UniProtKB - Q9UN81 (LORF1_HUMAN)
Protein
LINE-1 retrotransposable element ORF1 protein
Gene
L1RE1
Organism
Homo sapiens (Human)
Status
Functioni
Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.5 Publications
Miscellaneous
Long interspersed element-1/LINE-1/L1 retrotransposons are present in more than 500'000 full (6 kb) or truncated copies in the human genome. Most of them are inactive but 80 to 100 of those elements could be transcribed, translated and active in any individual. An active LINE-1 encodes for 2 proteins translated from a single RNA containing 2 non-overlapping ORFs, ORF1 and ORF2. ORF1p is described in this entry as a representative of all ORF1p potentially expressed by active elements. ORF2p is described in the related entry AC O00370.
GO - Molecular functioni
- identical protein binding Source: UniProtKB
- nucleotide binding Source: UniProtKB-KW
- single-stranded DNA binding Source: UniProtKB
- single-stranded RNA binding Source: UniProtKB
GO - Biological processi
- transposition, RNA-mediated Source: UniProtKB
Keywordsi
Ligand | Nucleotide-binding |
Enzyme and pathway databases
PathwayCommonsi | Q9UN81 |
Names & Taxonomyi
Protein namesi | Recommended name: LINE-1 retrotransposable element ORF1 proteinShort name: L1ORF1p Alternative name(s): LINE retrotransposable element 1 LINE1 retrotransposable element 1 |
Gene namesi | Name:L1RE1 Synonyms:LRE1 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
MIMi | 151626, gene |
neXtProti | NX_Q9UN81 |
Subcellular locationi
Nucleus
- nucleolus 1 Publication
Other locations
- Cytoplasmic ribonucleoprotein granule 2 Publications
- Stress granule 2 Publications
Note: Colocalizes with its encoding RNA in cytoplasmic ribonucleoprotein particle (PubMed:16183655). Mainly cytoplasmic, rarely detected in the nucleus, possibly within the nucleolus (PubMed:17562864).2 Publications
Nucleus
- nucleolus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
- cytoplasmic ribonucleoprotein granule Source: UniProtKB
- cytoplasmic stress granule Source: UniProtKB
- ribonucleoprotein complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 93 | L → A: Small decrease in localization to stress granules; when associated with A-100 and A-114. 1 Publication | 1 | |
Mutagenesisi | 100 | L → A: Small decrease in localization to stress granules; when associated with A-93 and A-114. 1 Publication | 1 | |
Mutagenesisi | 114 | L → A: Small decrease in localization to stress granules; when associated with A-93 and A-100. 1 Publication | 1 | |
Mutagenesisi | 116 | E → A: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with A-123. 1 Publication | 1 | |
Mutagenesisi | 123 | D → A: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with A-116. 1 Publication | 1 | |
Mutagenesisi | 132 | G → I: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with I-135 and I-142. 1 Publication | 1 | |
Mutagenesisi | 133 | K → S: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with A-137, A-140 and S-141. 1 Publication | 1 | |
Mutagenesisi | 135 | R → I: Loss of LINE-1 retrotransposition without effect on RNA-binding; when associated with I-132 and I-142. 1 Publication | 1 | |
Mutagenesisi | 137 | K → A: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-140 and S-141. 1 Publication | 1 | |
Mutagenesisi | 140 | K → A: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-137 and S-141. 1 Publication | 1 | |
Mutagenesisi | 141 | R → S: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-137 and A-140. 1 Publication | 1 | |
Mutagenesisi | 142 | N → I: Loss of LINE-1 retrotransposition without effect on RNA-binding; when associated with I-132 and I-135. 1 Publication | 1 | |
Mutagenesisi | 155 | R → A: No effect on subcellular localization; when associated with A-157. 1 Publication | 1 | |
Mutagenesisi | 157 | N → A: No effect on subcellular localization; when associated with A-155. Complete loss of localization to stress granules, slightly increased localization to the nucleus; when associated with G-159. 1 Publication | 1 | |
Mutagenesisi | 159 | R → A: Moderately alters RNA-binding activity. 1 Publication | 1 | |
Mutagenesisi | 159 | R → G: Decreased localization to stress granules. Complete loss of localization to stress granules, slightly increased localization to the nucleus; when associated with A-157. 1 Publication | 1 | |
Mutagenesisi | 165 | E → G: No effect on cytoplasmic localization, may increase nucleolar localization. 1 Publication | 1 | |
Mutagenesisi | 206 | R → A: Loss of RNA-binding activity; when associated with A-210 and A-211. 2 Publications | 1 | |
Mutagenesisi | 210 | R → A: Loss of RNA-binding activity; when associated with A-206 and A-211. 2 Publications | 1 | |
Mutagenesisi | 211 | R → A: Loss of RNA-binding activity; when associated with A-206 and A-210. 2 Publications | 1 | |
Mutagenesisi | 218 | I → Y: Moderately alters RNA-binding activity. 2 Publications | 1 | |
Mutagenesisi | 220 | R → A: Loss of LINE-1 retrotransposition without affecting RNA-binding. 2 Publications | 1 | |
Mutagenesisi | 235 | R → A: Loss of LINE-1 retrotransposition with decreased RNA-binding. 2 Publications | 1 | |
Mutagenesisi | 261 – 262 | RR → AA: Small decrease in localization to stress granules. 1 Publication | 2 | |
Mutagenesisi | 261 | R → A: Loss of LINE-1 retrotransposition with decreased RNA-binding. 2 Publications | 1 | |
Mutagenesisi | 261 | R → K: Loss of LINE-1 retrotransposition without affecting RNA-binding. 2 Publications | 1 | |
Mutagenesisi | 282 | Y → A: Loss of LINE-1 retrotransposition without affecting RNA-binding. 1 Publication | 1 |
Miscellaneous databases
Pharosi | Q9UN81, Tbio |
Genetic variation databases
BioMutai | HGNC:6686 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000425081 | 1 – 338 | LINE-1 retrotransposable element ORF1 proteinAdd BLAST | 338 |
Post-translational modificationi
Polyubiquitinated, probably by UBR2, which induces its degradation.1 Publication
Keywords - PTMi
Ubl conjugationProteomic databases
EPDi | Q9UN81 |
jPOSTi | Q9UN81 |
MassIVEi | Q9UN81 |
MaxQBi | Q9UN81 |
PeptideAtlasi | Q9UN81 |
PRIDEi | Q9UN81 |
PTM databases
iPTMneti | Q9UN81 |
PhosphoSitePlusi | Q9UN81 |
Interactioni
Subunit structurei
Binary interactionsi
Hide detailsQ9UN81
With | #Exp. | IntAct |
---|---|---|
itself | 4 | EBI-722458,EBI-722458 |
UPF1 [Q92900] | 6 | EBI-722458,EBI-373471 |
Q8TE30 | 15 | EBI-722458,EBI-8874509 |
GO - Molecular functioni
- identical protein binding Source: UniProtKB
Protein-protein interaction databases
DIPi | DIP-48676N |
IntActi | Q9UN81, 21 interactors |
Miscellaneous databases
RNActi | Q9UN81, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | Q9UN81 |
SMRi | Q9UN81 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 157 – 252 | RNA recognition motif (RRM) domainAdd BLAST | 96 | |
Regioni | 253 – 317 | C-terminal domain (CTD)Add BLAST | 65 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 49 – 153 | Sequence analysisAdd BLAST | 105 |
Domaini
The coiled coil domain mediates homotrimerization.
The RRM and the CTD domain are both required for proper RNA-binding activity.
Sequence similaritiesi
Belongs to the transposase 22 family.Curated
Keywords - Domaini
Coiled coilFamily and domain databases
Gene3Di | 3.30.250.20, 1 hit 3.30.70.1820, 1 hit |
InterProi | View protein in InterPro IPR042566, L1_C IPR035300, L1_dsRBD IPR043636, L1_RRM_dom IPR035301, L1_trimer IPR004244, Transposase_22 IPR042497, Transposase_L1_sf |
PANTHERi | PTHR11505, PTHR11505, 1 hit |
Pfami | View protein in Pfam PF17490, Tnp_22_dsRBD, 1 hit PF17489, Tnp_22_trimer, 1 hit PF02994, Transposase_22, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9UN81-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGKKQNRKTG NSKTQSASPP PKERSSSPAT EQSWMENDFD ELREEGFRRS
60 70 80 90 100
NYSELREDIQ TKGKEVENFE KNLEECITRI TNTEKCLKEL MELKTKAREL
110 120 130 140 150
REECRSLRSR CDQLEERVSA MEDEMNEMKR EGKFREKRIK RNEQSLQEIW
160 170 180 190 200
DYVKRPNLRL IGVPESDVEN GTKLENTLQD IIQENFPNLA RQANVQIQEI
210 220 230 240 250
QRTPQRYSSR RATPRHIIVR FTKVEMKEKM LRAAREKGRV TLKGKPIRLT
260 270 280 290 300
ADLSAETLQA RREWGPIFNI LKEKNFQPRI SYPAKLSFIS EGEIKYFIDK
310 320 330
QMLRDFVTTR PALKELLKEA LNMERNNRYQ PLQNHAKM
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 251 | A → V in AAB59367 (PubMed:10655552).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF148856 Genomic DNA Translation: AAD39214.1 M80343 Genomic DNA Translation: AAB59367.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF148856 Genomic DNA Translation: AAD39214.1 M80343 Genomic DNA Translation: AAB59367.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2LDY | NMR | - | A | 157-330 | [»] | |
2W7A | X-ray | 1.40 | A/B | 157-250 | [»] | |
2YKO | X-ray | 2.10 | A/B/C | 106-330 | [»] | |
2YKP | X-ray | 3.10 | A/B/C | 106-326 | [»] | |
2YKQ | X-ray | 3.10 | A/B/C | 106-326 | [»] | |
6FIA | X-ray | 2.65 | A/B/C/D/E/F | 53-152 | [»] | |
BMRBi | Q9UN81 | |||||
SMRi | Q9UN81 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-48676N |
IntActi | Q9UN81, 21 interactors |
PTM databases
iPTMneti | Q9UN81 |
PhosphoSitePlusi | Q9UN81 |
Genetic variation databases
BioMutai | HGNC:6686 |
Proteomic databases
EPDi | Q9UN81 |
jPOSTi | Q9UN81 |
MassIVEi | Q9UN81 |
MaxQBi | Q9UN81 |
PeptideAtlasi | Q9UN81 |
PRIDEi | Q9UN81 |
Protocols and materials databases
CPTCi | Q9UN81, 2 antibodies |
Organism-specific databases
MIMi | 151626, gene |
neXtProti | NX_Q9UN81 |
Enzyme and pathway databases
PathwayCommonsi | Q9UN81 |
Miscellaneous databases
Pharosi | Q9UN81, Tbio |
RNActi | Q9UN81, protein |
SOURCEi | Search... |
Family and domain databases
Gene3Di | 3.30.250.20, 1 hit 3.30.70.1820, 1 hit |
InterProi | View protein in InterPro IPR042566, L1_C IPR035300, L1_dsRBD IPR043636, L1_RRM_dom IPR035301, L1_trimer IPR004244, Transposase_22 IPR042497, Transposase_L1_sf |
PANTHERi | PTHR11505, PTHR11505, 1 hit |
Pfami | View protein in Pfam PF17490, Tnp_22_dsRBD, 1 hit PF17489, Tnp_22_trimer, 1 hit PF02994, Transposase_22, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LORF1_HUMAN | |
Accessioni | Q9UN81Primary (citable) accession number: Q9UN81 Secondary accession number(s): Q15605 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 22, 2014 |
Last sequence update: | May 1, 2000 | |
Last modified: | April 7, 2021 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families