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Database: UniProt
Entry: G5CB95_HETGA
LinkDB: G5CB95_HETGA
Original site: G5CB95_HETGA 
ID   G5CB95_HETGA            Unreviewed;       821 AA.
AC   G5CB95;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=GW7_05157 {ECO:0000313|EMBL:EHB18806.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB18806.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB18806.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; JH204765; EHB18806.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5CB95; -.
DR   STRING; 10181.G5CB95; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   eggNOG; KOG2995; Eukaryota.
DR   InParanoid; G5CB95; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd11785; SH3_SH3RF_C; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 4.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR   PANTHER; PTHR14167:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR   PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF14604; SH3_9; 2.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 4.
DR   SUPFAM; SSF50044; SH3-domain; 4.
DR   PROSITE; PS50002; SH3; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          115..174
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          177..240
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          408..469
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          762..821
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  87280 MW;  BF052A71A9D4D455 CRC64;
     MGCRAAKRGY MVAVGSEDAD QKAQAELDRD AQDPQGDWSA SSRDLSLNPD PGPPLDITWG
     LASQEVSLVL HLEDESASSR DLSLNPDPGP PLDITWGLAS QEVSLVLHLE DESLSQLPYG
     KALYSYEGKE PGDLKFNKGD VIILRRRVDE HWFHGELHGT RGFLPASYVQ CLRPLPQAPP
     QGTALYDFEM KDRDQDQDCL TFTKDEVLTV IRRVDDNWAE GMLGDRIGIF PLLYVQHRPG
     FSILLLKMRT YHMNTNCQLN DSAKQLIEMD KLCPAAAAAS SCAVPLPSDA STVASAGLGP
     TAGSSGAVSA FQRRMDSKKN AKKRHSFTAL SVTHKSSQAV THRHSMEISA PVLISSSDPR
     AAARIGELTH PPCSMPAQDP CSAGPVPTAV PRASTAAGEQ GTSPKVPLPL NVYLALYAYK
     PQKSDELELR KGEMYRVLEK CQDGWFKGAS MRTGLSGVFP GNYVTPISRA PGGAAGPPRN
     SALGGSPLAK GMATTMHPGG GSLSRPALPL TTPQAQAPHP AGSPPTGSCP HHTAQPATGQ
     TRGALSAAAH PSAQAQDRPT ATVTPLRTQS SPSRLPTTSL RPRSMVSPQP GQQSPVQTSP
     RPAIPFTSAA SAITPPSVST TSLSGDAGGG SSGGLSTSSP TSTGCRLEDK RGEKKEKKSG
     LLKLLAGAST RRKSRSPPSF SPTHDPLVAT DTSLLGATGP DMSSLSVHGR AGSCPIESEM
     RGAMGLEPLH RKTGSLDLNF CSSPARQAAL STAAIRPEPK PLPRERYRVV VSYPPQSEAE
     IELKEGDVVF VHRKRKDGWY EGTLQRNGRT GLFPGSFVES F
//
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