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RAD21 (human)

Overview RAD21 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. Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Found in a complex with SMC1A, SMC3, CDCA5, PDS5A/APRIN and PDS5B/SCC-112. Interacts with PDS5B and WAPAL; the interaction is direct. Belongs to the rad21 family. Note: This description may include information from UniProtKB. Cellular Component: nucleoplasm; cohesin complex; nuclear chromosome; nucleolus; nucleus; chromosome, pericentric region Molecular Function: protein binding Biological Process: regulation of transcription from RNA polymerase II promoter; M phase of mitotic cell cycle; apoptosis; cell division; double-strand break repair; meiotic recombination; mitotic cell cycle; mitotic prometaphase; mitotic metaphase/anaphase transition; DNA recombination; chromosome segregation Reference #:  O60216 (UniProtKB) Alt. Names/Synonyms: Double-strand-break repair protein rad21 homolog; FLJ25655; FLJ40596; hHR21; HR21; HRAD21; KIAA0078; MCD1; Nuclear matrix protein 1; NXP-1; NXP1; protein involved in DNA double-strand break repair; RAD21; RAD21 homolog (S. pombe); SCC1; SCC1 homolog Gene Symbols: RAD21 Molecular weight: 71,690 Da Basal Isoelectric point: 4.54  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below RAD21

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	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	4		S46-p	SSVESIIsPKVkMAL
0	1		K50-u	SIIsPKVkMALRtsG
0	2		T55-p	KVkMALRtsGHLLLG
0	2		S56-p	VkMALRtsGHLLLGV
0	2		Y67-p	LLGVVRIyHRKAKYL
0	2		K86-u	NEAFIKIkMAFRPGV
0	1		S134-p	IDVAQQFsLNQsRVE
0	2		S138-p	QQFsLNQsRVEEItM
0	2		T144-p	QsRVEEItMREEVGN
0	7		S153-p	REEVGNIsILQENDF
0	5		S175-p	REIMREGsAFEDDDM
0	5		Y211-p	EKINHLEyEDQykDD
0	4		Y215-p	HLEyEDQykDDNFGE
0	1		K216-u	LEyEDQykDDNFGEG
0	1		S277-p	VSMGGPDsPDsVDPV
0	1		S280-p	GGPDsPDsVDPVEPM
0	1		T289-p	DPVEPMPtMTDQTTL
0	1		T312-p	ALEPIDItVKETKAK
0	1		K330-u	KLIVDSVkELDSkTI
0	1		K335-u	SVkELDSkTIRAQLS
0	3		K358-u	LDLAPPTkKLMMWkE
0	2		K364-u	TkKLMMWkEtGGVEk
0	1		T366-p	KLMMWkEtGGVEkLF
0	15		K371-u	kEtGGVEkLFsLPAQ
0	1		S374-p	GGVEkLFsLPAQPLW
0	3		K387-u	LWNNRLLkLFTRCLt
0	3		T394-p	kLFTRCLtPLVPEDL
0	2		K406-u	EDLRKRRkGGEADNL
0	1		K418-u	DNLDEFLkEFENPEV
0	1		S454-p	EPSRLQEsVMEAsRT
0	1		S459-p	QEsVMEAsRTNIDEs
0	1		S466-p	sRTNIDEsAMPPPPP
0	1		K477-u	PPPPQGVkRKAGQID
0	3		S545-p	EEEDEDAsGGDQDQE
0	1		K573	GLQRALAKTGAESIS
0	10		K596-u	NRKQAAAkFYSFLVL
0	1		K605-u	YSFLVLKkQQAIELT
0	1		S618-p	LTQEEPYsDIIAtPG
0	2		T623-p	PYsDIIAtPGPRFHI

	mouse
S46	SSVESIISPKVKMAL
K50	SIISPKVKMALRTSG
T55	KVKMALRTSGHLLLG
S56	VKMALRTSGHLLLGV
Y67	LLGVVRIYHRKAKYL
K86	NEAFIKIKMAFRPGV
S134	IDVAQQFSLNQSRVE
S138	QQFSLNQSRVEEITM
T144	QSRVEEITMREEVGN
S153-p	REEVGNIsILQENDF
S175-p	REIMREGsAFEDDDM
Y211	EKMNHLEYEDQYKDD
Y215	HLEYEDQYKDDNFGE
K216	LEYEDQYKDDNFGEG
S277	GSLGGPDSPDSVDPV
S280	GGPDSPDSVDPVEPM
T289	DPVEPMPTMTDQTTL
T312	ALEPIDITVKETKAK
K330	KLIVDSVKELDSKTI
K335	SVKELDSKTIRAQLS
K358-u	LDLAPPTkKLMMWKE
K364	TkKLMMWKETGGVEK
T366	KLMMWKETGGVEKLF
K371	KETGGVEKLFFLPAQ
F374	GGVEKLFFLPAQPLW
K387-u	LWNNRLLkLFTRCLT
T394	kLFTRCLTPLVPEDL
K406-u	EDLRKRRkGGEADNL
K418	DNLDEFLKEFENPEV
S458	EPSRLQDSVMEASRT
S463	QDSVMEASRTTIEES
S470	SRTTIEESAMPPPPP
K481	PPPPQGVKRKAGQID
S549	EEEDEDASGGDQDQE
K577-u	GLQRALAkTGAESIS
K600	NRKQAAAKFYSFLVL
K609	YSFLVLKKQQAIELT
S622	LTQEEPYSDIIATPG
T627	PYSDIIATPGPRFHI

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