UniProt ID | CUL1_HUMAN | |
---|---|---|
UniProt AC | Q13616 | |
Protein Name | Cullin-1 | |
Gene Name | CUL1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 776 | |
Subcellular Localization | ||
Protein Description | 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. SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. [PubMed: 27565346 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(BTRC) and/or SCF(FBXW11) direct ubiquitination of CEP68] | |
Protein Sequence | MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRHWVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA | |
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 | Phosphorylation | ------MSSTRSQNP ------CCCCCCCCC | 40.18 | 25159151 | |
3 | Phosphorylation | -----MSSTRSQNPH -----CCCCCCCCCC | 26.92 | 25159151 | |
4 | Phosphorylation | ----MSSTRSQNPHG ----CCCCCCCCCCC | 27.34 | 26074081 | |
6 | Phosphorylation | --MSSTRSQNPHGLK --CCCCCCCCCCCHH | 34.10 | 29514088 | |
13 | Acetylation | SQNPHGLKQIGLDQI CCCCCCHHHCCHHHH | 44.45 | 26051181 | |
32 | Phosphorylation | RAGIQQVYTRQSMAK HHHHHHHHHHHHHHH | 7.59 | 20068231 | |
40 | Phosphorylation | TRQSMAKSRYMELYT HHHHHHHHHHHHHHH | 21.07 | 22210691 | |
50 | Phosphorylation | MELYTHVYNYCTSVH HHHHHHHHHHHHHHH | 7.88 | 22210691 | |
63 | Methylation | VHQSNQARGAGVPPS HHHHCCCCCCCCCCC | 26.23 | 24129315 | |
70 | Phosphorylation | RGAGVPPSKSKKGQT CCCCCCCCCCCCCCC | 43.41 | 20068231 | |
73 | Methylation | GVPPSKSKKGQTPGG CCCCCCCCCCCCCCC | 65.74 | - | |
74 | Ubiquitination | VPPSKSKKGQTPGGA CCCCCCCCCCCCCCC | 64.44 | - | |
77 | Phosphorylation | SKSKKGQTPGGAQFV CCCCCCCCCCCCCCH | 32.35 | 21815630 | |
99 | Phosphorylation | LKEFLKNYLTNLLKD HHHHHHHHHHHHHHC | 17.20 | 26657352 | |
101 | Phosphorylation | EFLKNYLTNLLKDGE HHHHHHHHHHHHCCC | 17.29 | 20068231 | |
114 | Phosphorylation | GEDLMDESVLKFYTQ CCCCCCHHHHHHHHH | 28.61 | 29209046 | |
131 | Ubiquitination | EDYRFSSKVLNGICA CHHCCCHHHHHHHHH | 49.93 | 21906983 | |
290 | Ubiquitination | TQDELARKCEQVLIE CHHHHHHHHHHHHHH | 36.19 | - | |
327 | Phosphorylation | GRMYNLVSRIQDGLG HHHHHHHHHHHHCHH | 27.17 | 27762562 | |
337 | Acetylation | QDGLGELKKLLETHI HHCHHHHHHHHHHHC | 36.75 | 27452117 | |
337 | 2-Hydroxyisobutyrylation | QDGLGELKKLLETHI HHCHHHHHHHHHHHC | 36.75 | - | |
342 | Phosphorylation | ELKKLLETHIHNQGL HHHHHHHHHCHHHHH | 26.54 | 30576142 | |
383 | Phosphorylation | KYNALVMSAFNNDAG HHCHHHHHHHCCCHH | 23.41 | 29507054 | |
409 | Phosphorylation | FINNNAVTKMAQSSS HHCHHHHHHHHHCCC | 16.82 | - | |
410 | Ubiquitination | INNNAVTKMAQSSSK HCHHHHHHHHHCCCC | 26.16 | 21906983 | |
417 | Ubiquitination | KMAQSSSKSPELLAR HHHHCCCCCHHHHHH | 72.48 | - | |
425 | Phosphorylation | SPELLARYCDSLLKK CHHHHHHHHHHHHHH | 8.59 | 21406692 | |
428 | Phosphorylation | LLARYCDSLLKKSSK HHHHHHHHHHHHHCC | 31.85 | 24719451 | |
431 | Acetylation | RYCDSLLKKSSKNPE HHHHHHHHHHCCCHH | 56.77 | 23749302 | |
432 | Ubiquitination | YCDSLLKKSSKNPEE HHHHHHHHHCCCHHH | 60.99 | - | |
464 | Ubiquitination | EDKDVFQKFYAKMLA CCHHHHHHHHHHHHH | 28.95 | 21890473 | |
464 | Malonylation | EDKDVFQKFYAKMLA CCHHHHHHHHHHHHH | 28.95 | 26320211 | |
466 | Phosphorylation | KDVFQKFYAKMLAKR HHHHHHHHHHHHHHH | 16.61 | 23403867 | |
468 | Acetylation | VFQKFYAKMLAKRLV HHHHHHHHHHHHHHH | 24.06 | 26051181 | |
468 | Ubiquitination | VFQKFYAKMLAKRLV HHHHHHHHHHHHHHH | 24.06 | 21890473 | |
468 | Malonylation | VFQKFYAKMLAKRLV HHHHHHHHHHHHHHH | 24.06 | 26320211 | |
472 | Neddylation | FYAKMLAKRLVHQNS HHHHHHHHHHHHCCC | 42.16 | - | |
493 | Ubiquitination | ASMISKLKQACGFEY HHHHHHHHHHHCCCC | 39.32 | - | |
503 | Acetylation | CGFEYTSKLQRMFQD HCCCCHHHHHHHHHH | 40.62 | 26051181 | |
522 | Ubiquitination | KDLNEQFKKHLTNSE CCHHHHHHHHCCCCC | 38.69 | - | |
583 | Phosphorylation | GRKLTWLYQLSKGEL CCCEEEEEECCCCCE | 10.04 | 26437602 | |
587 | Ubiquitination | TWLYQLSKGELVTNC EEEEECCCCCEECHH | 66.06 | - | |
647 | 2-Hydroxyisobutyrylation | LQILLKSKLLVLEDE HHHHHHCCCEEEECC | 44.23 | - | |
688 | Sulfoxidation | RVNINVPMKTEQKQE EEEEECCCCCHHHHH | 7.95 | 21406390 | |
689 | Ubiquitination | VNINVPMKTEQKQEQ EEEECCCCCHHHHHH | 42.72 | 21906983 | |
689 | Acetylation | VNINVPMKTEQKQEQ EEEECCCCCHHHHHH | 42.72 | 71287 | |
693 | Ubiquitination | VPMKTEQKQEQETTH CCCCCHHHHHHHHCC | 49.96 | - | |
708 | Ubiquitination | KNIEEDRKLLIQAAI CCHHHHHHHHHHHHH | 61.03 | 21906983 | |
720 | Ubiquitination | AAIVRIMKMRKVLKH HHHHHHHHHHHHHHH | 32.93 | - | |
720 | Neddylation | AAIVRIMKMRKVLKH HHHHHHHHHHHHHHH | 32.93 | 12504026 | |
751 | Ubiquitination | PRVPVIKKCIDILIE CCCHHHHHHHHHHHH | 25.87 | - | |
751 | Malonylation | PRVPVIKKCIDILIE CCCHHHHHHHHHHHH | 25.87 | 26320211 | |
769 | Ubiquitination | LERVDGEKDTYSYLA HHHCCCCCCCCCCCC | 61.98 | 21906983 | |
769 | Neddylation | LERVDGEKDTYSYLA HHHCCCCCCCCCCCC | 61.98 | - |
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 CUL1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CUL1_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 CUL1_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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Ubiquitylation | |
Reference | PubMed |
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-708 AND LYS-720, AND MASSSPECTROMETRY. |