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PHLB1_MOUSE
ID   PHLB1_MOUSE             Reviewed;        1371 AA.
AC   Q6PDH0; Q80TV2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Pleckstrin homology-like domain family B member 1;
DE   AltName: Full=Protein LL5-alpha;
GN   Name=Phldb1; Synonyms=Kiaa0638, Ll5a;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-1371 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   IDENTIFICATION OF THE GENE.
RX   PubMed=14532993;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human LL5A gene and mouse Ll5a gene
RT   in silico.";
RL   Int. J. Oncol. 23:1477-1483(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-520, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-223; SER-472;
RP   SER-503; SER-520; SER-522; THR-524; SER-535; SER-541; SER-553; SER-557;
RP   SER-580; SER-585 AND SER-1022, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-131 AND ARG-514, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PDH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDH0-2; Sequence=VSP_016741, VSP_016742, VSP_016743;
CC   -!- DOMAIN: The PH domain mediates the binding to phosphoinositides.
CC       {ECO:0000250}.
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DR   EMBL; BC058712; AAH58712.1; -; mRNA.
DR   EMBL; AK122336; BAC65618.1; -; mRNA.
DR   CCDS; CCDS23118.1; -. [Q6PDH0-1]
DR   RefSeq; NP_705765.3; NM_153537.4. [Q6PDH0-1]
DR   AlphaFoldDB; Q6PDH0; -.
DR   SMR; Q6PDH0; -.
DR   BioGRID; 221937; 6.
DR   STRING; 10090.ENSMUSP00000034611; -.
DR   iPTMnet; Q6PDH0; -.
DR   PhosphoSitePlus; Q6PDH0; -.
DR   jPOST; Q6PDH0; -.
DR   MaxQB; Q6PDH0; -.
DR   PaxDb; Q6PDH0; -.
DR   PeptideAtlas; Q6PDH0; -.
DR   PRIDE; Q6PDH0; -.
DR   ProteomicsDB; 289742; -. [Q6PDH0-1]
DR   ProteomicsDB; 289743; -. [Q6PDH0-2]
DR   Antibodypedia; 45815; 72 antibodies from 14 providers.
DR   DNASU; 102693; -.
DR   Ensembl; ENSMUST00000034611; ENSMUSP00000034611; ENSMUSG00000048537. [Q6PDH0-1]
DR   GeneID; 102693; -.
DR   KEGG; mmu:102693; -.
DR   UCSC; uc009peh.2; mouse. [Q6PDH0-1]
DR   CTD; 23187; -.
DR   MGI; MGI:2143230; Phldb1.
DR   VEuPathDB; HostDB:ENSMUSG00000048537; -.
DR   eggNOG; ENOG502QPZY; Eukaryota.
DR   GeneTree; ENSGT00940000155231; -.
DR   InParanoid; Q6PDH0; -.
DR   OMA; QEYVTLE; -.
DR   OrthoDB; 70229at2759; -.
DR   TreeFam; TF329165; -.
DR   BioGRID-ORCS; 102693; 6 hits in 71 CRISPR screens.
DR   ChiTaRS; Phldb1; mouse.
DR   PRO; PR:Q6PDH0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q6PDH0; protein.
DR   Bgee; ENSMUSG00000048537; Expressed in saccule of membranous labyrinth and 256 other tissues.
DR   ExpressionAtlas; Q6PDH0; baseline and differential.
DR   Genevisible; Q6PDH0; MM.
DR   GO; GO:0045180; C:basal cortex; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:MGI.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
DR   GO; GO:0010470; P:regulation of gastrulation; ISO:MGI.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR   CDD; cd00060; FHA; 1.
DR   CDD; cd14673; PH_PHLDB1_2; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR037810; PHLDB1/2/3_PH.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Methylation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1371
FT                   /note="Pleckstrin homology-like domain family B member 1"
FT                   /id="PRO_0000053892"
FT   DOMAIN          64..125
FT                   /note="FHA"
FT   DOMAIN          1261..1364
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          153..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..1020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          688..798
FT                   /evidence="ECO:0000255"
FT   COILED          1150..1216
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        158..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         131
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         431
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         463
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         514
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         524
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         565
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         580
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         585
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         976
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UU1"
FT   MOD_RES         1022
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         917
FT                   /note="E -> EYVTLEQLRVVWGTPPMPPSPSPGLPSWASASQDLAPITCLPPMLPS
FT                   SFASITRSSK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_016741"
FT   VAR_SEQ         1174
FT                   /note="R -> RVRLTGARRQQV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_016742"
FT   VAR_SEQ         1325
FT                   /note="K -> KKRFFHFTMVTE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_016743"
FT   CONFLICT        402
FT                   /note="R -> H (in Ref. 2; BAC65618)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1371 AA;  150070 MW;  E0E5204FF8C3C8C5 CRC64;
     MDPLNRSQLG PGCKTQAVVQ KGPLDLIETG QGLKVQTDKP HLVSLGSGRL STAITLLPLE
     EGRTVIGSAA RDISLQGPGL APEHCYIENL RGTLTLYPCG NACTIDGLPV RQPTRLTQGC
     MLCLGQSTFL RFNHPAEAKW MKSMIPAGVR APGPTYNPGS AESESLVNGN HTAQPATRAP
     SACASHSSLV SSIEKDLQEI MDSLVLEEPG AAGKKPAATS PLSPMANGGR YLLSPPTSPG
     AMSVGSSYEN TSPAFSPLSS PASSGSCASH SPSGQEPGPS VPPLVPARSS SYHLALQPPQ
     SRPSGSRSSD SPRLGRKGGH ERPPSPGLRG LLTDSPAATV LAEARRTTES PRLGGQLPVV
     AISLSEYPSS GARSQPASIP GSPKFQSPVP APRNKIGTLQ DRPPSPFREP PGTERVLTSS
     PSRQLVGRTF SDGLAATRTL QPPESPRLGR RGLDSMRELP PLSPSLSRRA LSPLPARTAP
     DPKLSREVAE SPRPRRWAAH GTSPEDFSLT LGARGRRTRS PSPTLGESLA PRKGSFSGRL
     SPAYSLGSLT GASPRQSPRA QRKLSSGDLR VPIPRERKNS ITEISDNEDE LLEYHRRQRQ
     ERLREQEMER LERQRLETIL NLCAEYSRAD GGPETGELPS IGEATAALAL AGRRPSRGLA
     GAIVVSGRCG EESGGASQRL WESMERSDEE NLKEECSSTE STQQEHEDAP GAKHQGEVLA
     VEEERAQVLG RVEQLKIRVK ELEQQLQEAA REAEMERALL QGEREAERAS LQKEQRAVDQ
     LQEKLVALET GIQKDRDKEA DALETETKLF EDLEFQQLER ESRVEEEREL AGQGLLRSKA
     ELLRSVSKRK ERLAVLDSQA GQIRAQAVQE SERLAREKNA ALQLLQKEKE KLNVLERRYH
     SLTGGRPFPK TTSTLKEMEK LLLPAVDLEQ WYQELMSGLG TGLAAASPRS SPPPLPAKAS
     RQLQVYRSKM DSDAASPLPR TRSGPLPSSS GSSSSSSQLS VATLGRSPSP KSALLAQNGT
     SSLPRNLAAT LQDIETKRQL ALQQKGHQVI EEQRRRLAEL KQKAAAEAQC QWDALHGAGP
     FSAGPSGFPA LMHHSILHHL PAGRERGEEG EHAYDTLSLE SSDSMETSIS TGGNSACSPD
     NMSSASGLDM GKIEEMEKML KEAHAEKSRL MESREREMEL RRQALEEERR RREQVERRLQ
     SESARRQQLV EKEVKLREKQ FSQARPLTRY LPNRKEDFDL KTHIESSGHG VDTCLHVVLS
     SKVCRGYLIK MGGKIKSWKK RWFVFDRLKR TLSYYVDKHE TKLKGVIYFQ AIEEVYYDHL
     RSAAKSPNPA LTFCVKTHDR LYYMVAPSAE AMRIWMDVIV TGAEGYTQFM N
 
 
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