RN145_HUMAN
ID RN145_HUMAN Reviewed; 663 AA.
AC Q96MT1; B7Z903; B7Z949; E7EVI7; Q8IVP7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=RING finger protein 145 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5SWK7};
GN Name=RNF145 {ECO:0000312|PROSITE:PS50089};
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 [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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).
CC -!- FUNCTION: E3 ubiquitin ligase that catalyzes the direct transfer of
CC ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate.
CC In response to bacterial infection, negatively regulates the phagocyte
CC oxidative burst by controlling the turnover of the NADPH oxidase
CC complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-
CC linked polyubiquitination and degradation of CYBB NADPH oxidase
CC catalytic subunits, both essential for the generation of antimicrobial
CC reactive oxygen species. Involved in the maintenance of cholesterol
CC homeostasis. In response to high sterol concentrations ubiquitinates
CC HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets
CC it for degradation. The interaction with INSIG1 is required for this
CC function. In addition, triggers ubiquitination of SCAP, likely
CC inhibiting its transport to the Golgi apparatus and the subsequent
CC processing/maturation of SREBPF2, ultimately down-regulating
CC cholesterol biosynthesis. {ECO:0000250|UniProtKB:Q5SWK7}.
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:0000250|UniProtKB:Q5SWK7};
CC -!- SUBUNIT: Interacts (via YLYF motif) with INSIG1 and INSIG2.
CC {ECO:0000250|UniProtKB:Q5SWK7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5SWK7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96MT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MT1-2; Sequence=VSP_037501;
CC Name=3;
CC IsoId=Q96MT1-3; Sequence=VSP_043661;
CC Name=4;
CC IsoId=Q96MT1-4; Sequence=VSP_043662;
CC Name=5;
CC IsoId=Q96MT1-5; Sequence=VSP_044539;
CC -!- SEQUENCE CAUTION:
CC Sequence=AK308394; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK056513; BAB71200.1; -; mRNA.
DR EMBL; AK304228; BAH14139.1; -; mRNA.
DR EMBL; AK304435; BAH14185.1; -; mRNA.
DR EMBL; AK308394; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC134043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042684; AAH42684.1; -; mRNA.
DR CCDS; CCDS4344.1; -. [Q96MT1-2]
DR CCDS; CCDS56390.1; -. [Q96MT1-1]
DR CCDS; CCDS56391.1; -. [Q96MT1-4]
DR CCDS; CCDS56392.1; -. [Q96MT1-3]
DR CCDS; CCDS56393.1; -. [Q96MT1-5]
DR RefSeq; NP_001186309.1; NM_001199380.1. [Q96MT1-5]
DR RefSeq; NP_001186310.1; NM_001199381.1. [Q96MT1-3]
DR RefSeq; NP_001186311.1; NM_001199382.1. [Q96MT1-4]
DR RefSeq; NP_001186312.1; NM_001199383.1. [Q96MT1-1]
DR RefSeq; NP_653327.1; NM_144726.2. [Q96MT1-2]
DR RefSeq; XP_016864627.1; XM_017009138.1. [Q96MT1-1]
DR AlphaFoldDB; Q96MT1; -.
DR SMR; Q96MT1; -.
DR BioGRID; 127521; 35.
DR IntAct; Q96MT1; 1.
DR STRING; 9606.ENSP00000430955; -.
DR iPTMnet; Q96MT1; -.
DR PhosphoSitePlus; Q96MT1; -.
DR BioMuta; RNF145; -.
DR DMDM; 152060502; -.
DR EPD; Q96MT1; -.
DR MassIVE; Q96MT1; -.
DR MaxQB; Q96MT1; -.
DR PaxDb; Q96MT1; -.
DR PeptideAtlas; Q96MT1; -.
DR PRIDE; Q96MT1; -.
DR ProteomicsDB; 18647; -.
DR ProteomicsDB; 77398; -. [Q96MT1-1]
DR ProteomicsDB; 77399; -. [Q96MT1-2]
DR ProteomicsDB; 77400; -. [Q96MT1-3]
DR ProteomicsDB; 77401; -. [Q96MT1-4]
DR Antibodypedia; 28490; 88 antibodies from 17 providers.
DR DNASU; 153830; -.
DR Ensembl; ENST00000274542.6; ENSP00000274542.2; ENSG00000145860.12. [Q96MT1-2]
DR Ensembl; ENST00000424310.7; ENSP00000409064.2; ENSG00000145860.12. [Q96MT1-1]
DR Ensembl; ENST00000518802.5; ENSP00000430955.1; ENSG00000145860.12. [Q96MT1-5]
DR Ensembl; ENST00000519865.5; ENSP00000430397.1; ENSG00000145860.12. [Q96MT1-1]
DR Ensembl; ENST00000520638.1; ENSP00000429071.1; ENSG00000145860.12. [Q96MT1-4]
DR Ensembl; ENST00000521606.6; ENSP00000430753.2; ENSG00000145860.12. [Q96MT1-3]
DR Ensembl; ENST00000611185.4; ENSP00000482720.1; ENSG00000145860.12. [Q96MT1-1]
DR GeneID; 153830; -.
DR KEGG; hsa:153830; -.
DR MANE-Select; ENST00000424310.7; ENSP00000409064.2; NM_001199383.2; NP_001186312.1.
DR UCSC; uc003lxo.2; human. [Q96MT1-1]
DR CTD; 153830; -.
DR DisGeNET; 153830; -.
DR GeneCards; RNF145; -.
DR HGNC; HGNC:20853; RNF145.
DR HPA; ENSG00000145860; Low tissue specificity.
DR neXtProt; NX_Q96MT1; -.
DR OpenTargets; ENSG00000145860; -.
DR PharmGKB; PA134876286; -.
DR VEuPathDB; HostDB:ENSG00000145860; -.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00940000157281; -.
DR HOGENOM; CLU_016467_1_0_1; -.
DR InParanoid; Q96MT1; -.
DR PhylomeDB; Q96MT1; -.
DR TreeFam; TF318635; -.
DR PathwayCommons; Q96MT1; -.
DR SignaLink; Q96MT1; -.
DR BioGRID-ORCS; 153830; 44 hits in 1117 CRISPR screens.
DR ChiTaRS; RNF145; human.
DR GenomeRNAi; 153830; -.
DR Pharos; Q96MT1; Tbio.
DR PRO; PR:Q96MT1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96MT1; protein.
DR Bgee; ENSG00000145860; Expressed in nasal cavity epithelium and 184 other tissues.
DR Genevisible; Q96MT1; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025754; TRC8_N_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13705; TRC8_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..663
FT /note="RING finger protein 145"
FT /id="PRO_0000294024"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 537..575
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 607..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..84
FT /note="YLYF motif"
FT /evidence="ECO:0000250|UniProtKB:Q5SWK7"
FT COMPBIAS 628..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 537
FT /evidence="ECO:0000250|UniProtKB:Q5SWK7"
FT VAR_SEQ 1
FT /note="M -> MMRNHRIASSLCGDQVFSKKKKKKKKNNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037501"
FT VAR_SEQ 1
FT /note="M -> MAEVVFSKKKKKKKKNNM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043661"
FT VAR_SEQ 1
FT /note="M -> MVFSKKKKKKKKNNM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043662"
FT VAR_SEQ 1
FT /note="M -> MHRDRISPSNSPTWSLQVFSKKKKKKKKNNM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044539"
FT CONFLICT 9
FT /note="A -> V (in Ref. 3; AAH42684)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="V -> A (in Ref. 3; AAH42684)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="R -> W (in Ref. 1; AK308394)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="A -> V (in Ref. 3; AAH42684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 75617 MW; EAE984696500ABD3 CRC64;
MAAKEKLEAV LNVALRVPSI MLLDVLYRWD VSSFFQQIQR SSLSNNPLFQ YKYLALNMHY
VGYILSVVLL TLPRQHLVQL YLYFLTALLL YAGHQISRDY VRSELEFAYE GPMYLEPLSM
NRFTTALIGQ LVVCTLCSCV MKTKQIWLFS AHMLPLLARL CLVPLETIVI INKFAMIFTG
LEVLYFLGSN LLVPYNLAKS AYRELVQVVE VYGLLALGMS LWNQLVVPVL FMVFWLVLFA
LQIYSYFSTR DQPASRERLL FLFLTSIAEC CSTPYSLLGL VFTVSFVALG VLTLCKFYLQ
GYRAFMNDPA MNRGMTEGVT LLILAVQTGL IELQVVHRAF LLSIILFIVV ASILQSMLEI
ADPIVLALGA SRDKSLWKHF RAVSLCLFLL VFPAYMAYMI CQFFHMDFWL LIIISSSILT
SLQVLGTLFI YVLFMVEEFR KEPVENMDDV IYYVNGTYRL LEFLVALCVV AYGVSETIFG
EWTVMGSMII FIHSYYNVWL RAQLGWKSFL LRRDAVNKIK SLPIATKEQL EKHNDICAIC
YQDMKSAVIT PCSHFFHAGC LKKWLYVQET CPLCHCHLKN SSQLPGLGTE PVLQPHAGAE
QNVMFQEGTE PPGQEHTPGT RIQEGSRDNN EYIARRPDNQ EGAFDPKEYP HSAKDEAHPV
ESA
