CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000882
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Double-strand-break repair protein rad21 homolog 
Protein Synonyms/Alias
 hHR21; Nuclear matrix protein 1; NXP-1; SCC1 homolog 
Gene Name
 RAD21 
Gene Synonyms/Alias
 HR21; KIAA0078; NXP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25WLAAHWDKKLTKAHVubiquitination[1, 2]
26LAAHWDKKLTKAHVFubiquitination[3]
29HWDKKLTKAHVFECNubiquitination[3]
50SIISPKVKMALRTSGubiquitination[3]
72RIYHRKAKYLLADCNubiquitination[3, 4, 5]
86NEAFIKIKMAFRPGVubiquitination[1, 2, 3, 6, 7]
216LEYEDQYKDDNFGEGubiquitination[6, 7, 8]
330KLIVDSVKELDSKTIubiquitination[3, 5, 6]
335SVKELDSKTIRAQLSubiquitination[3, 6, 9]
358LDLAPPTKKLMMWKEubiquitination[3, 6, 7, 8]
359DLAPPTKKLMMWKETubiquitination[3]
364TKKLMMWKETGGVEKubiquitination[1, 2, 3, 4, 6, 7, 8, 9]
371KETGGVEKLFSLPAQubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
387LWNNRLLKLFTRCLTubiquitination[1, 2, 3, 5, 6, 7, 9]
406EDLRKRRKGGEADNLubiquitination[5, 6, 7]
418DNLDEFLKEFENPEVubiquitination[6, 7]
477PPPPQGVKRKAGQIDubiquitination[6, 7]
573GLQRALAKTGAESISubiquitination[3, 4]
596NRKQAAAKFYSFLVLubiquitination[1, 2]
604FYSFLVLKKQQAIELubiquitination[1, 2, 3, 7]
605YSFLVLKKQQAIELTubiquitination[3, 6, 7]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional 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. 
Sequence Annotation
 REGION 287 403 Interaction with WAPAL and PDS5B.
 REGION 362 403 Interaction with STAG1.
 MOD_RES 46 46 Phosphoserine.
 MOD_RES 153 153 Phosphoserine.
 MOD_RES 175 175 Phosphoserine.  
Keyword
 Apoptosis; Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; Mental retardation; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 631 AA 
Protein Sequence
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL 60
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP 120
LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD 180
DMLVSTTTSN LLLESEQSTS NLNEKINHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG 240
IFDDPPALSE AGVMLPEQPA HDDMDEDDNV SMGGPDSPDS VDPVEPMPTM TDQTTLVPNE 300
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL 360
MMWKETGGVE KLFSLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF 420
ENPEVPREDQ QQQHQQRDVI DEPIIEEPSR LQESVMEASR TNIDESAMPP PPPQGVKRKA 480
GQIDPEPVMP PQQVEQMEIP PVELPPEEPP NICQLIPELE LLPEKEKEKE KEKEDDEEEE 540
DEDASGGDQD QEERRWNKRT QQMLHGLQRA LAKTGAESIS LLELCRNTNR KQAAAKFYSF 600
LVLKKQQAIE LTQEEPYSDI IATPGPRFHI I 631 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
 GO:0008278; C:cohesin complex; TAS:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0034991; C:nuclear meiotic cohesin complex; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0006302; P:double-strand break repair; TAS:ProtInc.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
 GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. 
Interpro
 IPR023093; Rad21/Rec8_C.
 IPR006909; Rad21/Rec8_C_eu.
 IPR006910; Rad21_Rec8_N. 
Pfam
 PF04824; Rad21_Rec8
 PF04825; Rad21_Rec8_N 
SMART
  
PROSITE
  
PRINTS