Q13616 (CUL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cullin-1
Short name=CUL-1

Gene names

Name:

CUL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	776 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. 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 exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. Ref.2 Ref.16 Ref.17 Ref.25 Ref.26 Ref.30
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit. Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Interacts with CHEK2; mediates CHEK2 ubiquitination and regulates its function. Part of a complex with TIP120A/CAND1 and RBX1. The unneddylated form interacts with TIP120A/CAND1 and the interaction mediates the exchange of the F-box substrate-specific subunit. Can self-associate. Interacts with FBXW8. Interacts with RNF7. Interacts with CUL7; the interaction seems to be mediated by FBXW8. Interacts with TRIM21. Interacts with COPS2. Interacts with Epstein-Barr virus BPLF1. Interacts with human adenovirus early E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBXW7) complex. Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30
Tissue specificity	Expressed in lung fibroblasts. Ref.2
Post-translational modification	Neddylated; which enhances the ubiquitination activity of SCF. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome.
Sequence similarities	Belongs to the cullin family.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome Notch signaling pathway Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 15103331. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell cycle arrest Traceable author statement Ref.1. Source: ProtInc cell proliferation Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway Traceable author statement Ref.1. Source: ProtInc negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc organ morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein monoubiquitination Inferred from electronic annotation. Source: Compara protein ubiquitination Inferred from direct assay PubMed 15103331. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SCF ubiquitin ligase complex Inferred from direct assay PubMed 15103331Ref.20Ref.28PubMed 21572392PubMed 21725316Ref.30. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAND1	Q86VP6	18	EBI-359390,EBI-456077
CDC34	P49427	3	EBI-359390,EBI-975634
MDM2	Q00987	3	EBI-359390,EBI-389668
RBX1	P62877	12	EBI-359390,EBI-398523
SKP1	P63208	6	EBI-359390,EBI-307486
SKP2	Q13309	8	EBI-359390,EBI-456291

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 776

776

Cullin-1

PRO_0000119787

Amino acid modifications

Cross-link

708

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Cross-link

720

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Ref.9 Ref.23

Experimental info

Sequence conflict

59 – 82

24

Missing in AAC50544. Ref.1

Sequence conflict

726

1

K → R in CAD97651. Ref.3

Secondary structure

1

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776

Helix Strand Turn

Details...

Helix

18 – 31

14

Turn

32 – 34

3

Helix

39 – 52

14

Helix

87 – 105

19

Turn

106 – 109

4

Turn

111 – 114

4

Helix

115 – 136

22

Helix

138 – 143

6

Beta strand

144 – 146

3

Helix

159 – 165

7

Helix

168 – 171

4

Turn

172 – 177

6

Helix

178 – 187

10

Turn

188 – 190

3

Helix

199 – 210

12

Beta strand

215 – 219

5

Helix

226 – 231

6

Helix

233 – 254

22

Helix

261 – 273

13

Turn

274 – 279

6

Beta strand

281 – 284

4

Helix

285 – 295

11

Beta strand

296 – 300

5

Helix

301 – 312

12

Helix

318 – 328

11

Helix

333 – 355

23

Helix

359 – 361

3

Helix

363 – 382

20

Turn

383 – 387

5

Helix

389 – 404

16

Helix

407 – 412

6

Helix

417 – 430

14

Helix

439 – 453

15

Helix

459 – 475

17

Helix

482 – 525

44

Turn

526 – 528

3

Beta strand

532 – 541

10

Turn

542 – 544

3

Helix

557 – 559

3

Helix

560 – 569

10

Turn

570 – 573

4

Beta strand

579 – 581

3

Helix

583 – 585

3

Beta strand

589 – 597

9

Beta strand

600 – 602

3

Helix

605 – 612

8

Helix

613 – 615

3

Beta strand

616 – 621

6

Helix

622 – 628

7

Helix

633 – 645

13

Turn

646 – 648

3

Beta strand

652 – 655

4

Turn

658 – 660

3

Beta strand

668 – 671

4

Beta strand

678 – 682

5

Helix

703 – 722

20

Beta strand

723 – 726

4

Helix

727 – 738

12

Turn

739 – 741

3

Helix

746 – 758

13

Beta strand

761 – 765

5

Beta strand

768 – 774

7

Sequences

	Sequence		Length	Mass (Da)
	Q13616 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 6625A1FFA7799BBA	FASTA	776	89,679
	10 20 30 40 50 60 MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN 70 80 90 100 110 120 QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT 130 140 150 160 170 180 QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT 190 200 210 220 230 240 NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT 250 260 270 280 290 300 ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL 310 320 330 340 350 360 EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL 370 380 390 400 410 420 NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE 430 440 450 460 470 480 LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA 490 500 510 520 530 540 SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL 550 560 570 580 590 600 SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT 610 620 630 640 650 660 LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE 670 680 690 700 710 720 VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK 730 740 750 760 770 MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Endometrium.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha." Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q. Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBX1, IDENTIFICATION IN SCF COMPLEX WITH RBX1; SKP1 AND SKP2.
[8]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBX1 AND RNF7.
[9]	"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] [Europe PMC] [Abstract] Cited for: NEDDYLATION AT LYS-720.
[10]	"Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha." Read M.A., Brownell J.E., Gladysheva T.B., Hottelet M., Parent L.A., Coggins M.B., Pierce J.W., Podust V.N., Luo R.-S., Chau V., Palombella V.J. Mol. Cell. Biol. 20:2326-2333(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NEDDYLATION.
[11]	"Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: chip profiling implicates its role in cell cycle regulation." Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y. Oncogene 19:2855-2866(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF7.
[12]	"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome." Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C., Wolf D.A., Wei N., Shevchenko A., Deshaies R.J. Science 292:1382-1385(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COPS2.
[13]	"CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex." Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. Mol. Cell 10:1519-1526(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIP120A.
[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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIP120A.
[15]	"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region." Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F. J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SCF(FBXO7) COMPLEX.
[16]	"Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase." Tintignac L.A., Lagirand J., Batonnet S., Sirri V., Leibovitch M.P., Leibovitch S.A. J. Biol. Chem. 280:2847-2856(2005) [PubMed] [Europe PMC] [Abstract] Cited for: RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, FUNCTION IN UBIQUITINATION OF MYOD1.
[17]	"FBW2 targets GCMa to the ubiquitin-proteasome degradation system." Yang C.S., Yu C., Chuang H.C., Chang C.W., Chang G.D., Yao T.P., Chen H. J. Biol. Chem. 280:10083-10090(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GCM1, FUNCTION IN UBIQUITINATION OF GCM1.
[18]	"FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle." Maragno A.L., Baqui M.M., Gomes M.D. Biochim. Biophys. Acta 1760:966-972(2006) [PubMed] [Europe PMC] [Abstract] Cited for: RECONSTITUTION OF THE SCF(FBXO25) COMPLEX.
[19]	"Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death." Lutz M., Wempe F., Bahr I., Zopf D., von Melchner H. FEBS Lett. 580:3921-3930(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SCF(FBXO33) COMPLEX WITH SKP1; RBX1 AND FBXO33.
[20]	"Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein." Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W. Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH TRIM21.
[21]	"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] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION.
[22]	"FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity." Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W. J. Biol. Chem. 282:1797-1804(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SCF(FBXO11) COMPLEX WITH SKP1; RBX1 AND FBXO11.
[23]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-708 AND LYS-720, MASS SPECTROMETRY. Tissue: Mammary cancer.
[24]	"Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases." Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L. J. Biol. Chem. 283:12717-12729(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBXO44; FBXO17 AND FBXO27, IDENTIFICATION IN SCF-COMPLEX.
[25]	"Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379." Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H. Mol. Cell. Biol. 28:5874-5885(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CHEK2 UBIQUITINATION, INTERACTION WITH CHEK2.
[26]	"Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase." Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T., Kitagawa M. J. Biol. Chem. 284:27766-27779(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
[27]	"A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases." Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M., Di Guglielmo C., Masucci M.G. Nat. Cell Biol. 12:351-361(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, DENEDDYLATION BY EPSTEIN-BARR VIRUS BPLF1.
[28]	"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation." D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M. Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
[29]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma." Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C., Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M., Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F. Nat. Cell Biol. 15:72-81(2013) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SCF(FBXO9) COMPLEX, FUNCTION.
[31]	"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex." Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P., Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W., Harper J.W., Pavletich N.P. Nature 416:703-709(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108 OF RBX1, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH RBX1; SKP1 AND SKP2.
[32]	"N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex." Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A. Science 334:674-678(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D1 AND UBE2M.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U58087 mRNA. Translation: AAC50544.1.
AF062536 mRNA. Translation: AAC36681.1.
BX537409 mRNA. Translation: CAD97651.1.
AC005229 Genomic DNA. Translation: AAM49153.1.
CH471146 Genomic DNA. Translation: EAW80074.1.
BC125119 mRNA. Translation: AAI25120.1.
BC125120 mRNA. Translation: AAI25121.1.

IPI

IPI00014310.

RefSeq

NP_003583.2. NM_003592.2.

UniGene

Hs.146806.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LDJ	X-ray	3.00	A	17-776	[»]
1LDK	X-ray	3.10	A	15-410	[»]
			B	411-776	[»]
1U6G	X-ray	3.10	A	1-776	[»]
3RTR	X-ray	3.21	A/C/E/G	411-776	[»]
3TDU	X-ray	1.50	C/D	702-776	[»]
3TDZ	X-ray	2.00	C/D	702-776	[»]
4F52	X-ray	3.00	A/C	411-690	[»]

ProteinModelPortal

Q13616.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17013N.

IntAct

Q13616. 40 interactions.

MINT

MINT-120495.

STRING

9606.ENSP00000326804.

PTM databases

PhosphoSite

Q13616.

Polymorphism databases

DMDM

19863257.

Proteomic databases

PaxDb

Q13616.

PeptideAtlas

Q13616.

PRIDE

Q13616.

Protocols and materials databases

DNASU

8454.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325222; ENSP00000326804; ENSG00000055130.
ENST00000409469; ENSP00000387160; ENSG00000055130.

GeneID

8454.

KEGG

hsa:8454.

UCSC

uc003wey.3. human.

Organism-specific databases

CTD

8454.

GeneCards

GC07P148395.

HGNC

HGNC:2551. CUL1.

HPA

CAB002676.

MIM

603134. gene.

neXtProt

NX_Q13616.

PharmGKB

PA27047.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5647.

HOGENOM

HOG000176713.

HOVERGEN

HBG106177.

InParanoid

Q13616.

KO

K03347.

OMA

SGVINCY.

OrthoDB

EOG4WH8K4.

PhylomeDB

Q13616.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_24941. Circadian Clock.
REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q13616.

Bgee

Q13616.

CleanEx

HS_CUL1.

Genevestigator

Q13616.

GermOnline

ENSG00000055130. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 2 hits.

InterPro

IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]

SMART

SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]

SUPFAM

SSF75632. Cullin_homology. 1 hit.
SSF74788. Cullin_repeat-like. 1 hit.

PROSITE

PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CUL1. human.

EvolutionaryTrace

Q13616.

GenomeRNAi

8454.

NextBio

31638.

SOURCE

Search...

Entry information

Entry name

CUL1_HUMAN

Accession

Primary (citable) accession number: Q13616
Secondary accession number(s): D3DWG3 , O60719, Q08AL6, Q8IYW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.