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0TNKS2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionTankyrase 2 (ec (tank2) (tankyrase ii) (tnks-2) (trf1- interacting ankyrin-related adp-ribose polymerase 2) (tankyrase-like protein) (tankyrase-related protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Poly(ADP-ribose) polymerase (PARP) modifies various nuclear proteins by poly(ADP-rybosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation.roliferation and tumor transformation and also in the regulation of the molecularevents involved in the recovery of the cell from DNA damage . Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins.hich decreases their affinity for DNA. The C-terminal catalytic domain of the polymerase is almost always associated with the N-terminal regulatory domain (see ).
  IPR001290:Poly(ADP-ribose) polymerase, catalytic region
This entry represents a second domain related to the SAM domain. Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing protein pathways.
  IPR011510:Sterile alpha motif homology 2
The sterile alpha motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms . SAM domains have been shown to homo- and hetero-oligomerise.orming multiple self-association architectures and also binding to various non-SAM domain-containing proteins .evertheless with a low affinity constant . SAM domains also appear to possess the ability to bind RNA . Smaug a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA binds to the 3 untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain.hich could be the RNA-binding surface. This electropositive potential is unique among all previously determined SAM-domain structures and is conserved among Smaug-SAM homologs. These results suggest that the SAM domain might have a primary role in RNA binding. Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces . In the case of the SAM domain of EphB2.ach of these interfaces is able to form dimers. The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures .
  IPR001660:Sterile alpha motif SAM
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing proteins pathway . SAM domains exhibit a conserved structure.onsisting of a 4-5-helical bundle of two orthogonally packed alpha-hairpins. However SAM domains display a diversity of function.eing involved in interactions with proteins.NA and RNA . The name sterile alpha motif arose from its presence in proteins that are essential for yeast sexual differentiation. The SAM domain has had various names.ncluding SPM.TN (pointed).EP (yeast sterility.ts-related.cG proteins).CR (N-terminal conserved region) and HLH (helix-loop-helix) domain.ll of which are related and can be classified as SAM domains. SAM domains occur in eukaryotic and in some bacterial proteins. Structures have been determined for several proteins that contain SAM domains.ncluding Ets-1 transcription factor.hich plays a role in the development and invasion of tumour cells by regulating the expression of matrix-degrading proteases ; Etv6 transcription factor.ene rearrangements of which have been demonstrated in several malignancies ; EphA4 receptor tyrosine kinase.hich is believed to be important for the correct localization of a motoneuron pool to a specific position in the spinal cord ; EphB2 receptor.hich is involved in spine morphogenesis via intersectin.dc42 and N-Wasp ; p73. p53 homologue involved in neuronal development ; and polyhomeotic.hich is a member of the Polycomb group of genes (Pc-G) required for the maintenance of the spatial expression pattern of homeotic genes .
  IPR013761:Sterile alpha motif-type
SequencesProtein: TNKS2_HUMAN (1166 aa)
mRNA: NM_025235
Local Annotation
Synapse Ontology
sdb:0265 cAMP mediated STP  (Evidence:keywords)
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentK00774
  Level 3 annotation:
    NAD ADP-ribosyltransferase
  Level 2 annotation:
    Other nucleotide metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 193 residues, 93548048-93548626Exon2: 77 residues, 93562719-93562944Exon3: 34 residues, 93566870-93566966Exon4: 14 residues, 93569006-93569043Exon5: 27 residues, 93569218-93569294Exon6: 33 residues, 93569675-93569770Exon7: 24 residues, 93572032-93572099Exon8: 64 residues, 93576753-93576940Exon9: 42 residues, 93578021-93578143Exon10: 32 residues, 93580659-93580751Exon11: 28 residues, 93580839-93580918Exon12: 59 residues, 93583589-93583761Exon13: 28 residues, 93586655-93586735Exon14: 50 residues, 93590297-93590443Exon15: 57 residues, 93591019-93591185Exon16: 75 residues, 93591908-93592128Exon17: 38 residues, 93594655-93594765Exon18: 65 residues, 93595488-93595677Exon19: 86 residues, 93598119-93598372Exon20: 29 residues, 93599248-93599331Exon21: 42 residues, 93600952-93601073Exon22: 34 residues, 93604765-93604863Exon23: 27 residues, 93605350-93605425Exon24: 37 residues, 93607161-93607267Exon25: 64 residues, 93609198-93609385Exon26: 54 residues, 93611735-93611892Exon27: 781 residues, 93612673-93615012Exon28: 2 residues, -Jump to TNKS2_HUMAN  
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