RD21L_HUMAN - dbPTM
RD21L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RD21L_HUMAN
UniProt AC Q9H4I0
Protein Name Double-strand-break repair protein rad21-like protein 1
Gene Name RAD21L1
Organism Homo sapiens (Human).
Sequence Length 556
Subcellular Localization Nucleus . Chromosome . In meiotic chromosomes, localized along axial elements in early meiosis: detectable on the axial elements in leptotene, and stays on the axial/lateral elements until mid pachytene. It then disappears and is replaced with RAD21.
Protein Description Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RAD21 reappears in later stages of prophase I. Involved in synaptonemal complex assembly, synapsis initiation and crossover recombination between homologous chromosomes during prophase I (By similarity)..
Protein Sequence MFYTHVLMSKRGPLAKIWLAAHWEKKLTKAHVFECNLEITIEKILSPKVKIALRTSGHLLLGVVRIYNRKAKYLLADCSEAFLKMKMTFCPGLVDLPKENFEASYNAITLPEEFHDFDTQNMNAIDVSEHFTQNQSRPEEITLRENFDNDLIFQAESFGEESEILRRHSFFDDNILLNSSGPLIEHSSGSLTGERSLFYDSGDGFGDEGAAGEMIDNLLQDDQNILLEDMHLNREISLPSEPPNSLAVEPDNSECICVPENEKMNETILLSTEEEGFTLDPIDISDIAEKRKGKKRRLLIDPIKELSSKVIHKQLTSFADTLMVLELAPPTQRLMMWKKRGGVHTLLSTAAQDLIHAELKMLFTKCFLSSGFKLGRKMIQKESVREEVGNQNIVETSMMQEPNYQQELSKPQTWKDVIGGSQHSSHEDTNKNINSEQDIVEMVSLAAEESSLMNDLFAQEIEYSPVELESLSNEENIETERWNGRILQMLNRLRESNKMGMQSFSLMKLCRNSDRKQAAAKFYSFLVLKKQLAIELSQSAPYADIIATMGPMFYNI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MFYTHVLMSK
-----CCCEEEECCC		8.4721406692
4Phosphorylation----MFYTHVLMSKR
----CCCEEEECCCC		8.3424719451
9PhosphorylationFYTHVLMSKRGPLAK
CCEEEECCCCCHHHH		18.2924719451
46PhosphorylationITIEKILSPKVKIAL
EEHHHHHCCCCEEEE		26.5824719451
482-HydroxyisobutyrylationIEKILSPKVKIALRT
HHHHHCCCCEEEEEC		53.43-
55PhosphorylationKVKIALRTSGHLLLG
CCEEEEECCCHHHHH		39.6520068231
56PhosphorylationVKIALRTSGHLLLGV
CEEEEECCCHHHHHH		20.1320068231
73PhosphorylationIYNRKAKYLLADCSE
HHCCCCCHHHHHCHH		16.2928509920
79PhosphorylationKYLLADCSEAFLKMK
CHHHHHCHHHHHHHH		32.2928509920
88PhosphorylationAFLKMKMTFCPGLVD
HHHHHHCCCCCCCCC		19.3028509920
192PhosphorylationEHSSGSLTGERSLFY
ECCCCCCCCCCEEEE		38.4024719451
272PhosphorylationNETILLSTEEEGFTL
CCEEEEECCCCCCCC		47.5922210691
307PhosphorylationIDPIKELSSKVIHKQ
HHHHHHHCHHHHHHH		29.2529449344
308PhosphorylationDPIKELSSKVIHKQL
HHHHHHCHHHHHHHH		43.4929449344
381AcetylationLGRKMIQKESVREEV
HHHHHHHHHHHHHHH		40.8225953088
403UbiquitinationTSMMQEPNYQQELSK
HHCCCCCCCHHHCCC		46.6322817900
408UbiquitinationEPNYQQELSKPQTWK
CCCCHHHCCCCCCHH		7.4821890473
416UbiquitinationSKPQTWKDVIGGSQH
CCCCCHHHHCCCCCC		28.9121890473
429PhosphorylationQHSSHEDTNKNINSE
CCCCCHHCCCCCCCH		45.1429759185
495 (in isoform 2)Phosphorylation-64.3526471730
496PhosphorylationMLNRLRESNKMGMQS
HHHHHHHHCCCCHHH		35.0023684312
498 (in isoform 2)Phosphorylation-46.2226471730
503PhosphorylationSNKMGMQSFSLMKLC
HCCCCHHHHHHHHHH		14.1223684312
505PhosphorylationKMGMQSFSLMKLCRN
CCCHHHHHHHHHHCC		32.5723684312
516UbiquitinationLCRNSDRKQAAAKFY
HHCCCCHHHHHHHHH		49.6422817900
521UbiquitinationDRKQAAAKFYSFLVL
CHHHHHHHHHHHHHH		39.8622817900
521 (in isoform 1)Ubiquitination-39.8621890473
523UbiquitinationKQAAAKFYSFLVLKK
HHHHHHHHHHHHHHH		9.6022817900
523PhosphorylationKQAAAKFYSFLVLKK
HHHHHHHHHHHHHHH		9.60-
524UbiquitinationQAAAKFYSFLVLKKQ
HHHHHHHHHHHHHHH		18.4222817900
528UbiquitinationKFYSFLVLKKQLAIE
HHHHHHHHHHHHHHH		6.6221890473
529UbiquitinationFYSFLVLKKQLAIEL
HHHHHHHHHHHHHHH		30.8721890473
536UbiquitinationKKQLAIELSQSAPYA
HHHHHHHHHCCCCHH		4.6421890473
537UbiquitinationKQLAIELSQSAPYAD
HHHHHHHHCCCCHHH		14.8621890473
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 RD21L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RD21L_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 RD21L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RD21L_HUMAN !!
Drug and Disease Associations
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.
Regulatory Network of RD21L_HUMAN

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Related Literatures of Post-Translational Modification

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