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Information on EC 2.7.11.35 - CRIK-subfamily protein kinase
for references in articles please use BRENDA:EC2.7.11.35
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.11 Protein-serine/threonine kinases
2.7.11.35 CRIK-subfamily protein kinase
IUBMB Comments
Requires Mg2+. Peptide array data show a preference for phosphorylation of Thr over Ser and a preference for basic residues in the -5 to -1 positions . CRIK is an animal-specific protein kinase that phosphorylates myosin light chain (cf. EC 2.7.11.18, myosin-light-chain kinase) and is involved in cytokinesis in both mammals and Drosophila. Human CRIK phosphorylates myosin light chain, MYL9/MRLC1 on T19/S20 and GLI2 on S149 . Drosophila CRIK (sticky) interacts with the kinesins Nebbish and Pavarotti, and human CRIK interacts with their orthologs, KIF14 and KIF23/MKLP1 to promote midbody formation during cytokinesis . In Drosophila, CRIK/Sticky catalytic activity was required for this function. Human CRIK is mostly highly expressed in brain, and mutations that alter splicing or kinase activity lead to microcephaly [5, 6], as do knockouts in mouse and rat, and mutations in its interacting partner, the kinesin KIF14 .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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=
+
[protein]-O-phospho-L-serine
+
=
+
[protein]-O-phospho-L-threonine
Synonyms
alpha-citron kinase, cit, CIT kinase, CIT-K, CITK, Citron, Citron K, Citron kinase, Citron Rho-Interacting Kinase, citron rho-interacting serine/threonine kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cit
CIT-K
Citron
Citron kinase
Citron Rho-Interacting Kinase
citron rho-interacting serine/threonine kinase
Citron-K
Citron-Kinase
CRIK
SGK21
-
-
-
-
Sticky/Citron Kinase
-
-
-
-
cit
-
-
-
-
Citron
-
-
-
-
Citron kinase
-
-
Citron Rho-Interacting Kinase
-
-
-
-
Citron-K
-
-
-
-
CRIK
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [protein]-L-serine = ADP + [protein]-O-phospho-L-serine
(1)
-
-
-
ATP + [protein]-L-threonine = ADP + [protein]-O-phospho-L-threonine
(2)
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
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ATP + [endothelial nitric oxide synthase]-L-threonine497
ADP + [endothelial nitric oxide synthase]-O-phospho-L-threonine497
-
Substrates: the enzyme mediates arsenite-induced decrease in endothelial nitric oxide synthase activity by increasing phosphorylation at threonine 497
Products: -
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ATP + [GLI2 protein]-L-serine149
ADP + [GLI2 protein]-O-phospho-L-serine149
-
Substrates: -
Products: -
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ATP + [myosin II regulatory light chain]-(L-threonine18)-(O-phospho-L-serine19)
ADP + [myosin II regulatory light chain]-(O-phospho-L-threonine18)-(O-phospho-L-serine19)
-
Substrates: -
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ATP + [myosin II regulatory light chain]-L-serine19
ADP + [myosin II regulatory light chain]-O-phospho-L-serine19
-
Substrates: -
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ATP + [regulatory myosin light chain]-L-serine19
ADP + [regulatory myosin light chain]-O-phospho-L-serine19
ATP + [regulatory myosin light chain]-L-threonine18
ADP + [regulatory myosin light chain]-O-phospho-L-threonine18
ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
Substrates: -
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ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
-
Substrates: -
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ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
Substrates: -
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ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
Substrates: -
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ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
Substrates: -
Products: -
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ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
-
Substrates: -
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ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
Substrates: -
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ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
Substrates: -
Products: -
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ATP + [regulatory myosin light chain]-L-serine19
ADP + [regulatory myosin light chain]-O-phospho-L-serine19
Substrates: -
Products: -
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ATP + [regulatory myosin light chain]-L-serine19
ADP + [regulatory myosin light chain]-O-phospho-L-serine19
Substrates: -
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ATP + [regulatory myosin light chain]-L-threonine18
ADP + [regulatory myosin light chain]-O-phospho-L-threonine18
Substrates: -
Products: -
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?
ATP + [regulatory myosin light chain]-L-threonine18
ADP + [regulatory myosin light chain]-O-phospho-L-threonine18
Substrates: -
Products: -
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additional information
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-
-
Substrates: KIF14 is required for the localization of the enzyme
Products: -
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additional information
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-
-
Substrates: the enzyme is capable of physically and functionally interacting with the actin-binding protein anillin
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additional information
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-
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Substrates: the enzyme interacts with BCAR4-protein
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additional information
?
-
Substrates: the enzyme does not phosphorylate myosin phosphatases
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additional information
?
-
-
Substrates: the enzyme does not phosphorylate the myosin binding subunit of myosin phosphatase
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additional information
?
-
Substrates: the enzyme does not phosphorylate myosin phosphatases
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
-
Substrates: -
Products: -
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?
ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-serine
ADP + [protein]-O-phospho-L-serine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-L-threonine
ADP + [protein]-O-phospho-L-threonine
Substrates: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
specifically expressed in mouse primary keratinocytes
brenda
enzyme levels of mRNA and protein are highest in embryonic liver and gradually decrease after birth
brenda
enzyme levels of mRNA and protein are highest in embryonic liver and gradually decrease after birth
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is dispersed to the cytoplasm in prometaphase and associated with midzone spindles by a Rho-independent signal. Rho is then activated, binds to the enzyme and translocates it to cell cortex, where the complex is then concentrated in the cleavage furrow by the action of actin cytoskeleton beneath the equator of dividing cells
brenda
the full-length enzyme localizes in corpuscular cytoplasmic structures
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
truncating enzyme mutations cause severe primary microcephaly
malfunction
enzyme deficiency triggers apoptosis in a small subset of embryonic liver cells. Enzyme loss causes a significant increase of G2 tetraploid nuclei in one-week-old liver
malfunction
enzyme deficiency triggers apoptosis in a small subset of embryonic liver cells. Enzyme loss causes a significant increase of G2 tetraploid nuclei in one-week-old liver
malfunction
-
enzyme depletion accelerates loss of F-actin proteins at the midbody and subsequent cytokinesis defects are reversed by restoring actin polymerization
malfunction
-
enzyme mutations are linked to the development of human microcephaly. Enzyme depletion causes failure of cytokinesis and dramatically decreased cell proliferation in a large panel of breast, cervical and colorectal cancer cell lines
malfunction
-
enzyme knockout mice display a dramatic testicular impairment, with embryonic and postnatal loss of undifferentiated germ cells and complete absence of mature spermatocyte. By contrast, the ovaries of mutant females appear essentially normal. Mutant cells display a severe cytokinesis defect, resulting in the production of multinucleated cells and apoptosis
malfunction
recessively inherited pathogenic variants of the enzyme are the genetic basis of severe microcephaly and neonatal death
malfunction
the flathead mutation is caused by a single base deletion in exon 1 of the enzyme gene leading to cytokinesis failure with dramatically reduced brain size
malfunction
-
flies bearing mutations in the enzyme gene are defective in both neuroblast and spermatocyte cytokinesis. Late telophases of both cell types display persistent midbodies associated with disorganized F actin and anillin structures
malfunction
-
overexpression of enzyme mutants results in the production of multinucleate cells. A kinase-active mutant causes abnormal contraction during cytokinesis
malfunction
-
enzyme knockdown in pancreatic ductal adenocarcinoma cells reduces the expression of cyclophilin A
malfunction
-
corticocollicular and callosally-projecting cortical pyramidal neurons of enzyme knockout mice display specific abnormalities of their dendritic arborizations
malfunction
-
postnatal neurogenesis in the dentate gyrus is eliminated by loss of enzyme function. Loss of enzyme function causes deficits in mitosis and an increase in apoptosis
malfunction
-
mutant enzyme larval brains contain polyploid and multinucleate cells
physiological function
the enzyme is an effector of the Rho signaling that is required for cytokinesis specifically in proliferating neuroprogenitors, as well as for postnatal brain development
physiological function
the enzyme regulates the G2/M transition in hepatocytes but is not essential for cytokinesis in hepatocytes
physiological function
the enzyme regulates the G2/M transition in hepatocytes but is not essential for cytokinesis in hepatocytes
physiological function
-
the enzyme enhances murine leukemia virion and HIV-1 virion production by modulating exocytosis
physiological function
-
the enzyme is required for KIF14 localization to the midbody and cytokinesis
physiological function
-
the enzyme is required for localization of F-actin and ANLN at the abscission sites, as well as for CHMP4B recruitment
physiological function
-
the enzyme activity is essential for brain development and cytokinesis
physiological function
-
the enzyme is specifically required for cytokinesis of the male germ line
physiological function
the enzyme is critical to building a normally sized human brain. The enzyme localizes to the cleavage furrow and midbody of mitotic cells, where it is required for the completion of cytokinesis
physiological function
the enzyme acts with RhoA to ensure the progression of cytokinesis in neuronal progenitors
physiological function
-
the enzyme is required for abscission at the end of cytokinesis
physiological function
-
the enzyme is a cytokinesis-specific upstream regulator of active RhoA that is specifically required for abscission during late cytokinesis. Overexpression of the enzyme and anillin leads to abscission delay. The enzyme is a crucial abscission regulator that may promote midbody stability through active RhoA and anillin
physiological function
-
the enzyme regulates cytokinesis at a step after Rho in the contractile process
physiological function
-
the enzyme acts at the top of the midbody-formation hierarchy by connecting and regulating a molecular network of contractile ring components and microtubule-associated proteins
physiological function
-
the enzyme plays both structural and regulatory roles in midbody formation. The enzyme recruits Nebbish (kinesin family member 14 ortholog) to the cleavage furrow, and both proteins are required for midbody formation and proper localization of Pavarotti (mitotic kinesin-like protein 1 ortholog) and Fascetto (protein regulator of cytokinesis 1 ortholog)
physiological function
-
the enzyme promotes ubiquitination of human immunodeficiency virus (HIV)-1 Gag protein. The enzyme interacts with HIV-1 Gag protein and causes budding of viral particles into the intracellular endosomal compartment
physiological function
-
the enzyme promotes the HIF1a-CypA signaling and growth of pancreatic ductal adenocarcinoma cells. Enzyme overexpression in pancreatic ductal adenocarcinoma cells promotes the expression of cyclophilin A
physiological function
-
the enzyme regulates neuronal differentiation. The enzyme is involved in the morphologic differentiation of N1E-115 neuroblastoma cells induced by serum starvation
physiological function
-
the enzyme is required for postnatal neurogenesis in the hippocampus
physiological function
-
the enzyme is required for cytokinesis and is an essential effector kinase of Pbl-RhoA signalling pathway in vivo
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D230V
the mutation impairs the kinase activity of the enzyme and causes primary microcephaly
G106V
the mutation impairs the kinase activity of the enzyme and causes primary microcephaly
K126A
K126Q
the mutation impairs the kinase activity of the enzyme and causes primary microcephaly
K126A
the mutation impairs the kinase activity of the enzyme and causes primary microcephaly
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is higher in pancreatic ductal adenocarcinoma cells compared with the normal epithelial cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
high enzyme expression in pancreatic ductal adenocarcinoma predicts poor overall and disease-free survival
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gruneberg, U.; Neef, R.; Li, X.; Chan, E.H.; Chalamalasetty, R.B.; Nigg, E.A.; Barr, F.A.
KIF14 and citron kinase act together to promote efficient cytokinesis
J. Cell Biol.
172
363-372
2006
Homo sapiens
brenda
Li, H.; Bielas, S.L.; Zaki, M.S.; Ismail, S.; Farfara, D.; Um, K.; Rosti, R.O.; Scott, E.C.; Tu, S.; Chi, N.C.; Gabriel, S.; Erson-Omay, E.Z.; Ercan-Sencicek, A.G.; Yasuno, K.; Caglayan, A.O.; Kaymakcalan, H.; Ekici, B.; Bilguvar, K.; Gunel, M.; Gleeson, J.G.
Biallelic mutations in citron kinase link mitotic cytokinesis to human primary microcephaly
Am. J. Hum. Genet.
99
501-510
2016
Homo sapiens (O14578)
brenda
Harding, B.N.; Moccia, A.; Drunat, S.; Soukarieh, O.; Tubeuf, H.; Chitty, L.S.; Verloes, A.; Gressens, P.; El Ghouzzi, V.; Joriot, S.; Di Cunto, F.; Martins, A.; Passemard, S.; Bielas, S.L.
Mutations in citron kinase cause recessive microlissencephaly with multinucleated neurons
Am. J. Hum. Genet.
99
511-520
2016
Homo sapiens (O14578)
brenda
Ding, J.; Zhao, J.; Sun, L.; Mi, Z.; Cen, S.
Citron kinase enhances ubiquitination of HIV-1 Gag protein and intracellular HIV-1 budding
Arch. Virol.
161
2441-2448
2016
Homo sapiens
brenda
Cong, L.; Bai, Z.; Du, Y.; Cheng, Y.
Citron Rho-interacting serine/threonine kinase promotes HIF1a-CypA signaling and growth of human pancreatic adenocarcinoma
BioMed Res. Int.
2020
9210891
2020
Homo sapiens
brenda
Di Cunto, F.; Ferrara, L.; Curtetti, R.; Imarisio, S.; Guazzone, S.; Broccoli, V.; Bulfone, A.; Altruda, F.; Vercelli, A.; Silengo, L.
Role of citron kinase in dendritic morphogenesis of cortical neurons
Brain Res. Bull.
60
319-327
2003
Homo sapiens
brenda
Xing, Z.; Lin, A.; Li, C.; Liang, K.; Wang, S.; Liu, Y.; Park, P.K.; Qin, L.; Wei, Y.; Hawke, D.H.; Hung, M.C.; Lin, C.; Yang, L.
lncRNA directs cooperative epigenetic regulation downstream of chemokine signals
Cell
159
1110-1125
2014
Homo sapiens
brenda
Ackman, J.B.; Ramos, R.L.; Sarkisian, M.R.; Loturco, J.J.
Citron kinase is required for postnatal neurogenesis in the hippocampus
Dev. Neurosci.
29
113-123
2007
Rattus norvegicus
brenda
Shandala, T.; Gregory, S.L.; Dalton, H.E.; Smallhorn, M.; Saint, R.
Citron kinase is an essential effector of the Pbl-activated Rho signalling pathway in Drosophila melanogaster
Development
131
5053-5063
2004
Drosophila melanogaster
brenda
Seo, J.; Cho, D.H.; Lee, H.J.; Sung, M.S.; Lee, J.Y.; Won, K.J.; Park, J.H.; Jo, I.
Citron Rho-interacting kinase mediates arsenite-induced decrease in endothelial nitric oxide synthase activity by increasing phosphorylation at threonine 497 Mechanism underlying arsenite-induced vascular dysfunction
Free Radic. Biol. Med.
90
133-144
2016
Rattus norvegicus
brenda
Shaheen, R.; Hashem, A.; Abdel-Salam, G.M.; Al-Fadhli, F.; Ewida, N.; Alkuraya, F.S.
Mutations in CIT, encoding citron rho-interacting serine/threonine kinase, cause severe primary microcephaly in humans
Hum. Genet.
135
1191-1197
2016
Homo sapiens (O14578)
brenda
Di Cunto, F.; Calautti, E.; Hsiao, J.; Ong, L.; Topley, G.; Turco, E.; Dotto, G.P.
Citron rho-interacting kinase, a novel tissue-specific Ser/Thr kinase encompassing the Rho-Rac-binding protein Citron
J. Biol. Chem.
273
29706-29711
1998
Mus musculus (P49025)
brenda
Liu, H.; Di Cunto, F.; Imarisio, S.; Reid, L.M.
Citron kinase is a cell cycle-dependent, nuclear protein required for G2/M transition of hepatocytes
J. Biol. Chem.
278
2541-2548
2003
Rattus norvegicus (E9PSL7), Mus musculus (P49025)
brenda
Eda, M.; Yonemura, S.; Kato, T.; Watanabe, N.; Ishizaki, T.; Madaule, P.; Narumiya, S.
Rho-dependent transfer of Citron-kinase to the cleavage furrow of dividing cells
J. Cell Sci.
114
3273-3284
2001
Homo sapiens
brenda
Cunto, F.D.; Imarisio, S.; Camera, P.; Boitani, C.; Altruda, F.; Silengo, L.
Essential role of citron kinase in cytokinesis of spermatogenic precursors
J. Cell Sci.
115
4819-4826
2002
Mus musculus
brenda
D'Avino, P.P.
Citron kinase - renaissance of a neglected mitotic kinase
J. Cell Sci.
130
1701-1708
2017
Homo sapiens
brenda
Dema, A.; Macaluso, F.; Sgro, F.; Berto, G.E.; Bianchi, F.T.; Chiotto, A.A.; Pallavicini, G.; Di Cunto, F.; Gai, M.
Citron kinase-dependent F-actin maintenance at midbody secondary ingression sites mediates abscission
J. Cell Sci.
131
jcs209080
2018
Homo sapiens
brenda
Sarkisian, M.; Li, W.; Di Cunto, F.; DMello, S.; LoTurco, J.
Citron-kinase, a protein essential to cytokinesis in neuronal progenitors, is deleted in the flathead mutant rat
J. Neurosci.
22
RC217
2002
Rattus norvegicus (E9PSL7)
brenda
Yamashiro, S.; Totsukawa, G.; Yamakita, Y.; Sasaki, Y.; Madaule, P.; Ishizaki, T.; Narumiya, S.; Matsumura, F.
Citron kinase, a Rho-dependent kinase, induces di-phosphorylation of regulatory light chain of myosin II
Mol. Biol. Cell
14
1745-1756
2003
Mus musculus
brenda
Naim, V.; Imarisio, S.; Di Cunto, F.; Gatti, M.; Bonaccorsi, S.
Drosophila citron kinase is required for the final steps of cytokinesis
Mol. Biol. Cell
15
5053-5063
2004
Drosophila melanogaster
brenda
Gai, M.; Camera, P.; Dema, A.; Bianchi, F.; Berto, G.; Scarpa, E.; Germena, G.; Di Cunto, F.
Citron kinase controls abscission through RhoA and anillin
Mol. Biol. Cell
22
3768-3778
2011
Homo sapiens
brenda
Madaule, P.; Eda, M.; Watanabe, N.; Fujisawa, K.; Matsuoka, T.; Bito, H.; Ishizaki, T.; Narumiya, S.
Role of citron kinase as a target of the small GTPase Rho in cytokinesis
Nature
394
491-494
1998
Homo sapiens
brenda
Johnson, J.L.; Yaron, T.M.; Huntsman, E.M.; Kerelsky, A.; Song, J.; Regev, A.; Lin, T.Y.; Liberatore, K.; Cizin, D.M.; Cohen, B.M.; Vasan, N.; Ma, Y.; Krismer, K.; Robles, J.T.; van de Kooij, B.; van Vlimmeren, A.E.; Andree-Busch, N.; Kaeufer, N.F.; Dorovkov, M.V.; Ryazanov, A.G.; Takagi, Y.; Kastenhuber, E.R.; Goncalves, M.D.; Hopkins, B.D.; Elemento, O.; Taatjes, D.J.; Maucuer, A.; Yamashita, A.; Degterev, A.; Uduman, M.; Lu, J.; Landry, S.D.; Zhang, B.; Cossentino, I.; Linding, R.; Blenis, J.; Hornbeck, P.V.; Turk, B.E.; Yaffe, M.B.; Cantley, L.C.
An atlas of substrate specificities for the human serine/threonine kinome
Nature
613
759-766
2023
Homo sapiens
brenda
Bassi, Z.I.; Audusseau, M.; Riparbelli, M.G.; Callaini, G.; DAvino, P.P.
Citron kinase controls a molecular network required for midbody formation in cytokinesis
Proc. Natl. Acad. Sci. USA
110
9782-9787
2013
Homo sapiens, Drosophila melanogaster
brenda
Loomis, R.J.; Holmes, D.A.; Elms, A.; Solski, P.A.; Der, C.J.; Su, L.
Citron kinase, a RhoA effector, enhances HIV-1 virion production by modulating exocytosis
Traffic
7
1643-1653
2006
Homo sapiens
brenda
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