Full text data of RNF123
RNF123
(KPC1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
E3 ubiquitin-protein ligase RNF123; 6.3.2.- (Kip1 ubiquitination-promoting complex protein 1; RING finger protein 123)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase RNF123; 6.3.2.- (Kip1 ubiquitination-promoting complex protein 1; RING finger protein 123)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00335085
IPI00335085 SPla/RYanodine receptor SPRY domain containing protein ubiquitin ligase complex, ubiquitin-protein ligase activity, zinc ion binding, protein ubiquitination soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00335085 SPla/RYanodine receptor SPRY domain containing protein ubiquitin ligase complex, ubiquitin-protein ligase activity, zinc ion binding, protein ubiquitination soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q5XPI4
ID RN123_HUMAN Reviewed; 1314 AA.
AC Q5XPI4; A1L4Q3; A6NLS5; Q5I022; Q6PFW4; Q71RH0; Q8IW18; Q9H0M8;
read moreAC Q9H5L8; Q9H9T2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=E3 ubiquitin-protein ligase RNF123;
DE EC=6.3.2.-;
DE AltName: Full=Kip1 ubiquitination-promoting complex protein 1;
DE AltName: Full=RING finger protein 123;
GN Name=RNF123; Synonyms=KPC1; ORFNames=FP1477;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15531880; DOI=10.1038/ncb1194;
RA Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F.,
RA Hatakeyama S., Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1)
RT at G1 phase.";
RL Nat. Cell Biol. 6:1229-1235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP HIS-854.
RC TISSUE=Brain, Eye, Lung, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 545-1314 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 535-1314 (ISOFORMS 1 AND 2),
RP AND VARIANT HIS-854.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 892-1314 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16227581; DOI=10.1128/MCB.25.21.9292-9303.2005;
RA Hara T., Kamura T., Kotoshiba S., Takahashi H., Fujiwara K.,
RA Onoyama I., Shirakawa M., Mizushima N., Nakayama K.;
RT "Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of
RT the cell cycle.";
RL Mol. Cell. Biol. 25:9292-9303(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalytic subunit of the KPC complex that acts as E3
CC ubiquitin-protein ligase. Required for poly-ubiquitination and
CC proteasome-mediated degradation of CDKN1B during G1 phase of the
CC cell cycle.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and
CC UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal
CC domain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XPI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XPI4-2; Sequence=VSP_020650;
CC -!- PTM: Ubiquitinated, leading to its degradation. Deubiquitinated by
CC USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation
CC (By similarity).
CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14139.1; Type=Erroneous initiation;
CC Sequence=BAB15607.1; Type=Erroneous initiation;
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DR EMBL; AY744152; AAU93470.1; -; mRNA.
DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041145; AAH41145.1; -; mRNA.
DR EMBL; BC057392; AAH57392.2; -; mRNA.
DR EMBL; BC088801; AAH88801.1; -; mRNA.
DR EMBL; BC130632; AAI30633.1; -; mRNA.
DR EMBL; AF370367; AAQ15203.1; -; mRNA.
DR EMBL; AK022627; BAB14139.1; ALT_INIT; mRNA.
DR EMBL; AK026968; BAB15607.1; ALT_INIT; mRNA.
DR EMBL; AL136729; CAB66663.2; -; mRNA.
DR RefSeq; NP_071347.2; NM_022064.3.
DR UniGene; Hs.553723; -.
DR PDB; 2MA6; NMR; -; A=1247-1304.
DR PDBsum; 2MA6; -.
DR ProteinModelPortal; Q5XPI4; -.
DR SMR; Q5XPI4; 106-266, 1249-1296.
DR IntAct; Q5XPI4; 8.
DR MINT; MINT-1187266; -.
DR PhosphoSite; Q5XPI4; -.
DR DMDM; 74748090; -.
DR PaxDb; Q5XPI4; -.
DR PRIDE; Q5XPI4; -.
DR DNASU; 63891; -.
DR Ensembl; ENST00000327697; ENSP00000328287; ENSG00000164068.
DR GeneID; 63891; -.
DR KEGG; hsa:63891; -.
DR UCSC; uc003cxh.4; human.
DR CTD; 63891; -.
DR GeneCards; GC03P049726; -.
DR HGNC; HGNC:21148; RNF123.
DR MIM; 614472; gene.
DR neXtProt; NX_Q5XPI4; -.
DR PharmGKB; PA134916827; -.
DR eggNOG; NOG303191; -.
DR HOVERGEN; HBG079909; -.
DR KO; K12169; -.
DR OMA; IVSVEDW; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR GeneWiki; RNF123; -.
DR GenomeRNAi; 63891; -.
DR NextBio; 65568; -.
DR PRO; PR:Q5XPI4; -.
DR ArrayExpress; Q5XPI4; -.
DR Bgee; Q5XPI4; -.
DR CleanEx; HS_RNF123; -.
DR Genevestigator; Q5XPI4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR018355; SPla/RYanodine_receptor_subgr.
DR InterPro; IPR003877; SPRY_rcpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Ligase; Metal-binding; Polymorphism; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1314 E3 ubiquitin-protein ligase RNF123.
FT /FTId=PRO_0000250447.
FT DOMAIN 74 254 B30.2/SPRY.
FT ZN_FING 1254 1292 RING-type.
FT COMPBIAS 1237 1244 Poly-Ala.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1295 1314 IVSVEDWEKGANTSTTSSAA -> TSNLLACLYPHWWEPSH
FT GPNCA (in isoform 2).
FT /FTId=VSP_020650.
FT VARIANT 51 51 P -> R (in dbSNP:rs2960546).
FT /FTId=VAR_027561.
FT VARIANT 387 387 R -> Q (in dbSNP:rs35620248).
FT /FTId=VAR_052106.
FT VARIANT 596 596 K -> E (in dbSNP:rs35726701).
FT /FTId=VAR_052107.
FT VARIANT 854 854 R -> H (in dbSNP:rs34823813).
FT /FTId=VAR_052108.
FT CONFLICT 809 809 K -> R (in Ref. 5; BAB14139).
FT STRAND 1250 1253
FT TURN 1255 1257
FT STRAND 1258 1261
FT STRAND 1264 1267
FT TURN 1268 1270
FT STRAND 1271 1273
FT HELIX 1275 1281
FT TURN 1282 1284
FT STRAND 1296 1300
SQ SEQUENCE 1314 AA; 148515 MW; A0F8F4D68EAFB8E1 CRC64;
MASKGAGMSF SRKSYRLTSD AEKSRVTGIV QEKLLNDYLN RIFSSSEHAP PAATSRKPLN
FQNLPEHLDQ LLQVDNEEEE SQGQVEGRLG PSTVVLDHTG GFEGLLLVDD DLLGVIGHSN
FGTIRSTTCV YKGKWLYEVL ISSQGLMQIG WCTISCRFNQ EEGVGDTHNS YAYDGNRVRK
WNVTTTNYGK AWAAGDIVSC LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS
FKESVAFNFG SRPLRYPVAG YRPLQDPPSA DLVRAQRLLG CFRAVLSVEL DPVEGRLLDK
ESSKWRLRGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGIVEKGT PTQAQSVVHQ
VLDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL QIHYLRLTIA ILRHEKSRKF
LLSNVLFDVL RSVVFFYIKS PLRVEEAGLQ ELIPTTWWPH CSSREGKEST EMKEETAEER
LRRRAYERGC QRLRKRIEVV EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS
GRGNMPMLCP PEYMVCFLHR LISALRYYWD EYKASNPHAS FSEEAYIPPQ VFYNGKVDYF
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQSTAMDD LDEDEEPAPA MAQRPMQALA
VGGPLPLPRP GWLSSPTLGR ANRFLSTAAV SLMTPRRPLS TSEKVKVRTL SVEQRTREDI
EGSHWNEGLL LGRPPEEPEQ PLTENSLLEV LDGAVMMYNL SVHQQLGKMV GVSDDVNEYA
MALRDTEDKL RRCPKRRKDI LAELTKSQKV FSEKLDHLSR RLAWVHATVY SQEKMLDIYW
LLRVCLRTIE HGDRTGSLFA FMPEFYLSVA INSYSALKNY FGPVHSMEEL PGYEETLTRL
AAILAKHFAD ARIVGTDIRD SLMQALASYV CYPHSLRAVE RIPEEQRIAM VRNLLAPYEQ
RPWAQTNWIL VRLWRGCGFG YRYTRLPHLL KTKLEDANLP SLQKPCPSTL LQQHMADLLQ
QGPDVAPSFL NSVLNQLNWA FSEFIGMIQE IQQAAERLER NFVDSRQLKV CATCFDLSVS
LLRVLEMTIT LVPEIFLDWT RPTSEMLLRR LAQLLNQVLN RVTAERNLFD RVVTLRLPGL
ESVDHYPILV AVTGILVQLL VRGPASEREQ ATSVLLADPC FQLRSICYLL GQPEPPAPGT
ALPAPDRKRF SLQSYADYIS ADELAQVEQM LAHLTSASAQ AAAASLPTSE EDLCPICYAH
PISAVFQPCG HKSCKACINQ HLMNNKDCFF CKTTIVSVED WEKGANTSTT SSAA
//
ID RN123_HUMAN Reviewed; 1314 AA.
AC Q5XPI4; A1L4Q3; A6NLS5; Q5I022; Q6PFW4; Q71RH0; Q8IW18; Q9H0M8;
read moreAC Q9H5L8; Q9H9T2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=E3 ubiquitin-protein ligase RNF123;
DE EC=6.3.2.-;
DE AltName: Full=Kip1 ubiquitination-promoting complex protein 1;
DE AltName: Full=RING finger protein 123;
GN Name=RNF123; Synonyms=KPC1; ORFNames=FP1477;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15531880; DOI=10.1038/ncb1194;
RA Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F.,
RA Hatakeyama S., Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1)
RT at G1 phase.";
RL Nat. Cell Biol. 6:1229-1235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP HIS-854.
RC TISSUE=Brain, Eye, Lung, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 545-1314 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 535-1314 (ISOFORMS 1 AND 2),
RP AND VARIANT HIS-854.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 892-1314 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16227581; DOI=10.1128/MCB.25.21.9292-9303.2005;
RA Hara T., Kamura T., Kotoshiba S., Takahashi H., Fujiwara K.,
RA Onoyama I., Shirakawa M., Mizushima N., Nakayama K.;
RT "Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of
RT the cell cycle.";
RL Mol. Cell. Biol. 25:9292-9303(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalytic subunit of the KPC complex that acts as E3
CC ubiquitin-protein ligase. Required for poly-ubiquitination and
CC proteasome-mediated degradation of CDKN1B during G1 phase of the
CC cell cycle.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and
CC UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal
CC domain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XPI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XPI4-2; Sequence=VSP_020650;
CC -!- PTM: Ubiquitinated, leading to its degradation. Deubiquitinated by
CC USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation
CC (By similarity).
CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14139.1; Type=Erroneous initiation;
CC Sequence=BAB15607.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AY744152; AAU93470.1; -; mRNA.
DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041145; AAH41145.1; -; mRNA.
DR EMBL; BC057392; AAH57392.2; -; mRNA.
DR EMBL; BC088801; AAH88801.1; -; mRNA.
DR EMBL; BC130632; AAI30633.1; -; mRNA.
DR EMBL; AF370367; AAQ15203.1; -; mRNA.
DR EMBL; AK022627; BAB14139.1; ALT_INIT; mRNA.
DR EMBL; AK026968; BAB15607.1; ALT_INIT; mRNA.
DR EMBL; AL136729; CAB66663.2; -; mRNA.
DR RefSeq; NP_071347.2; NM_022064.3.
DR UniGene; Hs.553723; -.
DR PDB; 2MA6; NMR; -; A=1247-1304.
DR PDBsum; 2MA6; -.
DR ProteinModelPortal; Q5XPI4; -.
DR SMR; Q5XPI4; 106-266, 1249-1296.
DR IntAct; Q5XPI4; 8.
DR MINT; MINT-1187266; -.
DR PhosphoSite; Q5XPI4; -.
DR DMDM; 74748090; -.
DR PaxDb; Q5XPI4; -.
DR PRIDE; Q5XPI4; -.
DR DNASU; 63891; -.
DR Ensembl; ENST00000327697; ENSP00000328287; ENSG00000164068.
DR GeneID; 63891; -.
DR KEGG; hsa:63891; -.
DR UCSC; uc003cxh.4; human.
DR CTD; 63891; -.
DR GeneCards; GC03P049726; -.
DR HGNC; HGNC:21148; RNF123.
DR MIM; 614472; gene.
DR neXtProt; NX_Q5XPI4; -.
DR PharmGKB; PA134916827; -.
DR eggNOG; NOG303191; -.
DR HOVERGEN; HBG079909; -.
DR KO; K12169; -.
DR OMA; IVSVEDW; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR GeneWiki; RNF123; -.
DR GenomeRNAi; 63891; -.
DR NextBio; 65568; -.
DR PRO; PR:Q5XPI4; -.
DR ArrayExpress; Q5XPI4; -.
DR Bgee; Q5XPI4; -.
DR CleanEx; HS_RNF123; -.
DR Genevestigator; Q5XPI4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR018355; SPla/RYanodine_receptor_subgr.
DR InterPro; IPR003877; SPRY_rcpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Ligase; Metal-binding; Polymorphism; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1314 E3 ubiquitin-protein ligase RNF123.
FT /FTId=PRO_0000250447.
FT DOMAIN 74 254 B30.2/SPRY.
FT ZN_FING 1254 1292 RING-type.
FT COMPBIAS 1237 1244 Poly-Ala.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1295 1314 IVSVEDWEKGANTSTTSSAA -> TSNLLACLYPHWWEPSH
FT GPNCA (in isoform 2).
FT /FTId=VSP_020650.
FT VARIANT 51 51 P -> R (in dbSNP:rs2960546).
FT /FTId=VAR_027561.
FT VARIANT 387 387 R -> Q (in dbSNP:rs35620248).
FT /FTId=VAR_052106.
FT VARIANT 596 596 K -> E (in dbSNP:rs35726701).
FT /FTId=VAR_052107.
FT VARIANT 854 854 R -> H (in dbSNP:rs34823813).
FT /FTId=VAR_052108.
FT CONFLICT 809 809 K -> R (in Ref. 5; BAB14139).
FT STRAND 1250 1253
FT TURN 1255 1257
FT STRAND 1258 1261
FT STRAND 1264 1267
FT TURN 1268 1270
FT STRAND 1271 1273
FT HELIX 1275 1281
FT TURN 1282 1284
FT STRAND 1296 1300
SQ SEQUENCE 1314 AA; 148515 MW; A0F8F4D68EAFB8E1 CRC64;
MASKGAGMSF SRKSYRLTSD AEKSRVTGIV QEKLLNDYLN RIFSSSEHAP PAATSRKPLN
FQNLPEHLDQ LLQVDNEEEE SQGQVEGRLG PSTVVLDHTG GFEGLLLVDD DLLGVIGHSN
FGTIRSTTCV YKGKWLYEVL ISSQGLMQIG WCTISCRFNQ EEGVGDTHNS YAYDGNRVRK
WNVTTTNYGK AWAAGDIVSC LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS
FKESVAFNFG SRPLRYPVAG YRPLQDPPSA DLVRAQRLLG CFRAVLSVEL DPVEGRLLDK
ESSKWRLRGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGIVEKGT PTQAQSVVHQ
VLDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL QIHYLRLTIA ILRHEKSRKF
LLSNVLFDVL RSVVFFYIKS PLRVEEAGLQ ELIPTTWWPH CSSREGKEST EMKEETAEER
LRRRAYERGC QRLRKRIEVV EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS
GRGNMPMLCP PEYMVCFLHR LISALRYYWD EYKASNPHAS FSEEAYIPPQ VFYNGKVDYF
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQSTAMDD LDEDEEPAPA MAQRPMQALA
VGGPLPLPRP GWLSSPTLGR ANRFLSTAAV SLMTPRRPLS TSEKVKVRTL SVEQRTREDI
EGSHWNEGLL LGRPPEEPEQ PLTENSLLEV LDGAVMMYNL SVHQQLGKMV GVSDDVNEYA
MALRDTEDKL RRCPKRRKDI LAELTKSQKV FSEKLDHLSR RLAWVHATVY SQEKMLDIYW
LLRVCLRTIE HGDRTGSLFA FMPEFYLSVA INSYSALKNY FGPVHSMEEL PGYEETLTRL
AAILAKHFAD ARIVGTDIRD SLMQALASYV CYPHSLRAVE RIPEEQRIAM VRNLLAPYEQ
RPWAQTNWIL VRLWRGCGFG YRYTRLPHLL KTKLEDANLP SLQKPCPSTL LQQHMADLLQ
QGPDVAPSFL NSVLNQLNWA FSEFIGMIQE IQQAAERLER NFVDSRQLKV CATCFDLSVS
LLRVLEMTIT LVPEIFLDWT RPTSEMLLRR LAQLLNQVLN RVTAERNLFD RVVTLRLPGL
ESVDHYPILV AVTGILVQLL VRGPASEREQ ATSVLLADPC FQLRSICYLL GQPEPPAPGT
ALPAPDRKRF SLQSYADYIS ADELAQVEQM LAHLTSASAQ AAAASLPTSE EDLCPICYAH
PISAVFQPCG HKSCKACINQ HLMNNKDCFF CKTTIVSVED WEKGANTSTT SSAA
//
MIM
614472
*RECORD*
*FIELD* NO
614472
*FIELD* TI
*614472 RING FINGER PROTEIN 123; RNF123
;;KIP1 UBIQUITINATION-PROMOTING COMPLEX 1; KPC1
read more*FIELD* TX
DESCRIPTION
RNF123 is a cytoplasmic E3 ubiquitin ligase with a role in cell cycle
progression (Kamura et al., 2004).
CLONING
By searching an EST database for sequences similar to rabbit Kpc1,
Kamura et al. (2004) identified human RNF123, which they called KPC1.
The deduced 1,314-amino acid protein has an N-terminal SPRY domain and a
C-terminal RING finger domain. Epitope-tagged KPC1 was expressed as a
cytoplasmic protein in transfected NIH-3T3 cells.
GENE FUNCTION
By immunoprecipitation analysis, Kamura et al. (2004) found that
epitope-tagged KPC1 interacted directly with KPC2 (UBAC1; 608129) and
exhibited pronounced E3 ubiquitin ligase activity toward p27(KIP1)
(CDKN1B; 600778), but not other substrates, in the presence of E1 (UBA1;
314370) and E2 (UBCH5A, or UBE2D1; 602961) enzymes. Both mono- and
polyubiquitinated forms of p27(KIP1) were detected, and
polyubiquitination required either UBC4 (UBE2D2; 602962) or UBCH5A. The
E3 activity of KPC1 toward p27(KIP1) was greater in the absence of PKC2.
Overexpression and knockdown studies with mouse fibroblasts revealed
that the KPC complex functioned in the cytoplasm, ubiquitinated
p27(KIP1) during G1 phase of the cell cycle, and required nuclear export
of p27(KIP1) by Crm1 (XPO1; 602559). Ubiquitination of p27(KIP1) at S
phase was performed by Skp2 (601436). Depletion of endogenous Kpc1 from
Skp2 -/- mouse embryonic fibroblasts resulted in p27(KIP1) accumulation
and a delay in cell cycle progression.
Using rat myoblast and fibroblast cell lines, Lu et al. (2009) showed
that the ubiquitin-specific protease Usp19 (614471) regulated p27(KIP1)
levels by deubiquitinating and stabilizing Kpc1 against proteasomal
degradation. Immunoprecipitation analysis revealed that Usp19 interacted
directly with Kpc1. Knockdown of Usp19 resulted in loss of Kpc1,
accumulation of p27(KIP1), inhibition of cell proliferation, and slower
progression from G0/G1 to S phase.
MAPPING
Hartz (2011) mapped the RPF123 gene to chromosome 3p21.31 based on an
alignment of the RPF123 sequence (GenBank GENBANK AK022627) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/24/2011.
2. Kamura, T.; Hara, T.; Matsumoto, M.; Ishida, N.; Okumura, F.; Hatakeyama,
S.; Yoshida, M.; Nakayama, K.; Nakayama, K. I.: Cytoplasmic ubiquitin
ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nature
Cell Biol. 6: 1229-1235, 2004.
3. Lu, Y.; Adegoke, O. A. J.; Nepveu, A.; Nakayama, K. I.; Bedard,
N.; Cheng, D.; Peng, J.; Wing, S. S.: USP19 deubiquitinating enzyme
supports cell proliferation by stabilizing KPC1, a ubiquitin ligase
for p27(Kip1). Molec. Cell. Biol. 29: 547-558, 2009. Note: Erratum:
Molec. Cell. Biol. 29: 3241 only, 2009.
*FIELD* CD
Patricia A. Hartz: 2/6/2012
*FIELD* ED
terry: 11/28/2012
mgross: 2/6/2012
*RECORD*
*FIELD* NO
614472
*FIELD* TI
*614472 RING FINGER PROTEIN 123; RNF123
;;KIP1 UBIQUITINATION-PROMOTING COMPLEX 1; KPC1
read more*FIELD* TX
DESCRIPTION
RNF123 is a cytoplasmic E3 ubiquitin ligase with a role in cell cycle
progression (Kamura et al., 2004).
CLONING
By searching an EST database for sequences similar to rabbit Kpc1,
Kamura et al. (2004) identified human RNF123, which they called KPC1.
The deduced 1,314-amino acid protein has an N-terminal SPRY domain and a
C-terminal RING finger domain. Epitope-tagged KPC1 was expressed as a
cytoplasmic protein in transfected NIH-3T3 cells.
GENE FUNCTION
By immunoprecipitation analysis, Kamura et al. (2004) found that
epitope-tagged KPC1 interacted directly with KPC2 (UBAC1; 608129) and
exhibited pronounced E3 ubiquitin ligase activity toward p27(KIP1)
(CDKN1B; 600778), but not other substrates, in the presence of E1 (UBA1;
314370) and E2 (UBCH5A, or UBE2D1; 602961) enzymes. Both mono- and
polyubiquitinated forms of p27(KIP1) were detected, and
polyubiquitination required either UBC4 (UBE2D2; 602962) or UBCH5A. The
E3 activity of KPC1 toward p27(KIP1) was greater in the absence of PKC2.
Overexpression and knockdown studies with mouse fibroblasts revealed
that the KPC complex functioned in the cytoplasm, ubiquitinated
p27(KIP1) during G1 phase of the cell cycle, and required nuclear export
of p27(KIP1) by Crm1 (XPO1; 602559). Ubiquitination of p27(KIP1) at S
phase was performed by Skp2 (601436). Depletion of endogenous Kpc1 from
Skp2 -/- mouse embryonic fibroblasts resulted in p27(KIP1) accumulation
and a delay in cell cycle progression.
Using rat myoblast and fibroblast cell lines, Lu et al. (2009) showed
that the ubiquitin-specific protease Usp19 (614471) regulated p27(KIP1)
levels by deubiquitinating and stabilizing Kpc1 against proteasomal
degradation. Immunoprecipitation analysis revealed that Usp19 interacted
directly with Kpc1. Knockdown of Usp19 resulted in loss of Kpc1,
accumulation of p27(KIP1), inhibition of cell proliferation, and slower
progression from G0/G1 to S phase.
MAPPING
Hartz (2011) mapped the RPF123 gene to chromosome 3p21.31 based on an
alignment of the RPF123 sequence (GenBank GENBANK AK022627) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/24/2011.
2. Kamura, T.; Hara, T.; Matsumoto, M.; Ishida, N.; Okumura, F.; Hatakeyama,
S.; Yoshida, M.; Nakayama, K.; Nakayama, K. I.: Cytoplasmic ubiquitin
ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nature
Cell Biol. 6: 1229-1235, 2004.
3. Lu, Y.; Adegoke, O. A. J.; Nepveu, A.; Nakayama, K. I.; Bedard,
N.; Cheng, D.; Peng, J.; Wing, S. S.: USP19 deubiquitinating enzyme
supports cell proliferation by stabilizing KPC1, a ubiquitin ligase
for p27(Kip1). Molec. Cell. Biol. 29: 547-558, 2009. Note: Erratum:
Molec. Cell. Biol. 29: 3241 only, 2009.
*FIELD* CD
Patricia A. Hartz: 2/6/2012
*FIELD* ED
terry: 11/28/2012
mgross: 2/6/2012