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GPTC8_MOUSE
ID   GPTC8_MOUSE             Reviewed;        1505 AA.
AC   A2A6A1; Q80TY1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=G patch domain-containing protein 8;
GN   Name=Gpatch8; Synonyms=Gpatc8, Kiaa0553;
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 840-1505.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915; SER-918 AND SER-1179,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-479, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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DR   EMBL; AL596258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK122307; BAC65589.1; -; mRNA.
DR   CCDS; CCDS48944.1; -.
DR   RefSeq; NP_001152964.1; NM_001159492.1.
DR   AlphaFoldDB; A2A6A1; -.
DR   SMR; A2A6A1; -.
DR   BioGRID; 231931; 7.
DR   STRING; 10090.ENSMUSP00000120649; -.
DR   iPTMnet; A2A6A1; -.
DR   PhosphoSitePlus; A2A6A1; -.
DR   EPD; A2A6A1; -.
DR   jPOST; A2A6A1; -.
DR   MaxQB; A2A6A1; -.
DR   PaxDb; A2A6A1; -.
DR   PeptideAtlas; A2A6A1; -.
DR   PRIDE; A2A6A1; -.
DR   ProteomicsDB; 271081; -.
DR   Antibodypedia; 52434; 35 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000143842; ENSMUSP00000120649; ENSMUSG00000034621.
DR   GeneID; 237943; -.
DR   KEGG; mmu:237943; -.
DR   UCSC; uc007lsb.2; mouse.
DR   CTD; 23131; -.
DR   MGI; MGI:1918667; Gpatch8.
DR   VEuPathDB; HostDB:ENSMUSG00000034621; -.
DR   eggNOG; KOG2184; Eukaryota.
DR   GeneTree; ENSGT00940000159523; -.
DR   HOGENOM; CLU_006418_0_0_1; -.
DR   InParanoid; A2A6A1; -.
DR   OMA; AEPEYYH; -.
DR   OrthoDB; 332880at2759; -.
DR   PhylomeDB; A2A6A1; -.
DR   TreeFam; TF332138; -.
DR   BioGRID-ORCS; 237943; 9 hits in 72 CRISPR screens.
DR   ChiTaRS; Gpatch8; mouse.
DR   PRO; PR:A2A6A1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; A2A6A1; protein.
DR   Bgee; ENSMUSG00000034621; Expressed in otic placode and 250 other tissues.
DR   Genevisible; A2A6A1; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Isopeptide bond; Metal-binding; Phosphoprotein;
KW   Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1505
FT                   /note="G patch domain-containing protein 8"
FT                   /id="PRO_0000379799"
FT   DOMAIN          40..86
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   ZN_FING         136..160
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          166..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..1304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          89..124
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        166..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..684
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..701
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..764
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..831
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..849
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..936
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..983
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1062
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         479
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         753
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         915
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         918
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         985
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         1013
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         1018
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         1037
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         1039
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         1085
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   MOD_RES         1179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        311
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   CROSSLNK        573
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   CROSSLNK        1109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKJ3"
FT   CONFLICT        954
FT                   /note="T -> I (in Ref. 2; BAC65589)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1505 AA;  164987 MW;  0BCC873DA8AE6DDF CRC64;
     MADRFSRFNE DRDFQGNHFD QYEEGHLEIE QASLDKPIES DNIGHRLLQK HGWKLGQGLG
     KSLQGRTDPI PIVVKYDVMG MGRMEMELDY AEDATERRRV LEVEKEDTEE LRQKYKDYVD
     KEKAIAKALE DLRANFYCEL CDKQYQKHQE FDNHINSYDH AHKQRLKDLK QREFARNVSS
     RSRKDEKKQE KALRRLHELA EQRKQAECAP GSGPMFRPTT VAVDEDGGEE DKDESSTNSG
     ASAVSSCGFG ADFSTDKGGS FTSVQITNTT GLSQAPGLAS QGISFGIKNN LGPPLQKLGV
     SFSFAKKAPV KLESIASVFK DHAEEGSSED GTKADEKSSD QGVQKVGDTD GTGNLDGKKE
     DEDPQDGGSL ASTLSKLKRM KREEGTGATE PEYYHYIPPA HCKVKPNFPF LLFMRASEQM
     EGDHSAHSKS APENRKSSSP KPQGCSKTAA SPGAERTVSE ASELQKEAAV AGPSEPGGKT
     ETKKGSGGGE DEQSVESRET SESPMCESNP KDISQATPAT KAGQGPKHPT GPFFPVLSKD
     ESTALQWPSE LLIFTKAEPS ISYSCNPLYF DFKLSRNKDA KAKGTEKPKD VAGSSKDHLQ
     SLDPREPNKS QEEEQDVVLS SEGRVDEPAS GAACSSLNKQ EPGGSHMSET EDTGRSHPSK
     KEPSGKSHRH KKKKKHKKSS KHKRKHKADT EEKSSKAESG EKSKKRKKRK RKKNKSSAAA
     DSERGPKSEP PGSGSPAPPR RRRRAQDDSQ RRSLPAEEGN SGKKDDGGGG SSCQDHSGRK
     HKGEPPTSSC QRRANTKHSS RSSHRSQPSS GDEDSDDASS HRLHQKSPSQ YSEEEEEEEE
     EEEEEDEDSG SEHSRSRSRS GHRHSSHRSS RRSYSSSSDA SSDQSCYSRQ HSYSDDSYSD
     YSDRSRRHSK RSHDSDDSDY TSSKHRSKRH KYSSSDDDYS LSCSQSRSRS RSHTRERSRS
     RGRSRSSSCS RSRSKRRSRS TTAHSWQRSR SYSRDRSRST RSPSQRSGSR KGSWGHESPE
     ERRSGRRDFI RSKIYRSQSP HYFQSGRGEG PGKKEDGRGD DSKGAGLPSQ NSNTGTGRGS
     ESDCSPEDKN SVTARLLLEK IQSRKVERKP NVCEEVLATP NKAGLKYKNP PQGYFGPKLP
     PSLGNKPVLP MIGKLPATRK SNKKCEESGL ERGEEQEHSE PEEGSPRSSD APFGHQFSEE
     AAGPLSDPPP EEPKSEEATA DHSVAPLGTP AHTDCYPGDP AISHNYLPDP SDGDTLESLD
     SGSQPGPVES SLLPIAPDLE HFPNYAPPSG EPSIESTDGT EDASLAPLES QPITFTPEEM
     EKYSKLQQAA QQHIQQQLLA KQVKAFPAST ALAPATPALQ PIHIQQPATA SATSITTVQH
     AILQHHAAAA AAAIGIHPHP HPQPLAQVHH IPQPHLTPIS LSHLTHSIIP GHPATFLASH
     PIHIIPASAI HPGPFTFHPV PHAALYPTLL APRPAAAAAT ALHLHPLLHP IFSGQDLQHP
     PSHGT
 
 
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