RN157_HUMAN
ID RN157_HUMAN Reviewed; 679 AA.
AC Q96PX1; Q8NB72; Q96N56;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin ligase RNF157 {ECO:0000303|PubMed:25342469};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25342469};
DE AltName: Full=RING finger protein 157;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF157 {ECO:0000305};
GN Name=RNF157; Synonyms=KIAA1917;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-679 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-679 (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH APBB1.
RX PubMed=25342469; DOI=10.1038/cdd.2014.163;
RA Matz A., Lee S.J., Schwedhelm-Domeyer N., Zanini D., Holubowska A.,
RA Kannan M., Farnworth M., Jahn O., Goepfert M.C., Stegmueller J.;
RT "Regulation of neuronal survival and morphology by the E3 ubiquitin ligase
RT RNF157.";
RL Cell Death Differ. 22:626-642(2015).
RN [6]
RP FUNCTION, INDUCTION, DOMAIN, INTERACTION WITH ATRN; MEGF8; TECR; MSI2;
RP PLRG1; BYSL; MTERF3; PSMA1; MRPS18B; PRPF4; FASTKD2; SLC25A1; SMU1; CNOT9;
RP MRPS2; MAGT1; CHD1; FXR2; EMD; PSMD8; HDAC1; RAN; HSD17B12; TXNDC5 AND
RP MRPL19, AND PHOSPHORYLATION AT SER-660; SER-661; SER-662 AND SER-663.
RX PubMed=28655764; DOI=10.1074/jbc.m117.792754;
RA Dogan T., Gnad F., Chan J., Phu L., Young A., Chen M.J., Doll S.,
RA Stokes M.P., Belvin M., Friedman L.S., Kirkpatrick D.S., Hoeflich K.P.,
RA Hatzivassiliou G.;
RT "Role of the E3 ubiquitin ligase RNF157 as a novel downstream effector
RT linking PI3K and MAPK signaling pathways to the cell cycle.";
RL J. Biol. Chem. 292:14311-14324(2017).
CC -!- FUNCTION: E3 ubiquitin ligase that ubiquitinates APBB1 for its
CC degradation by the proteasome and thus prevents apoptosis and promotes
CC survival of neurons (PubMed:25342469). Has a dual role in neurons as it
CC is also required for dendrite growth and maintenance for which its
CC ligase activity is not critical (PubMed:25342469). May act as a
CC scaffold molecule to regulate this process (PubMed:25342469). Acts as a
CC downstream effector of the interconnected PI3K and MAPK signaling
CC pathways and thus participates in the regulation of the cell cycle
CC (PubMed:28655764). {ECO:0000269|PubMed:25342469,
CC ECO:0000269|PubMed:28655764}.
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:25342469};
CC -!- SUBUNIT: Interacts with APBB1 (PubMed:25342469). Interacts with CHD1;
CC CHD1-binding controls RNF157 stability (PubMed:28655764). Interacts
CC with ATRN, MEGF8, TECR, MSI2, PLRG1, BYSL, MTERF3, PSMA1, MRPS18B,
CC PRPF4, FASTKD2, SLC25A1, SMU1, CNOT9, MRPS2, MAGT1, FXR2, EMD, PSMD8,
CC HDAC1, RAN, HSD17B12, TXNDC5 AND MRPL19 (PubMed:28655764).
CC {ECO:0000269|PubMed:25342469, ECO:0000269|PubMed:28655764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:M0R5D6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96PX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PX1-2; Sequence=VSP_021735;
CC -!- INDUCTION: Expression is cell cycle-specific with higher levels in
CC cells arrested in G1/S and G2/M (PubMed:28655764).
CC {ECO:0000269|PubMed:28655764}.
CC -!- DOMAIN: The D-box motifs play a key role in RNF157 stabilization
CC (PubMed:28655764). {ECO:0000269|PubMed:28655764}.
CC -!- PTM: Phosphorylation at Ser-660, Ser-661, Ser-662 and Ser-663
CC downstream of the PI3K and MAPK pathways influences the E3 ligase
CC activity and stability of RNF157 during the cell cycle in an anaphase-
CC promoting complex/cyclosome-CDH1-dependent manner (PubMed:28655764).
CC {ECO:0000269|PubMed:28655764}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67810.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB71053.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03669.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB067504; BAB67810.2; ALT_INIT; mRNA.
DR EMBL; AK055949; BAB71053.1; ALT_INIT; mRNA.
DR EMBL; AK091467; BAC03669.1; ALT_INIT; mRNA.
DR CCDS; CCDS32740.1; -. [Q96PX1-1]
DR CCDS; CCDS82208.1; -. [Q96PX1-2]
DR RefSeq; NP_001317430.1; NM_001330501.1. [Q96PX1-2]
DR RefSeq; NP_443148.1; NM_052916.2. [Q96PX1-1]
DR AlphaFoldDB; Q96PX1; -.
DR BioGRID; 125364; 44.
DR ELM; Q96PX1; -.
DR IntAct; Q96PX1; 1.
DR STRING; 9606.ENSP00000269391; -.
DR iPTMnet; Q96PX1; -.
DR PhosphoSitePlus; Q96PX1; -.
DR BioMuta; RNF157; -.
DR DMDM; 118573798; -.
DR jPOST; Q96PX1; -.
DR MassIVE; Q96PX1; -.
DR MaxQB; Q96PX1; -.
DR PaxDb; Q96PX1; -.
DR PeptideAtlas; Q96PX1; -.
DR PRIDE; Q96PX1; -.
DR ProteomicsDB; 77780; -. [Q96PX1-1]
DR ProteomicsDB; 77781; -. [Q96PX1-2]
DR Antibodypedia; 32383; 119 antibodies from 16 providers.
DR DNASU; 114804; -.
DR Ensembl; ENST00000269391.11; ENSP00000269391.4; ENSG00000141576.16. [Q96PX1-1]
DR Ensembl; ENST00000319945.10; ENSP00000321837.4; ENSG00000141576.16. [Q96PX1-2]
DR GeneID; 114804; -.
DR KEGG; hsa:114804; -.
DR MANE-Select; ENST00000269391.11; ENSP00000269391.4; NM_052916.3; NP_443148.1.
DR UCSC; uc002jqz.4; human. [Q96PX1-1]
DR CTD; 114804; -.
DR DisGeNET; 114804; -.
DR GeneCards; RNF157; -.
DR HGNC; HGNC:29402; RNF157.
DR HPA; ENSG00000141576; Group enriched (brain, retina, skeletal muscle, testis, tongue).
DR neXtProt; NX_Q96PX1; -.
DR OpenTargets; ENSG00000141576; -.
DR PharmGKB; PA134974884; -.
DR VEuPathDB; HostDB:ENSG00000141576; -.
DR eggNOG; KOG4265; Eukaryota.
DR GeneTree; ENSGT00390000009925; -.
DR HOGENOM; CLU_016631_2_0_1; -.
DR InParanoid; Q96PX1; -.
DR OrthoDB; 883624at2759; -.
DR PhylomeDB; Q96PX1; -.
DR TreeFam; TF314969; -.
DR PathwayCommons; Q96PX1; -.
DR SignaLink; Q96PX1; -.
DR BioGRID-ORCS; 114804; 12 hits in 1108 CRISPR screens.
DR ChiTaRS; RNF157; human.
DR GenomeRNAi; 114804; -.
DR Pharos; Q96PX1; Tbio.
DR PRO; PR:Q96PX1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96PX1; protein.
DR Bgee; ENSG00000141576; Expressed in lateral nuclear group of thalamus and 132 other tissues.
DR ExpressionAtlas; Q96PX1; baseline and differential.
DR Genevisible; Q96PX1; HS.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1_like---blasttree; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR045195; MGRN1/RNF157_mRING_C3HC5.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; PTHR22996; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lipoprotein; Metal-binding; Myristate;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..679
FT /note="E3 ubiquitin ligase RNF157"
FT /id="PRO_0000261614"
FT ZN_FING 277..316
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 339..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 329..332
FT /note="D-box 1"
FT /evidence="ECO:0000303|PubMed:28655764"
FT MOTIF 656..659
FT /note="D-box 2"
FT /evidence="ECO:0000303|PubMed:28655764"
FT COMPBIAS 339..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28655764"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28655764"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28655764"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28655764"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681"
FT VAR_SEQ 568..589
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021735"
FT VARIANT 80
FT /note="P -> H (in dbSNP:rs2289602)"
FT /id="VAR_029458"
FT VARIANT 208
FT /note="G -> R (in dbSNP:rs11539879)"
FT /id="VAR_029459"
FT VARIANT 596
FT /note="E -> V (in dbSNP:rs59053255)"
FT /id="VAR_061817"
SQ SEQUENCE 679 AA; 73579 MW; 44CE214D4CB7620D CRC64;
MGALTSRQHA GVEEVDIPSN SVYRYPPKSG SYFASHFIMG GEKFDSTHPE GYLFGENSDL
NFLGNRPVVF PYAAPPPQEP VKTLRSLVNI RKDTLRLVKC AEEVKSPGEE ASKAKVHYNV
EFTFDTDARV AITIYYQATE EFQNGIASYI PKDNSLQSET VQYKRGVCQQ FCLPSHTVDP
SEWAEEELGF DLDREVYPLV VHAVVDEGDE YFGHCHVLLG TFEKHTDGTF CVKPLKQKQV
VDGVSYLLQE IYGIENKYNT QDSKVAEDEV SDNSAECVVC LSDVRDTLIL PCRHLCLCNT
CADTLRYQAN NCPICRLPFR ALLQIRAMRK KLGPLSPTSF NPIISSQTSD SEEHPSSENI
PPGYEVVSLL EALNGPLTPS PAVPPLHVLG DGHLSGMLPS YGSDGHLPPV RTISPLDRLS
DSSSQGLKLK KSLSKSTSQN SSVLHEEEDE HSCSESETQL SQRPSVQHLG EECGVTPESE
NLTLSSSGAI DQSSCTGTPL SSTISSPEGP ASSSLAQSVM SMASSQISTD TVSSMSGSYI
APGTEEEGEA LSSPQPASRA PSEEGEGLPA ESPDSNFAGL PAGEQDAEGN DVIEEEDGSP
TQEGQRTCAF LGMECDNNND FDIASVKALD NKLCSEVCLP GAWQADDNAV SRNAQRRRLS
SSSLEDSETR PCVWGPLAV
