYTLTTIEDC WFHVNAKKSV FPKLMAMIRE
360 370 380 390 400
GGRGLAAVMY PYLLPFISKL PQSITEPKLD FFKNFLTSLV TGLSTERTKS
410 420 430 440 450
SSSECSAVIS AFFECLRFIM QQNLGEEEMV QMLINEQLIP FIDTVLKDSG
460 470 480 490 500
LHHGPMFDHL ADTLSSWEAK ADAERDPGAV YNLENVLLSF WGRLSEICTE
510 520 530 540 550
KIRQPEADVK SVLCVSSLVG VLQRPRSSLK LHRKKTAQVR FAINIPEAHK
560 570 580 590 600
GDEKSMSSEG ENSEGSDGGA QSPLSNTSSD LVSPLRKKPL EDLVCKLAEV
610 620 630 640 650
SISFVNERKS EQHLQFLSTL LDSFSSVQVF NILLSDKQKN VVKAKPLEIT
660 670 680 690 700
KLAEKNPAVK FLYHKLIGWL NDSQKEDGGF LVDILYSALR CCDSGVERKE
710 720 730 740 750
VLDDLTKEDL KWSSLLQVIE KACSSSDKHA LVTPWLKGSI LGEKLVALAD
760 770 780 790 800
CLCDKDLEAT TSESHSSEQW SLLRLALSQH VKNDYLIGEV YVGRIIVKLH
810 820 830 840 850
ETLSKTKDLS EAANSDSSVS FVCDVVHSFF SSAGGGLLMP PSEDLLLTLF
860 870 880 890 900
QLCAQSKERT HLPDFLICKL KNTLLSGVNL LVHQTASTYE QSTFLRLSVL
910 920 930 940 950
WLKDQVQSSA LDNTSLQVLL SAAGDLLGTL VESEDTSLLG VYIGSVMPSD
960 970 980 990 1000
SEWEKMRQAL PVQWLHRPLL EGRLSLNYEC FKTDFKEQDT KTLPNHLCTS
1010 1020 1030 1040 1050
SLLSKMILVA QKKKLVLEDN VLEKIIAELL YSLQWCEELD NAPSFLSGFC
1060 1070 1080 1090 1100
GILQKMNITY SNLSVLSETS SLLQLLFDRS RKNGTLWSLI IAKLILSRSI
1110 1120 1130 1140 1150
SSDEVKPYYK RKESFFPLTE GSLHTIQSLC PFLSKEEKKE FSAQCIPAFL
1160 1170 1180 1190 1200
GWTKEDLCSI NGAFGHLAIF NSCLQTRSID DKQLLHGILK IITSWRKQHE
1210 1220 1230 1240 1250
DIFLFSCNLS EASPEVLGLN IEIMRFLSLF LKHCAYPLPL ADSEWDFIMC
1260 1270 1280 1290 1300
SMLAWLETTS ENQALYSVPL VQLFACVSFD LACDLCAFFD SITPDIVDNL
1310 1320 1330 1340 1350
PVNLISEWKE FFSKGIHSLL LPLLVNAIGE NKDLSETSFQ NAMLKPMCET
1360 1370 1380 1390 1400
LTYISKDQLL SHKLPARLVA SQKTNLPEHL QTLLNTLTPL LLFRARPVQI
1410 1420 1430 1440 1450
AAYHMLCKLM PELPQHDQDN LRSYGDEEEE PALSPPAALM SLLSSQEELL
1460 1470 1480 1490 1500
ENVLGCVPVG QIVTVKPLSE DFCYVLGYLL TWKLILTFFK AASSQLRALY
1510 1520 1530 1540 1550
SMYLRKTKSL NKLLYHLFRL MPENPTYGET AIEVSSKDPK TFFTEEVQLS
1560 1570 1580 1590 1600
IRETATLPYH IPHLACSVYH MTLKDLPAMV RLWWNSSEKR VFNIVDRFTS
1610 1620 1630 1640 1650
KYVSNVLSFQ EISSVQTSTQ LFNGMTVKAR ATTREVMATY TIEDIVIELI
1660 1670 1680 1690 1700
IQLPSNYPLG SITVESGKRI GVAVQQWRNW MLQLSTYLTH QNGSIMEGLA
1710 1720 1730 1740 1750
LWKNNVDKRF EGVEDCMICF SVIHGFNYSL PKKACRTCKK KFHSACLYKW
1760
FTSSNKSTCP LCRETFF
Length:1,767
Mass (Da):198,921
Last modified:July 27, 2011 - v3
Checksum:iEFEC1BAAD32776C6
GO

Sequence cautioni

The sequence AAH27795.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD32287.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1009 – 10113VAQ → IAP in BAD32287 (PubMed:15368895).Curated
Sequence conflicti1042 – 10421A → P in BAD32287 (PubMed:15368895).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173009 mRNA. Translation: BAD32287.1. Different initiation.
AC140319 Genomic DNA. No translation available.
AK036725 mRNA. Translation: BAC29552.1.
BC027795 mRNA. Translation: AAH27795.1. Different initiation.
CCDSiCCDS37382.1.
RefSeqiNP_001074537.1. NM_001081068.1.
UniGeneiMm.249005.

Genome annotation databases

EnsembliENSMUST00000039449; ENSMUSP00000038775; ENSMUSG00000052299.
GeneIDi78913.
KEGGimmu:78913.
UCSCiuc033gzo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173009 mRNA. Translation: BAD32287.1. Different initiation.
AC140319 Genomic DNA. No translation available.
AK036725 mRNA. Translation: BAC29552.1.
BC027795 mRNA. Translation: AAH27795.1. Different initiation.
CCDSiCCDS37382.1.
RefSeqiNP_001074537.1. NM_001081068.1.
UniGeneiMm.249005.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219701. 1 interaction.
DIPiDIP-48713N.
STRINGi10090.ENSMUSP00000038775.

PTM databases

iPTMnetiQ6A009.
PhosphoSiteiQ6A009.

Proteomic databases

EPDiQ6A009.
MaxQBiQ6A009.
PaxDbiQ6A009.
PeptideAtlasiQ6A009.
PRIDEiQ6A009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039449; ENSMUSP00000038775; ENSMUSG00000052299.
GeneIDi78913.
KEGGimmu:78913.
UCSCiuc033gzo.1. mouse.

Organism-specific databases

CTDi26046.
MGIiMGI:1926163. Ltn1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0803. Eukaryota.
COG5219. LUCA.
GeneTreeiENSGT00390000016055.
InParanoidiQ6A009.
OMAiNSCLQTK.
OrthoDBiEOG7BZVRF.
TreeFamiTF314286.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiLtn1. mouse.
PROiQ6A009.
SOURCEiSearch...

Gene expression databases

BgeeiQ6A009.
CleanExiMM_ZFP294.
GenevisibleiQ6A009. MM.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001841. Znf_RING.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 1-1108.
    Strain: C57BL/6J.
    Tissue: Bone.
  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] OF 1314-1767.
    Tissue: Mammary tumor.
  5. "A mouse forward genetics screen identifies LISTERIN as an E3 ubiquitin ligase involved in neurodegeneration."
    Chu J., Hong N.A., Masuda C.A., Jenkins B.V., Nelms K.A., Goodnow C.C., Glynne R.J., Wu H., Masliah E., Joazeiro C.A., Kay S.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:2097-2103(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiLTN1_MOUSE
AccessioniPrimary (citable) accession number: Q6A009
Secondary accession number(s): E9QN94, Q6PIW6, Q8BZ44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Was named listerin because of the 'tilting' or 'listing' phenotype observed in mutant mice.1 Publication

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.