UniProt ID | CUL3_HUMAN | |
---|---|---|
UniProt AC | Q13618 | |
Protein Name | Cullin-3 | |
Gene Name | CUL3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 768 | |
Subcellular Localization | Nucleus . Golgi apparatus . Cell projection, cilium, flagellum . Cytoplasm. Detected along the length of the sperm flagellum and in the cytoplasm of the germ cells. | |
Protein Description | 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. BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. [PubMed: 27565346 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. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B)] | |
Protein Sequence | MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMYKLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLLESFNNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFRFMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSISNTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYLAKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMTILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIENGHIFTVNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHNVLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MSNLSKGTG ------CCCCCCCCC | 46.61 | 22814378 | |
5 | Phosphorylation | ---MSNLSKGTGSRK ---CCCCCCCCCCCC | 33.03 | 28634298 | |
6 | Ubiquitination | --MSNLSKGTGSRKD --CCCCCCCCCCCCC | 64.75 | - | |
8 | Phosphorylation | MSNLSKGTGSRKDTK CCCCCCCCCCCCCCH | 35.40 | 24719451 | |
10 | Phosphorylation | NLSKGTGSRKDTKMR CCCCCCCCCCCCHHH | 35.67 | 24719451 | |
29 | Phosphorylation | PMTMDEKYVNSIWDL CCCCCHHHHHHHHHH | 11.65 | 27642862 | |
47 | Ubiquitination | AIQEIQRKNNSGLSF HHHHHHHHCCCCCCH | 44.07 | - | |
50 | Phosphorylation | EIQRKNNSGLSFEEL HHHHHCCCCCCHHHH | 50.97 | - | |
58 | Phosphorylation | GLSFEELYRNAYTMV CCCHHHHHHHHHHHH | 12.71 | 22817900 | |
63 | Phosphorylation | ELYRNAYTMVLHKHG HHHHHHHHHHHHHHH | 9.82 | 20393185 | |
68 | Ubiquitination | AYTMVLHKHGEKLYT HHHHHHHHHHCCHHH | 49.50 | - | |
72 | Ubiquitination | VLHKHGEKLYTGLRE HHHHHHCCHHHCHHH | 51.92 | - | |
164 | Phosphorylation | IRDHLRQTLLDMIAR HHHHHHHHHHHHHHH | 23.89 | - | |
196 (in isoform 3) | Ubiquitination | - | 51.25 | 21890473 | |
235 | Acetylation | NSASVYIKKVEARIN CCCCEEEEEHHHHHH | 32.83 | 23236377 | |
235 | Ubiquitination | NSASVYIKKVEARIN CCCCEEEEEHHHHHH | 32.83 | - | |
236 | Ubiquitination | SASVYIKKVEARINE CCCEEEEEHHHHHHH | 35.43 | - | |
238 (in isoform 2) | Ubiquitination | - | 40.90 | 21890473 | |
254 | Ubiquitination | RVMHCLDKSTEEPIV HHHHHHCCCCCCCHH | 46.45 | - | |
262 | Ubiquitination | STEEPIVKVVERELI CCCCCHHHHHHHHHH | 41.08 | 21890473 | |
262 (in isoform 1) | Ubiquitination | - | 41.08 | 21890473 | |
270 (in isoform 3) | Ubiquitination | - | 29.18 | 21890473 | |
271 | Ubiquitination | VERELISKHMKTIVE HHHHHHHHHHHHHHH | 40.50 | - | |
283 (in isoform 3) | Ubiquitination | - | 43.21 | 21890473 | |
292 | Acetylation | VHMLKNGKTEDLGCM EEHHHCCCCCCCHHH | 59.12 | 25038526 | |
292 | Ubiquitination | VHMLKNGKTEDLGCM EEHHHCCCCCCCHHH | 59.12 | - | |
301 | Acetylation | EDLGCMYKLFSRVPN CCCHHHHHHHHCCCC | 19.03 | 26051181 | |
301 | Ubiquitination | EDLGCMYKLFSRVPN CCCHHHHHHHHCCCC | 19.03 | - | |
312 | Phosphorylation | RVPNGLKTMCECMSS CCCCHHHHHHHHHHH | 31.90 | - | |
312 (in isoform 2) | Ubiquitination | - | 31.90 | 21890473 | |
318 | Phosphorylation | KTMCECMSSYLREQG HHHHHHHHHHHHHHC | 27.73 | - | |
319 | Phosphorylation | TMCECMSSYLREQGK HHHHHHHHHHHHHCC | 10.99 | - | |
320 | Phosphorylation | MCECMSSYLREQGKA HHHHHHHHHHHHCCE | 11.50 | - | |
325 (in isoform 2) | Ubiquitination | - | 16.67 | 21890473 | |
326 | Ubiquitination | SYLREQGKALVSEEG HHHHHHCCEEECCCC | 37.94 | - | |
335 (in isoform 3) | Ubiquitination | - | 45.99 | 21890473 | |
336 | Ubiquitination | VSEEGEGKNPVDYIQ ECCCCCCCCHHHHHH | 54.50 | 21906983 | |
336 (in isoform 1) | Ubiquitination | - | 54.50 | 21890473 | |
349 | Ubiquitination | IQGLLDLKSRFDRFL HHHHHHHHHHHHHHH | 38.97 | 21890473 | |
349 (in isoform 1) | Ubiquitination | - | 38.97 | 21890473 | |
364 | Methylation | LESFNNDRLFKQTIA HHHCCCCCCCCEECC | 44.11 | - | |
376 | Phosphorylation | TIAGDFEYFLNLNSR ECCCCHHHHHCCCCC | 17.23 | 29116813 | |
377 (in isoform 2) | Ubiquitination | - | 2.61 | 21890473 | |
378 (in isoform 3) | Ubiquitination | - | 7.54 | 21890473 | |
387 | Phosphorylation | LNSRSPEYLSLFIDD CCCCCHHHHHHHHCH | 12.65 | 29116813 | |
389 | Phosphorylation | SRSPEYLSLFIDDKL CCCHHHHHHHHCHHH | 21.97 | 20068231 | |
395 | Ubiquitination | LSLFIDDKLKKGVKG HHHHHCHHHHHCCCC | 59.46 | - | |
398 | Ubiquitination | FIDDKLKKGVKGLTE HHCHHHHHCCCCCCH | 78.39 | - | |
401 | Ubiquitination | DKLKKGVKGLTEQEV HHHHHCCCCCCHHHH | 57.80 | 21906983 | |
401 (in isoform 1) | Ubiquitination | - | 57.80 | 21890473 | |
414 | Ubiquitination | EVETILDKAMVLFRF HHHHHHHHHHHHHHH | 34.63 | - | |
420 (in isoform 2) | Ubiquitination | - | 23.20 | 21890473 | |
425 | 2-Hydroxyisobutyrylation | LFRFMQEKDVFERYY HHHHHHCHHHHHHHH | 42.15 | - | |
425 | Ubiquitination | LFRFMQEKDVFERYY HHHHHHCHHHHHHHH | 42.15 | - | |
433 | Ubiquitination | DVFERYYKQHLARRL HHHHHHHHHHHHHHH | 23.47 | - | |
442 | Phosphorylation | HLARRLLTNKSVSDD HHHHHHHHCCCCCCH | 45.23 | 23532336 | |
444 | Ubiquitination | ARRLLTNKSVSDDSE HHHHHHCCCCCCHHH | 47.18 | 21906983 | |
444 (in isoform 1) | Ubiquitination | - | 47.18 | 21890473 | |
456 | Phosphorylation | DSEKNMISKLKTECG HHHHHHHHHHHHHHC | 22.59 | - | |
457 | Ubiquitination | SEKNMISKLKTECGC HHHHHHHHHHHHHCC | 42.98 | - | |
459 | Acetylation | KNMISKLKTECGCQF HHHHHHHHHHHCCCC | 46.12 | 23749302 | |
459 | Malonylation | KNMISKLKTECGCQF HHHHHHHHHHHCCCC | 46.12 | 26320211 | |
459 | Ubiquitination | KNMISKLKTECGCQF HHHHHHHHHHHCCCC | 46.12 | - | |
469 | Ubiquitination | CGCQFTSKLEGMFRD HCCCCHHHHHHHHCC | 47.72 | - | |
478 | Phosphorylation | EGMFRDMSISNTTMD HHHHCCCCCCCCCHH | 27.44 | 22817900 | |
483 | Phosphorylation | DMSISNTTMDEFRQH CCCCCCCCHHHHHHH | 27.20 | 22817900 | |
503 (in isoform 3) | Ubiquitination | - | 4.42 | 21890473 | |
510 | Phosphorylation | LTVRVLTTGYWPTQS EEEEEEECCCCCCCC | 24.90 | 28152594 | |
512 | Phosphorylation | VRVLTTGYWPTQSAT EEEEECCCCCCCCCC | 13.21 | 28152594 | |
515 | Phosphorylation | LTTGYWPTQSATPKC EECCCCCCCCCCCCC | 22.47 | 28348404 | |
517 | Phosphorylation | TGYWPTQSATPKCNI CCCCCCCCCCCCCCC | 36.27 | 28348404 | |
519 | Phosphorylation | YWPTQSATPKCNIPP CCCCCCCCCCCCCCC | 28.64 | 20068231 | |
536 | Methylation | RHAFEIFRRFYLAKH HHHHHHHHHHHHHHH | 33.20 | - | |
545 (in isoform 2) | Ubiquitination | - | 22.52 | 21890473 | |
556 | Phosphorylation | TLQHHMGSADLNATF EHHHHCCCCCCCCEE | 15.84 | 23879269 | |
562 | Phosphorylation | GSADLNATFYGPVKK CCCCCCCEEECCEEC | 19.13 | 23879269 | |
564 | Phosphorylation | ADLNATFYGPVKKED CCCCCEEECCEECCC | 19.03 | 23879269 | |
569 | Ubiquitination | TFYGPVKKEDGSEVG EEECCEECCCCCEEE | 62.36 | 21906983 | |
569 (in isoform 1) | Ubiquitination | - | 62.36 | 21890473 | |
573 | Phosphorylation | PVKKEDGSEVGVGGA CEECCCCCEEECCCE | 41.24 | 28555341 | |
583 | Phosphorylation | GVGGAQVTGSNTRKH ECCCEEEECCCHHHE | 23.86 | 24245541 | |
585 | Phosphorylation | GGAQVTGSNTRKHIL CCEEEECCCHHHEEE | 26.18 | 25056879 | |
587 | Phosphorylation | AQVTGSNTRKHILQV EEEECCCHHHEEEEE | 42.67 | 27732954 | |
602 (in isoform 3) | Ubiquitination | - | 1.47 | 21890473 | |
634 (in isoform 3) | Ubiquitination | - | 2.70 | 21890473 | |
638 | Malonylation | LQSLACGKPTQRVLT HHHHHCCCCCHHEEC | 44.79 | 26320211 | |
638 | Ubiquitination | LQSLACGKPTQRVLT HHHHHCCCCCHHEEC | 44.79 | - | |
644 (in isoform 2) | Ubiquitination | - | 6.53 | 21890473 | |
646 | Ubiquitination | PTQRVLTKEPKSKEI CCHHEECCCCCCCCC | 68.78 | - | |
651 | Acetylation | LTKEPKSKEIENGHI ECCCCCCCCCCCCEE | 69.69 | 23954790 | |
651 | Malonylation | LTKEPKSKEIENGHI ECCCCCCCCCCCCEE | 69.69 | 26320211 | |
651 | Ubiquitination | LTKEPKSKEIENGHI ECCCCCCCCCCCCEE | 69.69 | - | |
668 | Ubiquitination | VNDQFTSKLHRVKIQ ECHHHHCCCCEEEEE | 45.30 | 21890473 | |
668 (in isoform 1) | Ubiquitination | - | 45.30 | 21890473 | |
673 | Malonylation | TSKLHRVKIQTVAAK HCCCCEEEEEEHHHH | 29.11 | 26320211 | |
673 | Ubiquitination | TSKLHRVKIQTVAAK HCCCCEEEEEEHHHH | 29.11 | - | |
676 (in isoform 2) | Ubiquitination | - | 18.65 | 21890473 | |
680 | Acetylation | KIQTVAAKQGESDPE EEEEHHHHCCCCCHH | 49.45 | 26051181 | |
680 | Ubiquitination | KIQTVAAKQGESDPE EEEEHHHHCCCCCHH | 49.45 | - | |
684 | Phosphorylation | VAAKQGESDPERKET HHHHCCCCCHHHHHH | 66.35 | 24719451 | |
700 | Ubiquitination | QKVDDDRKHEIEAAI HHCCHHHHHHHHHHH | 53.21 | 21890473 | |
700 (in isoform 1) | Ubiquitination | - | 53.21 | 21890473 | |
712 | Ubiquitination | AAIVRIMKSRKKMQH HHHHHHHHHCHHHCC | 44.74 | - | |
737 | Phosphorylation | LKARFLPSPVVIKKR HHHHCCCCCCHHHHH | 32.26 | 25159151 | |
742 | 2-Hydroxyisobutyrylation | LPSPVVIKKRIEGLI CCCCCHHHHHHHHHH | 25.12 | - | |
742 | Acetylation | LPSPVVIKKRIEGLI CCCCCHHHHHHHHHH | 25.12 | 25953088 | |
742 | Malonylation | LPSPVVIKKRIEGLI CCCCCHHHHHHHHHH | 25.12 | 26320211 | |
743 | Malonylation | PSPVVIKKRIEGLIE CCCCHHHHHHHHHHH | 47.70 | 26320211 | |
743 | Phosphorylation | PSPVVIKKRIEGLIE CCCCHHHHHHHHHHH | 47.70 | 27251275 | |
743 | Ubiquitination | PSPVVIKKRIEGLIE CCCCHHHHHHHHHHH | 47.70 | - | |
764 | Phosphorylation | TPEDRKVYTYVA--- CCCCCCEEEEEC--- | 8.73 | 22448038 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CUL3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CUL3_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CUL3_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
614496 | Pseudohypoaldosteronism 2E (PHA2E) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND MASSSPECTROMETRY. | |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58, AND MASSSPECTROMETRY. |