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Q13616 (CUL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-1

Short name=CUL-1
Gene names
Name:CUL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length776 AA.
Sequence statusComplete.
Protein existenceEvidence 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(FBXO1) directs ubiquitination of BCL6 and DTL but 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. SCF(FBXO10) directs ubiquitination of BCL2. Ref.2 Ref.16 Ref.17 Ref.26 Ref.27 Ref.31 Ref.32 Ref.33

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(FBXO10) complex containing FBXO10. 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.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.35

Tissue specificity

Expressed in lung fibroblasts. Ref.2

Post-translational modification

Neddylated; which enhances the ubiquitination activity of SCF and prevents binding of the inhibitor CAND1. 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 processHost-virus interaction
Ubl conjugation pathway
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

Notch signaling pathway

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: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein monoubiquitination

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from direct assay PubMed 15103331. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay PubMed 15103331Ref.20Ref.29PubMed 21572392PubMed 21725316Ref.32. Source: UniProtKB

cullin-RING ubiquitin ligase complex

Inferred from direct assay PubMed 22405651. Source: MGI

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 776776Cullin-1
PRO_0000119787

Amino acid modifications

Cross-link708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23
Cross-link720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Ref.9 Ref.23 Ref.24 Ref.35

Experimental info

Sequence conflict59 – 8224Missing in AAC50544. Ref.1
Sequence conflict7261K → R in CAD97651. Ref.3

Secondary structure

......................................................................................................... 776
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13616 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 6625A1FFA7799BBA

FASTA77689,679
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
Tissue: Mammary cancer.
[24]"Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation."
Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.
Cell 134:995-1006(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NEDDYLATION AT LYS-720.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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].
[31]"FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas."
Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.
Nature 481:90-93(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF BCL6, IDENTIFICATION IN THE SCF(FBXO11) COMPLEX.
[32]"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.
[33]"Related F-box proteins control cell death in Caenorhabditis elegans and human lymphoma."
Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W., Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D., Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S., Staudt L.M.
Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF BCL2, IDENTIFICATION IN THE SCF(FBXO10) COMPLEX.
[34]"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.
[35]"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases."
Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., Zheng N.
Cell 119:517-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CAND1 AND ROC1, NEDDYLATION AT LYS-720, SUBUNIT.
[36]"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.
RefSeqNP_003583.2. NM_003592.2.
XP_005250117.1. XM_005250060.2.
UniGeneHs.146806.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LDJX-ray3.00A17-776[»]
1LDKX-ray3.10A15-410[»]
B411-776[»]
1U6GX-ray3.10A1-776[»]
3RTRX-ray3.21A/C/E/G411-776[»]
3TDUX-ray1.50C/D702-776[»]
3TDZX-ray2.00C/D702-776[»]
4F52X-ray3.00A/C411-690[»]
ProteinModelPortalQ13616.
SMRQ13616. Positions 17-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114032. 656 interactions.
DIPDIP-17013N.
IntActQ13616. 60 interactions.
MINTMINT-120495.
STRING9606.ENSP00000326804.

PTM databases

PhosphoSiteQ13616.

Polymorphism databases

DMDM19863257.

Proteomic databases

PaxDbQ13616.
PeptideAtlasQ13616.
PRIDEQ13616.

Protocols and materials databases

DNASU8454.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325222; ENSP00000326804; ENSG00000055130.
ENST00000409469; ENSP00000387160; ENSG00000055130.
ENST00000602748; ENSP00000473318; ENSG00000055130.
GeneID8454.
KEGGhsa:8454.
UCSCuc003wey.3. human.

Organism-specific databases

CTD8454.
GeneCardsGC07P148395.
HGNCHGNC:2551. CUL1.
HPACAB002676.
HPA050796.
MIM603134. gene.
neXtProtNX_Q13616.
PharmGKBPA27047.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5647.
HOGENOMHOG000176713.
HOVERGENHBG106177.
InParanoidQ13616.
KOK03347.
OMAYEIYQLA.
OrthoDBEOG7X3QQG.
PhylomeDBQ13616.
TreeFamTF101151.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_24941. Circadian Clock.
REACT_6900. Immune System.
SignaLinkQ13616.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13616.
BgeeQ13616.
CleanExHS_CUL1.
GenevestigatorQ13616.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCUL1. human.
EvolutionaryTraceQ13616.
GeneWikiCUL1.
GenomeRNAi8454.
NextBio31638.
PROQ13616.
SOURCESearch...

Entry information

Entry nameCUL1_HUMAN
AccessionPrimary (citable) accession number: Q13616
Secondary accession number(s): D3DWG3 expand/collapse secondary AC list , O60719, Q08AL6, Q8IYW1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM