Reviewed, UniProtKB/Swiss-Prot Q96EP1 (CHFR_HUMAN)

Names and origin

Protein names

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 names

Name:	CHFR
Synonyms:	RNF196

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	E3 ubiquitin-protein ligase required to transiently arrest cells in early prophase when they are exposed 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 promotes 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. This suggests that it may be involved in signaling the presence of mitotic stress caused by microtubule poisons. Ref.1 Ref.6 Ref.7 Ref.14 Ref.15
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Nucleus. Ref.7
Tissue specificity	Ubiquitous. Ref.1
Developmental stage	Weakly expressed in G1 phase, and highly expressed during S phase. Ref.7
Domain	The FHA domain may be required to interact with phosphorylated proteins.
Post-translational modification	Autoubiquitinated in vitro. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity.
Involvement in disease	Defects in CHFR may be involved in colon, lung and esophageal cancers and non small cell lung carcinomas (NSCLC). In addition, CHFR gene 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Contains 1 FHA domain. Contains 1 RING-type zinc finger.
Caution	Ref.6 and Ref.7 report that it can ubiquitinate and promote the degradation of substrates. Ref.6 reports that, in Xenopus extracts, it ubiquitinates PLK, a protein kinase involved in mitotic progression. However, as experiments have been done either in vitro or with extracts from Xenopus, there is actually little evidence for a role for CHFR in protein degradation in vivo.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle checkpoint Ref.1 Traceable author statement. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TPT1	P13693	2	EBI-718923,EBI-1783169

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96EP1-1)

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.

Isoform 2 (identifier: Q96EP1-2)

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

Isoform 3 (identifier: Q96EP1-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 664

664

E3 ubiquitin-protein ligase CHFR

PRO_0000055872

Regions

Domain

38 – 89

52

FHA

Zinc finger

304 – 343

40

RING-type

Amino acid modifications

Modified residue

130

1

Phosphothreonine By similarity

Modified residue

386

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

135 – 146

12

Missing in isoform 2.

VSP_009349

Alternative sequence

136 – 206

71

ANKEN…RSSSC → EMVPCCVAQAGLKLLGSSDP PTLASQSIVIT in isoform 3.

VSP_009350

Natural variant

166

1

P → L in a patient with NSCLC; homozygous. Ref.12

VAR_017582

Natural variant

202

1

R → P in a patient with NSCLC. Ref.12

VAR_017583

Natural variant

270

1

G → R Ref.8

VAR_017584

Natural variant

456

1

A → V: dbSNP rs2306541.

VAR_038192

Natural variant

497

1

A → V Common polymorphism. dbSNP rs2306541. Ref.8 Ref.4

VAR_017585

Natural variant

536

1

F → S in a patient with NSCLC. Ref.12

VAR_017586

Natural variant

580

1

V → M Common polymorphism. dbSNP rs2306536. Ref.1 Ref.8

VAR_017587

Experimental info

Mutagenesis

39

1

T → A: Abolishes phosphorylation but not autoubiquitination; when associated with A-205. Ref.13

Mutagenesis

205

1

S → A: Abolishes phosphorylation but not autoubiquitination; when associated with A-39. Ref.13

Mutagenesis

306

1

I → A: Abolishes autoubiquitination in vitro. Does not affect phosphorylation. Ref.6

Mutagenesis

332

1

W → A: Abolishes autoubiquitination in vitro. Ref.6

Sequence conflict

256

1

V → E in BAA91817. Ref.4

Sequence conflict

462

1

S → P in BAA91817. Ref.4

Sequence conflict

617

1

R → Q in BAA91817. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

664

Helix Strand Turn

Details...

Beta strand

17 – 21

5

Beta strand

26 – 28

3

Beta strand

31 – 33

3

Beta strand

35 – 43

9

Beta strand

46 – 49

4

Beta strand

61 – 65

5

Turn

67 – 69

3

Beta strand

72 – 76

5

Beta strand

78 – 80

3

Beta strand

82 – 90

9

Beta strand

92 – 97

6

Beta strand

102 – 106

5

Helix

112 – 114

3

Beta strand

116 – 123

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 2, 2004. Version 2. Checksum: 141A1E7FEFAE36A2	FASTA	664	73,386
	10 20 30 40 50 60 MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF PSNKLVSGDH 70 80 90 100 110 120 CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG DVIYLVYRKN EPEHNVAYLY 130 140 150 160 170 180 ESLSEKQGMT QESFEANKEN VFHGTKDTSG AGAGRGADPR VPPSSPATQV CFEEPQPSTS 190 200 210 220 230 240 TSDLFPTASA SSTEPSPAGR ERSSSCGSGG GGISPKGSGP SVASDEVSSF ASALPDRKTA 250 260 270 280 290 300 SFSSLEPQDQ EDLEPVKKKM RGDGDLDLNG QLLVAQPRRN AQTVHEDVRA AAGKPDKMEE 310 320 330 340 350 360 TLTCIICQDL LHDCVSLQPC MHTFCAACYS GWMERSSLCP TCRCPVERIC KNHILNNLVE 370 380 390 400 410 420 AYLIQHPDKS RSEEDVQSMD ARNKITQDML QPKVRRSFSD EEGSSEDLLE LSDVDSESSD 430 440 450 460 470 480 ISQPYVVCRQ CPEYRRQAAQ PPHCPAPEGE PGAPQALGDA PSTSVSLTTA VQDYVCPLQG 490 500 510 520 530 540 SHALCTCCFQ PMPDRRAERE QDPRVAPQQC AVCLQPFCHL YWGCTRTGCY GCLAPFCELN 550 560 570 580 590 600 LGDKCLDGVL NNNSYESDIL KNYLATRGLT WKNMLTESLV ALQRGVFLLS DYRVTGDTVL 610 620 630 640 650 660 CYCCGLRSFR ELTYQYRQNI PASELPVAVT SRPDCYWGRN CRTQVKAHHA MKFNHICEQT RFKN
	Isoform 2. Checksum: 572F2CE6D1743D80	FASTA	652	72,031
	10 20 30 40 50 60 MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF PSNKLVSGDH 70 80 90 100 110 120 CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG DVIYLVYRKN EPEHNVAYLY 130 140 150 160 170 180 ESLSEKQGMT QESFDTSGAG AGRGADPRVP PSSPATQVCF EEPQPSTSTS DLFPTASASS 190 200 210 220 230 240 TEPSPAGRER SSSCGSGGGG ISPKGSGPSV ASDEVSSFAS ALPDRKTASF SSLEPQDQED 250 260 270 280 290 300 LEPVKKKMRG DGDLDLNGQL LVAQPRRNAQ TVHEDVRAAA GKPDKMEETL TCIICQDLLH 310 320 330 340 350 360 DCVSLQPCMH TFCAACYSGW MERSSLCPTC RCPVERICKN HILNNLVEAY LIQHPDKSRS 370 380 390 400 410 420 EEDVQSMDAR NKITQDMLQP KVRRSFSDEE GSSEDLLELS DVDSESSDIS QPYVVCRQCP 430 440 450 460 470 480 EYRRQAAQPP HCPAPEGEPG APQALGDAPS TSVSLTTAVQ DYVCPLQGSH ALCTCCFQPM 490 500 510 520 530 540 PDRRAEREQD PRVAPQQCAV CLQPFCHLYW GCTRTGCYGC LAPFCELNLG DKCLDGVLNN 550 560 570 580 590 600 NSYESDILKN YLATRGLTWK NMLTESLVAL QRGVFLLSDY RVTGDTVLCY CCGLRSFREL 610 620 630 640 650 TYQYRQNIPA SELPVAVTSR PDCYWGRNCR TQVKAHHAMK FNHICEQTRF KN
	Isoform 3. Checksum: 8B6C80C7F64C2F89	FASTA	624	69,322
	10 20 30 40 50 60 MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF PSNKLVSGDH 70 80 90 100 110 120 CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG DVIYLVYRKN EPEHNVAYLY 130 140 150 160 170 180 ESLSEKQGMT QESFEEMVPC CVAQAGLKLL GSSDPPTLAS QSIVITGSGG GGISPKGSGP 190 200 210 220 230 240 SVASDEVSSF ASALPDRKTA SFSSLEPQDQ EDLEPVKKKM RGDGDLDLNG QLLVAQPRRN 250 260 270 280 290 300 AQTVHEDVRA AAGKPDKMEE TLTCIICQDL LHDCVSLQPC MHTFCAACYS GWMERSSLCP 310 320 330 340 350 360 TCRCPVERIC KNHILNNLVE AYLIQHPDKS RSEEDVQSMD ARNKITQDML QPKVRRSFSD 370 380 390 400 410 420 EEGSSEDLLE LSDVDSESSD ISQPYVVCRQ CPEYRRQAAQ PPHCPAPEGE PGAPQALGDA 430 440 450 460 470 480 PSTSVSLTTA VQDYVCPLQG SHALCTCCFQ PMPDRRAERE QDPRVAPQQC AVCLQPFCHL 490 500 510 520 530 540 YWGCTRTGCY GCLAPFCELN LGDKCLDGVL NNNSYESDIL KNYLATRGLT WKNMLTESLV 550 560 570 580 590 600 ALQRGVFLLS DYRVTGDTVL CYCCGLRSFR ELTYQYRQNI PASELPVAVT SRPDCYWGRN 610 620 CRTQVKAHHA MKFNHICEQT RFKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chfr defines a mitotic stress checkpoint that delays entry into metaphase." Scolnick D.M., Halazonetis T.D. Nature 406:430-435(2000) [PubMed: 10935642] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Teratocarcinoma.
[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: 16541075] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-497. Tissue: Placenta.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] 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: 11807090] [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: 11912157] [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: 11948416] [Abstract] Cited for: DISEASE, VARIANTS ARG-270; VAL-497 AND MET-580.
[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: 12538348] [Abstract] Cited for: DISEASE.
[10]	"Epigenetic inactivation of CHFR in human tumors." 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. Proc. Natl. Acad. Sci. U.S.A. 100:7818-7823(2003) [PubMed: 12810945] [Abstract] Cited for: DISEASE.
[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: 14695171] [Abstract] Cited for: DISEASE.
[12]	"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: 14612512] [Abstract] Cited for: VARIANTS NSCLC LEU-166; PRO-202 AND SER-536.
[13]	"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: 14638868] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF THR-39 AND SER-205.
[14]	"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: 14562038] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBE2V2, PHOSPHORYLATION.
[15]	"CHFR-associated early G2/M checkpoint defects in breast cancer cells." Erson A.E., Petty E.M. Mol. Carcinog. 39:26-33(2004) [PubMed: 14694445] [Abstract] Cited for: FUNCTION.
[16]	"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: 12121644] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 14-128.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF170724 mRNA. Translation: AAF91084.1.
AK001658 mRNA. Translation: BAA91817.1.
AK027687 mRNA. Translation: BAB55297.1.
AC127070 Genomic DNA. No translation available.
BC012072 mRNA. Translation: AAH12072.1.
AL137561 mRNA. Translation: CAB70812.1.

IPI

IPI00023513.
IPI00397548.
IPI00397549.

PIR

T46399.

RefSeq

NP_060693.1.

UniGene

Hs.656770

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LGP	X-ray	2.00	A	14-128	[»]
1LGQ	X-ray	2.10	A/B	14-124	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96EP1. 6 interactions.

Proteomic databases

PRIDE

Q96EP1.

Genome annotation databases

Ensembl

ENSG00000072609. Homo sapiens. [Contig view]

GeneID

55743.

KEGG

hsa:55743.

Organism-specific databases

GeneCards

GC12M131927.

H-InvDB

HIX0011141.

HGNC

HGNC:20455. CHFR.

MIM

605209. gene.

PharmGKB

PA134898949.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q96EP1.

HOVERGEN

Q96EP1.

OMA

Q96EP1. TLEDTST.

Gene expression databases

ArrayExpress

Q96EP1.

Bgee

Q96EP1.

CleanEx

HS_CHFR.

GermOnline

ENSG00000072609. Homo sapiens.

Family and domain databases

InterPro

IPR000253. FHA.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Gene3D

G3DSA:2.60.200.20. FHA. 1 hit.

Pfam

PF00498. FHA. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

SMART

SM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

60707.

SOURCE

Search...

Entry information

Entry name

CHFR_HUMAN

Accession

Primary (citable) accession number: Q96EP1
Secondary accession number(s): A6NEN5 , Q96SL3, Q9NRT4, Q9NT32, Q9NVD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	February 2, 2004
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)