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Protein

E3 ubiquitin-protein ligase CHFR

Gene

CHFR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.7 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri304 – 34340RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri633 – 65523PBZ-typeAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: Ensembl
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CHFR (EC:6.3.2.-)
Alternative name(s):
Checkpoint with forkhead and RING finger domains protein
RING finger protein 196
Gene namesi
Name:CHFR
Synonyms:RNF196
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20455. CHFR.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391T → A: Abolishes phosphorylation but not autoubiquitination; when associated with A-205. 1 Publication
Mutagenesisi205 – 2051S → A: Abolishes phosphorylation but not autoubiquitination; when associated with A-39. 1 Publication
Mutagenesisi306 – 3061I → A: Abolishes autoubiquitination. Does not affect phosphorylation. 2 Publications
Mutagenesisi332 – 3321W → A: Abolishes autoubiquitination in vitro. 1 Publication
Mutagenesisi632 – 6321R → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1. 1 Publication
Mutagenesisi635 – 6351C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-641. 1 Publication
Mutagenesisi641 – 6411C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-635. 1 Publication
Mutagenesisi642 – 6421R → A: Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1. 1 Publication
Mutagenesisi644 – 6441Q → A: Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1. 1 Publication

Organism-specific databases

PharmGKBiPA134898949.

Polymorphism and mutation databases

BioMutaiCHFR.
DMDMi41688511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 664664E3 ubiquitin-protein ligase CHFRPRO_0000055872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei386 – 3861PhosphothreonineBy similarity

Post-translational modificationi

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.
Autoubiquitinated; may regulate its cellular level.3 Publications
Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity.2 Publications

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96EP1.
MaxQBiQ96EP1.
PaxDbiQ96EP1.
PRIDEiQ96EP1.

PTM databases

iPTMnetiQ96EP1.
PhosphoSiteiQ96EP1.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

Weakly expressed in G1 phase, and highly expressed during S phase.1 Publication

Gene expression databases

BgeeiQ96EP1.
CleanExiHS_CHFR.
ExpressionAtlasiQ96EP1. baseline and differential.
GenevisibleiQ96EP1. HS.

Interactioni

Subunit structurei

Interacts with HDAC1 and HDAC2. Interacts with PML (with sumoylated form of PML).3 Publications

Protein-protein interaction databases

BioGridi120861. 44 interactions.
DIPiDIP-40098N.
IntActiQ96EP1. 19 interactions.
MINTiMINT-1381330.
STRINGi9606.ENSP00000392395.

Structurei

Secondary structure

1
664
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Beta strandi26 – 283Combined sources
Beta strandi31 – 333Combined sources
Beta strandi35 – 439Combined sources
Beta strandi46 – 494Combined sources
Beta strandi61 – 655Combined sources
Turni67 – 693Combined sources
Beta strandi72 – 765Combined sources
Beta strandi78 – 803Combined sources
Beta strandi82 – 909Combined sources
Beta strandi92 – 965Combined sources
Beta strandi102 – 1065Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1194Combined sources
Helixi433 – 4364Combined sources
Beta strandi482 – 4843Combined sources
Turni486 – 4883Combined sources
Beta strandi491 – 4933Combined sources
Helixi496 – 5005Combined sources
Turni511 – 5133Combined sources
Helixi519 – 5224Combined sources
Beta strandi532 – 5354Combined sources
Helixi536 – 5383Combined sources
Turni543 – 55210Combined sources
Helixi554 – 56613Combined sources
Helixi571 – 58313Combined sources
Beta strandi599 – 6013Combined sources
Helixi602 – 61817Combined sources
Helixi622 – 6243Combined sources
Helixi627 – 6304Combined sources
Helixi638 – 6403Combined sources
Helixi643 – 6453Combined sources
Helixi647 – 6526Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGPX-ray2.00A14-128[»]
1LGQX-ray2.10A/B14-124[»]
2XOCX-ray1.89A/B407-664[»]
2XOYX-ray2.60A/B407-664[»]
2XOZX-ray2.37A/B407-664[»]
2XP0X-ray1.98A/B394-664[»]
ProteinModelPortaliQ96EP1.
SMRiQ96EP1. Positions 14-125, 247-359, 424-663.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96EP1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 8952FHAPROSITE-ProRule annotationAdd
BLAST

Domaini

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.
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.

Sequence similaritiesi

Belongs to the CHFR family.Curated
Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 PBZ-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri304 – 34340RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri633 – 65523PBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00400000022306.
HOVERGENiHBG048005.
InParanoidiQ96EP1.
KOiK10644.
OMAiELAYQYR.
OrthoDBiEOG78D7JS.
PhylomeDBiQ96EP1.
TreeFamiTF330957.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96EP1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF
60 70 80 90 100
PSNKLVSGDH CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG
110 120 130 140 150
DVIYLVYRKN EPEHNVAYLY ESLSEKQGMT QESFEANKEN VFHGTKDTSG
160 170 180 190 200
AGAGRGADPR VPPSSPATQV CFEEPQPSTS TSDLFPTASA SSTEPSPAGR
210 220 230 240 250
ERSSSCGSGG GGISPKGSGP SVASDEVSSF ASALPDRKTA SFSSLEPQDQ
260 270 280 290 300
EDLEPVKKKM RGDGDLDLNG QLLVAQPRRN AQTVHEDVRA AAGKPDKMEE
310 320 330 340 350
TLTCIICQDL LHDCVSLQPC MHTFCAACYS GWMERSSLCP TCRCPVERIC
360 370 380 390 400
KNHILNNLVE AYLIQHPDKS RSEEDVQSMD ARNKITQDML QPKVRRSFSD
410 420 430 440 450
EEGSSEDLLE LSDVDSESSD ISQPYVVCRQ CPEYRRQAAQ PPHCPAPEGE
460 470 480 490 500
PGAPQALGDA PSTSVSLTTA VQDYVCPLQG SHALCTCCFQ PMPDRRAERE
510 520 530 540 550
QDPRVAPQQC AVCLQPFCHL YWGCTRTGCY GCLAPFCELN LGDKCLDGVL
560 570 580 590 600
NNNSYESDIL KNYLATRGLT WKNMLTESLV ALQRGVFLLS DYRVTGDTVL
610 620 630 640 650
CYCCGLRSFR ELTYQYRQNI PASELPVAVT SRPDCYWGRN CRTQVKAHHA
660
MKFNHICEQT RFKN
Length:664
Mass (Da):73,386
Last modified:February 2, 2004 - v2
Checksum:i141A1E7FEFAE36A2
GO
Isoform 2 (identifier: Q96EP1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-146: Missing.

Show »
Length:652
Mass (Da):72,031
Checksum:i572F2CE6D1743D80
GO
Isoform 3 (identifier: Q96EP1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-206: ANKENVFHGT...PAGRERSSSC → MVPCCVAQAGLKLLGSSDPPTLASQSIVIT

Show »
Length:623
Mass (Da):69,192
Checksum:iB747CD23B74368E7
GO
Isoform 4 (identifier: Q96EP1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-470: Missing.

Show »
Length:663
Mass (Da):73,315
Checksum:i302207777755B60C
GO
Isoform 5 (identifier: Q96EP1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-207: NVAYLYESLS...AGRERSSSCG → R

Note: No experimental confirmation available.
Show »
Length:572
Mass (Da):63,873
Checksum:iC3CFDEF89A9C85B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561V → E in BAA91817 (PubMed:14702039).Curated
Sequence conflicti462 – 4621S → P in BAA91817 (PubMed:14702039).Curated
Sequence conflicti599 – 5991V → A in BAG65178 (PubMed:14702039).Curated
Sequence conflicti617 – 6171R → Q in BAA91817 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1661P → L in a patient with non small cell lung carcinomas; homozygous. 1 Publication
VAR_017582
Natural varianti202 – 2021R → P in a patient with non small cell lung carcinomas. 1 Publication
VAR_017583
Natural varianti270 – 2701G → R.1 Publication
Corresponds to variant rs115096950 [ dbSNP | Ensembl ].
VAR_017584
Natural varianti497 – 4971A → V Common polymorphism. 2 Publications
Corresponds to variant rs2306541 [ dbSNP | Ensembl ].
VAR_017585
Natural varianti536 – 5361F → S in a patient with non small cell lung carcinomas. 1 Publication
VAR_017586
Natural varianti580 – 5801V → M Common polymorphism. 3 Publications
Corresponds to variant rs2306536 [ dbSNP | Ensembl ].
VAR_017587

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei115 – 20793NVAYL…SSSCG → R in isoform 5. CuratedVSP_038126Add
BLAST
Alternative sequencei135 – 14612Missing in isoform 2. 2 PublicationsVSP_009349Add
BLAST
Alternative sequencei136 – 20671ANKEN…RSSSC → MVPCCVAQAGLKLLGSSDPP TLASQSIVIT in isoform 3. 1 PublicationVSP_009350Add
BLAST
Alternative sequencei470 – 4701Missing in isoform 4. 1 PublicationVSP_038127

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170724 mRNA. Translation: AAF91084.1.
AK001658 mRNA. Translation: BAA91817.1.
AK027687 mRNA. Translation: BAB55297.1.
AK302785 mRNA. Translation: BAG63989.1.
AK304333 mRNA. Translation: BAG65178.1.
AC127070 Genomic DNA. No translation available.
BC012072 mRNA. Translation: AAH12072.1.
AL137561 mRNA. Translation: CAB70812.1.
CCDSiCCDS31937.1. [Q96EP1-3]
CCDS53847.1. [Q96EP1-5]
CCDS53848.1. [Q96EP1-2]
CCDS53849.1. [Q96EP1-1]
PIRiT46399.
RefSeqiNP_001154816.1. NM_001161344.1. [Q96EP1-1]
NP_001154817.1. NM_001161345.1. [Q96EP1-4]
NP_001154818.1. NM_001161346.1. [Q96EP1-2]
NP_001154819.1. NM_001161347.1. [Q96EP1-5]
NP_060693.2. NM_018223.2. [Q96EP1-3]
UniGeneiHs.720197.

Genome annotation databases

EnsembliENST00000266880; ENSP00000266880; ENSG00000072609. [Q96EP1-3]
ENST00000432561; ENSP00000392395; ENSG00000072609. [Q96EP1-1]
ENST00000443047; ENSP00000416431; ENSG00000072609. [Q96EP1-5]
ENST00000450056; ENSP00000398735; ENSG00000072609. [Q96EP1-2]
GeneIDi55743.
KEGGihsa:55743.
UCSCiuc001uld.3. human. [Q96EP1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170724 mRNA. Translation: AAF91084.1.
AK001658 mRNA. Translation: BAA91817.1.
AK027687 mRNA. Translation: BAB55297.1.
AK302785 mRNA. Translation: BAG63989.1.
AK304333 mRNA. Translation: BAG65178.1.
AC127070 Genomic DNA. No translation available.
BC012072 mRNA. Translation: AAH12072.1.
AL137561 mRNA. Translation: CAB70812.1.
CCDSiCCDS31937.1. [Q96EP1-3]
CCDS53847.1. [Q96EP1-5]
CCDS53848.1. [Q96EP1-2]
CCDS53849.1. [Q96EP1-1]
PIRiT46399.
RefSeqiNP_001154816.1. NM_001161344.1. [Q96EP1-1]
NP_001154817.1. NM_001161345.1. [Q96EP1-4]
NP_001154818.1. NM_001161346.1. [Q96EP1-2]
NP_001154819.1. NM_001161347.1. [Q96EP1-5]
NP_060693.2. NM_018223.2. [Q96EP1-3]
UniGeneiHs.720197.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGPX-ray2.00A14-128[»]
1LGQX-ray2.10A/B14-124[»]
2XOCX-ray1.89A/B407-664[»]
2XOYX-ray2.60A/B407-664[»]
2XOZX-ray2.37A/B407-664[»]
2XP0X-ray1.98A/B394-664[»]
ProteinModelPortaliQ96EP1.
SMRiQ96EP1. Positions 14-125, 247-359, 424-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120861. 44 interactions.
DIPiDIP-40098N.
IntActiQ96EP1. 19 interactions.
MINTiMINT-1381330.
STRINGi9606.ENSP00000392395.

PTM databases

iPTMnetiQ96EP1.
PhosphoSiteiQ96EP1.

Polymorphism and mutation databases

BioMutaiCHFR.
DMDMi41688511.

Proteomic databases

EPDiQ96EP1.
MaxQBiQ96EP1.
PaxDbiQ96EP1.
PRIDEiQ96EP1.

Protocols and materials databases

DNASUi55743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266880; ENSP00000266880; ENSG00000072609. [Q96EP1-3]
ENST00000432561; ENSP00000392395; ENSG00000072609. [Q96EP1-1]
ENST00000443047; ENSP00000416431; ENSG00000072609. [Q96EP1-5]
ENST00000450056; ENSP00000398735; ENSG00000072609. [Q96EP1-2]
GeneIDi55743.
KEGGihsa:55743.
UCSCiuc001uld.3. human. [Q96EP1-1]

Organism-specific databases

CTDi55743.
GeneCardsiCHFR.
HGNCiHGNC:20455. CHFR.
MIMi605209. gene.
neXtProtiNX_Q96EP1.
PharmGKBiPA134898949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00400000022306.
HOVERGENiHBG048005.
InParanoidiQ96EP1.
KOiK10644.
OMAiELAYQYR.
OrthoDBiEOG78D7JS.
PhylomeDBiQ96EP1.
TreeFamiTF330957.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiCHFR. human.
EvolutionaryTraceiQ96EP1.
GeneWikiiCHFR.
GenomeRNAii55743.
NextBioi60707.
PROiQ96EP1.
SOURCEiSearch...

Gene expression databases

BgeeiQ96EP1.
CleanExiHS_CHFR.
ExpressionAtlasiQ96EP1. baseline and differential.
GenevisibleiQ96EP1. HS.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Chfr defines a mitotic stress checkpoint that delays entry into metaphase."
    Scolnick D.M., Halazonetis T.D.
    Nature 406:430-435(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT MET-580.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), VARIANT MET-580.
    Tissue: Teratocarcinoma, Testis and Trachea.
  3. "The finished DNA sequence of human chromosome 12."
    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.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-497.
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-664.
    Tissue: Testis.
  6. "The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition."
    Kang D., Chen J., Wong J., Fang G.
    J. Cell Biol. 156:249-259(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOUBIQUITINATION, MUTAGENESIS OF ILE-306 AND TRP-332.
  7. "Chfr regulates a mitotic stress pathway through its RING-finger domain with ubiquitin ligase activity."
    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.
    Cancer Res. 62:1797-1801(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  8. "Aberrant hypermethylation of the CHFR prophase checkpoint gene in human lung cancers."
    Mizuno K., Osada H., Konishi H., Tatematsu Y., Yatabe Y., Mitsudomi T., Fujii Y., Takahashi T.
    Oncogene 21:2328-2333(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-270; VAL-497 AND MET-580, SILENCING IN PRIMARY CANCERS.
  9. "Frequent hypermethylation of the 5' CpG island of the mitotic stress checkpoint gene Chfr in colorectal and non-small cell lung cancer."
    Corn P.G., Summers M.K., Fogt F., Virmani A.K., Gazdar A.F., Halazonetis T.D., El-Deiry W.S.
    Carcinogenesis 24:47-51(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SILENCING IN PRIMARY CANCERS.
  10. Cited for: SILENCING IN PRIMARY CANCERS.
  11. "Epigenetic inactivation of CHFR and sensitivity to microtubule inhibitors in gastric cancer."
    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.
    Cancer Res. 63:8606-8613(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SILENCING IN PRIMARY CANCERS.
  12. "Promotion of mitosis by activated protein kinase B after DNA damage involves polo-like kinase 1 and checkpoint protein CHFR."
    Shtivelman E.
    Mol. Cancer Res. 1:959-969(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF THR-39 AND SER-205.
  13. "The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains."
    Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D.
    Oncogene 22:7101-7107(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBE2V2, PHOSPHORYLATION.
  14. "CHFR-associated early G2/M checkpoint defects in breast cancer cells."
    Erson A.E., Petty E.M.
    Mol. Carcinog. 39:26-33(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "PML bodies control the nuclear dynamics and function of the CHFR mitotic checkpoint protein."
    Daniels M.J., Marson A., Venkitaraman A.R.
    Nat. Struct. Mol. Biol. 11:1114-1121(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PML.
  16. "Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins."
    Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., West S.C.
    Nature 451:81-85(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PBZ-TYPE, POLY-ADP-RIBOSYLATION, ADP-RIBOSE-BINDING, MUTAGENESIS OF ARG-632; CYS-635; CYS-641; ARG-642 AND GLN-644.
  17. "The anti-proliferative effects of the CHFR depend on the forkhead associated domain, but not E3 ligase activity mediated by ring finger domain."
    Fukuda T., Kondo Y., Nakagama H.
    PLoS ONE 3:E1776-E1776(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN FHA.
  18. "Chfr is linked to tumour metastasis through the downregulation of HDAC1."
    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.
    Nat. Cell Biol. 11:295-302(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HDAC1 AND HDAC2, AUTOUBIQUITINATION, MUTAGENESIS OF ILE-306.
  19. "Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate."
    Stavridi E.S., Huyen Y., Loreto I.R., Scolnick D.M., Halazonetis T.D., Pavletich N.P., Jeffrey P.D.
    Structure 10:891-899(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 14-128.
  20. "Inactivating mutations targeting the chfr mitotic checkpoint gene in human lung cancer."
    Mariatos G., Bothos J., Zacharatos P., Summers M.K., Scolnick D.M., Kittas C., Halazonetis T.D., Gorgoulis V.G.
    Cancer Res. 63:7185-7189(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LEU-166; PRO-202 AND SER-536.

Entry informationi

Entry nameiCHFR_HUMAN
AccessioniPrimary (citable) accession number: Q96EP1
Secondary accession number(s): A6NEN5
, B4DZ77, B4E2L6, Q96SL3, Q9NRT4, Q9NT32, Q9NVD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: March 16, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.