Q9UM11 (FZR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fizzy-related protein homolog
Short name=Fzr

Alternative name(s):
CDC20-like protein 1
Cdh1/Hct1 homolog
Short name=hCDH1

Gene names

Name:	FZR1
Synonyms:	CDH1, FYR, FZR, KIAA1242

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	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key regulator of ligase activity of the anaphase promoting complex/cyclosome (APC/C), which confers substrate specificity upon the complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. Ref.9 Ref.15 Ref.19
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The unphosphorylated form interacts with APC/C during mitosis. Interacts with NINL. Interacts (in complex with the anaphase promoting complex APC) with MAD2L2; inhibits FZR1-mediated APC/C activation. Interacts with USP37. Ref.9 Ref.11 Ref.12 Ref.13 Ref.19
Subcellular location	Isoform 2: Nucleus Ref.4. Isoform 3: Cytoplasm Ref.4.
Tissue specificity	Isoform 2 is expressed at high levels in heart, liver, spleen and some cancer cell lines whereas isoform 3 is expressed only at low levels in these tissues. Ref.4
Post-translational modification	Phosphorylated during mitosis, probably by maturation promoting factor (MPF), leading to its dissociation of the APC/C. Following DNA damage, it is dephosphorylated by CDC14B in G2 phase, leading to its reassociation with the APC/C, and allowing an efficient G2 DNA damage checkpoint. Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the WD repeat CDC20/Fizzy family. Contains 7 WD repeats.
Sequence caution	The sequence AAD26623.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part. The sequence AAD26624.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence BAA86556.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA repair Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW G2/M transition DNA damage checkpoint Inferred from direct assay Ref.15. Source: UniProtKB S phase of mitotic cell cycle Traceable author statement. Source: Reactome activation of anaphase-promoting complex activity Inferred from direct assay Ref.12. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.15Ref.19. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of protein catabolic process Inferred from genetic interaction Ref.11. Source: UniProtKB positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein K11-linked ubiquitination Traceable author statement Ref.19. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular function	kinase activity Traceable author statement. Source: Reactome protein binding Inferred from physical interaction Ref.12Ref.15Ref.19. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC27	P30260	5	EBI-724997,EBI-994813
CLSPN	Q9HAW4	4	EBI-724997,EBI-1369377
MAD2L2	Q9UI95	2	EBI-724997,EBI-77889
VHL	P40337	2	EBI-724997,EBI-301246
VHL	P40337-1	2	EBI-724997,EBI-3504450
VHL	P40337-3	2	EBI-724997,EBI-301270

Alternative products

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

Isoform 1 (identifier: Q9UM11-1)

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: Q9UM11-2)

Also known as: CDH1alpha; Fzr1;

The sequence of this isoform differs from the canonical sequence as follows:
     481-483: Missing.

Note: Major.

Isoform 3 (identifier: Q9UM11-3)

Also known as: CDH1beta; Fzr2;

The sequence of this isoform differs from the canonical sequence as follows:
     130-218: Missing.
     481-483: Missing.

Note: Minor.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	Fizzy-related protein homolog		PRO_0000051001
Regions
	Repeat	182 – 222	41	WD 1
	Repeat	227 – 266	40	WD 2
	Repeat	269 – 306	38	WD 3
	Repeat	311 – 350	40	WD 4
	Repeat	353 – 395	43	WD 5
	Repeat	397 – 438	42	WD 6
	Repeat	441 – 480	40	WD 7
Amino acid modifications
	Modified residue	32	1	Phosphothreonine Ref.16
	Modified residue	36	1	Phosphoserine Ref.16 Ref.17 Ref.18
	Modified residue	39	1	Phosphoserine Ref.17
	Modified residue	40	1	Phosphoserine Ref.16
	Modified residue	91	1	Phosphotyrosine Ref.14
	Modified residue	92	1	Phosphoserine Ref.14
	Modified residue	137	1	Phosphoserine Ref.16
	Modified residue	138	1	Phosphoserine Ref.16
	Modified residue	146	1	Phosphoserine Ref.16
	Modified residue	151	1	Phosphoserine Ref.16 Ref.18
Natural variations
	Alternative sequence	130 – 218	89	Missing in isoform 3.		VSP_008503
	Alternative sequence	481 – 483	3	Missing in isoform 2 and isoform 3.		VSP_008504
Experimental info
	Mutagenesis	40	1	S → A: Constitutively active; when associated with A-121; A-151 and A-163. Ref.15
	Mutagenesis	121	1	T → A: Constitutively active; when associated with A-40; A-151 and A-163. Ref.15
	Mutagenesis	151	1	S → A: Constitutively active; when associated with A-40; A-121 and A-163. Ref.15
	Mutagenesis	163	1	S → A: Constitutively active; when associated with A-40; A-121 and A-151. Ref.15
	Sequence conflict	259	1	A → S in AAF20266. Ref.3
	Sequence conflict	275	1	G → W in AAF20266. Ref.3
	Sequence conflict	326	1	Q → H in BAA86954. Ref.2
	Sequence conflict	326	1	Q → H in BAA86955. Ref.2
	Sequence conflict	341	1	N → I in AAF20266. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: F6C8FDAF81D8103A	FASTA	496	55,179
	10 20 30 40 50 60 MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP SRAGANWSVN 70 80 90 100 110 120 FHRINENEKS PSQNRKAKDA TSDNGKDGLA YSALLKNELL GAGIEKVQDP QTEDRRLQPS 130 140 150 160 170 180 TPEKKGLFTY SLSTKRSSPD DGNDVSPYSL SPVSNKSQKL LRSPRKPTRK ISKIPFKVLD 190 200 210 220 230 240 APELQDDFYL NLVDWSSLNV LSVGLGTCVY LWSACTSQVT RLCDLSVEGD SVTSVGWSER 250 260 270 280 290 300 GNLVAVGTHK GFVQIWDAAA GKKLSMLEGH TARVGALAWN AEQLSSGSRD RMILQRDIRT 310 320 330 340 350 360 PPLQSERRLQ GHRQEVCGLK WSTDHQLLAS GGNDNKLLVW NHSSLSPVQQ YTEHLAAVKA 370 380 390 400 410 420 IAWSPHQHGL LASGGGTADR CIRFWNTLTG QPLQCIDTGS QVCNLAWSKH ANELVSTHGY 430 440 450 460 470 480 SQNQILVWKY PSLTQVAKLT GHSYRVLYLA MSPDGEAIVT GAGDETLRFW NVFSKTRSTK 490 VKWESVSVLN LFTRIR
	Isoform 2 (CDH1alpha) (Fzr1) [UniParc]. Checksum: 7C6A947EBB8A6D5C	FASTA	493	54,766
	10 20 30 40 50 60 MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP SRAGANWSVN 70 80 90 100 110 120 FHRINENEKS PSQNRKAKDA TSDNGKDGLA YSALLKNELL GAGIEKVQDP QTEDRRLQPS 130 140 150 160 170 180 TPEKKGLFTY SLSTKRSSPD DGNDVSPYSL SPVSNKSQKL LRSPRKPTRK ISKIPFKVLD 190 200 210 220 230 240 APELQDDFYL NLVDWSSLNV LSVGLGTCVY LWSACTSQVT RLCDLSVEGD SVTSVGWSER 250 260 270 280 290 300 GNLVAVGTHK GFVQIWDAAA GKKLSMLEGH TARVGALAWN AEQLSSGSRD RMILQRDIRT 310 320 330 340 350 360 PPLQSERRLQ GHRQEVCGLK WSTDHQLLAS GGNDNKLLVW NHSSLSPVQQ YTEHLAAVKA 370 380 390 400 410 420 IAWSPHQHGL LASGGGTADR CIRFWNTLTG QPLQCIDTGS QVCNLAWSKH ANELVSTHGY 430 440 450 460 470 480 SQNQILVWKY PSLTQVAKLT GHSYRVLYLA MSPDGEAIVT GAGDETLRFW NVFSKTRSTK 490 ESVSVLNLFT RIR
	Isoform 3 (CDH1beta) (Fzr2) [UniParc]. Checksum: A793194D88777035	FASTA	404	44,874
	10 20 30 40 50 60 MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP SRAGANWSVN 70 80 90 100 110 120 FHRINENEKS PSQNRKAKDA TSDNGKDGLA YSALLKNELL GAGIEKVQDP QTEDRRLQPS 130 140 150 160 170 180 TPEKKGLFTV TRLCDLSVEG DSVTSVGWSE RGNLVAVGTH KGFVQIWDAA AGKKLSMLEG 190 200 210 220 230 240 HTARVGALAW NAEQLSSGSR DRMILQRDIR TPPLQSERRL QGHRQEVCGL KWSTDHQLLA 250 260 270 280 290 300 SGGNDNKLLV WNHSSLSPVQ QYTEHLAAVK AIAWSPHQHG LLASGGGTAD RCIRFWNTLT 310 320 330 340 350 360 GQPLQCIDTG SQVCNLAWSK HANELVSTHG YSQNQILVWK YPSLTQVAKL TGHSYRVLYL 370 380 390 400 AMSPDGEAIV TGAGDETLRF WNVFSKTRST KESVSVLNLF TRIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Activation of the human anaphase-promoting complex by proteins of the CDC20/Fizzy family." Kramer E.R., Gieffers C., Hoelzl G., Hengstschlaeger M., Peters J.-M. Curr. Biol. 8:1207-1210(1998) [PubMed: 9811605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Parathyroid adenoma.
[2]	"Human homologue of Fizzy-related protein." Kotani S., Oyamatu T., Todokoro K. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[3]	"Identification of a human homolog of the Drosophila fizzy-related protein." Sudo T., Saya H. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"Differential expression, localization and activity of two alternatively spliced isoforms of human APC regulator CDH1." Zhou Y., Ching Y.-P., Ng R.W.M., Jin D.-Y. Biochem. J. 374:349-358(2003) [PubMed: 12797865] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed: 10574462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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). Tissue: Brain.
[9]	"Direct binding of CDC20 protein family members activates the anaphase-promoting complex in mitosis and G1." Fang G., Yu H., Kirschner M.W. Mol. Cell 2:163-171(1998) [PubMed: 9734353] [Abstract] Cited for: FUNCTION, INTERACTION WITH APC/C.
[10]	"Regulation of APC activity by phosphorylation and regulatory factors." Kotani S., Tanaka H., Yasuda H., Todokoro K. J. Cell Biol. 146:791-800(1999) [PubMed: 10459014] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1." Pfleger C.M., Salic A., Lee E., Kirschner M.W. Genes Dev. 15:1759-1764(2001) [PubMed: 11459825] [Abstract] Cited for: INTERACTION WITH MAD2L2.
[12]	"MAD2B is an inhibitor of the anaphase-promoting complex." Chen J., Fang G. Genes Dev. 15:1765-1770(2001) [PubMed: 11459826] [Abstract] Cited for: INTERACTION WITH MAD2L2.
[13]	"Cell cycle-dependent expression of centrosomal ninein-like protein in human cells is regulated by the anaphase-promoting complex." Wang Y., Zhan Q. J. Biol. Chem. 282:17712-17719(2007) [PubMed: 17403670] [Abstract] Cited for: INTERACTION WITH NINL.
[14]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91 AND SER-92, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint." Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M. Cell 134:256-267(2008) [PubMed: 18662541] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION BY CDC14, MUTAGENESIS OF SER-40; THR-121; SER-151 AND SER-163.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; SER-36; SER-40; SER-137; SER-138; SER-146 AND SER-151, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-151, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry." Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M. Mol. Cell 42:511-523(2011) [PubMed: 21596315] [Abstract] Cited for: FUNCTION, INTERACTION WITH USP37.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF102508 mRNA. Translation: AAD26624.1. Sequence problems. AF102507 mRNA. Translation: AAD26623.1. Sequence problems. AB013462 mRNA. Translation: BAA86954.1. AB013463 mRNA. Translation: BAA86955.1. AF080397 mRNA. Translation: AAF20266.1. AF083810 mRNA. Translation: AAD52030.1. AF433157 mRNA. Translation: AAL28117.1. BT007115 mRNA. Translation: AAP35779.1. AC005787 Genomic DNA. Translation: AAC62835.1. AC005786 Genomic DNA. Translation: AAC62836.1. AB033068 mRNA. Translation: BAA86556.1. Different initiation. BC013413 mRNA. Translation: AAH13413.1.
IPI	IPI00043958. IPI00099464. IPI00383919.
RefSeq	NP_001129669.1. NM_001136197.1. NP_001129670.1. NM_001136198.1. NP_057347.2. NM_016263.3.
UniGene	Hs.413133.
3D structure databases
ProteinModelPortal	Q9UM11.
SMR	Q9UM11. Positions 175-474.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38700N.
IntAct	Q9UM11. 16 interactions.
MINT	MINT-1415280.
STRING	Q9UM11.
PTM databases
PhosphoSite	Q9UM11.
Polymorphism databases
DMDM	37537753.
Proteomic databases
PRIDE	Q9UM11.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000395095; ENSP00000378529; ENSG00000105325.
GeneID	51343.
KEGG	hsa:51343.
UCSC	uc002lxt.1. human. uc002lxv.1. human. uc010dtk.1. human.
Organism-specific databases
CTD	51343.
GeneCards	GC19P003473.
HGNC	HGNC:24824. FZR1.
HPA	HPA043536.
MIM	603619. gene.
neXtProt	NX_Q9UM11.
PharmGKB	PA134896003.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13319.
GeneTree	ENSGT00580000081606.
HOVERGEN	HBG001024.
InParanoid	Q9UM11.
OMA	KWSPDNQ.
PhylomeDB	Q9UM11.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9UM11.
Bgee	Q9UM11.
CleanEx	HS_CDH1.
Genevestigator	Q9UM11.
GermOnline	ENSG00000105325. Homo sapiens.
Family and domain databases
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K03364.
Pfam	PF00400. WD40. 5 hits. [Graphical view]
SMART	SM00320. WD40. 6 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 3 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	54790.
SOURCE	Search...

Entry information

Entry name

FZR_HUMAN

Accession

Primary (citable) accession number: Q9UM11
Secondary accession number(s): O75869 , Q86U66, Q96NW8, Q9UI96, Q9ULH8, Q9UM10, Q9UNQ1, Q9Y2T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.