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Protein

E3 ubiquitin-protein ligase listerin

Gene

LTN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase 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 (PubMed:23685075, PubMed:25132172, PubMed:25578875). Ubiquitination leads to VCP/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity).By similarity3 Publications

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 fingeri1715 – 176248RING-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

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
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
Gene namesi
Name:LTN1
Synonyms:C21orf10, C21orf98, KIAA0714, RNF160, ZNF294
ORF Names:HSPC087
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:13082. LTN1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37658.

Polymorphism and mutation databases

BioMutaiLTN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17661766E3 ubiquitin-protein ligase listerinPRO_0000056304Add
BLAST

Post-translational modificationi

Autoubiquitinated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiO94822.
MaxQBiO94822.
PaxDbiO94822.
PRIDEiO94822.

PTM databases

iPTMnetiO94822.
PhosphoSiteiO94822.

Expressioni

Gene expression databases

BgeeiO94822.
CleanExiHS_RNF160.
ExpressionAtlasiO94822. baseline and differential.
GenevisibleiO94822. HS.

Organism-specific databases

HPAiCAB034164.
HPA029143.
HPA055604.

Interactioni

Subunit structurei

Component of the ribosome quality control complex (RQC), composed of at least the E3 ubiquitin ligase LTN1 and NEMF (PubMed:25578875). The complex probably also contains TCF25 as well as VCP/p97 and its ubiquitin-binding cofactors (By similarity). RQC forms a stable complex with 60S ribosomal subunits (PubMed:25578875).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IRF7Q929852EBI-1044684,EBI-968267
TIRAPP587532EBI-1044684,EBI-528644
TMEM173Q86WV62EBI-1044684,EBI-2800345

Protein-protein interaction databases

BioGridi117509. 66 interactions.
IntActiO94822. 39 interactions.
STRINGi9606.ENSP00000373846.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J92electron microscopy3.600/w/z1-1766[»]
ProteinModelPortaliO94822.
ModBaseiSearch...
MobiDBiSearch...

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
Repeati513 – 55139HEAT 7Sequence analysisAdd
BLAST
Repeati611 – 65848HEAT 8Sequence analysisAdd
BLAST
Repeati676 – 71439HEAT 9Sequence analysisAdd
BLAST
Repeati768 – 81043HEAT 10Sequence analysisAdd
BLAST
Repeati911 – 94939HEAT 11Sequence analysisAdd
BLAST
Repeati1068 – 110538HEAT 12Sequence analysisAdd
BLAST
Repeati1184 – 122744HEAT 13Sequence analysisAdd
BLAST
Repeati1314 – 135239HEAT 14Sequence analysisAdd
BLAST
Repeati1377 – 141438HEAT 15Sequence analysisAdd
BLAST
Repeati1475 – 151238HEAT 16Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the LTN1 family.Curated
Contains 16 HEAT repeats.Sequence analysis
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1715 – 176248RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0803. Eukaryota.
COG5219. LUCA.
GeneTreeiENSGT00390000016055.
HOVERGENiHBG083026.
InParanoidiO94822.
OMAiNSCLQTK.
OrthoDBiEOG7BZVRF.
PhylomeDBiO94822.
TreeFamiTF314286.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR016024. 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. 2 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94822-1) [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
MGGKNKQRTK GNLRPSNSGR AAELLAKEQG TVPGFIGFGT SQSDLGYVPA
60 70 80 90 100
IQGAEEIDSL VDSDFRMVLR KLSKKDVTTK LKAMQEFGTM CTERDTETVK
110 120 130 140 150
GVLPYWPRIF CKISLDHDRR VREATQQAFE KLILKVKKQL APYLKSLMGY
160 170 180 190 200
WLMAQCDTYT PAAFAAKDAF EAAFPPSKQP EAIAFCKDEI TSVLQDHLIK
210 220 230 240 250
ETPDTLSDPQ TVPEEEREAK FYRVVTCSLL ALKRLLCLLP DNELDSLEEK
260 270 280 290 300
FKSLLSQNKF WKYGKHSVPQ IRSAYFELVS ALCQRIPQLM KEEASKVSPS
310 320 330 340 350
VLLSIDDSDP IVCPALWEAV LYTLTTIEDC WLHVNAKKSV FPKLSTVIRE
360 370 380 390 400
GGRGLATVIY PYLLPFISKL PQSITNPKLD FFKNFLTSLV AGLSTERTKT
410 420 430 440 450
SSLESSAVIS AFFECLRFIM QQNLGEEEIE QMLVNDQLIP FIDAVLKDPG
460 470 480 490 500
LQHGQLFNHL AETLSSWEAK ADTEKDEKTA HNLENVLIHF WERLSEICVA
510 520 530 540 550
KISEPEADVE SVLGVSNLLQ VLQKPKSSLK SSKKKNGKVR FADEILESNK
560 570 580 590 600
ENEKCVSSEG EKIEGWELTT EPSLTHNSSG LLSPLRKKPL EDLVCKLADI
610 620 630 640 650
SINYVNERKS EQHLRFLSTL LDSFSSSRVF KMLLGDEKQS IVQAKPLEIA
660 670 680 690 700
KLVQKNPAVQ FLYQKLIGWL NEDQRKDFGF LVDILYSALR CCDNDMERKK
710 720 730 740 750
VLDDLTKVDL KWNSLLKIIE KACPSSDKHA LVTPWLKGDI LGEKLVNLAD
760 770 780 790 800
CLCNEDLESR VSSESHFSER WTLLSLVLSQ HVKNDYLIGD VYVERIIVRL
810 820 830 840 850
HETLFKTKKL SEAESSDSSV SFICDVAYNY FSSAKGCLLM PSSEDLLLTL
860 870 880 890 900
FQLCAQSKEK THLPDFLICK LKNTWLSGVN LLVHQTDSSY KESTFLHLSA
910 920 930 940 950
LWLKNQVQAS SLDINSLQVL LSAVDDLLNT LLESEDSYLM GVYIGSVMPN
960 970 980 990 1000
DSEWEKMRQS LPMQWLHRPL LEGRLSLNYE CFKTDFKEQD IKTLPSHLCT
1010 1020 1030 1040 1050
SALLSKMVLI ALRKETVLEN NELEKIIAEL LYSLQWCEEL DNPPIFLIGF
1060 1070 1080 1090 1100
CEILQKMNIT YDNLRVLGNT SGLLQLLFNR SREHGTLWSL IIAKLILSRS
1110 1120 1130 1140 1150
ISSDEVKPHY KRKESFFPLT EGNLHTIQSL CPFLSKEEKK EFSAQCIPAL
1160 1170 1180 1190 1200
LGWTKKDLCS TNGGFGHLAI FNSCLQTKSI DDGELLHGIL KIIISWKKEH
1210 1220 1230 1240 1250
EDIFLFSCNL SEASPEVLGV NIEIIRFLSL FLKYCSSPLA ESEWDFIMCS
1260 1270 1280 1290 1300
MLAWLETTSE NQALYSIPLV QLFACVSCDL ACDLSAFFDS TTLDTIGNLP
1310 1320 1330 1340 1350
VNLISEWKEF FSQGIHSLLL PILVTVTGEN KDVSETSFQN AMLKPMCETL
1360 1370 1380 1390 1400
TYISKEQLLS HKLPARLVAD QKTNLPEYLQ TLLNTLAPLL LFRARPVQIA
1410 1420 1430 1440 1450
VYHMLYKLMP ELPQYDQDNL KSYGDEEEEP ALSPPAALMS LLSIQEDLLE
1460 1470 1480 1490 1500
NVLGCIPVGQ IVTIKPLSED FCYVLGYLLT WKLILTFFKA ASSQLRALYS
1510 1520 1530 1540 1550
MYLRKTKSLN KLLYHLFRLM PENPTYAETA VEVPNKDPKT FFTEELQLSI
1560 1570 1580 1590 1600
RETTMLPYHI PHLACSVYHM TLKDLPAMVR LWWNSSEKRV FNIVDRFTSK
1610 1620 1630 1640 1650
YVSSVLSFQE ISSVQTSTQL FNGMTVKARA TTREVMATYT IEDIVIELII
1660 1670 1680 1690 1700
QLPSNYPLGS IIVESGKRVG VAVQQWRNWM LQLSTYLTHQ NGSIMEGLAL
1710 1720 1730 1740 1750
WKNNVDKRFE GVEDCMICFS VIHGFNYSLP KKACRTCKKK FHSACLYKWF
1760
TSSNKSTCPL CRETFF
Length:1,766
Mass (Da):200,552
Last modified:November 30, 2010 - v6
Checksum:i9312CB2283C50AEE
GO
Isoform 2 (identifier: O94822-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-1766: Missing.

Show »
Length:437
Mass (Da):49,183
Checksum:i9EAF5B0CB7F3043B
GO
Isoform 3 (identifier: O94822-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDRVGGGKGPGGSYYRVSSSAARSRKLCPGRVNRGLSAQSTAATATM

Note: No experimental confirmation available.
Show »
Length:1,812
Mass (Da):205,177
Checksum:i4FC0E178DB35D4E5
GO

Sequence cautioni

The sequence AAF28910.1 differs from that shown. Reason: Frameshift at positions 213, 328, 333, 342, 352 and 354. Curated
The sequence AAH29371.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA34434.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA91976.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB90430.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → K in BAA91976 (PubMed:14702039).Curated
Sequence conflicti108 – 1081R → T in DB452437 (Ref. 7) Curated
Sequence conflicti133 – 1331I → T in BAA91976 (PubMed:14702039).Curated
Sequence conflicti141 – 1411A → G in AAF28910 (Ref. 6) Curated
Sequence conflicti150 – 1501Y → D in BAB14589 (PubMed:14702039).Curated
Sequence conflicti372 – 3721Q → H in BAB14589 (PubMed:14702039).Curated
Sequence conflicti372 – 3721Q → H in BAA91976 (PubMed:14702039).Curated
Sequence conflicti413 – 4131F → Y in BAA91976 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti403 – 4031L → S.4 Publications
Corresponds to variant rs2254796 [ dbSNP | Ensembl ].
VAR_020957
Natural varianti500 – 5001A → V.
Corresponds to variant rs16983580 [ dbSNP | Ensembl ].
VAR_057218
Natural varianti565 – 5651G → C.
Corresponds to variant rs34191159 [ dbSNP | Ensembl ].
VAR_057219
Natural varianti761 – 7611V → I.
Corresponds to variant rs34635840 [ dbSNP | Ensembl ].
VAR_057220

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDRVGGGKGPGGSYYRVSSS AARSRKLCPGRVNRGLSAQS TAATATM in isoform 3. 1 PublicationVSP_044911
Alternative sequencei438 – 17661329Missing in isoform 2. 1 PublicationVSP_040138Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018257 mRNA. Translation: BAA34434.2. Different initiation.
AF129075 Genomic DNA. No translation available.
AF260011 Genomic DNA. No translation available.
AL163248 Genomic DNA. Translation: CAB90429.3.
AL163249 Genomic DNA. Translation: CAB90430.1. Sequence problems.
BC029371 mRNA. Translation: AAH29371.1. Sequence problems.
BC140790 mRNA. Translation: AAI40791.1.
BC150284 mRNA. Translation: AAI50285.1.
AK001915 mRNA. Translation: BAA91976.1. Different initiation.
AK023499 mRNA. Translation: BAB14589.1.
AF161350 mRNA. Translation: AAF28910.1. Frameshift.
DB452437 mRNA. No translation available.
CCDSiCCDS33527.2. [O94822-3]
RefSeqiNP_001307695.1. NM_001320766.1.
NP_056380.2. NM_015565.2. [O94822-3]
UniGeneiHs.288773.

Genome annotation databases

EnsembliENST00000361371; ENSP00000354977; ENSG00000198862. [O94822-1]
ENST00000389194; ENSP00000373846; ENSG00000198862. [O94822-3]
ENST00000614971; ENSP00000478783; ENSG00000198862. [O94822-3]
GeneIDi26046.
KEGGihsa:26046.
UCSCiuc002ymr.2. human. [O94822-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018257 mRNA. Translation: BAA34434.2. Different initiation.
AF129075 Genomic DNA. No translation available.
AF260011 Genomic DNA. No translation available.
AL163248 Genomic DNA. Translation: CAB90429.3.
AL163249 Genomic DNA. Translation: CAB90430.1. Sequence problems.
BC029371 mRNA. Translation: AAH29371.1. Sequence problems.
BC140790 mRNA. Translation: AAI40791.1.
BC150284 mRNA. Translation: AAI50285.1.
AK001915 mRNA. Translation: BAA91976.1. Different initiation.
AK023499 mRNA. Translation: BAB14589.1.
AF161350 mRNA. Translation: AAF28910.1. Frameshift.
DB452437 mRNA. No translation available.
CCDSiCCDS33527.2. [O94822-3]
RefSeqiNP_001307695.1. NM_001320766.1.
NP_056380.2. NM_015565.2. [O94822-3]
UniGeneiHs.288773.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J92electron microscopy3.600/w/z1-1766[»]
ProteinModelPortaliO94822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117509. 66 interactions.
IntActiO94822. 39 interactions.
STRINGi9606.ENSP00000373846.

PTM databases

iPTMnetiO94822.
PhosphoSiteiO94822.

Polymorphism and mutation databases

BioMutaiLTN1.

Proteomic databases

EPDiO94822.
MaxQBiO94822.
PaxDbiO94822.
PRIDEiO94822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361371; ENSP00000354977; ENSG00000198862. [O94822-1]
ENST00000389194; ENSP00000373846; ENSG00000198862. [O94822-3]
ENST00000614971; ENSP00000478783; ENSG00000198862. [O94822-3]
GeneIDi26046.
KEGGihsa:26046.
UCSCiuc002ymr.2. human. [O94822-1]

Organism-specific databases

CTDi26046.
GeneCardsiLTN1.
HGNCiHGNC:13082. LTN1.
HPAiCAB034164.
HPA029143.
HPA055604.
MIMi613083. gene.
neXtProtiNX_O94822.
PharmGKBiPA37658.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0803. Eukaryota.
COG5219. LUCA.
GeneTreeiENSGT00390000016055.
HOVERGENiHBG083026.
InParanoidiO94822.
OMAiNSCLQTK.
OrthoDBiEOG7BZVRF.
PhylomeDBiO94822.
TreeFamiTF314286.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii26046.
PROiO94822.
SOURCEiSearch...

Gene expression databases

BgeeiO94822.
CleanExiHS_RNF160.
ExpressionAtlasiO94822. baseline and differential.
GenevisibleiO94822. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR016024. 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. 2 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-403.
    Tissue: Brain.
  2. Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    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), VARIANT SER-403.
    Tissue: Bone marrow.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-696 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-1766 (ISOFORM 2), VARIANT SER-403.
    Tissue: Placenta.
  6. "Human partial CDS from CD34+ stem cells."
    Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-473 (ISOFORM 1), VARIANT SER-403.
    Tissue: Umbilical cord blood.
  7. "RIKEN full-length enriched human cDNA library."
    Arakawa T., Carninci P., Fukuda S., Hasegawa A., Hayashida K., Hori F., Kai C., Kawai J., Kojima M., Murata M., Nakamura M., Nishiyori H., Nomura K., Ohno M., Sasaki D., Shibazaki E., Tagami M., Tagami Y., Hayashizaki Y.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORM 3).
    Tissue: Testis.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation."
    Shao S., von der Malsburg K., Hegde R.S.
    Mol. Cell 50:637-648(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Reconstitution of a minimal ribosome-associated ubiquitination pathway with purified factors."
    Shao S., Hegde R.S.
    Mol. Cell 55:880-890(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Structure and assembly pathway of the ribosome quality control complex."
    Shao S., Brown A., Santhanam B., Hegde R.S.
    Mol. Cell 57:433-444(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.

Entry informationi

Entry nameiLTN1_HUMAN
AccessioniPrimary (citable) accession number: O94822
Secondary accession number(s): A6NL41
, A7E2D0, B2RTS0, C9J7U3, J3KPL4, Q05C47, Q9H8M4, Q9NUY5, Q9P0E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 30, 2010
Last modified: June 8, 2016
This is version 151 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.