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P20L1_RAT
ID   P20L1_RAT               Reviewed;        1015 AA.
AC   Q4V9H5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=PHD finger protein 20-like protein 1;
GN   Name=Phf20l1;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4V9H5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4V9H5-2; Sequence=VSP_040415, VSP_040416, VSP_040417,
CC                                  VSP_040418;
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DR   EMBL; AABR03056473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03057010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03057503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03057556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03059315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03059948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096896; AAH96896.1; -; mRNA.
DR   RefSeq; NP_001258368.1; NM_001271439.1. [Q4V9H5-1]
DR   RefSeq; XP_008763758.1; XM_008765536.2. [Q4V9H5-2]
DR   AlphaFoldDB; Q4V9H5; -.
DR   SMR; Q4V9H5; -.
DR   STRING; 10116.ENSRNOP00000007587; -.
DR   iPTMnet; Q4V9H5; -.
DR   PhosphoSitePlus; Q4V9H5; -.
DR   jPOST; Q4V9H5; -.
DR   PaxDb; Q4V9H5; -.
DR   PRIDE; Q4V9H5; -.
DR   GeneID; 314964; -.
DR   KEGG; rno:314964; -.
DR   UCSC; RGD:1560141; rat. [Q4V9H5-1]
DR   CTD; 51105; -.
DR   RGD; 1560141; Phf20l1.
DR   eggNOG; KOG1844; Eukaryota.
DR   HOGENOM; CLU_1053614_0_0_1; -.
DR   InParanoid; Q4V9H5; -.
DR   OMA; YKETAPM; -.
DR   OrthoDB; 147824at2759; -.
DR   PhylomeDB; Q4V9H5; -.
DR   TreeFam; TF106475; -.
DR   PRO; PR:Q4V9H5; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000046527; Expressed in quadriceps femoris and 18 other tissues.
DR   Genevisible; Q4V9H5; RN.
DR   GO; GO:0044545; C:NSL complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd04508; TUDOR; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR014002; Agenet_dom_plant.
DR   InterPro; IPR022255; DUF3776.
DR   InterPro; IPR040477; KDM4_Tudor_2.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR043449; PHF20-like.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15856; PTHR15856; 1.
DR   Pfam; PF12618; DUF3776; 1.
DR   Pfam; PF02820; MBT; 1.
DR   Pfam; PF18104; Tudor_2; 1.
DR   SMART; SM00743; Agenet; 2.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Isopeptide bond; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1015
FT                   /note="PHD finger protein 20-like protein 1"
FT                   /id="PRO_0000336003"
FT   DOMAIN          11..71
FT                   /note="Tudor 1"
FT   DOMAIN          85..141
FT                   /note="Tudor 2"
FT   ZN_FING         681..729
FT                   /note="PHD-type"
FT   REGION          183..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          859..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..579
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW92"
FT   MOD_RES         907
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW92"
FT   CROSSLNK        75
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW92"
FT   CROSSLNK        79
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW92"
FT   CROSSLNK        530
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW92"
FT   CROSSLNK        849
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW92"
FT   VAR_SEQ         142
FT                   /note="G -> GQFLF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040415"
FT   VAR_SEQ         240
FT                   /note="F -> FV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040416"
FT   VAR_SEQ         311
FT                   /note="A -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040417"
FT   VAR_SEQ         312..1015
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040418"
SQ   SEQUENCE   1015 AA;  114084 MW;  4E903BC422BEF08E CRC64;
     MSKKPPNRPG ITFEIGARLE ALDYLQKWYP SRIEKIDYEE GKMLVHFERW SHRYDEWIYW
     DSNRLRPLER PSLRKEGLKD EEDLFDFKAG EEVLARWTDC RYYPAKIEAI NKEGTFTVQF
     YDGVIRCLKR MHIKAMPEDA KGQVKSQHPL SWCCPIDPAG SCNQSMGSED WIALVKAAAA
     AAAKNKTGSK PRTSANSNKE KERDGGKWFK VPSKKAETST CIVTAEIEKK EELPTSSEPF
     GLHIDSVPKI VFPQPESTLT NKRKNNQGNS FQAKRARLNK ITGLLASKAV GVDGAEKKED
     CSATAPVLEQ AISPKPQSQK KNEAVISSSA NTQKPALLSS TLSSGKARSK KCKHESGESS
     GCIKAPKSPL APELIQAKDL TLVSQLSSVI NKTSSPQPVN PPRPCKHSER RRRSQRLATL
     PMPDDSLEKL SSSSSATDGK VFSISSQNQQ ESSVPEVPAI AYVPLQKLGP CLPLDLSCGS
     EVTGSQAPDS SYPGGECPRE EKEETPLFAN PTSKVVSDVK GAAAATGILK TEKKVKLEEK
     TSTAFGKRKE KDKERKEKRD KDHYKPKQKK KKKKKKKSKQ HDYSDYEDSS LDFLERCSSP
     LTRSSGSSLA PRSTFTEKTT TYQYPRAILS VDLSGENLSD VEFLDDSSTE SLLLSGDEYN
     QDFDSTNFEE SQDEDDALNE IVRCICELDE ENGFMIQCEE CLCWQHSVCM GLLEDSIPEQ
     YICYICRDPP GQRWNAKYRY DKEWLNNGRM YGLSFVKENY SHLNAKKIVS THHLLADVYG
     ITEVLHGLQL KIGILKNKHH PDLRLWAYSG KRKDQDQVVA GAERKVILQD TANSEGRKYV
     QNHKEPPLKM EETYITSEHS YQKPQSFSQD CHSLTDPGSS DDDDVSSFEE DGELHVADNS
     HLLYSVKERG VSEKNPASEN KVFVYNDKKG MEGPGDAHLQ WQLNLLTHIE NVQNEVTSRM
     DLIEKEVDVL ESWLDFTGEL EPPDPLARLP QLKRHIKQLL LDMGKVQQIA TLCSV
 
 
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