Q8BQ33 · TICRR_MOUSE
- ProteinTreslin
- GeneTicrr
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1889 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with TOPBP1 by participating in CDK2-mediated loading of CDC45L onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Biological Process | DNA repair | |
Biological Process | DNA replication | |
Biological Process | mitotic DNA replication checkpoint signaling | |
Biological Process | mitotic G2 DNA damage checkpoint signaling | |
Biological Process | regulation of DNA-templated DNA replication initiation | |
Biological Process | response to ionizing radiation |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTreslin
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8BQ33
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000296624 | 1-1889 | Treslin | |||
Sequence: MACCHKVMLLVDTAGVSAPHSPARRAALRLLTYLSCRFGLARVHWTFKFFDSQGARSRPSRVSDFRELGSRSWEDFEEELEARLGDRPPGAHLPGPTPRATHTHGALMETLLDYQWDRPEITSPTKPILRSSGRRLLDADGEAREAQAALGGFGNAVFLLAPCPHSQRELLQFVSGCEAQAQRVPLTPKQVMEKVLPKRVQEVMIARNITLYWVDTTERSKLWASPDHVGYWTVCELLHHGGGTILPAETWSLGFTKARETVLPCGGELSHKPHPSPWISALPIDATVNCLLYNSEYEASFPRIEGTLFLPVQGKEIEETWAISLEPLAMHQRHFQKPVRIVLRGSVAQWSLPVSSALGTDSWMLQSPEEHRSTQRLLFQELVSRLTAEEFHLVASVDPGEGWPPITGIISPFSANAMILTVFRAKEAEFQSHFLQTAATEGSQDTASLFSDVVDSVLNQSHNLFEDPASSAPCVPEWVQQELSHTSSWSPALVEKWFPFSNASGATSDLMESFWLLHAASPDNDESSKTESELTRCLSELYQRSHEESTVVNQERSRKKRGIPRTPVRQKMNTMSRSLKMLNVARLNVKAQKLHPDGSPDTAVEKGLQKAVIGRTADKLEDRGRILRSSKLKEFKTEEELLAYIHDNYQKAVATEEITLYSCAQNMVSTIKMFLKSKDIKELEVACLSHVNSNLLKTSKTLRQNLAGKMDTEDKVGECQLQVFLRLEMCEQCPSVLDRPDEVERIVEEVTDLLRLVCLTKDSAYLSEFLEEILRLYIGSIPGTIGQLYHSLGLKIPQKLAGVLPTGFFSDDSMSQESMSPPPSSSTHRSVSAITESEQLEELRTRSAKKRRKNALIRHKSIAEISQTLRQIEVPKVSKRATRNENSHSASIQLPVPRKDTIQEVTKVRRNLFNQEMLSPSKRGLKKGLPRSHSVSALECLHHKQDKFKKTKSSTFQGYCKLLTKSVAETPVHKQISRRLLHRQIKGRSSDPGPDIHVVEESPEKEDEMTLRRSPRIKQLSFSRTNSGSFYSVSQPKSRSVQRIHSSQQESEQRENFPVQSIQSPKTLLFGALSEIPSSSKKGSAQIKRSLRSMLDSEISTSYETPKKSNQKSPSFSKTTPRRFPRTAQTLLYTPERLQNSPTEMTSAEGTISEATIKTPSSHGYNSPFASKVTSQKTVSPAKEETSPPLTKLPSTPRESDVQPPQCSSDCTWPHSVNSSPEGPYYPASPPPMAGQARSQCLTPIRYSFRTPPRTALAGTSKQQEHQELPLPRASQTQEPPQGLEKKALKIPKKPAHTSTSPLSPEEHYSGCDVSPHQPRNSLSASPPPGELNWKEHQTSPSVTSSVSCPVPSTPPRTPQRMTCPIPPSPPSKLRRSCRKKSCPPQDFPECHPGPSAAPVLSSATSPGAVTGSREEQSQFSEGQSYLGTGFRSDCHVSSPVLTASDTKCLPLIDEAQLHGLKNQEVKSGILPGEEGEEPESTIADELPSVSDPGILVPAPSSVSSSSELLPYPLCCTADGKQRQDAAQQGSPRASEATSSPQTYEVELEMQASGLPKLRIKKIDPGVLLEAEALGKEAPLGEEGALPALCMPKASKSSGRTEHPYLSPPCLRPSHSTPGKNGGQTFICQSCTPSRCPPSTPSPFQADAGVSWTPSPKQSGKTTPEIIKDWPRRKRAVDCSAGPSAGRGEASMDLPGSLSLLEPEPEGKERSLEQDLSKVLISEEFELEGVCQLPDQSPPKDSASVTEETSWGQFGLGRKRFLSAKEESEYKVKRVCDSLSEDPQASKQKECSPRWSALPLHSVGDDEVFVSGSTPPSGCMVRSCLSASGLQALTQSPLLFQGRTPSSHSTDTRDEEVDVFPSTAEESPFSHTLSRKRPFRTYTRKKLIS | ||||||
Modified residue | 295 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 599 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 820 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 861 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 919 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 934 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1002 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1027 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1078 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1134 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1141 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1406 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 812-836 | Disordered | ||||
Sequence: DSMSQESMSPPPSSSTHRSVSAITE | ||||||
Region | 979-1063 | Disordered | ||||
Sequence: RLLHRQIKGRSSDPGPDIHVVEESPEKEDEMTLRRSPRIKQLSFSRTNSGSFYSVSQPKSRSVQRIHSSQQESEQRENFPVQSIQ | ||||||
Compositional bias | 984-1014 | Basic and acidic residues | ||||
Sequence: QIKGRSSDPGPDIHVVEESPEKEDEMTLRRS | ||||||
Compositional bias | 1016-1063 | Polar residues | ||||
Sequence: RIKQLSFSRTNSGSFYSVSQPKSRSVQRIHSSQQESEQRENFPVQSIQ | ||||||
Compositional bias | 1098-1223 | Polar residues | ||||
Sequence: EISTSYETPKKSNQKSPSFSKTTPRRFPRTAQTLLYTPERLQNSPTEMTSAEGTISEATIKTPSSHGYNSPFASKVTSQKTVSPAKEETSPPLTKLPSTPRESDVQPPQCSSDCTWPHSVNSSPEG | ||||||
Region | 1098-1421 | Disordered | ||||
Sequence: EISTSYETPKKSNQKSPSFSKTTPRRFPRTAQTLLYTPERLQNSPTEMTSAEGTISEATIKTPSSHGYNSPFASKVTSQKTVSPAKEETSPPLTKLPSTPRESDVQPPQCSSDCTWPHSVNSSPEGPYYPASPPPMAGQARSQCLTPIRYSFRTPPRTALAGTSKQQEHQELPLPRASQTQEPPQGLEKKALKIPKKPAHTSTSPLSPEEHYSGCDVSPHQPRNSLSASPPPGELNWKEHQTSPSVTSSVSCPVPSTPPRTPQRMTCPIPPSPPSKLRRSCRKKSCPPQDFPECHPGPSAAPVLSSATSPGAVTGSREEQSQFS | ||||||
Compositional bias | 1254-1282 | Polar residues | ||||
Sequence: RTALAGTSKQQEHQELPLPRASQTQEPPQ | ||||||
Compositional bias | 1315-1351 | Polar residues | ||||
Sequence: SPHQPRNSLSASPPPGELNWKEHQTSPSVTSSVSCPV | ||||||
Compositional bias | 1352-1372 | Pro residues | ||||
Sequence: PSTPPRTPQRMTCPIPPSPPS | ||||||
Compositional bias | 1399-1421 | Polar residues | ||||
Sequence: PVLSSATSPGAVTGSREEQSQFS | ||||||
Region | 1471-1508 | Disordered | ||||
Sequence: LPGEEGEEPESTIADELPSVSDPGILVPAPSSVSSSSE | ||||||
Region | 1520-1543 | Disordered | ||||
Sequence: GKQRQDAAQQGSPRASEATSSPQT | ||||||
Compositional bias | 1522-1543 | Polar residues | ||||
Sequence: QRQDAAQQGSPRASEATSSPQT | ||||||
Region | 1629-1714 | Disordered | ||||
Sequence: QSCTPSRCPPSTPSPFQADAGVSWTPSPKQSGKTTPEIIKDWPRRKRAVDCSAGPSAGRGEASMDLPGSLSLLEPEPEGKERSLEQ | ||||||
Compositional bias | 1644-1662 | Polar residues | ||||
Sequence: FQADAGVSWTPSPKQSGKT | ||||||
Region | 1730-1751 | Disordered | ||||
Sequence: VCQLPDQSPPKDSASVTEETSW | ||||||
Compositional bias | 1737-1751 | Polar residues | ||||
Sequence: SPPKDSASVTEETSW | ||||||
Region | 1841-1875 | Disordered | ||||
Sequence: QGRTPSSHSTDTRDEEVDVFPSTAEESPFSHTLSR |
Sequence similarities
Belongs to the treslin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,889
- Mass (Da)208,335
- Last updated2007-07-24 v2
- ChecksumEF97B85B7BFD3027
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RQ28 | A0A0U1RQ28_MOUSE | Ticrr | 409 | ||
A0A0U1RNX1 | A0A0U1RNX1_MOUSE | Ticrr | 968 | ||
Q3UV49 | Q3UV49_MOUSE | Ticrr | 718 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 3; BAC31045 | ||||
Sequence: V → G | ||||||
Compositional bias | 984-1014 | Basic and acidic residues | ||||
Sequence: QIKGRSSDPGPDIHVVEESPEKEDEMTLRRS | ||||||
Compositional bias | 1016-1063 | Polar residues | ||||
Sequence: RIKQLSFSRTNSGSFYSVSQPKSRSVQRIHSSQQESEQRENFPVQSIQ | ||||||
Compositional bias | 1098-1223 | Polar residues | ||||
Sequence: EISTSYETPKKSNQKSPSFSKTTPRRFPRTAQTLLYTPERLQNSPTEMTSAEGTISEATIKTPSSHGYNSPFASKVTSQKTVSPAKEETSPPLTKLPSTPRESDVQPPQCSSDCTWPHSVNSSPEG | ||||||
Compositional bias | 1254-1282 | Polar residues | ||||
Sequence: RTALAGTSKQQEHQELPLPRASQTQEPPQ | ||||||
Compositional bias | 1315-1351 | Polar residues | ||||
Sequence: SPHQPRNSLSASPPPGELNWKEHQTSPSVTSSVSCPV | ||||||
Compositional bias | 1352-1372 | Pro residues | ||||
Sequence: PSTPPRTPQRMTCPIPPSPPS | ||||||
Compositional bias | 1399-1421 | Polar residues | ||||
Sequence: PVLSSATSPGAVTGSREEQSQFS | ||||||
Sequence conflict | 1513 | in Ref. 3; BAC28152 | ||||
Sequence: P → A | ||||||
Compositional bias | 1522-1543 | Polar residues | ||||
Sequence: QRQDAAQQGSPRASEATSSPQT | ||||||
Compositional bias | 1644-1662 | Polar residues | ||||
Sequence: FQADAGVSWTPSPKQSGKT | ||||||
Compositional bias | 1737-1751 | Polar residues | ||||
Sequence: SPPKDSASVTEETSW |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC114988 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC158582 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC058634 EMBL· GenBank· DDBJ | AAH58634.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC158103 EMBL· GenBank· DDBJ | AAI58104.1 EMBL· GenBank· DDBJ | mRNA | ||
AK033104 EMBL· GenBank· DDBJ | BAC28152.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK041726 EMBL· GenBank· DDBJ | BAC31045.1 EMBL· GenBank· DDBJ | mRNA | ||
AK051639 EMBL· GenBank· DDBJ | BAC34701.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |