位置:首页 > 蛋白库 > RN157_HUMAN
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024