| UniProt ID | RAD21_HUMAN | |
|---|---|---|
| UniProt AC | O60216 | |
| Protein Name | Double-strand-break repair protein rad21 homolog | |
| Gene Name | RAD21 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 631 | |
| Subcellular Localization | Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except | |
| Protein Description | Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Also plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway.. | |
| Protein Sequence | MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPIIEEPSRLQESVMEASRTNIDESAMPPPPPQGVKRKAGQIDPEPVMPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MFYAHFVL -------CCCEEEEE | 5.38 | - | |
| 9 | Phosphorylation | FYAHFVLSKRGPLAK CCEEEEECCCCHHHH | 18.27 | 19413330 | |
| 25 | Ubiquitination | WLAAHWDKKLTKAHV HHHHHHCHHCCHHEE | 44.48 | 21890473 | |
| 26 | Ubiquitination | LAAHWDKKLTKAHVF HHHHHCHHCCHHEEE | 59.94 | - | |
| 29 | Ubiquitination | HWDKKLTKAHVFECN HHCHHCCHHEEEECC | 47.10 | - | |
| 39 | Phosphorylation | VFECNLESSVESIIS EEECCCCHHHHHHHC | 42.73 | 27251275 | |
| 40 | Phosphorylation | FECNLESSVESIISP EECCCCHHHHHHHCH | 22.11 | 30266825 | |
| 43 | Phosphorylation | NLESSVESIISPKVK CCCHHHHHHHCHHHH | 24.06 | 30266825 | |
| 46 | Phosphorylation | SSVESIISPKVKMAL HHHHHHHCHHHHHHH | 19.59 | 30266825 | |
| 48 | Ubiquitination | VESIISPKVKMALRT HHHHHCHHHHHHHHH | 47.93 | - | |
| 48 | Sumoylation | VESIISPKVKMALRT HHHHHCHHHHHHHHH | 47.93 | 28112733 | |
| 50 | Ubiquitination | SIISPKVKMALRTSG HHHCHHHHHHHHHCC | 25.28 | - | |
| 55 | Phosphorylation | KVKMALRTSGHLLLG HHHHHHHHCCHHHHH | 39.65 | 19835603 | |
| 56 | Phosphorylation | VKMALRTSGHLLLGV HHHHHHHCCHHHHHH | 20.13 | 19835603 | |
| 67 | Phosphorylation | LLGVVRIYHRKAKYL HHHHHHHHHHHCCHH | 5.75 | 19835603 | |
| 72 | Acetylation | RIYHRKAKYLLADCN HHHHHHCCHHHCCCC | 39.19 | 25953088 | |
| 72 | Ubiquitination | RIYHRKAKYLLADCN HHHHHHCCHHHCCCC | 39.19 | - | |
| 84 | Ubiquitination | DCNEAFIKIKMAFRP CCCHHHHHHHHHCCC | 29.80 | - | |
| 86 | Acetylation | NEAFIKIKMAFRPGV CHHHHHHHHHCCCCC | 21.12 | 25953088 | |
| 86 | Ubiquitination | NEAFIKIKMAFRPGV CHHHHHHHHHCCCCC | 21.12 | 21890473 | |
| 87 | Sulfoxidation | EAFIKIKMAFRPGVV HHHHHHHHHCCCCCC | 4.92 | 21406390 | |
| 134 | Phosphorylation | IDVAQQFSLNQSRVE CCHHHHHCCCHHHHE | 23.28 | 22067460 | |
| 138 | Phosphorylation | QQFSLNQSRVEEITM HHHCCCHHHHEEEEC | 36.90 | 25159151 | |
| 144 | Phosphorylation | QSRVEEITMREEVGN HHHHEEEECCHHCCC | 17.29 | 21815630 | |
| 153 | Phosphorylation | REEVGNISILQENDF CHHCCCEEEECCCCC | 22.65 | 28176443 | |
| 175 | Phosphorylation | REIMREGSAFEDDDM HHHHHHCCCCCCCCC | 25.65 | 30278072 | |
| 185 | Phosphorylation | EDDDMLVSTTTSNLL CCCCCEEEECHHHHH | 18.97 | 19690332 | |
| 186 | Phosphorylation | DDDMLVSTTTSNLLL CCCCEEEECHHHHHH | 26.98 | 18669648 | |
| 187 | Phosphorylation | DDMLVSTTTSNLLLE CCCEEEECHHHHHHC | 22.26 | 26552605 | |
| 188 | Phosphorylation | DMLVSTTTSNLLLES CCEEEECHHHHHHCC | 18.73 | 26552605 | |
| 189 | Phosphorylation | MLVSTTTSNLLLESE CEEEECHHHHHHCCH | 24.32 | 28464451 | |
| 195 | Phosphorylation | TSNLLLESEQSTSNL HHHHHHCCHHHCCCH | 40.69 | 30108239 | |
| 198 | Phosphorylation | LLLESEQSTSNLNEK HHHCCHHHCCCHHHH | 29.74 | 30108239 | |
| 199 | Phosphorylation | LLESEQSTSNLNEKI HHCCHHHCCCHHHHH | 22.71 | 30108239 | |
| 200 | Phosphorylation | LESEQSTSNLNEKIN HCCHHHCCCHHHHHH | 44.56 | 30108239 | |
| 211 | Phosphorylation | EKINHLEYEDQYKDD HHHHCHHHHHHHCCC | 31.03 | 28796482 | |
| 215 | Phosphorylation | HLEYEDQYKDDNFGE CHHHHHHHCCCCCCC | 28.80 | 29978859 | |
| 216 | Sumoylation | LEYEDQYKDDNFGEG HHHHHHHCCCCCCCC | 53.63 | 28112733 | |
| 216 | Ubiquitination | LEYEDQYKDDNFGEG HHHHHHHCCCCCCCC | 53.63 | 21890473 | |
| 249 | Phosphorylation | FDDPPALSEAGVMLP CCCCHHHHHCCCCCC | 27.75 | 24275569 | |
| 277 | Phosphorylation | VSMGGPDSPDSVDPV CCCCCCCCCCCCCCC | 33.47 | 22067460 | |
| 280 | Phosphorylation | GGPDSPDSVDPVEPM CCCCCCCCCCCCCCC | 31.63 | 22067460 | |
| 289 | Phosphorylation | DPVEPMPTMTDQTTL CCCCCCCCCCCCCEE | 26.84 | 22067460 | |
| 312 | Phosphorylation | ALEPIDITVKETKAK HCCCCEEEECCCHHH | 23.06 | 22817900 | |
| 323 | Ubiquitination | TKAKRKRKLIVDSVK CHHHHHHHEEEHHHH | 45.67 | - | |
| 328 | Phosphorylation | KRKLIVDSVKELDSK HHHEEEHHHHHHCCH | 24.97 | 23828894 | |
| 330 | 2-Hydroxyisobutyrylation | KLIVDSVKELDSKTI HEEEHHHHHHCCHHH | 57.41 | - | |
| 330 | Acetylation | KLIVDSVKELDSKTI HEEEHHHHHHCCHHH | 57.41 | 26051181 | |
| 330 | Ubiquitination | KLIVDSVKELDSKTI HEEEHHHHHHCCHHH | 57.41 | 21890473 | |
| 335 | 2-Hydroxyisobutyrylation | SVKELDSKTIRAQLS HHHHHCCHHHHHHHC | 47.87 | - | |
| 335 | Ubiquitination | SVKELDSKTIRAQLS HHHHHCCHHHHHHHC | 47.87 | 21890473 | |
| 342 | Phosphorylation | KTIRAQLSDYSDIVT HHHHHHHCCHHHHHH | 23.56 | 20068231 | |
| 344 | Phosphorylation | IRAQLSDYSDIVTTL HHHHHCCHHHHHHHH | 12.60 | 20068231 | |
| 345 | Phosphorylation | RAQLSDYSDIVTTLD HHHHCCHHHHHHHHC | 26.33 | 20068231 | |
| 349 | Phosphorylation | SDYSDIVTTLDLAPP CCHHHHHHHHCCCCC | 23.21 | 20068231 | |
| 350 | Phosphorylation | DYSDIVTTLDLAPPT CHHHHHHHHCCCCCC | 13.84 | 20068231 | |
| 357 | Phosphorylation | TLDLAPPTKKLMMWK HHCCCCCCCEEEEEE | 39.49 | 20068231 | |
| 358 | Ubiquitination | LDLAPPTKKLMMWKE HCCCCCCCEEEEEEC | 50.08 | 21890473 | |
| 359 | Ubiquitination | DLAPPTKKLMMWKET CCCCCCCEEEEEECC | 44.06 | - | |
| 364 | Ubiquitination | TKKLMMWKETGGVEK CCEEEEEECCCCCHH | 27.74 | 21890473 | |
| 366 | Phosphorylation | KLMMWKETGGVEKLF EEEEEECCCCCHHHH | 35.19 | 22067460 | |
| 371 | Ubiquitination | KETGGVEKLFSLPAQ ECCCCCHHHHCCCCC | 53.04 | 21890473 | |
| 374 | Phosphorylation | GGVEKLFSLPAQPLW CCCHHHHCCCCCCCC | 43.83 | 20068231 | |
| 387 | Ubiquitination | LWNNRLLKLFTRCLT CCCHHHHHHHHHHHC | 46.26 | 21890473 | |
| 387 | Acetylation | LWNNRLLKLFTRCLT CCCHHHHHHHHHHHC | 46.26 | 26051181 | |
| 394 | Phosphorylation | KLFTRCLTPLVPEDL HHHHHHHCCCCHHHH | 20.43 | 23898821 | |
| 406 | Ubiquitination | EDLRKRRKGGEADNL HHHHHHCCCCCCCCH | 75.26 | 21890473 | |
| 418 | Ubiquitination | DNLDEFLKEFENPEV CCHHHHHHHHCCCCC | 66.72 | 21890473 | |
| 418 | Sumoylation | DNLDEFLKEFENPEV CCHHHHHHHHCCCCC | 66.72 | 28112733 | |
| 449 | Phosphorylation | EPIIEEPSRLQESVM CHHCCCHHHHHHHHH | 49.23 | 21712546 | |
| 454 | Phosphorylation | EPSRLQESVMEASRT CHHHHHHHHHHHHCC | 17.50 | 21815630 | |
| 456 | Sulfoxidation | SRLQESVMEASRTNI HHHHHHHHHHHCCCC | 5.05 | 21406390 | |
| 459 | Phosphorylation | QESVMEASRTNIDES HHHHHHHHCCCCCCC | 26.74 | 29255136 | |
| 466 | Phosphorylation | SRTNIDESAMPPPPP HCCCCCCCCCCCCCC | 26.56 | 22817900 | |
| 468 | Sulfoxidation | TNIDESAMPPPPPQG CCCCCCCCCCCCCCC | 7.73 | 21406390 | |
| 477 | Acetylation | PPPPQGVKRKAGQID CCCCCCCCCCCCCCC | 55.81 | 25953088 | |
| 477 | Ubiquitination | PPPPQGVKRKAGQID CCCCCCCCCCCCCCC | 55.81 | 21890473 | |
| 545 | Phosphorylation | EEEDEDASGGDQDQE HHHCCCCCCCCHHHH | 56.48 | 23927012 | |
| 573 | Ubiquitination | GLQRALAKTGAESIS HHHHHHHHHCHHHHH | 48.63 | - | |
| 573 | Acetylation | GLQRALAKTGAESIS HHHHHHHHHCHHHHH | 48.63 | 25953088 | |
| 585 | Glutathionylation | SISLLELCRNTNRKQ HHHHHHHHHCCCHHH | 1.99 | 22555962 | |
| 596 | Ubiquitination | NRKQAAAKFYSFLVL CHHHHHHHHHHHHHH | 39.86 | 21890473 | |
| 596 | Acetylation | NRKQAAAKFYSFLVL CHHHHHHHHHHHHHH | 39.86 | 25953088 | |
| 598 | Phosphorylation | KQAAAKFYSFLVLKK HHHHHHHHHHHHHHH | 9.60 | - | |
| 604 | Ubiquitination | FYSFLVLKKQQAIEL HHHHHHHHHHHHHHC | 40.85 | 21890473 | |
| 604 | Acetylation | FYSFLVLKKQQAIEL HHHHHHHHHHHHHHC | 40.85 | 26051181 | |
| 605 | Ubiquitination | YSFLVLKKQQAIELT HHHHHHHHHHHHHCC | 43.40 | 21890473 | |
| 617 | Phosphorylation | ELTQEEPYSDIIATP HCCCCCCCCCCCCCC | 23.43 | 28796482 | |
| 618 | Phosphorylation | LTQEEPYSDIIATPG CCCCCCCCCCCCCCC | 32.80 | 28796482 | |
| 623 | Phosphorylation | PYSDIIATPGPRFHI CCCCCCCCCCCCCCC | 20.54 | 25159151 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD21_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 RAD21_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 614701 | Cornelia de Lange syndrome 4 (CDLS4) | |||||
| 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 |
| "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-175, ANDMASS SPECTROMETRY. | |
| "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY. | |
| "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-46; SER-153 AND SER-175,AND MASS SPECTROMETRY. | |
