YLPM1_RAT
ID YLPM1_RAT Reviewed; 1376 AA.
AC P0CB49;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=YLP motif-containing protein 1;
DE AltName: Full=Nuclear protein ZAP3;
GN Name=Ylpm1; Synonyms=Zap, Zap3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1CA.
RX PubMed=14724321; DOI=10.1074/mcp.m300115-mcp200;
RA Tran H.T., Ulke A., Morrice N., Johannes C.J., Moorhead G.B.;
RT "Proteomic characterization of protein phosphatase complexes of the
RT mammalian nucleus.";
RL Mol. Cell. Proteomics 3:257-265(2004).
RN [3]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION
RP IN A COMPLEX WITH ILF2; ILF3; KHDRBS1; RBMX; NCOA5 AND PPP1CA, INTERACTION
RP WITH PPP1CA AND NCOA5, AND TISSUE SPECIFICITY.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA and NCOA5. Forms a complex with ILF2,
CC ILF3, KHDRBS1, RBMX, NCOA5 and PPP1CA. {ECO:0000269|PubMed:14724321,
CC ECO:0000269|PubMed:17890166}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14724321,
CC ECO:0000269|PubMed:17890166}. Nucleus speckle {ECO:0000250}.
CC Note=Migrates to nucleolar caps upon blockage of transcription.
CC -!- TISSUE SPECIFICITY: High level expression seen in the brain, adipose
CC tissue, heart and kidney, with a low level expression in muscle, spleen
CC and lung (at protein level). {ECO:0000269|PubMed:17890166}.
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DR AlphaFoldDB; P0CB49; -.
DR CORUM; P0CB49; -.
DR STRING; 10116.ENSRNOP00000006492; -.
DR CarbonylDB; P0CB49; -.
DR jPOST; P0CB49; -.
DR PaxDb; P0CB49; -.
DR PRIDE; P0CB49; -.
DR UCSC; RGD:1564946; rat.
DR RGD; 1564946; Ylpm1.
DR eggNOG; KOG2400; Eukaryota.
DR InParanoid; P0CB49; -.
DR PRO; PR:P0CB49; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:RGD.
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 1: Evidence at protein level;
KW Isopeptide bond; Methylation; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1376
FT /note="YLP motif-containing protein 1"
FT /id="PRO_0000386651"
FT REGION 1..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1333
FT /note="Involved in interaction with PPP1CA"
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..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..602
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..798
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 675
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49750"
FT CROSSLNK 886
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49750"
FT CROSSLNK 943
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49750"
SQ SEQUENCE 1376 AA; 154270 MW; 4BEA2E67C0D31AE5 CRC64;
MYPNWGRYGG SSHYPPPPVP PPPPPVALPE ASPGPGYSSS TAPAAPSSSG FMSFREQHLA
QLQQLQQMHQ KQMQCVLQPH HLPPPPLPPP PVMPGGGYGD WQPPPPPMPP PPGPALSYQK
QQQYKHQMIH HQRDGPPGLV PMELESPPES PPVPPGSYMP PSQSYMPPPQ PPPSYYPPSS
AQPYLPPAQP SPSKPQLPPP PPSIPSGNKT TIQQEPLETG AKNKNAEQKQ AAPEPDPSTM
TPQEQQQYWY RQHLLSLQQR TKVHLPGHKK GLVTAKDVPE PIKEEAPVPA TSQIAEPLAA
EEPPLPPPNE EMPPPLPPEE PQNNSSEMSE DPEEDARLKQ LQAAAAHWQQ HQQHRVGFQY
QGIMQRHTQL QQILQQYQQV IQHSPHIQTM SLDVQLRHYE MQQQQFQRLY QEWEREFQLW
EEQLHSYPHK DQLEEYEKQW KSWQGHMRAT QTYLQEKVTS FQAVKNQYMG NMAMPPPFVP
YSQMPPPLPT MPPPVLPPSL PPPVMPPALP STIPPPGMPP PVMPPSLPTS VPPPGMPPSL
SSAVLPPPSL SSAGPPPVLP PPSLSGAPPV LPLPPLSSAT PPPGIPPPGV PQGMPPQLTA
PVPPASSSQN SQVPEKPRQA LLPTPVSFGS TPPSPYHPPP QSEQGNSKPL NKVFSSEQGL
GESSSALSQS VIAAKDTPVK SGGLLADPPK GSFLEGPRGP REQKEQLQKL KDFGSEPQTA
DHLPPPDSRL QNTSRPGMYP PPGSYRPPPP MGKPPGSIVR PSAPPARSCV PMTRPPVPIP
PPPPPPPPPP PPPPVIKPKT SSVKQERWDE DSFFGLWDTN DDQGLNSEFK RDTAAIPSAP
VLPPPPVHPS IPPPGPMPMG MPPMSKPPPV QHTVDYGHGR DMPTNKVEQI PYGERITLRP
DPLPERSAFD ADHAGQRDRY DRDRDREPYF DRQSNMTDHR DFKRDRETHR DRDRVLDYER
DRFDRERRPR DDRNQSYRDK KDHSSSRRGG FDRPSYDRKS DRPPYEGPPM FGGERRTYPE
ERMPLPAPSL GHQPPPVPRV EKKPESKNVD DILKPPGRES RPERIVVIMR GLPGSGKTHV
AKLIRDKEVE FGGPAPRVLS LDDYFIAEVE KEEKDPDSGK KVKKKVMEYE YEADMEETYR
TSMFKTFKKT LDDGFFPFII LDAINDRVRH FDQFWSAAKT KGFEVYLAEM SADNQTCGKR
NIHGRKLKEI NKMAEHWEAA PRHMMRLDIR SLLQDAAIEE VEMEDFDANI EDQKEEKKDA
EEEESELGYI PKSKWEMDTS EAKLDKLDGL RTGTKRKRDW EAIASRMEDY LQLPDDYETR
ASEPGKKRVR WADLEEKKDA DRKRAIGFVV GQTDWEKITD ESGHLAERAL NRTKYI
