UniProt ID | CUL2_HUMAN | |
---|---|---|
UniProt AC | Q13617 | |
Protein Name | Cullin-2 | |
Gene Name | CUL2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 745 | |
Subcellular Localization | ||
Protein Description | Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. [PubMed: 27565346 May serve as a rigid scaffold in the complex and 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 ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF] | |
Protein Sequence | MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA | |
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 |
---|---|---|---|---|---|
16 | Ubiquitination | DFDETWNKLLTTIKA CCHHHHHHHHHHHHH | 36.11 | 21906983 | |
22 | Ubiquitination | NKLLTTIKAVVMLEY HHHHHHHHHHHHHHH | 32.79 | - | |
43 | Phosphorylation | NDRFSDIYALCVAYP CCHHHHHHHHHHHCC | 9.86 | 24114839 | |
49 | Phosphorylation | IYALCVAYPEPLGER HHHHHHHCCCCCCCC | 6.42 | 24114839 | |
107 | Phosphorylation | YMDCLYRYLNTQFIK HHHHHHHHHHHHHHH | 7.25 | 28442448 | |
110 | Phosphorylation | CLYRYLNTQFIKKNK HHHHHHHHHHHHHCC | 23.43 | 28152594 | |
126 (in isoform 2) | Phosphorylation | - | 11.14 | 27642862 | |
149 | Ubiquitination | LALDMWRKLMVEPLQ HHHHHHHHHCHHHHH | 25.97 | - | |
151 | Sulfoxidation | LDMWRKLMVEPLQAI HHHHHHHCHHHHHHH | 3.44 | 21406390 | |
168 | Ubiquitination | RMLLREIKNDRGGED HHHHHHHHCCCCCCC | 48.30 | - | |
224 | Phosphorylation | EYYKQEASNLLQESN HHHHHHHHHHHHHCC | 27.53 | 20068231 | |
238 | Ubiquitination | NCSQYMEKVLGRLKD CHHHHHHHHHHHHCH | 26.65 | - | |
252 | Ubiquitination | DEEIRCRKYLHPSSY HHCHHHHHHCCHHHH | 56.65 | - | |
298 | Phosphorylation | KNDMANMYVLLRAVS HHHHHHHHHHHHHHH | 6.43 | 20860994 | |
382 | Ubiquitination | VVNYREPKSVCKAPE HCCCCCCHHHCCCHH | 51.25 | - | |
393 | Acetylation | KAPELLAKYCDNLLK CCHHHHHHHHHHHHH | 46.51 | 19608861 | |
393 | Ubiquitination | KAPELLAKYCDNLLK CCHHHHHHHHHHHHH | 46.51 | 19608861 | |
400 | Acetylation | KYCDNLLKKSAKGMT HHHHHHHHHHHCCCC | 48.09 | 25953088 | |
401 | Ubiquitination | YCDNLLKKSAKGMTE HHHHHHHHHHCCCCH | 56.46 | - | |
404 | Ubiquitination | NLLKKSAKGMTENEV HHHHHHHCCCCHHHH | 57.20 | 21906983 | |
412 | Acetylation | GMTENEVEDRLTSFI CCCHHHHHHHHHHHH | 31.10 | 19608861 | |
414 | Methylation | TENEVEDRLTSFITV CHHHHHHHHHHHHHH | 26.76 | - | |
416 | Phosphorylation | NEVEDRLTSFITVFK HHHHHHHHHHHHHHH | 23.61 | 24719451 | |
417 | Phosphorylation | EVEDRLTSFITVFKY HHHHHHHHHHHHHHH | 21.17 | 24719451 | |
419 (in isoform 2) | Malonylation | - | 3.00 | 32601280 | |
423 | Ubiquitination | TSFITVFKYIDDKDV HHHHHHHHHCCCHHH | 36.64 | - | |
424 | Phosphorylation | SFITVFKYIDDKDVF HHHHHHHHCCCHHHH | 9.71 | 24719451 | |
428 | Ubiquitination | VFKYIDDKDVFQKFY HHHHCCCHHHHHHHH | 52.63 | - | |
433 | Ubiquitination | DDKDVFQKFYARMLA CCHHHHHHHHHHHHH | 28.95 | 21890473 | |
433 | Acetylation | DDKDVFQKFYARMLA CCHHHHHHHHHHHHH | 28.95 | 25953088 | |
435 (in isoform 2) | Phosphorylation | - | 10.59 | 24719451 | |
436 (in isoform 2) | Phosphorylation | - | 8.11 | 24719451 | |
443 (in isoform 2) | Phosphorylation | - | 3.14 | 24719451 | |
452 | Ubiquitination | HGLSMSMDSEEAMIN HHHCCCCCCHHHHHH | 45.66 | 21890473 | |
462 | Ubiquitination | EAMINKLKQACGYEF HHHHHHHHHHHCCHH | 37.14 | - | |
472 | Acetylation | CGYEFTSKLHRMYTD HCCHHHHHHHHHHCC | 45.30 | 25953088 | |
477 | Phosphorylation | TSKLHRMYTDMSVSA HHHHHHHHCCCCCEE | 10.27 | 22817900 | |
478 | Phosphorylation | SKLHRMYTDMSVSAD HHHHHHHCCCCCEEH | 18.84 | 22210691 | |
481 | Phosphorylation | HRMYTDMSVSADLNN HHHHCCCCCEEHHHH | 18.74 | - | |
568 | Phosphorylation | TGEVKMNYLGKPYVA CCCCCHHCCCCCEEE | 17.21 | 28111955 | |
573 | Phosphorylation | MNYLGKPYVAMVTTY HHCCCCCEEEEEEHH | 12.34 | 28111955 | |
578 | Phosphorylation | KPYVAMVTTYQMAVL CCEEEEEEHHHHHHH | 13.50 | 28111955 | |
579 | Phosphorylation | PYVAMVTTYQMAVLL CEEEEEEHHHHHHHH | 10.59 | 28111955 | |
580 | Phosphorylation | YVAMVTTYQMAVLLA EEEEEEHHHHHHHHH | 6.21 | 28111955 | |
591 | Phosphorylation | VLLAFNNSETVSYKE HHHHHCCCCCCCHHH | 35.43 | 28111955 | |
593 | Phosphorylation | LAFNNSETVSYKELQ HHHCCCCCCCHHHHH | 17.99 | 28111955 | |
595 | Phosphorylation | FNNSETVSYKELQDS HCCCCCCCHHHHHCC | 37.60 | 28111955 | |
596 | Phosphorylation | NNSETVSYKELQDST CCCCCCCHHHHHCCC | 12.26 | 28111955 | |
602 | Phosphorylation | SYKELQDSTQMNEKE CHHHHHCCCCCCHHH | 13.95 | 29083192 | |
603 | Phosphorylation | YKELQDSTQMNEKEL HHHHHCCCCCCHHHH | 39.88 | 29083192 | |
608 | Acetylation | DSTQMNEKELTKTIK CCCCCCHHHHHHHHH | 53.68 | 23236377 | |
608 | Ubiquitination | DSTQMNEKELTKTIK CCCCCCHHHHHHHHH | 53.68 | 21906983 | |
611 | Phosphorylation | QMNEKELTKTIKSLL CCCHHHHHHHHHHHH | 27.51 | 29083192 | |
612 | Acetylation | MNEKELTKTIKSLLD CCHHHHHHHHHHHHC | 61.96 | 23236377 | |
613 | Phosphorylation | NEKELTKTIKSLLDV CHHHHHHHHHHHHCH | 28.53 | 29083192 | |
616 | Phosphorylation | ELTKTIKSLLDVKMI HHHHHHHHHHCHHCC | 30.25 | 24961811 | |
627 | Ubiquitination | VKMINHDSEKEDIDA HHCCCCCCCCCCCCC | 42.91 | 21890473 | |
635 (in isoform 2) | Phosphorylation | - | 43.07 | 24719451 | |
637 | Phosphorylation | EDIDAESSFSLNMNF CCCCCCCCCEEECCC | 15.45 | - | |
652 | Malonylation | SSKRTKFKITTSMQK CCCCCEEEEEECCCC | 40.47 | 26320211 | |
656 | Phosphorylation | TKFKITTSMQKDTPQ CEEEEEECCCCCCHH | 15.57 | 23186163 | |
659 | Malonylation | KITTSMQKDTPQEME EEEECCCCCCHHHHH | 55.73 | 26320211 | |
659 | Ubiquitination | KITTSMQKDTPQEME EEEECCCCCCHHHHH | 55.73 | - | |
661 | Phosphorylation | TTSMQKDTPQEMEQT EECCCCCCHHHHHHH | 33.63 | 25159151 | |
668 | Phosphorylation | TPQEMEQTRSAVDED CHHHHHHHHHHCHHH | 17.18 | 23186163 | |
671 (in isoform 2) | Malonylation | - | 14.97 | 26320211 | |
677 | Malonylation | SAVDEDRKMYLQAAI HHCHHHHHHHHHHHH | 44.19 | 26320211 | |
678 (in isoform 2) | Malonylation | - | 4.15 | 26320211 | |
689 | Neddylation | AAIVRIMKARKVLRH HHHHHHHHHHHHHHH | 42.54 | 11818338 | |
689 | Ubiquitination | AAIVRIMKARKVLRH HHHHHHHHHHHHHHH | 42.54 | - | |
696 (in isoform 2) | Malonylation | - | 21.54 | 26320211 | |
714 | Phosphorylation | SRARFNPSISMIKKC HHHHCCCCHHHHHHH | 28.53 | 28348404 | |
716 | Phosphorylation | ARFNPSISMIKKCIE HHCCCCHHHHHHHHH | 20.84 | 28348404 | |
719 | Acetylation | NPSISMIKKCIEVLI CCCHHHHHHHHHHHH | 32.71 | 25953088 | |
719 | Malonylation | NPSISMIKKCIEVLI CCCHHHHHHHHHHHH | 32.71 | 26320211 | |
719 | Neddylation | NPSISMIKKCIEVLI CCCHHHHHHHHHHHH | 32.71 | - | |
720 | Ubiquitination | PSISMIKKCIEVLID CCHHHHHHHHHHHHC | 29.53 | - | |
720 | Malonylation | PSISMIKKCIEVLID CCHHHHHHHHHHHHC | 29.53 | 26320211 | |
738 (in isoform 2) | Malonylation | - | 19.37 | 26320211 | |
739 (in isoform 2) | Malonylation | - | 53.52 | 26320211 |
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 CUL2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CUL2_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 CUL2_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-393, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-661, AND MASSSPECTROMETRY. |