GOLI_HUMAN
ID GOLI_HUMAN Reviewed; 419 AA.
AC Q86XS8; J3KN31; Q32P32; Q59EL1; Q641P9; Q6P177; Q7L2U2; Q9P0J9;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=E3 ubiquitin-protein ligase RNF130;
DE EC=2.3.2.27 {ECO:0000269|PubMed:16549277};
DE AltName: Full=Goliath homolog;
DE Short=H-Goliath;
DE AltName: Full=RING finger protein 130;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF130 {ECO:0000305};
DE Flags: Precursor;
GN Name=RNF130 {ECO:0000312|EMBL:AAH17100.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=13679316; DOI=10.1095/biolreprod.103.018820;
RA Guais A., Solhonne B., Melaine N., Guellaeen G., Bulle F.;
RT "Goliath, a ring-H2 mitochondrial protein, regulated by luteinizing
RT hormone/human chorionic gonadotropin in rat Leydig cells.";
RL Biol. Reprod. 70:204-213(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, Lung {ECO:0000312|EMBL:AAH17100.2},
RC Mammary gland {ECO:0000312|EMBL:AAH82267.1}, and
RC Skin {ECO:0000312|EMBL:AAH65244.1};
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-419 (ISOFORM 1).
RC TISSUE=Adrenal gland {ECO:0000312|EMBL:AAF67007.1};
RA Gu J., Fu S., Ren S., Jin W., Gu Y., Huang Q., Dong H., Yu Y., Fu G.,
RA Wang Y., Chen Z., Han Z.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND LACK OF GLYCOSYLATION.
RX PubMed=16549277; DOI=10.1016/j.gene.2006.01.028;
RA Guais A., Siegrist S., Solhonne B., Jouault H., Guellaen G., Bulle F.;
RT "h-Goliath, paralog of GRAIL, is a new E3 ligase protein, expressed in
RT human leukocytes.";
RL Gene 374:112-120(2006).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-40.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: May have a role during the programmed cell death of
CC hematopoietic cells (By similarity). Acts as an E3 ubiquitin-protein
CC ligase. {ECO:0000250, ECO:0000269|PubMed:16549277}.
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:0000269|PubMed:16549277};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:16549277}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:16549277}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86XS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XS8-2; Sequence=VSP_055642, VSP_055643;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC leukocytes. Not expressed in erythroblasts.
CC {ECO:0000269|PubMed:16549277}.
CC -!- PTM: In vivo measurements suggest this protein is glycosylated
CC (PubMed:19159218). In contrast, in vitro experiments failed to detect
CC glycosylation (PubMed:16549277). {ECO:0000269|PubMed:16549277,
CC ECO:0000269|PubMed:19159218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67007.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD93037.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY083998; AAM08686.1; -; mRNA.
DR EMBL; AB209800; BAD93037.1; ALT_INIT; mRNA.
DR EMBL; AC010285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53773.1; -; Genomic_DNA.
DR EMBL; BC017100; AAH17100.2; -; mRNA.
DR EMBL; BC065244; AAH65244.1; -; mRNA.
DR EMBL; BC082267; AAH82267.1; -; mRNA.
DR EMBL; BC108306; AAI08307.1; -; mRNA.
DR EMBL; AF155650; AAF67007.1; ALT_FRAME; mRNA.
DR CCDS; CCDS4451.1; -. [Q86XS8-1]
DR CCDS; CCDS64340.1; -. [Q86XS8-2]
DR RefSeq; NP_001267730.1; NM_001280801.1. [Q86XS8-2]
DR RefSeq; NP_060904.2; NM_018434.5. [Q86XS8-1]
DR AlphaFoldDB; Q86XS8; -.
DR SMR; Q86XS8; -.
DR BioGRID; 120928; 43.
DR IntAct; Q86XS8; 29.
DR MINT; Q86XS8; -.
DR STRING; 9606.ENSP00000430237; -.
DR GlyGen; Q86XS8; 6 sites.
DR iPTMnet; Q86XS8; -.
DR PhosphoSitePlus; Q86XS8; -.
DR BioMuta; RNF130; -.
DR DMDM; 56749089; -.
DR EPD; Q86XS8; -.
DR jPOST; Q86XS8; -.
DR MassIVE; Q86XS8; -.
DR MaxQB; Q86XS8; -.
DR PaxDb; Q86XS8; -.
DR PeptideAtlas; Q86XS8; -.
DR PRIDE; Q86XS8; -.
DR ProteomicsDB; 70329; -. [Q86XS8-1]
DR Antibodypedia; 2993; 114 antibodies from 24 providers.
DR DNASU; 55819; -.
DR Ensembl; ENST00000261947.4; ENSP00000261947.4; ENSG00000113269.14. [Q86XS8-2]
DR Ensembl; ENST00000521389.6; ENSP00000430237.1; ENSG00000113269.14. [Q86XS8-1]
DR GeneID; 55819; -.
DR KEGG; hsa:55819; -.
DR MANE-Select; ENST00000521389.6; ENSP00000430237.1; NM_018434.6; NP_060904.2.
DR UCSC; uc003mll.2; human. [Q86XS8-1]
DR CTD; 55819; -.
DR DisGeNET; 55819; -.
DR GeneCards; RNF130; -.
DR HGNC; HGNC:18280; RNF130.
DR HPA; ENSG00000113269; Low tissue specificity.
DR MIM; 619163; gene.
DR neXtProt; NX_Q86XS8; -.
DR OpenTargets; ENSG00000113269; -.
DR PharmGKB; PA134871556; -.
DR VEuPathDB; HostDB:ENSG00000113269; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000157465; -.
DR HOGENOM; CLU_049885_2_1_1; -.
DR InParanoid; Q86XS8; -.
DR OMA; NADEAEW; -.
DR PhylomeDB; Q86XS8; -.
DR TreeFam; TF317486; -.
DR PathwayCommons; Q86XS8; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q86XS8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55819; 11 hits in 1125 CRISPR screens.
DR ChiTaRS; RNF130; human.
DR GenomeRNAi; 55819; -.
DR Pharos; Q86XS8; Tdark.
DR PRO; PR:Q86XS8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86XS8; protein.
DR Bgee; ENSG00000113269; Expressed in monocyte and 198 other tissues.
DR ExpressionAtlas; Q86XS8; baseline and differential.
DR Genevisible; Q86XS8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0012501; P:programmed cell death; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..419
FT /note="E3 ubiquitin-protein ligase RNF130"
FT /id="PRO_0000030718"
FT TOPO_DOM 28..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 105..176
FT /note="PA"
FT ZN_FING 264..305
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 384
FT /note="K -> R (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055642"
FT VAR_SEQ 385..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055643"
FT CONFLICT 114
FT /note="T -> A (in Ref. 5; AAH65244)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="N -> T (in Ref. 6; AAF67007)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="P -> N (in Ref. 5; AAH82267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46405 MW; 74E8D987334F3B8E CRC64;
MSCAGRAGPA RLAALALLTC SLWPARADNA SQEYYTALIN VTVQEPGRGA PLTFRIDRGR
YGLDSPKAEV RGQVLAPLPL HGVADHLGCD PQTRFFVPPN IKQWIALLQR GNCTFKEKIS
RAAFHNAVAV VIYNNKSKEE PVTMTHPGTG DIIAVMITEL RGKDILSYLE KNISVQMTIA
VGTRMPPKNF SRGSLVFVSI SFIVLMIISS AWLIFYFIQK IRYTNARDRN QRRLGDAAKK
AISKLTTRTV KKGDKETDPD FDHCAVCIES YKQNDVVRIL PCKHVFHKSC VDPWLSEHCT
CPMCKLNILK ALGIVPNLPC TDNVAFDMER LTRTQAVNRR SALGDLAGDN SLGLEPLRTS
GISPLPQDGE LTPRTGEINI AVTKEWFIIA SFGLLSALTL CYMIIRATAS LNANEVEWF
