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Database: UniProt
Entry: A0A2R9BFQ3_PANPA
LinkDB: A0A2R9BFQ3_PANPA
Original site: A0A2R9BFQ3_PANPA 
ID   A0A2R9BFQ3_PANPA        Unreviewed;       730 AA.
AC   A0A2R9BFQ3;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cyclin T2 {ECO:0000313|Ensembl:ENSPPAP00000028038.1};
GN   Name=CCNT2 {ECO:0000313|Ensembl:ENSPPAP00000028038.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000028038.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000028038.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; AJFE02079610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02079611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003822851.1; XM_003822803.3.
DR   AlphaFoldDB; A0A2R9BFQ3; -.
DR   STRING; 9597.ENSPPAP00000028038; -.
DR   Ensembl; ENSPPAT00000050882.1; ENSPPAP00000028038.1; ENSPPAG00000037070.1.
DR   GeneID; 100990651; -.
DR   KEGG; pps:100990651; -.
DR   CTD; 905; -.
DR   GeneTree; ENSGT00940000155759; -.
DR   OMA; SCSVKQY; -.
DR   OrthoDB; 4848076at2759; -.
DR   Proteomes; UP000240080; Unplaced.
DR   Bgee; ENSPPAG00000037070; Expressed in cerebellum and 6 other cell types or tissues.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0097322; F:7SK snRNA binding; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0070063; F:RNA polymerase binding; IEA:Ensembl.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR   GO; GO:0019085; P:early viral transcription; IEA:Ensembl.
DR   GO; GO:0019086; P:late viral transcription; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR   CDD; cd20596; CYCLIN_CCNT2_rpt1; 1.
DR   CDD; cd20598; CYCLIN_CCNT2_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR047321; CYCLIN_CCNT2_rpt1.
DR   InterPro; IPR047322; CYCLIN_CCNT2_rpt2.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF43; CYCLIN-T2; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF21797; CycT2-like_C; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT   DOMAIN          42..141
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          154..242
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          341..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..576
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  80999 MW;  FD36738C5128CC6B CRC64;
     MASGRGASSR WFFTREQLEN TPSRRCGVEA DKELSCRQQA ANLIQEMGQR LNVSQLTINT
     AIVYMHRFYM HHSFTKFNKN IISSTALFLA AKVEEQARKL EHVIKVAHAC LHPLEPLLDT
     KCDAYLQQTQ ELVILETIML QTLGFEITIE HPHTDVVKCT QLVRASKDLA QTSYFMATNS
     LHLTTFCLQY KPTVIACVCI HLACKWSNWE IPVSTDGKHW WEYVDPTVTL ELLDELTHEF
     LQILEKTPNR LKKIRNWRAN QAARKPKVDG QVSETPLLGS SLVQNSILVD SVTGVPTNPS
     FQKPSTSAFP APVPLNSGNI SVQDSHTSDN LSMLATGMPS TSYGLSSHQE WPQHQDSART
     EQLYSQKQET SLSGSQYNIN FQQGPSISLH SGLHHRPDKI SDHSSVKQEY THKAGSSKHH
     GPISATPGII PQKMSLDKYR EKRKLETLDL DVRDHYIAAQ VEQQHKQGQS QAASSSSVTS
     PIKMKIPIAN TEKYMADKKE KSGSLKLRIP IPPTDKSASK EELKMKIKVS SSERHSSSDE
     GSGKSKHSSP HISRDHKEKH KEHPSSRHHT SSHKHSHSHS GSSSGGSKHS ADGIPPTVLR
     SPVGLSSDGI SSSSSSSRKR LHVNDASHNH HSKMSKSSKS SGSSSSSSSS VKQYISSHNS
     VFNHPLPPPP PVTYQVGYGH LSTLVKLDKK PVETNGPDAN HEYSTSSQHM DYKDTFDMLD
     SLLSAQGMNM
//
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