ID G3QUM1_GORGO Unreviewed; 685 AA.
AC G3QUM1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Ring finger protein 6 {ECO:0000313|Ensembl:ENSGGOP00000006426.3};
GN Name=RNF6 {ECO:0000313|Ensembl:ENSGGOP00000006426.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000006426.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000006426.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000006426.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000006426.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RNF12 family.
CC {ECO:0000256|ARBA:ARBA00038418}.
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DR EMBL; CABD030088270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004054327.1; XM_004054279.2.
DR RefSeq; XP_004054328.1; XM_004054280.2.
DR RefSeq; XP_004054329.1; XM_004054281.2.
DR RefSeq; XP_004054330.1; XM_004054282.2.
DR RefSeq; XP_018895450.1; XM_019039905.1.
DR RefSeq; XP_018895451.1; XM_019039906.1.
DR AlphaFoldDB; G3QUM1; -.
DR STRING; 9593.ENSGGOP00000006426; -.
DR Ensembl; ENSGGOT00000006596.3; ENSGGOP00000006426.3; ENSGGOG00000006568.3.
DR GeneID; 101150058; -.
DR KEGG; ggo:101150058; -.
DR CTD; 6049; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000158530; -.
DR HOGENOM; CLU_025933_0_0_1; -.
DR InParanoid; G3QUM1; -.
DR OMA; DISRDHT; -.
DR OrthoDB; 5474929at2759; -.
DR TreeFam; TF325756; -.
DR Proteomes; UP000001519; Chromosome 13.
DR Bgee; ENSGGOG00000006568; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16673; RING-H2_RNF6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45931:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF6; 1.
DR PANTHER; PTHR45931; SI:CH211-59O9.10; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 632..673
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 78107 MW; 0CD9D496F8157ED7 CRC64;
MNQSRSRSDG GSEETLSQDH NHHENERRWQ QERLHREEAY YQFINELNDE DYRLMRDHNL
LGTPGEITSE ELQQRLDGVK EQLASQPDLR DGTNYRDSEV PRESSHEDSL LEWLNTFRRT
GNATRSGQNG NQTWRAVSRT NPNNGEFRFS LEIHVNHENR GFEIHGEDYT DIPLSDSNRD
HTANRQQRST SPVARRTRSQ TSVNFNGSSS NIPRTRLASR GQNPAEGSFS TLGRLRNGIG
GAAGIPRANA SRTNFSSYTN QSGGSELRQR EGQRFGAAHV WENGARSNVT VRNTNQRLEP
IRLRSTSNSR SRSPIQRQSG TVYHNSQRES RPVQQTTRRS VRRRGRTRVF LEQDRERERR
GTAYTPFSNS RLVSRITVEE GEESSRSSTA VRRHPTITLD LQVRRIRPGE NRDRDSIANR
TRSRVGLAEN TVTIESNSGG FRRTISRLER SGIRTYVSTI TVPLRRISEN ELVEPSSVAL
RSILRQIMTG FGELSSLMEA DSESELQRNG QHLPDMHSER SNLGTVNNRS QHREGSSQDR
QAQGDSTEMH GENETTQPHT RNSDSRGGRQ LRNPNNLVET GTLPILRLAH FFLLNESDDD
DRIRGLTKEQ IDNLSTRHYE HNSIDSELGK ICSVCISDYV TGNKLRQLPC MHEFHIHCID
RWLSENCTCP ICRQPVLGSN IANSG
//
