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CCNL1_PONAB
ID   CCNL1_PONAB             Reviewed;         172 AA.
AC   Q5RD50;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cyclin-L1;
GN   Name=CCNL1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing. Functions in association with
CC       cyclin-dependent kinases (CDKs). May play a role in the regulation of
CC       RNA polymerase II (pol II). Inhibited by the CDK-specific inhibitor
CC       CDKN1A/p21. {ECO:0000250|UniProtKB:Q9UK58}.
CC   -!- SUBUNIT: Interacts with POLR2A via its hyperphosphorylated C-terminal
CC       domain (CTD) (By similarity). Interacts with CDK11A, CDK11B, CDK12 and
CC       CDK13. May form a ternary complex with CDK11B and casein kinase II
CC       (CKII). Interacts with pre-mRNA-splicing factors, including at least
CC       SRSF1, SRSF2 AND SRSF7/SLU7 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9R1Q2, ECO:0000250|UniProtKB:Q9UK58}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9UK58}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in
CC       nuclear intrachromatin granules clusters (IGC), also called nuclear
CC       speckles, which are storage compartments for nuclear proteins involved
CC       in mRNA processing. {ECO:0000250|UniProtKB:Q9UK58}.
CC   -!- DOMAIN: Contains a RS region (arginine-serine dipeptide repeat) within
CC       the C-terminal domain which is the hallmark of the SR family of
CC       splicing factors. This region probably plays a role in protein-protein
CC       interactions (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR858068; CAH90307.1; -; Transcribed_RNA.
DR   AlphaFoldDB; Q5RD50; -.
DR   SMR; Q5RD50; -.
DR   STRING; 9601.ENSPPYP00000015917; -.
DR   Ensembl; ENSPPYT00000039021; ENSPPYP00000028787; ENSPPYG00000014237.
DR   eggNOG; KOG0835; Eukaryota.
DR   GeneTree; ENSGT00940000159135; -.
DR   InParanoid; Q5RD50; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:UniProt.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR015431; Cyclin_L1.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; PTHR10026; 1.
DR   PANTHER; PTHR10026:SF64; PTHR10026:SF64; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; SSF47954; 1.
PE   3: Inferred from homology;
KW   Cyclin; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..172
FT                   /note="Cyclin-L1"
FT                   /id="PRO_0000080483"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..168
FT                   /note="Cyclin-like"
SQ   SEQUENCE   172 AA;  18322 MW;  972B0E52D25720E1 CRC64;
     MASGPHSTAT AAAAASSAAP SAGGSSSGTT TTTTTTTGGI LIGDRLYSEV SLTIDHSLIP
     EERLSPTPSM QDGLDLPSET DLRILGCELI QAAGILLRLP QVAMATGQVL FHRFFYSKSF
     VKHSFEIVAM ACINLASKIE EAPRRIRDVI NVFHHLRQLR GKSDQLHLPK PG
 
 
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