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0CTRO_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCIT
DescriptionCitron rho-interacting kinase (ec 2.7.1.37) (crik) (rho-interacting, serine/threonine-protein kinase 21).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Based on sequence similarities a domain of homology has been identified in the following proteins :Citron and Citron kinase. These two proteins interact with the GTP-bound forms of the small GTPases Rho and Rac but not with Cdc42.Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCKalpha). This serine/threonine kinase interacts with the GTP-bound form of the small GTPase Cdc42 and to a lesser extent with that of Rac.NCK Interacting Kinase (NIK). serine/threonine protein kinase.ROM-1 and ROM-2.rom yeast. These proteins are GDP/GTP exchange proteins (GEPs) for the small GTP binding protein Rho1.This domain.alled the citron homology domain.s often found after cysteine rich and pleckstrin homology (PH) domains at the C-terminal end of the proteins . It acts as a regulatory domain and could be involved in macromolecular interactions .
  IPR001180:Citron-like
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . CAUTION: Despite SMART having created two different HMMs for Serine/Threonine protein kinase and for Tyrosine protein kinase.arge number of proteins match both signatures.s SMART considers it to be natural for these two closely related families.
  IPR002290:Serine/threonine protein kinase
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
Protein kinases are responsible for the phosphorylation of proteins.otentially for regulating their activity. This domain is found in a large variety of protein kinases with different functions and dependencies. Protein kinase C.or example.s a calcium-activated.hospholipid-dependent serine- and threonine-specific enzyme. It is activated by diacylglycerol which.n turn.hosphorylates a range ofcellular proteins. This domain is most often found associated with .
  IPR000961:Protein kinase, C-terminal
Diacylglycerol (DAG) is an important second messenger. Phorbol esters (PE) are analogues of DAG and potent tumor promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases.ollectively known as protein kinase C (PKC) . Phorbol esters can directly stimulate PKC. The N-terminal region of PKC.nown as C1.as been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain.hich is about 50 amino-acid residues long.nd which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
  IPR002219:Protein kinase C, phorbol ester/diacylglycerol binding
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
IPR001180:CNH 
Evalue:-106.638272163982 
Location:1592-1889IPR002290:S_TKc 
Evalue:-87.3565473235138 
Location:97-360IPR000961:S_TK_X 
Evalue:-16.6777807052661 
Location:361-423IPR001849:PH 
Evalue:-14.3098039627075 
Location:1444-1563IPR002219:C1 
Evalue:-8.72124639904717 
Location:1363-1411IPR005479:CPSASE_2 
Evalue:0 
Location:1130-1137
SequencesProtein: CTRO_HUMAN (2027 aa)
mRNA: NM_007174
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK00870
  Level 3 annotation:
    protein kinase
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 823 residues, 118607977-118610443Exon2: 103 residues, 118612338-118612642Exon3: 62 residues, 118619846-118620026Exon4: 28 residues, 118620163-118620242Exon5: 29 residues, 118622932-118623013Exon6: 45 residues, 118623811-118623940Exon7: 38 residues, 118624037-118624146Exon8: 33 residues, 118626550-118626643Exon9: 48 residues, 118630366-118630506Exon10: 47 residues, 118632438-118632574Exon11: 29 residues, 118632727-118632808Exon12: 58 residues, 118634365-118634535Exon13: 37 residues, 118634778-118634883Exon14: 32 residues, 118635390-118635482Exon15: 62 residues, 118635655-118635836Exon16: 48 residues, 118636384-118636522Exon17: 57 residues, 118640432-118640597Exon18: 56 residues, 118640886-118641049Exon19: 38 residues, 118642665-118642773Exon20: 49 residues, 118643496-118643637Exon21: 37 residues, 118650689-118650794Exon22: 47 residues, 118652682-118652818Exon23: 66 residues, 118656351-118656545Exon24: 68 residues, 118657347-118657545Exon25: 20 residues, 118664598-118664652Exon26: 68 residues, 118674237-118674435Exon27: 60 residues, 118679557-118679732Exon28: 38 residues, 118680777-118680887Exon29: 41 residues, 118683125-118683242Exon30: 34 residues, 118689273-118689369Exon31: 44 residues, 118692971-118693097Exon32: 49 residues, 118694956-118695097Exon33: 20 residues, 118697972-118698026Exon34: 19 residues, 118698544-118698595Exon35: 59 residues, 118698858-118699029Exon36: 42 residues, 118704704-118704824Exon37: 50 residues, 118706094-118706238Exon38: 37 residues, 118707146-118707252Exon39: 63 residues, 118725392-118725576Exon40: 53 residues, 118745006-118745160Exon41: 70 residues, 118747351-118747555Exon42: 33 residues, 118754957-118755051Exon43: 49 residues, 118756272-118756415Exon44: 36 residues, 118772360-118772462Exon45: 60 residues, 118779709-118779885Exon46: 49 residues, 118791246-118791388Exon47: 38 residues, 118798259-118798368Exon48: 16 residues, 118799435-118799478Exon49: 2 residues, -Jump to CTRO_HUMANExon1: 822 residues, 118607980-118610443Exon2: 103 residues, 118612338-118612642Exon3: 62 residues, 118619846-118620026Exon4: 28 residues, 118620163-118620242Exon5: 29 residues, 118622932-118623013Exon6: 45 residues, 118623811-118623940Exon7: 38 residues, 118624037-118624146Exon8: 33 residues, 118626550-118626643Exon9: 48 residues, 118630366-118630506Exon10: 47 residues, 118632438-118632574Exon11: 29 residues, 118632727-118632808Exon12: 58 residues, 118634365-118634535Exon13: 37 residues, 118634778-118634883Exon14: 32 residues, 118635390-118635482Exon15: 62 residues, 118635655-118635836Exon16: 48 residues, 118636384-118636522Exon17: 57 residues, 118640432-118640597Exon18: 56 residues, 118640886-118641049Exon19: 38 residues, 118642665-118642773Exon20: 49 residues, 118643496-118643637Exon21: 37 residues, 118650689-118650794Exon22: 47 residues, 118652682-118652818Exon23: 66 residues, 118656351-118656545Exon24: 68 residues, 118657347-118657545Exon25: 20 residues, 118664598-118664652Exon26: 68 residues, 118674237-118674435Exon27: 60 residues, 118679557-118679732Exon28: 38 residues, 118680777-118680887Exon29: 41 residues, 118683125-118683242Exon30: 34 residues, 118689273-118689369Exon31: 49 residues, 118694956-118695097Exon32: 20 residues, 118697972-118698026Exon33: 19 residues, 118698544-118698595Exon34: 59 residues, 118698858-118699029Exon35: 42 residues, 118704704-118704824Exon36: 50 residues, 118706094-118706238Exon37: 37 residues, 118707146-118707252Exon38: 63 residues, 118725392-118725576Exon39: 53 residues, 118745006-118745160Exon40: 70 residues, 118747351-118747555Exon41: 33 residues, 118754957-118755051Exon42: 49 residues, 118756272-118756415Exon43: 36 residues, 118772360-118772462Exon44: 60 residues, 118779709-118779885Exon45: 49 residues, 118791246-118791388Exon46: 38 residues, 118798259-118798368Exon47: 15 residues, 118799435-118799475Exon48: 2 residues, -Jump to CTRO_HUMAN  
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Loci Cluster (Details)Loci: 4079 119017288-119038982 ~-22K 9812(RAB35)(-)Loci: 4080 119132639-119187892 ~-55K 9820(PXN)(-)Loci: 2793 119360286-119362912 ~-3K 9830(COX6A1)(+)Loci: 4081 119383853-119391941 ~-8K 9835(SFRS9)(-)Loci: 2794 119392042-119420680 ~-29K 9836(DNCL1)(+)Loci: 2795 119572753-119589508 ~-17K 9842(CABP1)(+)Loci: 4078 118607977-118799478 ~-192K 9809(CIT)(-)Link out to UCSC