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   27-MAR-2024, entry version 163.
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; 36.
DR   IntAct; Q96MT1; 1.
DR   MINT; Q96MT1; -.
DR   STRING; 9606.ENSP00000430955; -.
DR   iPTMnet; Q96MT1; -.
DR   PhosphoSitePlus; Q96MT1; -.
DR   SwissPalm; Q96MT1; -.
DR   BioMuta; RNF145; -.
DR   DMDM; 152060502; -.
DR   EPD; Q96MT1; -.
DR   MassIVE; Q96MT1; -.
DR   MaxQB; Q96MT1; -.
DR   PaxDb; 9606-ENSP00000430955; -.
DR   PeptideAtlas; 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; 93 antibodies from 18 providers.
DR   DNASU; 153830; -.
DR   Ensembl; ENST00000274542.6; ENSP00000274542.2; ENSG00000145860.13. [Q96MT1-2]
DR   Ensembl; ENST00000424310.7; ENSP00000409064.2; ENSG00000145860.13. [Q96MT1-1]
DR   Ensembl; ENST00000518802.5; ENSP00000430955.1; ENSG00000145860.13. [Q96MT1-5]
DR   Ensembl; ENST00000519865.5; ENSP00000430397.1; ENSG00000145860.13. [Q96MT1-1]
DR   Ensembl; ENST00000520638.1; ENSP00000429071.1; ENSG00000145860.13. [Q96MT1-4]
DR   Ensembl; ENST00000521606.6; ENSP00000430753.2; ENSG00000145860.13. [Q96MT1-3]
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   AGR; HGNC:20853; -.
DR   CTD; 153830; -.
DR   DisGeNET; 153830; -.
DR   GeneCards; RNF145; -.
DR   HGNC; HGNC:20853; RNF145.
DR   HPA; ENSG00000145860; Low tissue specificity.
DR   MIM; 620640; gene.
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   OrthoDB; 2912447at2759; -.
DR   PhylomeDB; Q96MT1; -.
DR   TreeFam; TF318635; -.
DR   PathwayCommons; Q96MT1; -.
DR   SignaLink; Q96MT1; -.
DR   SIGNOR; Q96MT1; -.
DR   BioGRID-ORCS; 153830; 45 hits in 1193 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 186 other cell types or tissues.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16684; RING-H2_RNF145; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047823; RNF145_RING-H2.
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   PANTHER; PTHR22763:SF167; RING FINGER PROTEIN 145; 1.
DR   PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR   Pfam; PF13705; TRC8_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q96MT1; HS.
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
//