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E3 ubiquitin-protein ligase CHFR (EC 2.3.2.27) (Checkpoint with forkhead and RING finger domains protein) (RING finger protein 196) (RING-type E3 ubiquitin transferase CHFR)

 CHFR_HUMAN              Reviewed;         664 AA.
Q96EP1; A6NEN5; B4DZ77; B4E2L6; Q96SL3; Q9NRT4; Q9NT32; Q9NVD5;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
02-FEB-2004, sequence version 2.
28-MAR-2018, entry version 163.
RecName: Full=E3 ubiquitin-protein ligase CHFR;
EC=2.3.2.27 {ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19182791};
AltName: Full=Checkpoint with forkhead and RING finger domains protein;
AltName: Full=RING finger protein 196;
AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000305};
Name=CHFR; Synonyms=RNF196;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND VARIANT MET-580.
PubMed=10935642; DOI=10.1038/35019108;
Scolnick D.M., Halazonetis T.D.;
"Chfr defines a mitotic stress checkpoint that delays entry into
metaphase.";
Nature 406:430-435(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND
VARIANT MET-580.
TISSUE=Teratocarcinoma, Testis, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
VAL-497.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-664.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
FUNCTION, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, AND MUTAGENESIS OF
ILE-306 AND TRP-332.
PubMed=11807090; DOI=10.1083/jcb.200108016;
Kang D., Chen J., Wong J., Fang G.;
"The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and
inhibits Cdc2 at the G2 to M transition.";
J. Cell Biol. 156:249-259(2002).
[7]
FUNCTION, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, SUBCELLULAR
LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=11912157;
Chaturvedi P., Sudakin V., Bobiak M.L., Fisher P.W., Mattern M.R.,
Jablonski S.A., Hurle M.R., Zhu Y., Yen T.J., Zhou B.-B.;
"Chfr regulates a mitotic stress pathway through its RING-finger
domain with ubiquitin ligase activity.";
Cancer Res. 62:1797-1801(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
VARIANTS ARG-270; VAL-497 AND MET-580, AND SILENCING IN PRIMARY
CANCERS.
PubMed=11948416; DOI=10.1038/sj.onc.1205402;
Mizuno K., Osada H., Konishi H., Tatematsu Y., Yatabe Y.,
Mitsudomi T., Fujii Y., Takahashi T.;
"Aberrant hypermethylation of the CHFR prophase checkpoint gene in
human lung cancers.";
Oncogene 21:2328-2333(2002).
[10]
SILENCING IN PRIMARY CANCERS.
PubMed=12538348; DOI=10.1093/carcin/24.1.47;
Corn P.G., Summers M.K., Fogt F., Virmani A.K., Gazdar A.F.,
Halazonetis T.D., El-Deiry W.S.;
"Frequent hypermethylation of the 5' CpG island of the mitotic stress
checkpoint gene Chfr in colorectal and non-small cell lung cancer.";
Carcinogenesis 24:47-51(2003).
[11]
SILENCING IN PRIMARY CANCERS.
PubMed=12810945; DOI=10.1073/pnas.1337066100;
Toyota M., Sasaki Y., Satoh A., Ogi K., Kikuchi T., Suzuki H.,
Mita H., Tanaka N., Itoh F., Issa J.-P.J., Jair K.-W., Schuebel K.E.,
Imai K., Tokino T.;
"Epigenetic inactivation of CHFR in human tumors.";
Proc. Natl. Acad. Sci. U.S.A. 100:7818-7823(2003).
[12]
SILENCING IN PRIMARY CANCERS.
PubMed=14695171;
Satoh A., Toyota M., Itoh F., Sasaki Y., Suzuki H., Ogi K.,
Kikuchi T., Mita H., Yamashita T., Kojima T., Kusano M., Fujita M.,
Hosokawa M., Endo T., Tokino T., Imai K.;
"Epigenetic inactivation of CHFR and sensitivity to microtubule
inhibitors in gastric cancer.";
Cancer Res. 63:8606-8613(2003).
[13]
PHOSPHORYLATION, AND MUTAGENESIS OF THR-39 AND SER-205.
PubMed=14638868;
Shtivelman E.;
"Promotion of mitosis by activated protein kinase B after DNA damage
involves polo-like kinase 1 and checkpoint protein CHFR.";
Mol. Cancer Res. 1:959-969(2003).
[14]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2V2, AND
PHOSPHORYLATION.
PubMed=14562038; DOI=10.1038/sj.onc.1206831;
Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D.;
"The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form
Lys63-linked polyubiquitin chains.";
Oncogene 22:7101-7107(2003).
[15]
FUNCTION.
PubMed=14694445; DOI=10.1002/mc.10161;
Erson A.E., Petty E.M.;
"CHFR-associated early G2/M checkpoint defects in breast cancer
cells.";
Mol. Carcinog. 39:26-33(2004).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
PubMed=15467728; DOI=10.1038/nsmb837;
Daniels M.J., Marson A., Venkitaraman A.R.;
"PML bodies control the nuclear dynamics and function of the CHFR
mitotic checkpoint protein.";
Nat. Struct. Mol. Biol. 11:1114-1121(2004).
[17]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN PBZ-TYPE,
POLY-ADP-RIBOSYLATION, ADP-RIBOSE-BINDING, AND MUTAGENESIS OF ARG-632;
CYS-635; CYS-641; ARG-642 AND GLN-644.
PubMed=18172500; DOI=10.1038/nature06420;
Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J.,
West S.C.;
"Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint
proteins.";
Nature 451:81-85(2008).
[18]
DOMAIN FHA.
PubMed=18335050; DOI=10.1371/journal.pone.0001776;
Fukuda T., Kondo Y., Nakagama H.;
"The anti-proliferative effects of the CHFR depend on the forkhead
associated domain, but not E3 ligase activity mediated by ring finger
domain.";
PLoS ONE 3:E1776-E1776(2008).
[19]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HDAC1 AND HDAC2,
AUTOUBIQUITINATION, AND MUTAGENESIS OF ILE-306.
PubMed=19182791; DOI=10.1038/ncb1837;
Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J.,
Chung C.H., Deshaies R.J., Seol J.H.;
"Chfr is linked to tumour metastasis through the downregulation of
HDAC1.";
Nat. Cell Biol. 11:295-302(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 14-128.
PubMed=12121644; DOI=10.1016/S0969-2126(02)00776-1;
Stavridi E.S., Huyen Y., Loreto I.R., Scolnick D.M., Halazonetis T.D.,
Pavletich N.P., Jeffrey P.D.;
"Crystal structure of the FHA domain of the Chfr mitotic checkpoint
protein and its complex with tungstate.";
Structure 10:891-899(2002).
[21]
VARIANTS LEU-166; PRO-202 AND SER-536.
PubMed=14612512;
Mariatos G., Bothos J., Zacharatos P., Summers M.K., Scolnick D.M.,
Kittas C., Halazonetis T.D., Gorgoulis V.G.;
"Inactivating mutations targeting the chfr mitotic checkpoint gene in
human lung cancer.";
Cancer Res. 63:7185-7189(2003).
-!- FUNCTION: E3 ubiquitin-protein ligase that functions in the
antephase checkpoint by actively delaying passage into mitosis in
response to microtubule poisons. Acts in early prophase before
chromosome condensation, when the centrosome move apart from each
other along the periphery of the nucleus. Probably involved in
signaling the presence of mitotic stress caused by microtubule
poisons by mediating the 'Lys-48'-linked ubiquitination of target
proteins, leading to their degradation by the proteasome. Promotes
the ubiquitination and subsequent degradation of AURKA and PLK1.
Probably acts as a tumor suppressor, possibly by mediating the
polyubiquitination of HDAC1, leading to its degradation. May also
promote the formation of 'Lys-63'-linked polyubiquitin chains and
functions with the specific ubiquitin-conjugating UBC13-MMS2
(UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated
at 'Lys-63' are usually not targeted for degradation, but are
rather involved in signaling cellular stress.
{ECO:0000269|PubMed:10935642, ECO:0000269|PubMed:11807090,
ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:14562038,
ECO:0000269|PubMed:14694445, ECO:0000269|PubMed:18172500,
ECO:0000269|PubMed:19182791}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:11807090,
ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:14562038,
ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19182791}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with HDAC1 and HDAC2. Interacts with PML (with
sumoylated form of PML). {ECO:0000269|PubMed:14562038,
ECO:0000269|PubMed:15467728, ECO:0000269|PubMed:19182791}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body
{ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:15467728,
ECO:0000269|PubMed:18172500}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q96EP1-1; Sequence=Displayed;
Name=2;
IsoId=Q96EP1-2; Sequence=VSP_009349;
Name=3;
IsoId=Q96EP1-3; Sequence=VSP_009350;
Name=4;
IsoId=Q96EP1-4; Sequence=VSP_038127;
Name=5;
IsoId=Q96EP1-5; Sequence=VSP_038126;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10935642}.
-!- DEVELOPMENTAL STAGE: Weakly expressed in G1 phase, and highly
expressed during S phase. {ECO:0000269|PubMed:11912157}.
-!- DOMAIN: The PBZ-type zinc finger (also named CYR) mediates non-
covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is
dependent on the presence of zinc and is required for its function
in antephase checkpoint.
-!- DOMAIN: The FHA domain plays a key role in the anti-proliferative
properties of the protein and is involved in initiating a cell
cycle arrest at G2/M. The FHA domain may be required to interact
with phosphorylated proteins.
-!- PTM: Poly-ADP-ribosylated. In addition to binding non covalently
poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also
covalently poly-ADP-ribosylated by PARP1.
-!- PTM: Autoubiquitinated; may regulate its cellular level.
{ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:11912157,
ECO:0000269|PubMed:19182791}.
-!- PTM: Phosphorylated by PKB. Phosphorylation may affect its E3
ligase activity. {ECO:0000269|PubMed:14562038,
ECO:0000269|PubMed:14638868}.
-!- MISCELLANEOUS: CHFR is silenced in many primary cancers because of
CpG methylation and deacetylated histones on its promoter region.
This however raises the question of whether CHFR silencing is a
consequence or a cause of primary cancers.
-!- SIMILARITY: Belongs to the CHFR family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CHFRID526.html";
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EMBL; AF170724; AAF91084.1; -; mRNA.
EMBL; AK001658; BAA91817.1; -; mRNA.
EMBL; AK027687; BAB55297.1; -; mRNA.
EMBL; AK302785; BAG63989.1; -; mRNA.
EMBL; AK304333; BAG65178.1; -; mRNA.
EMBL; AC127070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012072; AAH12072.1; -; mRNA.
EMBL; AL137561; CAB70812.1; -; mRNA.
CCDS; CCDS31937.1; -. [Q96EP1-3]
CCDS; CCDS53847.1; -. [Q96EP1-5]
CCDS; CCDS53848.1; -. [Q96EP1-2]
CCDS; CCDS53849.1; -. [Q96EP1-1]
PIR; T46399; T46399.
RefSeq; NP_001154816.1; NM_001161344.1. [Q96EP1-1]
RefSeq; NP_001154817.1; NM_001161345.1. [Q96EP1-4]
RefSeq; NP_001154818.1; NM_001161346.1. [Q96EP1-2]
RefSeq; NP_001154819.1; NM_001161347.1. [Q96EP1-5]
RefSeq; NP_060693.2; NM_018223.2. [Q96EP1-3]
UniGene; Hs.720197; -.
PDB; 1LGP; X-ray; 2.00 A; A=14-128.
PDB; 1LGQ; X-ray; 2.10 A; A/B=14-124.
PDB; 2XOC; X-ray; 1.89 A; A/B=407-664.
PDB; 2XOY; X-ray; 2.60 A; A/B=407-664.
PDB; 2XOZ; X-ray; 2.37 A; A/B=407-664.
PDB; 2XP0; X-ray; 1.98 A; A/B=394-664.
PDBsum; 1LGP; -.
PDBsum; 1LGQ; -.
PDBsum; 2XOC; -.
PDBsum; 2XOY; -.
PDBsum; 2XOZ; -.
PDBsum; 2XP0; -.
ProteinModelPortal; Q96EP1; -.
SMR; Q96EP1; -.
BioGrid; 120861; 47.
DIP; DIP-40098N; -.
IntAct; Q96EP1; 20.
STRING; 9606.ENSP00000392395; -.
iPTMnet; Q96EP1; -.
PhosphoSitePlus; Q96EP1; -.
BioMuta; CHFR; -.
DMDM; 41688511; -.
EPD; Q96EP1; -.
MaxQB; Q96EP1; -.
PaxDb; Q96EP1; -.
PeptideAtlas; Q96EP1; -.
PRIDE; Q96EP1; -.
DNASU; 55743; -.
Ensembl; ENST00000266880; ENSP00000266880; ENSG00000072609. [Q96EP1-3]
Ensembl; ENST00000432561; ENSP00000392395; ENSG00000072609. [Q96EP1-1]
Ensembl; ENST00000443047; ENSP00000416431; ENSG00000072609. [Q96EP1-5]
Ensembl; ENST00000450056; ENSP00000398735; ENSG00000072609. [Q96EP1-2]
GeneID; 55743; -.
KEGG; hsa:55743; -.
UCSC; uc001uld.3; human. [Q96EP1-1]
CTD; 55743; -.
DisGeNET; 55743; -.
EuPathDB; HostDB:ENSG00000072609.17; -.
GeneCards; CHFR; -.
HGNC; HGNC:20455; CHFR.
HPA; HPA045768; -.
MIM; 605209; gene.
neXtProt; NX_Q96EP1; -.
OpenTargets; ENSG00000072609; -.
PharmGKB; PA134898949; -.
eggNOG; KOG0802; Eukaryota.
eggNOG; COG5243; LUCA.
GeneTree; ENSGT00400000022306; -.
HOVERGEN; HBG048005; -.
InParanoid; Q96EP1; -.
KO; K10644; -.
OMA; HLYWGCA; -.
OrthoDB; EOG091G03AR; -.
PhylomeDB; Q96EP1; -.
TreeFam; TF330957; -.
UniPathway; UPA00143; -.
ChiTaRS; CHFR; human.
EvolutionaryTrace; Q96EP1; -.
GeneWiki; CHFR; -.
GenomeRNAi; 55743; -.
PRO; PR:Q96EP1; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000072609; -.
CleanEx; HS_CHFR; -.
ExpressionAtlas; Q96EP1; baseline and differential.
Genevisible; Q96EP1; HS.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
CDD; cd00060; FHA; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00498; FHA; 1.
SMART; SM00240; FHA; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing; Cell cycle;
Cell division; Complete proteome; Metal-binding; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 664 E3 ubiquitin-protein ligase CHFR.
/FTId=PRO_0000055872.
DOMAIN 38 89 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
ZN_FING 304 343 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 633 655 PBZ-type.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 386 386 Phosphothreonine.
{ECO:0000250|UniProtKB:Q810L3}.
VAR_SEQ 115 207 NVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGR
GADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPS
PAGRERSSSCG -> R (in isoform 5).
{ECO:0000305}.
/FTId=VSP_038126.
VAR_SEQ 135 146 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009349.
VAR_SEQ 136 206 ANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQ
PSTSTSDLFPTASASSTEPSPAGRERSSSC -> MVPCCVA
QAGLKLLGSSDPPTLASQSIVIT (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_009350.
VAR_SEQ 470 470 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038127.
VARIANT 166 166 P -> L (in a patient with non small cell
lung carcinomas; homozygous).
{ECO:0000269|PubMed:14612512}.
/FTId=VAR_017582.
VARIANT 202 202 R -> P (in a patient with non small cell
lung carcinomas).
{ECO:0000269|PubMed:14612512}.
/FTId=VAR_017583.
VARIANT 270 270 G -> R (in dbSNP:rs115096950).
{ECO:0000269|PubMed:11948416}.
/FTId=VAR_017584.
VARIANT 497 497 A -> V (common polymorphism;
dbSNP:rs2306541).
{ECO:0000269|PubMed:11948416,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_017585.
VARIANT 536 536 F -> S (in a patient with non small cell
lung carcinomas).
{ECO:0000269|PubMed:14612512}.
/FTId=VAR_017586.
VARIANT 580 580 V -> M (common polymorphism;
dbSNP:rs2306536).
{ECO:0000269|PubMed:10935642,
ECO:0000269|PubMed:11948416,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_017587.
MUTAGEN 39 39 T->A: Abolishes phosphorylation but not
autoubiquitination; when associated with
A-205. {ECO:0000269|PubMed:14638868}.
MUTAGEN 205 205 S->A: Abolishes phosphorylation but not
autoubiquitination; when associated with
A-39. {ECO:0000269|PubMed:14638868}.
MUTAGEN 306 306 I->A: Abolishes autoubiquitination. Does
not affect phosphorylation.
{ECO:0000269|PubMed:11807090,
ECO:0000269|PubMed:19182791}.
MUTAGEN 332 332 W->A: Abolishes autoubiquitination in
vitro. {ECO:0000269|PubMed:11807090}.
MUTAGEN 632 632 R->A: Abolishes poly(ADP-ribose)-binding
and poly-ADP-ribosylation by PARP1.
{ECO:0000269|PubMed:18172500}.
MUTAGEN 635 635 C->A: Abolishes poly(ADP-ribose)-binding
and poly-ADP-ribosylation by PARP1; when
associated with A-641.
{ECO:0000269|PubMed:18172500}.
MUTAGEN 641 641 C->A: Abolishes poly(ADP-ribose)-binding
and poly-ADP-ribosylation by PARP1; when
associated with A-635.
{ECO:0000269|PubMed:18172500}.
MUTAGEN 642 642 R->A: Impairs poly(ADP-ribose)-binding
and poly-ADP-ribosylation by PARP1.
{ECO:0000269|PubMed:18172500}.
MUTAGEN 644 644 Q->A: Impairs poly(ADP-ribose)-binding
and poly-ADP-ribosylation by PARP1.
{ECO:0000269|PubMed:18172500}.
CONFLICT 256 256 V -> E (in Ref. 2; BAA91817).
{ECO:0000305}.
CONFLICT 462 462 S -> P (in Ref. 2; BAA91817).
{ECO:0000305}.
CONFLICT 599 599 V -> A (in Ref. 2; BAG65178).
{ECO:0000305}.
CONFLICT 617 617 R -> Q (in Ref. 2; BAA91817).
{ECO:0000305}.
STRAND 17 19 {ECO:0000244|PDB:1LGP}.
STRAND 26 28 {ECO:0000244|PDB:1LGP}.
STRAND 31 33 {ECO:0000244|PDB:1LGP}.
STRAND 35 43 {ECO:0000244|PDB:1LGP}.
STRAND 46 49 {ECO:0000244|PDB:1LGP}.
STRAND 61 65 {ECO:0000244|PDB:1LGP}.
TURN 67 69 {ECO:0000244|PDB:1LGP}.
STRAND 72 76 {ECO:0000244|PDB:1LGP}.
STRAND 78 80 {ECO:0000244|PDB:1LGP}.
STRAND 82 90 {ECO:0000244|PDB:1LGQ}.
STRAND 92 96 {ECO:0000244|PDB:1LGQ}.
STRAND 102 106 {ECO:0000244|PDB:1LGP}.
HELIX 112 114 {ECO:0000244|PDB:1LGP}.
STRAND 116 119 {ECO:0000244|PDB:1LGP}.
HELIX 433 436 {ECO:0000244|PDB:2XOC}.
STRAND 482 484 {ECO:0000244|PDB:2XOC}.
TURN 486 488 {ECO:0000244|PDB:2XOC}.
STRAND 491 493 {ECO:0000244|PDB:2XOC}.
HELIX 496 500 {ECO:0000244|PDB:2XOC}.
TURN 511 513 {ECO:0000244|PDB:2XOC}.
HELIX 519 522 {ECO:0000244|PDB:2XOC}.
STRAND 532 535 {ECO:0000244|PDB:2XOC}.
HELIX 536 538 {ECO:0000244|PDB:2XOC}.
TURN 543 552 {ECO:0000244|PDB:2XOC}.
HELIX 554 566 {ECO:0000244|PDB:2XOC}.
HELIX 571 583 {ECO:0000244|PDB:2XOC}.
STRAND 599 601 {ECO:0000244|PDB:2XOC}.
HELIX 602 618 {ECO:0000244|PDB:2XOC}.
HELIX 622 624 {ECO:0000244|PDB:2XOC}.
HELIX 627 630 {ECO:0000244|PDB:2XOC}.
HELIX 638 640 {ECO:0000244|PDB:2XOC}.
HELIX 643 645 {ECO:0000244|PDB:2XP0}.
HELIX 647 652 {ECO:0000244|PDB:2XOC}.
SEQUENCE 664 AA; 73386 MW; 141A1E7FEFAE36A2 CRC64;
MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF PSNKLVSGDH
CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG DVIYLVYRKN EPEHNVAYLY
ESLSEKQGMT QESFEANKEN VFHGTKDTSG AGAGRGADPR VPPSSPATQV CFEEPQPSTS
TSDLFPTASA SSTEPSPAGR ERSSSCGSGG GGISPKGSGP SVASDEVSSF ASALPDRKTA
SFSSLEPQDQ EDLEPVKKKM RGDGDLDLNG QLLVAQPRRN AQTVHEDVRA AAGKPDKMEE
TLTCIICQDL LHDCVSLQPC MHTFCAACYS GWMERSSLCP TCRCPVERIC KNHILNNLVE
AYLIQHPDKS RSEEDVQSMD ARNKITQDML QPKVRRSFSD EEGSSEDLLE LSDVDSESSD
ISQPYVVCRQ CPEYRRQAAQ PPHCPAPEGE PGAPQALGDA PSTSVSLTTA VQDYVCPLQG
SHALCTCCFQ PMPDRRAERE QDPRVAPQQC AVCLQPFCHL YWGCTRTGCY GCLAPFCELN
LGDKCLDGVL NNNSYESDIL KNYLATRGLT WKNMLTESLV ALQRGVFLLS DYRVTGDTVL
CYCCGLRSFR ELTYQYRQNI PASELPVAVT SRPDCYWGRN CRTQVKAHHA MKFNHICEQT
RFKN


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