Reviewed, UniProtKB/Swiss-Prot Q13618 (CUL3_HUMAN)

Names and origin

Protein names

Recommended name:
    Cullin-3
      Short name=CUL-3

Gene names

Name:	CUL3
Synonyms:	KIAA0617

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	768 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 By similarity. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the susbstrate recognition component. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Forms neddylation-dependent homodimers. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein acting as both, adapter to cullin and substrate recognition subunit. The BCR complex may be active as a heterodimeric complex, in which NEDD8, covalently attached to one CUL3 molecule, binds to the C-terminus of a second CUL3 molecule. Interacts with RBX1, RNF7, CYCE and TIP120A/CAND1. Part of the BCR(SPOP) containing SPOP. Part of the probable BCR(KLHL9-KLHL13) complex with BTB domain proteins KLHL9 and KLHL13. Part of the BCR(KBTBD10) complex containing KBTBD10. Part of the BCR(ENC1) complex containing ENC1. Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with KLHL9, KLHL13, GAN, ZBTB16, KLHL21, KLHL3, KLHL15, KLHL20, C16orf44, GMCL1L, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN. Ref.10 Ref.13 Ref.14 Ref.15 Ref.20 Ref.21 Ref.23
Subcellular location	Nucleus. Golgi apparatus. Ref.10
Tissue specificity	Widely expressed.
Post-translational modification	Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-protein ligase activity of the BCR complex. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.
Sequence similarities	Belongs to the cullin family.
Sequence caution	The sequence AAC28621.1 differs from that shown. Reason: Frameshift at position 452. The sequence AAC36682.1 differs from that shown. Reason: Frameshift at positions 159 and 179.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Golgi apparatus Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Ref.8 Traceable author statement. Source: ProtInc cell cycle arrest Ref.8 Traceable author statement. Source: ProtInc cyclin catabolic process Ref.10 Inferred from direct assay. Source: MGI induction of apoptosis by intracellular signals Ref.8 Traceable author statement. Source: ProtInc positive regulation of cell proliferation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cullin-RING ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ubiquitin protein ligase binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAND1	Q86VP6	1	EBI-456129,EBI-456077
CASP8	Q14790	3	EBI-456129,EBI-78060
TNFSF10	P50591	2	EBI-456129,EBI-495373

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13618-1)

Also known as: Cul-3 Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13618-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Isoform 3 (identifier: Q13618-3)

Also known as: Cul-3 Short;

The sequence of this isoform differs from the canonical sequence as follows:
     23-88: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 768	768	Cullin-3		PRO_0000119793
Amino acid modifications
	Modified residue	58	1	Phosphotyrosine Ref.18
	Modified residue	450	1	Phosphoserine By similarity
	Modified residue	737	1	Phosphoserine Ref.16
	Cross-link	712		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity
Natural variations
	Alternative sequence	1 – 24	24	Missing in isoform 2.		VSP_008824
	Alternative sequence	23 – 88	66	Missing in isoform 3.		VSP_008825
	Natural variant	13	1	D → H: dbSNP rs2969802.		VAR_017194
	Natural variant	184	1	R → S: dbSNP rs17480168.		VAR_048839
	Natural variant	567	1	V → I: dbSNP rs3738952.		VAR_017195
Experimental info
	Sequence conflict	13	1	D → G in AAC36682. Ref.3
	Sequence conflict	397	1	K → T in AAQ01660. Ref.4
	Sequence conflict	481	1	N → T in AAQ01660. Ref.4
	Sequence conflict	609	1	E → G in AAH31844. Ref.7
	Sequence conflict	666	1	T → I in AAQ01660. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Cul-3 Long) [UniParc]. Last modified January 24, 2001. Version 2. Checksum: A1A02022480BF099	FASTA	768	88,930
	10 20 30 40 50 60 MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN 70 80 90 100 110 120 AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR 130 140 150 160 170 180 DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR 190 200 210 220 230 240 GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR 250 260 270 280 290 300 INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLGCMY 310 320 330 340 350 360 KLFSRVPNGL KTMCECMSSY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLLESF 370 380 390 400 410 420 NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR 430 440 450 460 470 480 FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS 490 500 510 520 530 540 NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL 550 560 570 580 590 600 AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT 610 620 630 640 650 660 ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIENGHIFT 670 680 690 700 710 720 VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN 730 740 750 760 VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
	Isoform 2. Checksum: AD845C2516117B9F	FASTA	744	86,234
	10 20 30 40 50 60 MDEKYVNSIW DLLKNAIQEI QRKNNSGLSF EELYRNAYTM VLHKHGEKLY TGLREVVTEH 70 80 90 100 110 120 LINKVREDVL NSLNNNFLQT LNQAWNDHQT AMVMIRDILM YMDRVYVQQN NVENVYNLGL 130 140 150 160 170 180 IIFRDQVVRY GCIRDHLRQT LLDMIARERK GEVVDRGAIR NACQMLMILG LEGRSVYEED 190 200 210 220 230 240 FEAPFLEMSA EFFQMESQKF LAENSASVYI KKVEARINEE IERVMHCLDK STEEPIVKVV 250 260 270 280 290 300 ERELISKHMK TIVEMENSGL VHMLKNGKTE DLGCMYKLFS RVPNGLKTMC ECMSSYLREQ 310 320 330 340 350 360 GKALVSEEGE GKNPVDYIQG LLDLKSRFDR FLLESFNNDR LFKQTIAGDF EYFLNLNSRS 370 380 390 400 410 420 PEYLSLFIDD KLKKGVKGLT EQEVETILDK AMVLFRFMQE KDVFERYYKQ HLARRLLTNK 430 440 450 460 470 480 SVSDDSEKNM ISKLKTECGC QFTSKLEGMF RDMSISNTTM DEFRQHLQAT GVSLGGVDLT 490 500 510 520 530 540 VRVLTTGYWP TQSATPKCNI PPAPRHAFEI FRRFYLAKHS GRQLTLQHHM GSADLNATFY 550 560 570 580 590 600 GPVKKEDGSE VGVGGAQVTG SNTRKHILQV STFQMTILML FNNREKYTFE EIQQETDIPE 610 620 630 640 650 660 RELVRALQSL ACGKPTQRVL TKEPKSKEIE NGHIFTVNDQ FTSKLHRVKI QTVAAKQGES 670 680 690 700 710 720 DPERKETRQK VDDDRKHEIE AAIVRIMKSR KKMQHNVLVA EVTQQLKARF LPSPVVIKKR 730 740 IEGLIEREYL ARTPEDRKVY TYVA
	Isoform 3 (Cul-3 Short). Checksum: 2CDE8E7AF43C898A	FASTA	702	81,093
	10 20 30 40 50 60 MSNLSKGTGS RKDTKMRIRA FPVREDVLNS LNNNFLQTLN QAWNDHQTAM VMIRDILMYM 70 80 90 100 110 120 DRVYVQQNNV ENVYNLGLII FRDQVVRYGC IRDHLRQTLL DMIARERKGE VVDRGAIRNA 130 140 150 160 170 180 CQMLMILGLE GRSVYEEDFE APFLEMSAEF FQMESQKFLA ENSASVYIKK VEARINEEIE 190 200 210 220 230 240 RVMHCLDKST EEPIVKVVER ELISKHMKTI VEMENSGLVH MLKNGKTEDL GCMYKLFSRV 250 260 270 280 290 300 PNGLKTMCEC MSSYLREQGK ALVSEEGEGK NPVDYIQGLL DLKSRFDRFL LESFNNDRLF 310 320 330 340 350 360 KQTIAGDFEY FLNLNSRSPE YLSLFIDDKL KKGVKGLTEQ EVETILDKAM VLFRFMQEKD 370 380 390 400 410 420 VFERYYKQHL ARRLLTNKSV SDDSEKNMIS KLKTECGCQF TSKLEGMFRD MSISNTTMDE 430 440 450 460 470 480 FRQHLQATGV SLGGVDLTVR VLTTGYWPTQ SATPKCNIPP APRHAFEIFR RFYLAKHSGR 490 500 510 520 530 540 QLTLQHHMGS ADLNATFYGP VKKEDGSEVG VGGAQVTGSN TRKHILQVST FQMTILMLFN 550 560 570 580 590 600 NREKYTFEEI QQETDIPERE LVRALQSLAC GKPTQRVLTK EPKSKEIENG HIFTVNDQFT 610 620 630 640 650 660 SKLHRVKIQT VAAKQGESDP ERKETRQKVD DDRKHEIEAA IVRIMKSRKK MQHNVLVAEV 670 680 690 700 TQQLKARFLP SPVVIKKRIE GLIEREYLAR TPEDRKVYTY VA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression analysis of a novel salicylate suppressible gene, Hs-CUL-3, a member of cullin/Cdc53 family." Du M., Sansores-Garcia L., Zu Z., Wu K.K. J. Biol. Chem. 273:24289-24292(1998) [PubMed: 9733711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A." Michel J.J., Xiong Y. Cell Growth Differ. 9:435-449(1998) [PubMed: 9663463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon carcinoma.
[4]	"Cloning and characterization of a new isoform of CUL3 gene in testis." Xu M., Huang X.Y., Yin L.L., Xu Z.Y., Lu L., Zhou Z.M., Sha J.H. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Testis.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Ovary, Skin and Uterus.
[8]	"cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family." Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M. Cell 85:829-839(1996) [PubMed: 8681378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 192-768.
[9]	Yu W., Sarginson J., Gibbs R.A. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 398-768. Tissue: Brain.
[10]	"Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cells." Singer J.D., Gurian-West M., Clurman B., Roberts J.M. Genes Dev. 13:2375-2387(1999) [PubMed: 10500095] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CYCE, NEDDYLATION.
[11]	"In vitro ubiquitination of cyclin D1 by ROC1-CUL1 and ROC1-CUL3." Maeda I., Ohta T., Koizumi H., Fukuda M. FEBS Lett. 494:181-185(2001) [PubMed: 11311237] [Abstract] Cited for: FUNCTION.
[12]	"Covalent modification of all members of human cullin family proteins by NEDD8." Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K. Oncogene 18:6829-6834(1999) [PubMed: 10597293] [Abstract] Cited for: NEDDYLATION.
[13]	"ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity." Ohta T., Michel J.J., Schottelius A.J., Xiong Y. Mol. Cell 3:535-541(1999) [PubMed: 10230407] [Abstract] Cited for: INTERACTION WITH RBX1 AND RNF7.
[14]	"TIP120A associates with cullins and modulates ubiquitin ligase activity." Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B. J. Biol. Chem. 278:15905-15910(2003) [PubMed: 12609982] [Abstract] Cited for: INTERACTION WITH TIP120A.
[15]	"Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases." Furukawa M., He Y.J., Borchers C., Xiong Y. Nat. Cell Biol. 5:1001-1007(2003) [PubMed: 14528312] [Abstract] Cited for: INTERACTION WITH GAN; ZBTB16; KLHL9; KLHL13; KLHL211; KLHL3; KLHL15; KLHL20; C16ORF44; GMCL1L; BTBD1 AND SPOP.
[16]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway." Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M. J. Biol. Chem. 280:30091-30099(2005) [PubMed: 15983046] [Abstract] Cited for: IDENTIFICATION IN THE BCR(KBTBD10) COMPLEX, IDENTIFICATION IN THE BCR(ENC1) COMPLEX, IDENTIFICATION IN A COMPLEX WITH RBX1 AND GAN.
[18]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58, MASS SPECTROMETRY.
[19]	"Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase." Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M. Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed: 15897469] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SPOP AND BMI1, IDENTIFICATION IN A COMPLEX WITH SPOP AND H2AFY, FUNCTION.
[20]	"BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase." Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H. J. Biol. Chem. 281:12664-12672(2006) [PubMed: 16524876] [Abstract] Cited for: IDENTIFICATION IN THE BCR(SPOP) COMPLEX, INTERACTION WITH SPOP, FUNCTION IN UBIQUITINATION OF DAXX.
[21]	"A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells." Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M. Dev. Cell 12:887-900(2007) [PubMed: 17543862] [Abstract] Cited for: FUNCTION, INTERACTION WITH KLHL9 AND KLHL13.
[22]	"Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization." Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T. Cell. Signal. 19:1071-1080(2007) [PubMed: 17254749] [Abstract] Cited for: SELF-ASSOCIATION.
[23]	"The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer." Wimuttisuk W., Singer J.D. Mol. Biol. Cell 18:899-909(2007) [PubMed: 17192413] [Abstract] Cited for: BCR COMPLEX HOMODIMERIZATION.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF064087 mRNA. Translation: AAC36304.1. AB014517 mRNA. Translation: BAA31592.2. Different initiation. AF062537 mRNA. Translation: AAC36682.1. Frameshift. AY337761 mRNA. Translation: AAQ01660.1. AK291151 mRNA. Translation: BAF83840.1. CH471063 Genomic DNA. Translation: EAW70828.1. BC031844 mRNA. Translation: AAH31844.1. BC039598 mRNA. Translation: AAH39598.1. BC092409 mRNA. Translation: AAH92409.1. U58089 mRNA. Translation: AAC50546.1. AF052147 mRNA. Translation: AAC28621.1. Frameshift.
IPI	IPI00014312. IPI00382458. IPI00382459.
RefSeq	NP_003581.1.
UniGene	Hs.372286
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13618. 8 interactions.
STRING	Q13618.
PTM databases
PhosphoSite	Q13618.
Proteomic databases
PRIDE	Q13618.
Genome annotation databases
Ensembl	ENST00000264414; ENSP00000264414; ENSG00000036257; Homo sapiens. [Genome view] ENST00000344951; ENSP00000343601; ENSG00000036257; Homo sapiens. [Genome view] ENST00000409096; ENSP00000387200; ENSG00000036257; Homo sapiens. [Genome view] ENST00000409777; ENSP00000386525; ENSG00000036257; Homo sapiens. [Genome view] ENST00000432260; ENSP00000400361; ENSG00000036257; Homo sapiens. [Genome view] ENST00000436172; ENSP00000400935; ENSG00000036257; Homo sapiens. [Genome view] ENST00000451538; ENSP00000410575; ENSG00000036257; Homo sapiens. [Genome view] ENST00000454323; ENSP00000400558; ENSG00000036257; Homo sapiens. [Genome view]
GeneID	8452.
KEGG	hsa:8452.
UCSC	uc002vny.1. human. uc010fwy.1. human.
Organism-specific databases
CTD	8452.
GeneCards	GC02M225043.
H-InvDB	HIX0002888.
HGNC	HGNC:2553. CUL3.
HPA	CAB002678.
MIM	603136. gene.
PharmGKB	PA27049.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q13618.
HOVERGEN	Q13618.
OMA	EREYLQR.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
Gene expression databases
ArrayExpress	Q13618.
Bgee	Q13618.
CleanEx	HS_CUL3.
Genevestigator	Q13618.
GermOnline	ENSG00000036257. Homo sapiens.
Family and domain databases
InterPro	IPR016157. Cullin_CS. IPR016158. Cullin_homology. IPR001373. Cullin_N. IPR019559. Cullin_neddylation_domain. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.
Pfam	PF00888. Cullin. 1 hit. PF10557. Cullin_Nedd8. 1 hit. [Graphical view]
SMART	SM00182. CULLIN. 1 hit. [Graphical view]
PROSITE	PS01256. CULLIN_1. 1 hit. PS50069. CULLIN_2. 1 hit. [Graphical view]
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Entry information

Entry name

CUL3_HUMAN

Accession

Primary (citable) accession number: Q13618
Secondary accession number(s): A8K536 , O75415, Q569L3, Q9UBI8, Q9UET7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 24, 2001
Last modified:	November 3, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.