Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fizzy-related protein homolog

Gene

FZR1

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

Functioni

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.3 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9UM11.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Fizzy-related protein homolog
Short name:
Fzr
Alternative name(s):
CDC20-like protein 1
Cdh1/Hct1 homolog
Short name:
hCDH1
Gene namesi
Name:FZR1
Synonyms:CDH1, FYR, FZR, KIAA1242
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:24824. FZR1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401S → A: Constitutively active; when associated with A-121; A-151 and A-163. 1 Publication
Mutagenesisi121 – 1211T → A: Constitutively active; when associated with A-40; A-151 and A-163. 1 Publication
Mutagenesisi151 – 1511S → A: Constitutively active; when associated with A-40; A-121 and A-163. 1 Publication
Mutagenesisi163 – 1631S → A: Constitutively active; when associated with A-40; A-121 and A-151. 1 Publication

Organism-specific databases

PharmGKBiPA134896003.

Polymorphism and mutation databases

BioMutaiFZR1.
DMDMi37537753.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Fizzy-related protein homologPRO_0000051001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphothreonineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei69 – 691N6-acetyllysine1 Publication
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei151 – 1511PhosphoserineCombined sources
Modified residuei159 – 1591N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated. Deacetylated by SIRT2 at Lys-69 and Lys-159; deacetylation enhances the interaction of FZR1 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C).1 Publication
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. Phosphorylated by MAK.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UM11.
PaxDbiQ9UM11.
PeptideAtlasiQ9UM11.
PRIDEiQ9UM11.

PTM databases

iPTMnetiQ9UM11.
PhosphoSiteiQ9UM11.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9UM11.
CleanExiHS_CDH1.
ExpressionAtlasiQ9UM11. baseline and differential.
GenevisibleiQ9UM11. HS.

Organism-specific databases

HPAiHPA043536.

Interactioni

Subunit structurei

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 SIRT2 and USP37. Interacts (via WD repeats) with MAK.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC27P302608EBI-724997,EBI-994813
CLSPNQ9HAW44EBI-724997,EBI-1369377
MAD2L2Q9UI952EBI-724997,EBI-77889
MAKP207947EBI-724997,EBI-3911321
RAD17O759432EBI-724997,EBI-968231
RRM2P313502EBI-724997,EBI-2339245
SIRT2Q8IXJ6-22EBI-724997,EBI-5240785
SKP2Q133092EBI-724997,EBI-456291
VHLP403372EBI-724997,EBI-301246
VHLP40337-12EBI-724997,EBI-3504450
VHLP40337-32EBI-724997,EBI-301270

Protein-protein interaction databases

BioGridi119489. 138 interactions.
DIPiDIP-38700N.
IntActiQ9UM11. 29 interactions.
MINTiMINT-1415280.
STRINGi9606.ENSP00000378529.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60R1-496[»]
ProteinModelPortaliQ9UM11.
SMRiQ9UM11. Positions 42-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati182 – 22241WD 1Add
BLAST
Repeati227 – 26640WD 2Add
BLAST
Repeati269 – 30638WD 3Add
BLAST
Repeati311 – 35040WD 4Add
BLAST
Repeati353 – 39543WD 5Add
BLAST
Repeati397 – 43842WD 6Add
BLAST
Repeati441 – 48040WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat CDC20/Fizzy family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0305. Eukaryota.
ENOG410XQ8I. LUCA.
GeneTreeiENSGT00840000129804.
HOVERGENiHBG001024.
InParanoidiQ9UM11.
KOiK03364.
OMAiIEKSHNQ.
OrthoDBiEOG76X602.
PhylomeDBiQ9UM11.
TreeFamiTF101066.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024977. Apc4_WD40_dom.
IPR033010. Cdc20/Fizzy.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19918. PTHR19918. 1 hit.
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UM11-1) [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
MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP
60 70 80 90 100
SRAGANWSVN FHRINENEKS PSQNRKAKDA TSDNGKDGLA YSALLKNELL
110 120 130 140 150
GAGIEKVQDP QTEDRRLQPS TPEKKGLFTY SLSTKRSSPD DGNDVSPYSL
160 170 180 190 200
SPVSNKSQKL LRSPRKPTRK ISKIPFKVLD APELQDDFYL NLVDWSSLNV
210 220 230 240 250
LSVGLGTCVY LWSACTSQVT RLCDLSVEGD SVTSVGWSER GNLVAVGTHK
260 270 280 290 300
GFVQIWDAAA GKKLSMLEGH TARVGALAWN AEQLSSGSRD RMILQRDIRT
310 320 330 340 350
PPLQSERRLQ GHRQEVCGLK WSTDHQLLAS GGNDNKLLVW NHSSLSPVQQ
360 370 380 390 400
YTEHLAAVKA IAWSPHQHGL LASGGGTADR CIRFWNTLTG QPLQCIDTGS
410 420 430 440 450
QVCNLAWSKH ANELVSTHGY SQNQILVWKY PSLTQVAKLT GHSYRVLYLA
460 470 480 490
MSPDGEAIVT GAGDETLRFW NVFSKTRSTK VKWESVSVLN LFTRIR
Length:496
Mass (Da):55,179
Last modified:October 3, 2003 - v2
Checksum:iF6C8FDAF81D8103A
GO
Isoform 2 (identifier: Q9UM11-2) [UniParc]FASTAAdd to basket

Also known as: CDH1alpha, Fzr1

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

Note: Major.
Show »
Length:493
Mass (Da):54,766
Checksum:i7C6A947EBB8A6D5C
GO
Isoform 3 (identifier: Q9UM11-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:404
Mass (Da):44,874
Checksum:iA793194D88777035
GO

Sequence cautioni

The sequence AAD26623.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAD26624.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAA86556.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591A → S in AAF20266 (Ref. 3) Curated
Sequence conflicti275 – 2751G → W in AAF20266 (Ref. 3) Curated
Sequence conflicti326 – 3261Q → H in BAA86954 (Ref. 2) Curated
Sequence conflicti326 – 3261Q → H in BAA86955 (Ref. 2) Curated
Sequence conflicti341 – 3411N → I in AAF20266 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 21889Missing in isoform 3. 2 PublicationsVSP_008503Add
BLAST
Alternative sequencei481 – 4833Missing in isoform 2 and isoform 3. 7 PublicationsVSP_008504

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12109.1. [Q9UM11-2]
CCDS45916.1. [Q9UM11-1]
CCDS45917.1. [Q9UM11-3]
RefSeqiNP_001129669.1. NM_001136197.1. [Q9UM11-3]
NP_001129670.1. NM_001136198.1. [Q9UM11-1]
NP_057347.2. NM_016263.3. [Q9UM11-2]
XP_005259630.1. XM_005259573.3. [Q9UM11-1]
UniGeneiHs.413133.

Genome annotation databases

EnsembliENST00000313639; ENSP00000321800; ENSG00000105325. [Q9UM11-3]
ENST00000395095; ENSP00000378529; ENSG00000105325. [Q9UM11-1]
ENST00000441788; ENSP00000410369; ENSG00000105325. [Q9UM11-2]
GeneIDi51343.
KEGGihsa:51343.
UCSCiuc002lxt.3. human. [Q9UM11-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12109.1. [Q9UM11-2]
CCDS45916.1. [Q9UM11-1]
CCDS45917.1. [Q9UM11-3]
RefSeqiNP_001129669.1. NM_001136197.1. [Q9UM11-3]
NP_001129670.1. NM_001136198.1. [Q9UM11-1]
NP_057347.2. NM_016263.3. [Q9UM11-2]
XP_005259630.1. XM_005259573.3. [Q9UM11-1]
UniGeneiHs.413133.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60R1-496[»]
ProteinModelPortaliQ9UM11.
SMRiQ9UM11. Positions 42-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119489. 138 interactions.
DIPiDIP-38700N.
IntActiQ9UM11. 29 interactions.
MINTiMINT-1415280.
STRINGi9606.ENSP00000378529.

PTM databases

iPTMnetiQ9UM11.
PhosphoSiteiQ9UM11.

Polymorphism and mutation databases

BioMutaiFZR1.
DMDMi37537753.

Proteomic databases

MaxQBiQ9UM11.
PaxDbiQ9UM11.
PeptideAtlasiQ9UM11.
PRIDEiQ9UM11.

Protocols and materials databases

DNASUi51343.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313639; ENSP00000321800; ENSG00000105325. [Q9UM11-3]
ENST00000395095; ENSP00000378529; ENSG00000105325. [Q9UM11-1]
ENST00000441788; ENSP00000410369; ENSG00000105325. [Q9UM11-2]
GeneIDi51343.
KEGGihsa:51343.
UCSCiuc002lxt.3. human. [Q9UM11-1]

Organism-specific databases

CTDi51343.
GeneCardsiFZR1.
HGNCiHGNC:24824. FZR1.
HPAiHPA043536.
MIMi603619. gene.
neXtProtiNX_Q9UM11.
PharmGKBiPA134896003.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0305. Eukaryota.
ENOG410XQ8I. LUCA.
GeneTreeiENSGT00840000129804.
HOVERGENiHBG001024.
InParanoidiQ9UM11.
KOiK03364.
OMAiIEKSHNQ.
OrthoDBiEOG76X602.
PhylomeDBiQ9UM11.
TreeFamiTF101066.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9UM11.

Miscellaneous databases

ChiTaRSiFZR1. human.
GeneWikiiFZR1.
GenomeRNAii51343.
PROiQ9UM11.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UM11.
CleanExiHS_CDH1.
ExpressionAtlasiQ9UM11. baseline and differential.
GenevisibleiQ9UM11. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024977. Apc4_WD40_dom.
IPR033010. Cdc20/Fizzy.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR19918. PTHR19918. 1 hit.
PfamiPF12894. ANAPC4_WD40. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NINL.
  14. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION BY CDC14, MUTAGENESIS OF SER-40; THR-121; SER-151 AND SER-163.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; SER-36; SER-138; SER-146 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH USP37.
  19. "SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity."
    Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I., Gius D., Deng C.X.
    Cancer Cell 20:487-499(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-69 AND LYS-159, DEACETYLATION BY SIRT2, INTERACTION WITH SIRT2.
  20. "Male germ cell-associated kinase is overexpressed in prostate cancer cells and causes mitotic defects via deregulation of APC/C(CDH1)."
    Wang L.Y., Kung H.J.
    Oncogene 31:2907-2918(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAK, PHOSPHORYLATION.
  21. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-138 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiFZR_HUMAN
AccessioniPrimary (citable) accession number: Q9UM11
Secondary accession number(s): O75869
, Q86U66, Q96NW8, Q9UI96, Q9ULH8, Q9UM10, Q9UNQ1, Q9Y2T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: July 6, 2016
This is version 157 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.