HUMAN:CUL1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CUL1
Protein Name(s)	Cullin-1 CUL-1
External Links
UniProt	Q13616
EMBL	U58087 AF062536 BX537409 AC005229 CH471146 BC125119 BC125120
CCDS	CCDS34772.1
RefSeq	NP_003583.2 XP_005250117.1
UniGene	Hs.146806
PDB	1LDJ 1LDK 1U6G 3RTR 3TDU 3TDZ 4F52 4P5O
PDBsum	1LDJ 1LDK 1U6G 3RTR 3TDU 3TDZ 4F52 4P5O
ProteinModelPortal	Q13616
SMR	Q13616
BioGrid	114032
DIP	DIP-17013N
IntAct	Q13616
MINT	MINT-120495
STRING	9606.ENSP00000326804
PhosphoSite	Q13616
DMDM	19863257
MaxQB	Q13616
PaxDb	Q13616
PeptideAtlas	Q13616
PRIDE	Q13616
DNASU	8454
Ensembl	ENST00000325222 ENST00000409469 ENST00000602748 ENST00000617797
GeneID	8454
KEGG	hsa:8454
UCSC	uc003wey.3
CTD	8454
GeneCards	GC07P148395
HGNC	HGNC:2551
HPA	CAB002676 HPA050796
MIM	603134
neXtProt	NX_Q13616
PharmGKB	PA27047
eggNOG	COG5647
GeneTree	ENSGT00760000119212
HOGENOM	HOG000176713
HOVERGEN	HBG106177
InParanoid	Q13616
KO	K03347
OMA	RMYNLLS
OrthoDB	EOG7X3QQG
PhylomeDB	Q13616
TreeFam	TF101151
Reactome	REACT_11063 REACT_115697 REACT_118656 REACT_118780 REACT_160243 REACT_160254 REACT_160305 REACT_160315 REACT_206597 REACT_22442 REACT_231645 REACT_24941 REACT_267605 REACT_6821 REACT_75842 REACT_821 REACT_9003
SignaLink	Q13616
UniPathway	UPA00143
ChiTaRS	CUL1
EvolutionaryTrace	Q13616
GeneWiki	CUL1
GenomeRNAi	8454
NextBio	31638
PRO	PR:Q13616
Proteomes	UP000005640
Bgee	Q13616
CleanEx	HS_CUL1
ExpressionAtlas	Q13616
Genevestigator	Q13616
GO	GO:0031461 GO:0005829 GO:0005654 GO:1990452 GO:0019005 GO:0031145 GO:0007050 GO:0008283 GO:0000082 GO:0000086 GO:0097193 GO:0000278 GO:0008285 GO:0007219 GO:0009887 GO:0051437 GO:0006513 GO:0016567 GO:0051439 GO:0031146 GO:0016032
Gene3D	1.10.10.10
InterPro	IPR016157 IPR016158 IPR001373 IPR019559 IPR016159 IPR011991
Pfam	PF00888 PF10557
SMART	SM00182 SM00884
SUPFAM	SSF74788 SSF75632
PROSITE	PS01256 PS50069

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:25585578^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:11956208^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990452	Parkin-FBXW7-Cul1 ubiquitin ligase complex	PMID:12628165^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	C	part_of:(UBERON:0001870)	Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:28007894^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	PMID:15103331^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9WTX6	P		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:23263282^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:21725316^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:21572392^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:20596027^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:16880511^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:15103331^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9WTX6	C		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:15103331^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0061630	ubiquitin protein ligase activity	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000231993 SGD:S000002290	F		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0261268 MGI:MGI:1347360 MGI:MGI:1349658 MGI:MGI:1914487 PANTHER:PTN000231993 PomBase:SPAC17G6.12 SGD:S000002290 UniProtKB:Q13616 UniProtKB:Q13618 UniProtKB:Q13619 UniProtKB:Q5AJB7 WB:WBGene00000837 WB:WBGene00000839	P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015509 FB:FBgn0032956 FB:FBgn0033260 FB:FBgn0039632 FB:FBgn0261268 PANTHER:PTN000231993 UniProtKB:Q13617 UniProtKB:Q93034	F		Seeded From UniProt	complete
part_of	GO:0031461	cullin-RING ubiquitin ligase complex	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000231993 UniProtKB:Q13616 UniProtKB:Q57UJ3	C		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1349658 PANTHER:PTN000231993 PomBase:SPAC17G6.12 SGD:S000002290 UniProtKB:Q13616 UniProtKB:Q5AJB7	P		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015509 MGI:MGI:1349658 PANTHER:PTN000231993 PomBase:SPAC17G6.12 SGD:S000002290 UniProtKB:Q13616 dictyBase:DDB_G0291972	C		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1914487 PANTHER:PTN000231993 SGD:S000002290 SGD:S000003235 UniProtKB:Q13618 UniProtKB:Q57UJ3	P		Seeded From UniProt	complete
part_of	GO:0031461	cullin-RING ubiquitin ligase complex	PMID:22405651^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WTX6 ensembl:ENSMUSP00000031697	P		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WTX6 ensembl:ENSMUSP00000031697	C		Seeded From UniProt	complete
involved_in	GO:0009887	animal organ morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WTX6 ensembl:ENSMUSP00000031697	P		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WTX6 ensembl:ENSMUSP00000031697	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WTX6 ensembl:ENSMUSP00000031697	P		Seeded From UniProt	complete
involved_in	GO:0006513	protein monoubiquitination	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WTX6 ensembl:ENSMUSP00000031697	P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001373 InterPro:IPR016157	P		Seeded From UniProt	complete
part_of	GO:0031461	cullin-RING ubiquitin ligase complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016157	C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001373 InterPro:IPR016157	F		Seeded From UniProt	complete
involved_in	GO:0097193	intrinsic apoptotic signaling pathway	PMID:8681378^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	PMID:8681378^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901990	regulation of mitotic cell cycle phase transition	Reactome:R-HSA-174113	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070498	interleukin-1-mediated signaling pathway	Reactome:R-HSA-9020702	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051403	stress-activated MAPK cascade	Reactome:R-HSA-450294	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050852	T cell receptor signaling pathway	Reactome:R-HSA-202403	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043687	post-translational protein modification	Reactome:R-HSA-597592	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038095	Fc-epsilon receptor signaling pathway	Reactome:R-HSA-2454202	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038061	NIK/NF-kappaB signaling	Reactome:R-HSA-5676590	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	Reactome:R-HSA-8854051	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016055	Wnt signaling pathway	Reactome:R-HSA-195721	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010972	negative regulation of G2/M transition of mitotic cell cycle	Reactome:R-HSA-8854041 Reactome:R-HSA-8853496	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010265	SCF complex assembly	Reactome:R-HSA-8854052	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	Reactome:R-HSA-917937	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-983157 Reactome:R-HSA-983156 Reactome:R-HSA-983147 Reactome:R-HSA-983140 Reactome:R-HSA-8956200 Reactome:R-HSA-8956040 Reactome:R-HSA-8955289 Reactome:R-HSA-8955241 Reactome:R-HSA-8952620 Reactome:R-HSA-8952618 Reactome:R-HSA-8854052 Reactome:R-HSA-8854051 Reactome:R-HSA-8854044 Reactome:R-HSA-8854041 Reactome:R-HSA-8853496 Reactome:R-HSA-5691176 Reactome:R-HSA-5691167 Reactome:R-HSA-5691131 Reactome:R-HSA-5691108 Reactome:R-HSA-5684250 Reactome:R-HSA-5684248 Reactome:R-HSA-5610746 Reactome:R-HSA-5610742 Reactome:R-HSA-5607728 Reactome:R-HSA-5607725 Reactome:R-HSA-5607723 Reactome:R-HSA-3000339 Reactome:R-HSA-3000335 Reactome:R-HSA-2130286 Reactome:R-HSA-2130282 Reactome:R-HSA-2130279 Reactome:R-HSA-209125 Reactome:R-HSA-209063 Reactome:R-HSA-174209 Reactome:R-HSA-174203 Reactome:R-HSA-174159 Reactome:R-HSA-1370500 Reactome:R-HSA-1170539 Reactome:R-HSA-1168643 Reactome:R-HSA-1168642	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-9604628 Reactome:R-NUL-2064883 Reactome:R-NUL-2064853 Reactome:R-HSA-8939706 Reactome:R-HSA-8939688 Reactome:R-HSA-68946 Reactome:R-HSA-2220978 Reactome:R-HSA-2220967 Reactome:R-HSA-187575 Reactome:R-HSA-187574 Reactome:R-HSA-187552 Reactome:R-HSA-187545 Reactome:R-HSA-1363331 Reactome:R-HSA-1363328	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002223	stimulatory C-type lectin receptor signaling pathway	Reactome:R-HSA-5621481	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000209	protein polyubiquitination	Reactome:R-HSA-983168	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000086	G2/M transition of mitotic cell cycle	Reactome:R-HSA-69275	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00143	P		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Chu, WK et al. (2015) FBH1 influences DNA replication fork stability and homologous recombination through ubiquitylation of RAD51. Nat Commun 6 5931 PubMed GONUTS page
↑ Kim, J et al. (2002) The novel human DNA helicase hFBH1 is an F-box protein. J. Biol. Chem. 277 24530-7 PubMed GONUTS page
↑ Staropoli, JF et al. (2003) Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37 735-49 PubMed GONUTS page
↑ Reiterer, V et al. (2017) The pseudophosphatase STYX targets the F-box of FBXW7 and inhibits SCFFBXW7 function. EMBO J. 36 260-273 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Yada, M et al. (2004) Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. EMBO J. 23 2116-25 PubMed GONUTS page
↑ Fernández-Sáiz, V et al. (2013) SCFFbxo9 and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma. Nat. Cell Biol. 15 72-81 PubMed GONUTS page
↑ Puklowski, A et al. (2011) The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication. Nat. Cell Biol. 13 1004-9 PubMed GONUTS page
↑ Cui, Y et al. (2011) SCFFBXL¹⁵ regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1. EMBO J. 30 2675-89 PubMed GONUTS page
↑ D'Angiolella, V et al. (2010) SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. Nature 466 138-42 PubMed GONUTS page
↑ Sabile, A et al. (2006) Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein. Mol. Cell. Biol. 26 5994-6004 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Tron, AE et al. (2012) The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. Mol. Cell 46 67-78 PubMed GONUTS page
↑ ^13.0 ^13.1 Kipreos, ET et al. (1996) cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. Cell 85 829-39 PubMed GONUTS page

[PMID:25585578-1] Chu, WK et al. (2015) FBH1 influences DNA replication fork stability and homologous recombination through ubiquitylation of RAD51. Nat Commun 6 5931 PubMed GONUTS page

[PMID:11956208-2] Kim, J et al. (2002) The novel human DNA helicase hFBH1 is an F-box protein. J. Biol. Chem. 277 24530-7 PubMed GONUTS page

[PMID:12628165-3] Staropoli, JF et al. (2003) Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37 735-49 PubMed GONUTS page

[PMID:28007894-4] Reiterer, V et al. (2017) The pseudophosphatase STYX targets the F-box of FBXW7 and inhibits SCFFBXW7 function. EMBO J. 36 260-273 PubMed GONUTS page

[PMID:15103331-5] 5.0 ^5.1 ^5.2 Yada, M et al. (2004) Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. EMBO J. 23 2116-25 PubMed GONUTS page

[PMID:23263282-6] Fernández-Sáiz, V et al. (2013) SCFFbxo9 and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma. Nat. Cell Biol. 15 72-81 PubMed GONUTS page

[PMID:21725316-7] Puklowski, A et al. (2011) The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication. Nat. Cell Biol. 13 1004-9 PubMed GONUTS page

[PMID:21572392-8] Cui, Y et al. (2011) SCFFBXL¹⁵ regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1. EMBO J. 30 2675-89 PubMed GONUTS page

[PMID:20596027-9] D'Angiolella, V et al. (2010) SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. Nature 466 138-42 PubMed GONUTS page

[PMID:16880511-10] Sabile, A et al. (2006) Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein. Mol. Cell. Biol. 26 5994-6004 PubMed GONUTS page

[PMID:21873635-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:22405651-12] Tron, AE et al. (2012) The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. Mol. Cell 46 67-78 PubMed GONUTS page

[PMID:8681378-13] 13.0 ^13.1 Kipreos, ET et al. (1996) cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. Cell 85 829-39 PubMed GONUTS page

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HUMAN:CUL1

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