YLPM1_MOUSE
ID YLPM1_MOUSE Reviewed; 1386 AA.
AC Q9R0I7; E9QKY3; Q7TMM4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=YLP motif-containing protein 1;
DE AltName: Full=Nuclear protein ZAP3;
GN Name=Ylpm1; Synonyms=Zap, Zap3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal liver;
RX PubMed=10716735; DOI=10.1073/pnas.97.7.3062;
RA Misawa K., Nosaka T., Morita S., Kaneko A., Nakahata T., Asano S.,
RA Kitamura T.;
RT "A method to identify cDNAs based on localization of green fluorescent
RT protein fusion products.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3062-3066(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1303-1386.
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15511642; DOI=10.1016/j.mod.2004.07.005;
RA Armstrong L., Lako M., van Herpe I., Evans J., Saretzki G., Hole N.;
RT "A role for nucleoprotein Zap3 in the reduction of telomerase activity
RT during embryonic stem cell differentiation.";
RL Mech. Dev. 121:1509-1522(2004).
CC -!- FUNCTION: Plays a role in the reduction of telomerase activity during
CC differentiation of embryonic stem cells by binding to the core promoter
CC of TERT and controlling its down-regulation.
CC {ECO:0000269|PubMed:15511642}.
CC -!- SUBUNIT: Interacts with PPP1CA and NCOA5. Forms a complex with ILF2,
CC ILF3, KHDRBS1, RBMX, NCOA5 and PPP1CA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000269|PubMed:10716735}. Note=Migrates to nucleolar caps upon
CC blockage of transcription. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the 7.5 dpc embryos.
CC {ECO:0000269|PubMed:15511642}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB033168; BAA85182.1; -; mRNA.
DR EMBL; AC127582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR974585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055465; AAH55465.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q9R0I7; -.
DR SMR; Q9R0I7; -.
DR IntAct; Q9R0I7; 5.
DR iPTMnet; Q9R0I7; -.
DR PhosphoSitePlus; Q9R0I7; -.
DR EPD; Q9R0I7; -.
DR jPOST; Q9R0I7; -.
DR MaxQB; Q9R0I7; -.
DR PeptideAtlas; Q9R0I7; -.
DR PRIDE; Q9R0I7; -.
DR ProteomicsDB; 275227; -.
DR Antibodypedia; 62380; 17 antibodies from 7 providers.
DR Ensembl; ENSMUST00000101202; ENSMUSP00000098763; ENSMUSG00000021244.
DR MGI; MGI:1926195; Ylpm1.
DR VEuPathDB; HostDB:ENSMUSG00000021244; -.
DR eggNOG; KOG2400; Eukaryota.
DR GeneTree; ENSGT00440000039837; -.
DR HOGENOM; CLU_001969_0_0_1; -.
DR InParanoid; Q9R0I7; -.
DR ChiTaRS; Ylpm1; mouse.
DR PRO; PR:Q9R0I7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9R0I7; protein.
DR Bgee; ENSMUSG00000021244; Expressed in saccule of membranous labyrinth and 259 other tissues.
DR ExpressionAtlas; Q9R0I7; baseline and differential.
DR Genevisible; Q9R0I7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032204; P:regulation of telomere maintenance; IDA:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026314; YLP_motif_con_p1.
DR PANTHER; PTHR13413; PTHR13413; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Methylation; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1386
FT /note="YLP motif-containing protein 1"
FT /id="PRO_0000066299"
FT REGION 1..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1343
FT /note="Involved in interaction with PPP1CA"
FT /evidence="ECO:0000250"
FT COMPBIAS 13..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..769
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..877
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 683
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49750"
FT CROSSLNK 894
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49750"
FT CROSSLNK 951
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49750"
FT CONFLICT 75
FT /note="C -> S (in Ref. 1; BAA85182)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="G -> S (in Ref. 1; BAA85182)"
FT /evidence="ECO:0000305"
FT CONFLICT 1280
FT /note="I -> T (in Ref. 1; BAA85182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1386 AA; 155129 MW; FBCCEA15A97411C7 CRC64;
MYPNWGRYGG SSHYPPPPVP PPPPPVALPE ASPGPGYSSS TAPAAPSSSG FMSFREQHLA
QLQQLQQMHQ KQMQCVLQPH HLPPPPLPPP PVMPGGGYGD WQPPPPPMPP PPGPALSYQK
QQQYKHQMIH HQRDGPPGLV PMELESPPES PPVPPGSYMP PSQSYMPPPQ PPPSYYPPSS
AQPYLPPAQP GPSKPQLPPP PSIPSGNKTA IQQEPLESGA KNKTAEQKQA APEPDPSTMT
PQEQQQYWYR QHLLSLQQRT KVHLPGHKKG LVTAKDVPEP IKEEAPGPAA SQVAEPLAAE
KPPLPPPNEE APPPLSPEEP QSEDSEDSED SEEDARFKQL KAIAAHWQAA AAHWQQQQQQ
RVGFQYQGIM QRHTQLQQIL QQYQQVIQHS PHIQTMSLDV QLRHYEMQQQ QFQHLFQDWE
REFQLWEEQL HSYPHKDQLQ EYEKQWKTWQ GHMKATQTYL QEKVNSFQTV KSQYLGNMAM
PPPFVPYSQM PPPLPTMPPP VLPPSLPPPV MPPALPTSIP PPGMPPPVMP PSLPTSVPPP
GMPPSLSSGP PPVLPPPALS SAGSPPVLPP PALPGGPPIL PLPPLSSATP PPGIPPPGAP
QGMPPQLTAP LPPASGSQNS QIPEKPRQAL LPTPVSFGST PPSPYHPPPQ SEQVNSKPLN
KVFSSEQGLG ESSALSQSII AAKDTPVKSG GLLADPPKGS FLEGPRGPRE QKEQLQKLKD
FGSEPQMADH LPPPDSRLQN PSRPGMYPPP GSYRPPPPMG KPPGSIVRPS APPARSSIPM
TRPPVPIPPP PPPPPPPPPP PPVIKSKTSS VKQERWDEDS FFGLWDTNDD QGLNSEFKRD
TATIPSAPVL PPPPVHSSIP PPGPMPMGMP PMSKPPPVQH TVDYGHGRDM PTNKVEQIPY
GERITLRPDP LPERSTFDAD HAGQRDRYDR DRDREPYFDR PSNITDHRDF KRDRETHRDR
DRDRVLDYER DRFDRERRPR DDRNQSYRDK KDHSSSRRGG FDRPSYDRKS DRPPYEGPPM
FGGERRTYPE ERMPLPAPAL GHQPPPVPRV EKKPESKNVD DILKPPGRES RPERIVVIMR
GLPGSGKTHV AKLIRDKEVE FGGPAPRVLS LDDYFIAEVE KEEKDPDSGK KVKKKVMEYE
YEADMEETYR TSMFKTFKKT LDDGFFPFII LDAINDRVRH FDQFWSAAKT KGFEVYLAEM
SADNQTCGKR NIHGRKLKEI NKMAEHWEVA PRHMMRLDIR SLLQDAAIEE VEMEDFDANI
EDQKEEKKDA EEEESELGYI PKSKWEMDTS EAKLDKLDGL RTGTKRKRDW EAIASRMEDY
LQLPDDYETR ASEPGKKRVR WADLEEKKDA DRKRAIGFVV GQTDWEKITD ESGHLAERAL
NRTKYI
