ID  P40457;
PN  Protein MLP2;
GN  MLP2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus, nuclear pore complex {ECO:0000269|PubMed:24152732}. Note=Nuclear periphery, excluded from nuclear envelope adjacent to nucleolus.
DR  UNIPROT: P40457;
DR  UNIPROT: D6VVD8;
DE  Function: Together with the closely related MLP1, involved in the structural and functional organization of perinuclear chromatin (PubMed:10638763). MLP1/MLP2 associate with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732, PubMed:10617624). Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732). Together with MLP1, 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). Plays a role in the incorporation of components into the spindle pole body (PubMed:10617624, PubMed:14718167, PubMed:16027220). Involved in double-strand break repair, probably also mediated by the YKU70/YKU80 (HDF1/HDF2) heterodimer (PubMed:10638763, PubMed:14718167, PubMed:16027220). {ECO:0000269|PubMed:10085285, ECO:0000269|PubMed:10617624, ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:11862215, ECO:0000269|PubMed:12490156, ECO:0000269|PubMed:14718167, ECO:0000269|PubMed:16027220, ECO:0000269|PubMed:24152732}.
DE  Reference Proteome: Yes;
DE  Interaction: P06704; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P14906; IntAct: EBI-3769975; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3765175; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06411; IntAct: EBI-857722; Score: 0.00
DE  Interaction: Q06512; IntAct: EBI-7126570; Score: 0.40
DE  Interaction: P36106; IntAct: EBI-8221031; Score: 0.22
DE  Interaction: Q02455; IntAct: EBI-2212926; Score: 0.40
DE  Interaction: P38863; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P53540; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P33419; IntAct: EBI-2212931; Score: 0.52
DE  Interaction: P36094; IntAct: EBI-2212931; Score: 0.52
DE  Interaction: P39723; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P32380; IntAct: EBI-2212931; Score: 0.52
DE  Interaction: Q12365; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P06787; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P53865; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P53159; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: Q06677; IntAct: EBI-3758629; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3772417; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-3775422; Score: 0.35
DE  Interaction: P32590; IntAct: EBI-3776771; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781048; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3787834; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790519; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3794434; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799310; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3806012; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812471; Score: 0.35
DE  Interaction: P20081; IntAct: EBI-16269289; Score: 0.35
DE  Interaction: P53916; IntAct: EBI-16285181; Score: 0.35
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005816;
GO  GO:0043021;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:1901925;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0051300;
GO  GO:0034398;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDKISEFLNVPFESLQGVTYPVLRKLYKKIAKFERSEEEVTKLNVLVDEIKSQYYSRISKLKQLLDESSEQKNTAKEEL
SQ  NGLKDQLNEERSRYRREIDALKKQLHVSHEAMREVNDEKRVKEEYDIWQSRDQGNDSLNDDLNKENKLLRRKLMEMENIL
SQ  QRCKSNAISLQLKYDTSVQEKELMLQSKKLIEEKLSSFSKKTLTEEVTKSSHVENLEEKLYQMQSNYESVFTYNKFLLNQ
SQ  NKQLSQSVEEKVLEMKNLKDTASVEKAEFSKEMTLQKNMNDLLRSQLTSLEKDCSLRAIEKNDDNSCRNPEHTDVIDELI
SQ  DTKLRLEKSKNECQRLQNIVMDCTKEEEATMTTSAVSPTVGKLFSDIKVLKRQLIKERNQKFQLQNQLEDFILELEHKTP
SQ  ELISFKERTKSLEHELKRSTELLETVSLTKRKQEREITSLRQKINGCEANIHSLVKQRLDLARQVKLLLLNTSAIQETAS
SQ  PLSQDELISLRKILESSNIVNENDSQAIITERLVEFSNVNELQEKNVELLNCIRILADKLENYEGKQDKTLQKVENQTIK
SQ  EAKDAIIELENINAKMETRINILLRERDSYKLLASTEENKANTNSVTSMEAAREKKIRELEAELSSTKVENSAIIQNLRK
SQ  ELLIYKKSQCKKKTTLEDFENFKGLAKEKERMLEEAIDHLKAELEKQKSWVPSYIHVEKERASTELSQSRIKIKSLEYEI
SQ  SKLKKETASFIPTKESLTRDFEQCCKEKKELQMRLKESEISHNENKMDFSSKEGQYKAKIKELENNLERLRSDLQSKIQE
SQ  IESIRSCKDSQLKWAQNTIDDTEMKMKSLLTELSNKETTIEKLSSEIENLDKELRKTKFQYKFLDQNSDASTLEPTLRKE
SQ  LEQIQVQLKDANSQIQAYEEIISSNENALIELKNELAKTKENYDAKIELEKKEKWAREEDLSRLRGELGEIRALQPKLKE
SQ  GALHFVQQSEKLRNEVERIQKMIEKIEKMSTIVQLCKKKEMSQYQSTMKENKDLSELVIRLEKDAADCQAELTKTKSSLY
SQ  SAQDLLDKHERKWMEEKADYERELISNIEQTESLRVENSVLIEKVDDTAANNGDKDHLKLVSLFSNLRHERNSLETKLTT
SQ  CKRELAFVKQKNDSLEKTINDLQRTQTLSEKEYQCSAVIIDEFKDITKEVTQVNILKENNAILQKSLKNVTEKNREIYKQ
SQ  LNDRQEEISRLQRDLIQTKEQVSINSNKILVYESEMEQCKQRYQDLSQQQKDAQKKDIEKLTNEISDLKGKLSSAENANA
SQ  DLENKFNRLKKQAHEKLDASKKQQAALTNELNELKAIKDKLEQDLHFENAKVIDLDTKLKAHELQSEDVSRDHEKDTYRT
SQ  LMEEIESLKKELQIFKTANSSSDAFEKLKVNMEKEKDRIIDERTKEFEKKLQETLNKSTSSEAEYSKDIETLKKEWLKEY
SQ  EDETLRRIKEAEENLKKRIRLPSEERIQKIISKRKEELEEEFRKKLKENAGSLTFLDNKGSGEDAEEELWNSPSKGNSER
SQ  PSAVAGFINQKNLKPQEQLKNVKNDVSFNDSQSMVTNKENNIVDSSAAGNKAIPTFSFGKPFFSSNTSSLQSFQNPFTAS
SQ  QSNINTNAPLRTLNIQPEVAVKAAINFSNVTDLTNNSTDGAKITEIGSTSKRPIESGTSSDPDTKKVKESPANDQASNE
//