CUL1_PONAB
ID CUL1_PONAB Reviewed; 776 AA.
AC Q5R4G6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Cullin-1;
DE Short=CUL-1;
GN Name=CUL1;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
CC F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the
CC ubiquitination of proteins involved in cell cycle progression, signal
CC transduction and transcription. SCF complexes and ARIH1 collaborate in
CC tandem to mediate ubiquitination of target proteins. In the SCF
CC complex, serves as a rigid scaffold that organizes the SKP1-F-box
CC protein and RBX1 subunits. May contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme. The
CC E3 ubiquitin-protein ligase activity of the complex is dependent on the
CC neddylation of the cullin subunit and exchange of the substrate
CC recognition component is mediated by TIP120A/CAND1. The functional
CC specificity of the SCF complex depends on the F-box protein as
CC substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct
CC ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11)
CC directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs
CC ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and
CC probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of
CC CEP68. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip
CC and is involved in regulation of G1/S transition. SCF(SKP2) directs
CC ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and
CC probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E,
CC NOTCH1 released notch intracellular domain (NICD), and probably PSEN1.
CC SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs
CC ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and
CC DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs
CC ubiquitination of BCL6 and DTL but does not seem to direct
CC ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA
CC at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-
CC RELA dimer to translocate into the nucleus and to activate
CC transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3)
CC and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9)
CC directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs
CC ubiquitination of BCL2. Interacts with COPS9. Interacts with KAT7,
CC probably as part of an SCF complex; the interaction mediates KAT7
CC ubiquitination. {ECO:0000250|UniProtKB:Q13616,
CC ECO:0000250|UniProtKB:Q9WTX6}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q13616}.
CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-
CC box domain-containing protein as substrate-specific subunit. Component
CC of the SCF(FBXW11) complex containing FBXW11. Component of the
CC SCF(SKP2) complex containing SKP2, in which it interacts directly with
CC SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing
CC FBXW2. Component of the SCF(FBXO32) complex containing FBXO32.
CC Component of the probable SCF(FBXO7) complex containing FBXO7.
CC Component of the SCF(FBXO10) complex containing FBXO10. Component of
CC the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25)
CC complex containing FBXO25. Component of the SCF(FBXO33) complex
CC containing FBXO33. Component of the probable SCF(FBXO4) complex
CC containing FBXO4. Component of the SCF(FBXO44) complex, composed of
CC SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of
CC SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of
CC a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a
CC SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2.
CC Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and
CC FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1
CC and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1,
CC RBX1, SKP1 and CCNF (By similarity). Interacts with CCNF (By
CC similarity). Component of the SCF(FBXL3) complex composed of CUL1,
CC SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of
CC CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of
CC CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of
CC CUL1, SKP1, RBX1 and FBXW7. Interacts with CHEK2; mediates CHEK2
CC ubiquitination and regulates its function. Part of a complex with
CC TIP120A/CAND1 and RBX1. The unneddylated form interacts with
CC TIP120A/CAND1 and the interaction mediates the exchange of the F-box
CC substrate-specific subunit. Can self-associate. Interacts with FBXW8.
CC Interacts with RNF7. Interacts with CUL7; the interaction seems to be
CC mediated by FBXW8. Interacts with TRIM21. Interacts with COPS2.
CC Interacts with DCUN1D1 and UBE2M. Interacts with DCUN1D3. Interacts
CC with DCUN1D4. Identified in a complex with RBX1 and GLMN (By
CC similarity). Interacts with CEP68 as part of the SCF(FBXW11) complex;
CC the interaction is probably mediated by FBXW11 and the complex also
CC contains CDK5RAP2 and PCNT. Interacts (when neddylated) with ARIH1;
CC leading to activate the E3 ligase activity of ARIH1. Interacts with
CC COPS9. Interacts with UBXN1 (By similarity). Interacts with KAT7,
CC probably as part of an SCF complex; the interaction mediates KAT7
CC ubiquitination (By similarity). Interacts with NOTCH2 (By similarity).
CC Part of a complex that contains DCUN1D5, CUL1 and RBX1; this
CC interaction is bridged by CUL1 (By similarity). Interacts (unneddylated
CC form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these
CC interactions promote the cullin neddylation (By similarity).
CC {ECO:0000250|UniProtKB:Q13616, ECO:0000250|UniProtKB:Q9WTX6}.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF and
CC prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN) complex.
CC {ECO:0000250|UniProtKB:Q13616}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; CR861282; CAH93350.1; -; mRNA.
DR RefSeq; NP_001126972.1; NM_001133500.1.
DR RefSeq; NP_001128951.1; NM_001135479.2.
DR RefSeq; XP_009241654.1; XM_009243379.1.
DR RefSeq; XP_009241655.1; XM_009243380.1.
DR AlphaFoldDB; Q5R4G6; -.
DR SMR; Q5R4G6; -.
DR STRING; 9601.ENSPPYP00000020352; -.
DR Ensembl; ENSPPYT00000021153; ENSPPYP00000020352; ENSPPYG00000018146.
DR GeneID; 100189917; -.
DR KEGG; pon:100189917; -.
DR CTD; 8454; -.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000154774; -.
DR HOGENOM; CLU_004747_6_1_1; -.
DR InParanoid; Q5R4G6; -.
DR OMA; GVYTAVH; -.
DR OrthoDB; 1040292at2759; -.
DR TreeFam; TF101151; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Methylation; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..776
FT /note="Cullin-1"
FT /id="PRO_0000119789"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT CROSSLNK 720
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 776 AA; 89679 MW; 6625A1FFA7799BBA CRC64;
MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA
