UniProt ID | CUL4A_HUMAN | |
---|---|---|
UniProt AC | Q13619 | |
Protein Name | Cullin-4A | |
Gene Name | CUL4A | |
Organism | Homo sapiens (Human). | |
Sequence Length | 759 | |
Subcellular Localization | ||
Protein Description | Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins. 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 E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL.. | |
Protein Sequence | MADEAPRKGSFSALVGRTNGLTKPAALAAAPAKPGGAGGSKKLVIKNFRDRPRLPDNYTQDTWRKLHEAVRAVQSSTSIRYNLEELYQAVENLCSHKVSPMLYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSTLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIVINPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDNPNQYHYVA | |
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 |
---|---|---|---|---|---|
8 | Acetylation | MADEAPRKGSFSALV CCCCCCCCCCHHHHH | 58.82 | 26051181 | |
8 | Sumoylation | MADEAPRKGSFSALV CCCCCCCCCCHHHHH | 58.82 | 28112733 | |
8 | Ubiquitination | MADEAPRKGSFSALV CCCCCCCCCCHHHHH | 58.82 | - | |
10 | Phosphorylation | DEAPRKGSFSALVGR CCCCCCCCHHHHHCC | 21.04 | 29255136 | |
12 | Phosphorylation | APRKGSFSALVGRTN CCCCCCHHHHHCCCC | 23.53 | 30266825 | |
22 | Phosphorylation | VGRTNGLTKPAALAA HCCCCCCCCHHHHHC | 36.06 | 22817900 | |
23 | Acetylation | GRTNGLTKPAALAAA CCCCCCCCHHHHHCC | 37.39 | 26051181 | |
33 | Acetylation | ALAAAPAKPGGAGGS HHHCCCCCCCCCCCC | 43.04 | 26051181 | |
33 | Ubiquitination | ALAAAPAKPGGAGGS HHHCCCCCCCCCCCC | 43.04 | 18781797 | |
40 | Phosphorylation | KPGGAGGSKKLVIKN CCCCCCCCCEEEEEC | 26.21 | 29514088 | |
41 | Acetylation | PGGAGGSKKLVIKNF CCCCCCCCEEEEECC | 54.09 | 12435295 | |
42 | Acetylation | GGAGGSKKLVIKNFR CCCCCCCEEEEECCC | 50.08 | 12436343 | |
58 | Phosphorylation | RPRLPDNYTQDTWRK CCCCCCCCCHHHHHH | 17.10 | 27642862 | |
75 | Phosphorylation | EAVRAVQSSTSIRYN HHHHHHHCCCCCCCC | 29.05 | 20860994 | |
76 | Phosphorylation | AVRAVQSSTSIRYNL HHHHHHCCCCCCCCH | 14.75 | 21406692 | |
77 | Phosphorylation | VRAVQSSTSIRYNLE HHHHHCCCCCCCCHH | 33.16 | 21406692 | |
78 | Phosphorylation | RAVQSSTSIRYNLEE HHHHCCCCCCCCHHH | 13.66 | 21406692 | |
99 | Phosphorylation | NLCSHKVSPMLYKQL HHHHCCCCHHHHHHH | 14.92 | 19413330 | |
104 | Acetylation | KVSPMLYKQLRQACE CCCHHHHHHHHHHHH | 38.60 | 25953088 | |
104 | Malonylation | KVSPMLYKQLRQACE CCCHHHHHHHHHHHH | 38.60 | 26320211 | |
104 | Ubiquitination | KVSPMLYKQLRQACE CCCHHHHHHHHHHHH | 38.60 | - | |
104 (in isoform 1) | Ubiquitination | - | 38.60 | 21890473 | |
133 | Acetylation | LDSVLFLKKINTCWQ CHHHHHHHHHHHHCH | 44.25 | 27452117 | |
133 | Ubiquitination | LDSVLFLKKINTCWQ CHHHHHHHHHHHHCH | 44.25 | - | |
151 | Phosphorylation | RQMIMIRSIFLFLDR HHHHHHHHHHHHCCC | 13.53 | 21712546 | |
159 | Phosphorylation | IFLFLDRTYVLQNST HHHHCCCCHHHCCCC | 20.04 | 23898821 | |
160 | Phosphorylation | FLFLDRTYVLQNSTL HHHCCCCHHHCCCCC | 10.48 | 23898821 | |
165 | Phosphorylation | RTYVLQNSTLPSIWD CCHHHCCCCCCCHHH | 20.54 | 23898821 | |
166 | Phosphorylation | TYVLQNSTLPSIWDM CHHHCCCCCCCHHHH | 50.68 | 23898821 | |
169 | Phosphorylation | LQNSTLPSIWDMGLE HCCCCCCCHHHHHHH | 39.15 | 23898821 | |
180 | Phosphorylation | MGLELFRTHIISDKM HHHHHHHHHHCCCHH | 15.30 | 23898821 | |
184 | Phosphorylation | LFRTHIISDKMVQSK HHHHHHCCCHHHCCC | 30.49 | 23898821 | |
186 | Ubiquitination | RTHIISDKMVQSKTI HHHHCCCHHHCCCCC | 33.89 | - | |
216 | Phosphorylation | VDRSLLRSLLGMLSD HCHHHHHHHHHHHCC | 28.10 | 20068231 | |
227 | Phosphorylation | MLSDLQVYKDSFELK HHCCHHHHHCCEEEE | 8.98 | 22817900 | |
234 | Ubiquitination | YKDSFELKFLEETNC HHCCEEEEEHHHHCC | 40.48 | - | |
259 | Phosphorylation | QEREVPEYLNHVSKR HHHCHHHHHHHHHHH | 13.51 | - | |
265 | Ubiquitination | EYLNHVSKRLEEEGD HHHHHHHHHHHHCCC | 60.97 | - | |
276 | O-linked_Glycosylation | EEGDRVITYLDHSTQ HCCCCEEEEEECCCC | 18.38 | 28510447 | |
284 | Acetylation | YLDHSTQKPLIACVE EEECCCCCCHHHHHH | 41.71 | 26051181 | |
284 | Malonylation | YLDHSTQKPLIACVE EEECCCCCCHHHHHH | 41.71 | 26320211 | |
284 | Ubiquitination | YLDHSTQKPLIACVE EEECCCCCCHHHHHH | 41.71 | - | |
292 | Acetylation | PLIACVEKQLLGEHL CHHHHHHHHHHHHHH | 26.33 | 26051181 | |
322 (in isoform 2) | Ubiquitination | - | 1.59 | 21890473 | |
330 | Methylation | YQLFSRVRGGQQALL HHHHHHHHHHHHHHH | 42.27 | - | |
354 (in isoform 2) | Ubiquitination | - | 27.99 | 21890473 | |
357 | Ubiquitination | AIVINPEKDKDMVQD EEEECCCCCHHHHHH | 71.92 | - | |
359 | Ubiquitination | VINPEKDKDMVQDLL EECCCCCHHHHHHHH | 59.81 | - | |
369 | Ubiquitination | VQDLLDFKDKVDHVI HHHHHHHHHHHCHHH | 57.20 | - | |
391 | Ubiquitination | ERFVNLMKESFETFI HHHHHHHHHHHHHHH | 54.06 | - | |
396 (in isoform 2) | Ubiquitination | - | 28.01 | 21890473 | |
404 | Ubiquitination | FINKRPNKPAELIAK HHHCCCCCCHHHHHH | 48.57 | - | |
411 | Ubiquitination | KPAELIAKHVDSKLR CCHHHHHHHHHHHHH | 36.85 | - | |
416 | Ubiquitination | IAKHVDSKLRAGNKE HHHHHHHHHHCCCCC | 37.21 | - | |
422 | Acetylation | SKLRAGNKEATDEEL HHHHCCCCCCCHHHH | 48.05 | 26051181 | |
422 | Ubiquitination | SKLRAGNKEATDEEL HHHHCCCCCCCHHHH | 48.05 | 21906983 | |
422 (in isoform 1) | Ubiquitination | - | 48.05 | 21890473 | |
425 | Phosphorylation | RAGNKEATDEELERT HCCCCCCCHHHHHHH | 45.06 | 20860994 | |
453 | Phosphorylation | KDVFEAFYKKDLAKR HHHHHHHHCHHHHHH | 24.95 | - | |
454 | Ubiquitination | DVFEAFYKKDLAKRL HHHHHHHCHHHHHHH | 33.10 | 2190698 | |
454 (in isoform 1) | Ubiquitination | - | 33.10 | 21890473 | |
465 | Acetylation | AKRLLVGKSASVDAE HHHHHCCCCCCCHHH | 35.06 | 25953088 | |
465 | Malonylation | AKRLLVGKSASVDAE HHHHHCCCCCCCHHH | 35.06 | 26320211 | |
465 | Ubiquitination | AKRLLVGKSASVDAE HHHHHCCCCCCCHHH | 35.06 | - | |
473 | Acetylation | SASVDAEKSMLSKLK CCCCHHHHHHHHHHH | 42.77 | 25953088 | |
477 | Phosphorylation | DAEKSMLSKLKHECG HHHHHHHHHHHHHHC | 27.57 | 24260401 | |
480 | Acetylation | KSMLSKLKHECGAAF HHHHHHHHHHHCHHH | 40.88 | 26051181 | |
480 | Ubiquitination | KSMLSKLKHECGAAF HHHHHHHHHHHCHHH | 40.88 | - | |
490 | Ubiquitination | CGAAFTSKLEGMFKD HCHHHHHHHHHHHCC | 47.72 | - | |
496 | Acetylation | SKLEGMFKDMELSKD HHHHHHHCCCCCCHH | 47.47 | 26051181 | |
496 | Ubiquitination | SKLEGMFKDMELSKD HHHHHHHCCCCCCHH | 47.47 | - | |
496 (in isoform 1) | Ubiquitination | - | 47.47 | 21890473 | |
502 | Ubiquitination | FKDMELSKDIMVHFK HCCCCCCHHHHHHHH | 64.99 | - | |
541 | Acetylation | PTYTPMEVHLTPEMI CCCCCCEEECCHHHH | 3.49 | 19608861 | |
541 (in isoform 2) | Acetylation | - | 3.49 | - | |
555 | Acetylation | IKLQEVFKAFYLGKH HHHHHHHHHHHCCCC | 42.64 | 129845 | |
561 | Acetylation | FKAFYLGKHSGRKLQ HHHHHCCCCCCCCEE | 31.81 | 25953088 | |
561 | Ubiquitination | FKAFYLGKHSGRKLQ HHHHHCCCCCCCCEE | 31.81 | - | |
615 | Sulfoxidation | FSFEEIKMATGIEDS CCHHHHHHHHCCCHH | 5.05 | 21406390 | |
633 | S-nitrosylation | RTLQSLACGKARVLI HHHHHHHCCCEEEEE | 7.53 | 22126794 | |
635 | Acetylation | LQSLACGKARVLIKS HHHHHCCCEEEEEEC | 32.67 | 25953088 | |
635 | Malonylation | LQSLACGKARVLIKS HHHHHCCCEEEEEEC | 32.67 | 26320211 | |
635 | Ubiquitination | LQSLACGKARVLIKS HHHHHCCCEEEEEEC | 32.67 | - | |
641 | Acetylation | GKARVLIKSPKGKEV CCEEEEEECCCCCCC | 57.45 | 19608861 | |
642 | Phosphorylation | KARVLIKSPKGKEVE CEEEEEECCCCCCCC | 25.50 | 23911959 | |
646 | Acetylation | LIKSPKGKEVEDGDK EEECCCCCCCCCCCE | 65.79 | 26051181 | |
646 | Ubiquitination | LIKSPKGKEVEDGDK EEECCCCCCCCCCCE | 65.79 | - | |
661 | Ubiquitination | FIFNGEFKHKLFRIK EEECCCCCCEEEEEE | 35.21 | - | |
683 | Phosphorylation | ETVEEQVSTTERVFQ HHHHHHHHHHHHHHH | 29.34 | 24719451 | |
684 | Phosphorylation | TVEEQVSTTERVFQD HHHHHHHHHHHHHHH | 33.54 | 25627689 | |
692 | Methylation | TERVFQDRQYQIDAA HHHHHHHHHHHHHHH | 26.73 | - | |
702 | Dimethylation | QIDAAIVRIMKMRKT HHHHHHHHHHHHHHH | 19.71 | - | |
705 | Ubiquitination | AAIVRIMKMRKTLGH HHHHHHHHHHHHHCC | 32.93 | - | |
708 | Ubiquitination | VRIMKMRKTLGHNLL HHHHHHHHHHCCCHH | 44.60 | - | |
724 | Ubiquitination | SELYNQLKFPVKPGD HHHHHHCCCCCCCCC | 37.55 | - | |
728 | Acetylation | NQLKFPVKPGDLKKR HHCCCCCCCCCHHHH | 43.45 | 25953088 | |
728 | Ubiquitination | NQLKFPVKPGDLKKR HHCCCCCCCCCHHHH | 43.45 | - | |
733 | Malonylation | PVKPGDLKKRIESLI CCCCCCHHHHHHHHH | 44.75 | 26320211 | |
733 | Ubiquitination | PVKPGDLKKRIESLI CCCCCCHHHHHHHHH | 44.75 | - | |
738 | Phosphorylation | DLKKRIESLIDRDYM CHHHHHHHHHCHHHH | 28.40 | 26074081 | |
742 | Methylation | RIESLIDRDYMERDK HHHHHHCHHHHHHCC | 29.93 | - | |
744 | Phosphorylation | ESLIDRDYMERDKDN HHHHCHHHHHHCCCC | 11.19 | 26074081 | |
749 | Ubiquitination | RDYMERDKDNPNQYH HHHHHHCCCCCCCCC | 66.67 | - |
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 CUL4A_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CUL4A_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 CUL4A_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
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. |
loading...
Phosphorylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY. | |
"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 SER-10, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY. | |
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, UBIQUITINATION[LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY. | |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227, AND MASSSPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, UBIQUITINATION[LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY. |