Q02455 · MLP1_YEAST
- ProteinProtein MLP1
- GeneMLP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1875 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Together with the closely related MLP2, involved in the structural and functional organization of perinuclear chromatin (PubMed:10638763).
Together with MLP2, associates with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732).
Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732).
Together with MLP2, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing (PubMed:11862215).
MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring (PubMed:12490156).
Recognizes the 5'-splice site of pre-mRNAs and retains unspliced pre-mRNA in the nucleus without affecting splicing itself (PubMed:12490156, PubMed:12531921, PubMed:14718167).
Together with MLP2, associates with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732).
Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732).
Together with MLP2, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing (PubMed:11862215).
MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring (PubMed:12490156).
Recognizes the 5'-splice site of pre-mRNAs and retains unspliced pre-mRNA in the nucleus without affecting splicing itself (PubMed:12490156, PubMed:12531921, PubMed:14718167).
Miscellaneous
Present with 2710 molecules/cell in log phase SD medium.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nuclear envelope | |
Cellular Component | nuclear pore | |
Cellular Component | nuclear pore nuclear basket | |
Cellular Component | nucleoplasm | |
Molecular Function | mRNA binding | |
Molecular Function | promoter-terminator loop anchoring activity | |
Molecular Function | ribonucleoprotein complex binding | |
Molecular Function | structural constituent of nuclear pore | |
Biological Process | DNA repair | |
Biological Process | mRNA export from nucleus | |
Biological Process | negative regulation of protein import into nucleus during spindle assembly checkpoint | |
Biological Process | nuclear mRNA surveillance | |
Biological Process | nucleocytoplasmic transport | |
Biological Process | poly(A)+ mRNA export from nucleus | |
Biological Process | protein import into nucleus | |
Biological Process | protein localization to nuclear pore | |
Biological Process | telomere tethering at nuclear periphery |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein MLP1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ02455
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Distributed fairly evenly along a C-shaped portion of the nuclear periphery, where the spindle pole body localizes in 90% of the cases.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000096501 | 2-1875 | Protein MLP1 | |||
Sequence: SDHDTPMESIQNGENSDERLNAIASFFGCSLEQVKSFDGDVVKHLNDKLLQFNELKSENLKVTVSFDELKASSLKKIDGLKTEMENVIRENDKIRKERNDTFVKFESVENEKMKLSSELEFVKRKLDDLTEEKKETQSNQQRTLKILDERLKEIELVRVENNRSNSECKKLRSTIMDLETKQQGYITNDLNSRTELERKTQELTLLQSNNDWLEKELRSKNEQYLSYRQKTDKVILDIRNELNRLRNDFQMERTNNDVLKQKNNELSKSLQEKLLEIKGLSDSLNSEKQEFSAEMSLKQRLVDLLESQLNAVKEELNSIRELNTAKVIADDSKKQTPENEDLLKELQLTKEKLAQCEKECLRLSSITDEADEDNENLSAKSSSDFIFLKKQLIKERRTKEHLQNQIETFIVELEHKVPIINSFKERTDMLENELNNAALLLEHTSNEKNAKVKELNAKNQKLVECENDLQTLTKQRLDLCRQIQYLLITNSVSNDSKGPLRKEEIQFIQNIMQEDDSTITESDSQKVVTERLVEFKNIIQLQEKNAELLKVVRNLADKLESKEKKSKQSLQKIESETVNEAKEAIITLKSEKMDLESRIEELQKELEELKTSVPNEDASYSNVTIKQLTETKRDLESQVQDLQTRISQITRESTENMSLLNKEIQDLYDSKSDISIKLGKEKSSRILAEERFKLLSNTLDLTKAENDQLRKRFDYLQNTILKQDSKTHETLNEYVSCKSKLSIVETELLNLKEEQKLRVHLEKNLKQELNKLSPEKDSLRIMVTQLQTLQKEREDLLEETRKSCQKKIDELEDALSELKKETSQKDHHIKQLEEDNNSNIEWYQNKIEALKKDYESVITSVDSKQTDIEKLQYKVKSLEKEIEEDKIRLHTYNVMDETINDDSLRKELEKSKINLTDAYSQIKEYKDLYETTSQSLQQTNSKLDESFKDFTNQIKNLTDEKTSLEDKISLLKEQMFNLNNELDLQKKGMEKEKADFKKRISILQNNNKEVEAVKSEYESKLSKIQNDLDQQTIYANTAQNNYEQELQKHADVSKTISELREQLHTYKGQVKTLNLSRDQLENALKENEKSWSSQKESLLEQLDLSNSRIEDLSSQNKLLYDQIQIYTAADKEVNNSTNGPGLNNILITLRRERDILDTKVTVAERDAKMLRQKISLMDVELQDARTKLDNSRVEKENHSSIIQQHDDIMEKLNQLNLLRESNITLRNELENNNNKKKELQSELDKLKQNVAPIESELTALKYSMQEKEQELKLAKEEVHRWKKRSQDILEKHEQLSSSDYEKLESEIENLKEELENKERQGAEAEEKFNRLRRQAQERLKTSKLSQDSLTEQVNSLRDAKNVLENSLSEANARIEELQNAKVAQGNNQLEAIRKLQEDAEKASRELQAKLEESTTSYESTINGLNEEITTLKEEIEKQRQIQQQLQATSANEQNDLSNIVESMKKSFEEDKIKFIKEKTQEVNEKILEAQERLNQPSNINMEEIKKKWESEHEQEVSQKIREAEEALKKRIRLPTEEKINKIIERKKEELEKEFEEKVEERIKSMEQSGEIDVVLRKQLEAKVQEKQKELENEYNKKLQEELKDVPHSSHISDDERDKLRAEIESRLREEFNNELQAIKKKSFDEGKQQAMMKTTLLERKLAKMESQLSETKQSAESPPKSVNNVQNPLLGLPRKIEENSNSPFNPLLSGEKLLKLNSKSSSGGFNPFTSPSPNKHLQNDNDKRESLANKTDPPTHLEPSFNIPASRGLISSSSTLSTDTNDEELTSNNPAQKDSSNRNVQSEEDTEKKKEGEPVKRGEAIEEQTKSNKRPIDEVGELKNDEDDTTENINESKKIKTEDEEEKETDKVNDENSI | ||||||
Modified residue | 337 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 379 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1670 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1710 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1733 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1803 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
May be phosphorylated by CDC28.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the nuclear pore complex (NPC) (PubMed:24152732).
NPC constitutes the exclusive means of nucleocytoplasmic transport (PubMed:24152732).
NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope (PubMed:24152732).
Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof (PubMed:24152732).
Interacts with NAB2, a hnRNP required for mRNA export (PubMed:12531921).
Interacts with MLP2 (PubMed:16027220).
NPC constitutes the exclusive means of nucleocytoplasmic transport (PubMed:24152732).
NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope (PubMed:24152732).
Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof (PubMed:24152732).
Interacts with NAB2, a hnRNP required for mRNA export (PubMed:12531921).
Interacts with MLP2 (PubMed:16027220).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q02455 | MLP2 P40457 | 3 | EBI-11009, EBI-25261 | |
BINARY | Q02455 | NAB2 P32505 | 4 | EBI-11009, EBI-11770 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 69-487 | |||||
Sequence: ELKASSLKKIDGLKTEMENVIRENDKIRKERNDTFVKFESVENEKMKLSSELEFVKRKLDDLTEEKKETQSNQQRTLKILDERLKEIELVRVENNRSNSECKKLRSTIMDLETKQQGYITNDLNSRTELERKTQELTLLQSNNDWLEKELRSKNEQYLSYRQKTDKVILDIRNELNRLRNDFQMERTNNDVLKQKNNELSKSLQEKLLEIKGLSDSLNSEKQEFSAEMSLKQRLVDLLESQLNAVKEELNSIRELNTAKVIADDSKKQTPENEDLLKELQLTKEKLAQCEKECLRLSSITDEADEDNENLSAKSSSDFIFLKKQLIKERRTKEHLQNQIETFIVELEHKVPIINSFKERTDMLENELNNAALLLEHTSNEKNAKVKELNAKNQKLVECENDLQTLTKQRLDLCRQIQYL | ||||||
Coiled coil | 531-1678 | |||||
Sequence: ERLVEFKNIIQLQEKNAELLKVVRNLADKLESKEKKSKQSLQKIESETVNEAKEAIITLKSEKMDLESRIEELQKELEELKTSVPNEDASYSNVTIKQLTETKRDLESQVQDLQTRISQITRESTENMSLLNKEIQDLYDSKSDISIKLGKEKSSRILAEERFKLLSNTLDLTKAENDQLRKRFDYLQNTILKQDSKTHETLNEYVSCKSKLSIVETELLNLKEEQKLRVHLEKNLKQELNKLSPEKDSLRIMVTQLQTLQKEREDLLEETRKSCQKKIDELEDALSELKKETSQKDHHIKQLEEDNNSNIEWYQNKIEALKKDYESVITSVDSKQTDIEKLQYKVKSLEKEIEEDKIRLHTYNVMDETINDDSLRKELEKSKINLTDAYSQIKEYKDLYETTSQSLQQTNSKLDESFKDFTNQIKNLTDEKTSLEDKISLLKEQMFNLNNELDLQKKGMEKEKADFKKRISILQNNNKEVEAVKSEYESKLSKIQNDLDQQTIYANTAQNNYEQELQKHADVSKTISELREQLHTYKGQVKTLNLSRDQLENALKENEKSWSSQKESLLEQLDLSNSRIEDLSSQNKLLYDQIQIYTAADKEVNNSTNGPGLNNILITLRRERDILDTKVTVAERDAKMLRQKISLMDVELQDARTKLDNSRVEKENHSSIIQQHDDIMEKLNQLNLLRESNITLRNELENNNNKKKELQSELDKLKQNVAPIESELTALKYSMQEKEQELKLAKEEVHRWKKRSQDILEKHEQLSSSDYEKLESEIENLKEELENKERQGAEAEEKFNRLRRQAQERLKTSKLSQDSLTEQVNSLRDAKNVLENSLSEANARIEELQNAKVAQGNNQLEAIRKLQEDAEKASRELQAKLEESTTSYESTINGLNEEITTLKEEIEKQRQIQQQLQATSANEQNDLSNIVESMKKSFEEDKIKFIKEKTQEVNEKILEAQERLNQPSNINMEEIKKKWESEHEQEVSQKIREAEEALKKRIRLPTEEKINKIIERKKEELEKEFEEKVEERIKSMEQSGEIDVVLRKQLEAKVQEKQKELENEYNKKLQEELKDVPHSSHISDDERDKLRAEIESRLREEFNNELQAIKKKSFDEGKQQAMMKTTLLERKLAKMESQLSETKQSAES | ||||||
Motif | 1496-1565 | Required for nuclear localization | ||||
Sequence: QPSNINMEEIKKKWESEHEQEVSQKIREAEEALKKRIRLPTEEKINKIIERKKEELEKEFEEKVEERIKS | ||||||
Region | 1641-1690 | Disordered | ||||
Sequence: KKSFDEGKQQAMMKTTLLERKLAKMESQLSETKQSAESPPKSVNNVQNPL | ||||||
Compositional bias | 1668-1689 | Polar residues | ||||
Sequence: QLSETKQSAESPPKSVNNVQNP | ||||||
Compositional bias | 1716-1737 | Polar residues | ||||
Sequence: KLNSKSSSGGFNPFTSPSPNKH | ||||||
Region | 1716-1875 | Disordered | ||||
Sequence: KLNSKSSSGGFNPFTSPSPNKHLQNDNDKRESLANKTDPPTHLEPSFNIPASRGLISSSSTLSTDTNDEELTSNNPAQKDSSNRNVQSEEDTEKKKEGEPVKRGEAIEEQTKSNKRPIDEVGELKNDEDDTTENINESKKIKTEDEEEKETDKVNDENSI | ||||||
Compositional bias | 1738-1752 | Basic and acidic residues | ||||
Sequence: LQNDNDKRESLANKT | ||||||
Compositional bias | 1766-1798 | Polar residues | ||||
Sequence: ASRGLISSSSTLSTDTNDEELTSNNPAQKDSSN | ||||||
Compositional bias | 1799-1875 | Basic and acidic residues | ||||
Sequence: RNVQSEEDTEKKKEGEPVKRGEAIEEQTKSNKRPIDEVGELKNDEDDTTENINESKKIKTEDEEEKETDKVNDENSI | ||||||
Coiled coil | 1834-1866 | |||||
Sequence: DEVGELKNDEDDTTENINESKKIKTEDEEEKET |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,875
- Mass (Da)218,456
- Last updated1994-06-01 v2
- Checksum683A0D34C9066867
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 301 | in Ref. 1; AAA34783 | ||||
Sequence: R → A | ||||||
Compositional bias | 1668-1689 | Polar residues | ||||
Sequence: QLSETKQSAESPPKSVNNVQNP | ||||||
Compositional bias | 1716-1737 | Polar residues | ||||
Sequence: KLNSKSSSGGFNPFTSPSPNKH | ||||||
Compositional bias | 1738-1752 | Basic and acidic residues | ||||
Sequence: LQNDNDKRESLANKT | ||||||
Compositional bias | 1766-1798 | Polar residues | ||||
Sequence: ASRGLISSSSTLSTDTNDEELTSNNPAQKDSSN | ||||||
Compositional bias | 1799-1875 | Basic and acidic residues | ||||
Sequence: RNVQSEEDTEKKKEGEPVKRGEAIEEQTKSNKRPIDEVGELKNDEDDTTENINESKKIKTEDEEEKETDKVNDENSI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L01992 EMBL· GenBank· DDBJ | AAA34783.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X73541 EMBL· GenBank· DDBJ | CAA51948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28320 EMBL· GenBank· DDBJ | CAA82174.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA09245.1 EMBL· GenBank· DDBJ | Genomic DNA |