Full text data of KCMF1
KCMF1
(FIGC, ZZZ1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
E3 ubiquitin-protein ligase KCMF1; 6.3.2.- (FGF-induced in gastric cancer; Potassium channel modulatory factor; PCMF; ZZ-type zinc finger-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase KCMF1; 6.3.2.- (FGF-induced in gastric cancer; Potassium channel modulatory factor; PCMF; ZZ-type zinc finger-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9P0J7
ID KCMF1_HUMAN Reviewed; 381 AA.
AC Q9P0J7; Q4ZG04; Q53SC7; Q9BWK2; Q9H8P5; Q9UFE8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=E3 ubiquitin-protein ligase KCMF1;
DE EC=6.3.2.-;
DE AltName: Full=FGF-induced in gastric cancer;
DE AltName: Full=Potassium channel modulatory factor;
DE Short=PCMF;
DE AltName: Full=ZZ-type zinc finger-containing protein 1;
GN Name=KCMF1; Synonyms=FIGC, ZZZ1;
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], FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=15581609; DOI=10.1016/j.febslet.2004.10.071;
RA Jang J.-H.;
RT "FIGC, a novel FGF-induced ubiquitin-protein ligase in gastric
RT cancers.";
RL FEBS Lett. 578:21-25(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Ren S., Li Y., Huang C., Jiang C., Gu W., Zhou J., Yu Y., Xu S.,
RA Wang Y., Fu G., Chen Z., Han Z.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-381.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-212, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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).
CC -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC ubiquitination.
CC -!- TISSUE SPECIFICITY: Spleen, small intestine, ovary, peripheral
CC blood, lung, kidney and pancreas. Expressed at low levels in the
CC thymus, prostate, testis, colon, heart, brain, placenta and liver.
CC -!- INDUCTION: Up-regulated by FGF2 in gastric cancer cells.
CC -!- SIMILARITY: Belongs to the KCMF1 family.
CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX88897.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KCMF1ID46364ch2p11.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB083199; BAC43745.1; -; mRNA.
DR EMBL; AF155652; AAF67009.1; -; mRNA.
DR EMBL; AK023403; BAB14563.1; -; mRNA.
DR EMBL; AK314761; BAG37299.1; -; mRNA.
DR EMBL; AC022210; AAY24192.1; -; Genomic_DNA.
DR EMBL; AC078974; AAX88897.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC000178; AAH00178.1; -; mRNA.
DR EMBL; AL122115; CAB59274.1; -; mRNA.
DR PIR; T34540; T34540.
DR RefSeq; NP_064507.3; NM_020122.4.
DR UniGene; Hs.654968; -.
DR ProteinModelPortal; Q9P0J7; -.
DR SMR; Q9P0J7; 2-58.
DR DIP; DIP-47300N; -.
DR STRING; 9606.ENSP00000386738; -.
DR DMDM; 205815553; -.
DR PaxDb; Q9P0J7; -.
DR PRIDE; Q9P0J7; -.
DR DNASU; 56888; -.
DR Ensembl; ENST00000409785; ENSP00000386738; ENSG00000176407.
DR GeneID; 56888; -.
DR KEGG; hsa:56888; -.
DR UCSC; uc002sox.4; human.
DR CTD; 56888; -.
DR GeneCards; GC02P085198; -.
DR H-InvDB; HIX0020753; -.
DR HGNC; HGNC:20589; KCMF1.
DR HPA; HPA030383; -.
DR HPA; HPA030384; -.
DR MIM; 614719; gene.
DR neXtProt; NX_Q9P0J7; -.
DR PharmGKB; PA134967694; -.
DR eggNOG; NOG291083; -.
DR HOGENOM; HOG000007727; -.
DR HOVERGEN; HBG101229; -.
DR OMA; QQTIQNS; -.
DR GenomeRNAi; 56888; -.
DR NextBio; 62289; -.
DR PRO; PR:Q9P0J7; -.
DR ArrayExpress; Q9P0J7; -.
DR Bgee; Q9P0J7; -.
DR CleanEx; HS_KCMF1; -.
DR Genevestigator; Q9P0J7; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR008598; Di19_Zn_binding.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR000433; Znf_ZZ.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; FALSE_NEG.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Complete proteome; Ligase; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 381 E3 ubiquitin-protein ligase KCMF1.
FT /FTId=PRO_0000349219.
FT ZN_FING 3 50 ZZ-type.
FT ZN_FING 78 101 C2H2-type.
FT COILED 225 257 Potential.
FT COMPBIAS 333 336 Poly-Ser.
FT COMPBIAS 376 380 Poly-Pro.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 212 212 Phosphoserine.
FT CONFLICT 95 95 E -> G (in Ref. 3; BAB14563).
FT CONFLICT 242 242 Q -> R (in Ref. 1; BAC43745 and 2;
FT AAF67009).
SQ SEQUENCE 381 AA; 41945 MW; 23B2279C56CF199B CRC64;
MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD
FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVTSE HAETSTEVIC PICAALPGGD
PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRSN MHFTSSSTGG
LSSSQSSYSP SNREAMDPIA ELLSQLSGVR RSAGGQLNSS GPSASQLQQL QMQLQLERQH
AQAARQQLET ARNATRRTNT SSVTTTITQS TATTNIANTE SSQQTLQNSQ FLLTRLNDPK
MSETERQSME SERADRSLFV QELLLSTLVR EESSSSDEDD RGEMADFGAM GCVDIMPLDV
ALENLNLKES NKGNEPPPPP L
//
ID KCMF1_HUMAN Reviewed; 381 AA.
AC Q9P0J7; Q4ZG04; Q53SC7; Q9BWK2; Q9H8P5; Q9UFE8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=E3 ubiquitin-protein ligase KCMF1;
DE EC=6.3.2.-;
DE AltName: Full=FGF-induced in gastric cancer;
DE AltName: Full=Potassium channel modulatory factor;
DE Short=PCMF;
DE AltName: Full=ZZ-type zinc finger-containing protein 1;
GN Name=KCMF1; Synonyms=FIGC, ZZZ1;
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], FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=15581609; DOI=10.1016/j.febslet.2004.10.071;
RA Jang J.-H.;
RT "FIGC, a novel FGF-induced ubiquitin-protein ligase in gastric
RT cancers.";
RL FEBS Lett. 578:21-25(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Ren S., Li Y., Huang C., Jiang C., Gu W., Zhou J., Yu Y., Xu S.,
RA Wang Y., Fu G., Chen Z., Han Z.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-381.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-212, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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).
CC -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC ubiquitination.
CC -!- TISSUE SPECIFICITY: Spleen, small intestine, ovary, peripheral
CC blood, lung, kidney and pancreas. Expressed at low levels in the
CC thymus, prostate, testis, colon, heart, brain, placenta and liver.
CC -!- INDUCTION: Up-regulated by FGF2 in gastric cancer cells.
CC -!- SIMILARITY: Belongs to the KCMF1 family.
CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX88897.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KCMF1ID46364ch2p11.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB083199; BAC43745.1; -; mRNA.
DR EMBL; AF155652; AAF67009.1; -; mRNA.
DR EMBL; AK023403; BAB14563.1; -; mRNA.
DR EMBL; AK314761; BAG37299.1; -; mRNA.
DR EMBL; AC022210; AAY24192.1; -; Genomic_DNA.
DR EMBL; AC078974; AAX88897.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC000178; AAH00178.1; -; mRNA.
DR EMBL; AL122115; CAB59274.1; -; mRNA.
DR PIR; T34540; T34540.
DR RefSeq; NP_064507.3; NM_020122.4.
DR UniGene; Hs.654968; -.
DR ProteinModelPortal; Q9P0J7; -.
DR SMR; Q9P0J7; 2-58.
DR DIP; DIP-47300N; -.
DR STRING; 9606.ENSP00000386738; -.
DR DMDM; 205815553; -.
DR PaxDb; Q9P0J7; -.
DR PRIDE; Q9P0J7; -.
DR DNASU; 56888; -.
DR Ensembl; ENST00000409785; ENSP00000386738; ENSG00000176407.
DR GeneID; 56888; -.
DR KEGG; hsa:56888; -.
DR UCSC; uc002sox.4; human.
DR CTD; 56888; -.
DR GeneCards; GC02P085198; -.
DR H-InvDB; HIX0020753; -.
DR HGNC; HGNC:20589; KCMF1.
DR HPA; HPA030383; -.
DR HPA; HPA030384; -.
DR MIM; 614719; gene.
DR neXtProt; NX_Q9P0J7; -.
DR PharmGKB; PA134967694; -.
DR eggNOG; NOG291083; -.
DR HOGENOM; HOG000007727; -.
DR HOVERGEN; HBG101229; -.
DR OMA; QQTIQNS; -.
DR GenomeRNAi; 56888; -.
DR NextBio; 62289; -.
DR PRO; PR:Q9P0J7; -.
DR ArrayExpress; Q9P0J7; -.
DR Bgee; Q9P0J7; -.
DR CleanEx; HS_KCMF1; -.
DR Genevestigator; Q9P0J7; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR008598; Di19_Zn_binding.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR000433; Znf_ZZ.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; FALSE_NEG.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Complete proteome; Ligase; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 381 E3 ubiquitin-protein ligase KCMF1.
FT /FTId=PRO_0000349219.
FT ZN_FING 3 50 ZZ-type.
FT ZN_FING 78 101 C2H2-type.
FT COILED 225 257 Potential.
FT COMPBIAS 333 336 Poly-Ser.
FT COMPBIAS 376 380 Poly-Pro.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 212 212 Phosphoserine.
FT CONFLICT 95 95 E -> G (in Ref. 3; BAB14563).
FT CONFLICT 242 242 Q -> R (in Ref. 1; BAC43745 and 2;
FT AAF67009).
SQ SEQUENCE 381 AA; 41945 MW; 23B2279C56CF199B CRC64;
MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD
FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVTSE HAETSTEVIC PICAALPGGD
PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRSN MHFTSSSTGG
LSSSQSSYSP SNREAMDPIA ELLSQLSGVR RSAGGQLNSS GPSASQLQQL QMQLQLERQH
AQAARQQLET ARNATRRTNT SSVTTTITQS TATTNIANTE SSQQTLQNSQ FLLTRLNDPK
MSETERQSME SERADRSLFV QELLLSTLVR EESSSSDEDD RGEMADFGAM GCVDIMPLDV
ALENLNLKES NKGNEPPPPP L
//
MIM
614719
*RECORD*
*FIELD* NO
614719
*FIELD* TI
*614719 POTASSIUM CHANNEL MODULATORY FACTOR 1; KCMF1
;;DIFFERENTIALLY EXPRESSED IN BRANCHING TUBULOGENESIS 91; DEBT91;;
read moreBASIC FIBROBLAST GROWTH FACTOR-INDUCED GENE IN GASTRIC CANCER; FIGC
*FIELD* TX
CLONING
Li et al. (2003) cloned 2 splice variants of mouse Kcmf1, which they
called Debt91, from a mouse heart cDNA library. The deduced proteins
contain 331 and 381 amino acids and differ at their N termini. The
full-length protein is serine and threonine rich and has a cysteine- and
histidine-rich N terminus that is predicted to form zinc fingers. It
also has a bipartite nuclear localization signal, 3 possible
glycosylation sites, and multiple potential phosphorylation sites.
Northern blot analysis detected 2 transcripts in adult mouse heart,
skeletal muscle, and kidney, but only the smaller transcript was
expressed in liver and testis. No significant expression was detected in
brain, spleen, and lung. The smaller transcript was highly expressed
throughout mouse embryonic development, with high expression after day
15. Database analysis revealed high conservation of the DEBT91 protein
among human, mouse, fly, snail, and worm, particularly at the N-terminal
end.
By differential screening for basic FGF (FGF2; 134920)-inducible genes
in SNU-16 gastric cancer cells, followed by 5-prime and 3-prime RACE of
a brain cDNA library, Jang (2004) cloned human KCMF1, which he called
FIGC. The deduced 381-amino acid protein has a calculated molecular mass
of 42 kD. It has an N-terminal C6H2-type RING finger domain and a
proline-rich C terminus. The ring finger domain of FIGC has an
acidic-rich spacer region. Northern blot analysis detected FIGC
expression in human spleen, small intestine, ovary, peripheral blood,
lung, skeletal muscle, kidney, and pancreas, with much lower expression
in thymus, prostate, testis, colon, heart, brain, placenta, and liver.
GENE FUNCTION
Jang (2004) found that basic FGF induced expression of FIGC in SNU-16
human gastric cancer cells. Recombinant FIGC functioned as a
ubiquitin-protein ligase in the presence of ATP, ubiquitin (191339),
recombinant rabbit E1 (see 314370), and the E2 enzyme UBCH5B (602962),
resulting in FIGC polyubiquitination.
Beilke et al. (2010) observed upregulated nuclear KCMF1 expression in
pancreatic cancers and several other adenocarcinomas. Overexpression of
KCMF1 in HEK293 cells resulted in elevated cell proliferation,
migration, and formation of tumor nodules in vivo.
MAPPING
Hartz (2012) mapped the KCMF1 gene to chromosome 2p11.2 based on the
alignment of the KCMF1 sequence (GenBank GENBANK AF155652) with the
genomic sequence (GRCh37).
Li et al. (2003) mapped the mouse Kcmf1 gene to a region of chromosome 6
that shares homology of synteny with human chromosome 2p11.2.
ANIMAL MODEL
Beilke et al. (2010) developed a line of mice with reduced Kcmf1
expression. Knockdown of Kcmf1 reduced development of TGF-alpha (TGFA;
190170)-dependent tumors compared with controls.
*FIELD* RF
1. Beilke, S.; Oswald, F.; Genze, F.; Wirth, T.; Adler, G.; Wagner,
M.: The zinc-finger protein KCMF1 is overexpressed during pancreatic
cancer development and downregulation of KCMF1 inhibits pancreatic
cancer development in mice. Oncogene 29: 4058-4067, 2010.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 7/13/2012.
3. Jang, J.-H.: FIGC, a novel FGF-induced ubiquitin-protein ligase
in gastric cancers. FEBS Lett. 578: 21-25, 2004.
4. Li, Z.; Stuart, R. O.; Eraly, S. A.; Gittes, G.; Beier, D. R.;
Nigam, S. K.: Debt91, a putative zinc finger protein differentially
expressed during epithelial morphogenesis. Biochem. Biophys. Res.
Commun. 306: 623-628, 2003.
*FIELD* CD
Patricia A. Hartz: 7/13/2012
*FIELD* ED
mgross: 07/13/2012
*RECORD*
*FIELD* NO
614719
*FIELD* TI
*614719 POTASSIUM CHANNEL MODULATORY FACTOR 1; KCMF1
;;DIFFERENTIALLY EXPRESSED IN BRANCHING TUBULOGENESIS 91; DEBT91;;
read moreBASIC FIBROBLAST GROWTH FACTOR-INDUCED GENE IN GASTRIC CANCER; FIGC
*FIELD* TX
CLONING
Li et al. (2003) cloned 2 splice variants of mouse Kcmf1, which they
called Debt91, from a mouse heart cDNA library. The deduced proteins
contain 331 and 381 amino acids and differ at their N termini. The
full-length protein is serine and threonine rich and has a cysteine- and
histidine-rich N terminus that is predicted to form zinc fingers. It
also has a bipartite nuclear localization signal, 3 possible
glycosylation sites, and multiple potential phosphorylation sites.
Northern blot analysis detected 2 transcripts in adult mouse heart,
skeletal muscle, and kidney, but only the smaller transcript was
expressed in liver and testis. No significant expression was detected in
brain, spleen, and lung. The smaller transcript was highly expressed
throughout mouse embryonic development, with high expression after day
15. Database analysis revealed high conservation of the DEBT91 protein
among human, mouse, fly, snail, and worm, particularly at the N-terminal
end.
By differential screening for basic FGF (FGF2; 134920)-inducible genes
in SNU-16 gastric cancer cells, followed by 5-prime and 3-prime RACE of
a brain cDNA library, Jang (2004) cloned human KCMF1, which he called
FIGC. The deduced 381-amino acid protein has a calculated molecular mass
of 42 kD. It has an N-terminal C6H2-type RING finger domain and a
proline-rich C terminus. The ring finger domain of FIGC has an
acidic-rich spacer region. Northern blot analysis detected FIGC
expression in human spleen, small intestine, ovary, peripheral blood,
lung, skeletal muscle, kidney, and pancreas, with much lower expression
in thymus, prostate, testis, colon, heart, brain, placenta, and liver.
GENE FUNCTION
Jang (2004) found that basic FGF induced expression of FIGC in SNU-16
human gastric cancer cells. Recombinant FIGC functioned as a
ubiquitin-protein ligase in the presence of ATP, ubiquitin (191339),
recombinant rabbit E1 (see 314370), and the E2 enzyme UBCH5B (602962),
resulting in FIGC polyubiquitination.
Beilke et al. (2010) observed upregulated nuclear KCMF1 expression in
pancreatic cancers and several other adenocarcinomas. Overexpression of
KCMF1 in HEK293 cells resulted in elevated cell proliferation,
migration, and formation of tumor nodules in vivo.
MAPPING
Hartz (2012) mapped the KCMF1 gene to chromosome 2p11.2 based on the
alignment of the KCMF1 sequence (GenBank GENBANK AF155652) with the
genomic sequence (GRCh37).
Li et al. (2003) mapped the mouse Kcmf1 gene to a region of chromosome 6
that shares homology of synteny with human chromosome 2p11.2.
ANIMAL MODEL
Beilke et al. (2010) developed a line of mice with reduced Kcmf1
expression. Knockdown of Kcmf1 reduced development of TGF-alpha (TGFA;
190170)-dependent tumors compared with controls.
*FIELD* RF
1. Beilke, S.; Oswald, F.; Genze, F.; Wirth, T.; Adler, G.; Wagner,
M.: The zinc-finger protein KCMF1 is overexpressed during pancreatic
cancer development and downregulation of KCMF1 inhibits pancreatic
cancer development in mice. Oncogene 29: 4058-4067, 2010.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 7/13/2012.
3. Jang, J.-H.: FIGC, a novel FGF-induced ubiquitin-protein ligase
in gastric cancers. FEBS Lett. 578: 21-25, 2004.
4. Li, Z.; Stuart, R. O.; Eraly, S. A.; Gittes, G.; Beier, D. R.;
Nigam, S. K.: Debt91, a putative zinc finger protein differentially
expressed during epithelial morphogenesis. Biochem. Biophys. Res.
Commun. 306: 623-628, 2003.
*FIELD* CD
Patricia A. Hartz: 7/13/2012
*FIELD* ED
mgross: 07/13/2012