Reviewed, UniProtKB/Swiss-Prot Q61550 (RAD21_MOUSE)

Names and origin

Protein names

Recommended name:
    Double-strand-break repair protein rad21 homolog
Alternative name(s):
    Pokeweed agglutinin-binding protein 29
      Short name=PW29
    SCC1 homolog

Gene names

Name:	Rad21
Synonyms:	Hr21

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. 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 By similarity. 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.
Subunit structure	Found in a complex with SMC1A, SMC3, CDCA5, PDS5A/APRIN and PDS5B/SCC-112 By similarity. 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.
Subcellular location	Nucleus. Note: Associates with chromatin. Once cleaved by caspase-3, the C-terminal 64 kDa cleavage product translocates to the cytoplasm, where it may trigger apoptosis By similarity. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Tissue specificity	Widely expressed with highest levels in testis, brain, kidney, heart and thymus. Lowest levels in skeletal muscle. Ref.2
Developmental stage	Abundance does not change during cell cycle.
Domain	The C-terminal part associates with the head of SMC1A, while the N-terminal part binds to the head of SMC3 By similarity.
Post-translational modification	Cleaved by separase/ESPL1 at the onset of anaphase. Cleaved by caspase-3 and caspase-7 at the beginning of apoptosis. The cleavage by ESPL1 and caspase-3 take place at different sites By similarity. Phosphorylated; becomes hyperphosphorylated in M phase of cell cycle. The large dissociation of cohesin from chromosome arms during prophase may be partly due to its phosphorylation by PLK By similarity.
Miscellaneous	Seems to bind calcium.
Sequence similarities	Belongs to the rad21 family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Chromosome partition DNA damage DNA repair Mitosis
Cellular component	Nucleus
Ligand	Calcium
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear chromosome Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Double-strand-break repair protein rad21 homolog		PRO_0000097873
Regions
	Compositional bias	473 – 514	42	Pro-rich
	Compositional bias	499 – 557	59	Glu-rich
Sites
	Site	172 – 173	2	Cleavage; by ESPL1 By similarity
	Site	279 – 280	2	Cleavage; by caspase-3 or caspase-7 By similarity
	Site	454 – 455	2	Cleavage; by ESPL1 By similarity
Amino acid modifications
	Modified residue	46	1	Phosphoserine By similarity
	Modified residue	153	1	Phosphoserine By similarity
	Modified residue	175	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	147	1	E → G in BAB23527. Ref.4
	Sequence conflict	205	1	K → E in BAB23527. Ref.4
	Sequence conflict	374	1	S → F in BAB23527. Ref.4
	Sequence conflict	544	1	Missing in BAA08408. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q61550-1 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: 2ECAACB8E35F987E	FASTA	635	72,023
	10 20 30 40 50 60 MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL 70 80 90 100 110 120 LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP 130 140 150 160 170 180 LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD 190 200 210 220 230 240 DMLVSTSASN LLLEPEQSTS NLNEKMNHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG 250 260 270 280 290 300 IFDDPPALSE AGVMLPEQPA HDDMDEDDNG SLGGPDSPDS VDPVEPMPTM TDQTTLVPNE 310 320 330 340 350 360 EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL 370 380 390 400 410 420 MMWKETGGVE KLFSLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF 430 440 450 460 470 480 ENPEVPREEQ QPQQQQPQPQ RDVIDEPIIE EPSRLQDSVM EASRTTIEES AMPPPPPQGV 490 500 510 520 530 540 KRKAGQIDPE PSIPPQQVEQ MEIPPVELPP EEPPNICQLI PELELLPEKE KEKEKEKEEE 550 560 570 580 590 600 EEEEDEDASG GDQDQEERRW NKRTQQMLHG LQRALAKTGA ESISLLELCR NTNRKQAAAK 610 620 630 FYSFLVLKKQ QAIELTQEEP YSDIIATPGP RFHII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and sequence analysis of a novel calcium binding protein with oligoproline motif." Yu S., Ozawa M., Naved A.F., Miyauchi T., Muramatsu H., Muramatsu T. Cell Struct. Funct. 20:263-268(1995) [PubMed: 8521526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CALCIUM-BINDING.
[2]	"Sequence conservation of the rad21 Schizosaccharomyces pombe DNA double-strand break repair gene in human and mouse." McKay M.J., Troelstra C., van der Spek P., Kanaar R., Smit B., Hagemeijer A., Bootsma D., Hoeijmakers J.H.J. Genomics 36:305-315(1996) [PubMed: 8812457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Testis.
[3]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Lung.
[5]	"Characterization of the components of the putative mammalian sister chromatid cohesion complex." Darwiche N., Freeman L.A., Strunnikov A. Gene 233:39-47(1999) [PubMed: 10375619] [Abstract] Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3 AND SMC1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D49429 mRNA. Translation: BAA08408.1. X98293 mRNA. Translation: CAA66939.1. AF332086 mRNA. Translation: AAK56114.1. AF332085 mRNA. Translation: AAK56113.1. AK004746 mRNA. Translation: BAB23527.1.
IPI	IPI00329840.
PIR	JC4248.
RefSeq	NP_033035.2.
UniGene	Mm.182628 Mm.470496
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q61550.
Genome annotation databases
Ensembl	ENSMUSG00000022314. Mus musculus. [Contig view]
GeneID	19357.
KEGG	mmu:19357.
Organism-specific databases
MGI	MGI:108016. Rad21.
Phylogenomic databases
HOGENOM	Q61550.
HOVERGEN	Q61550.
Gene expression databases
ArrayExpress	Q61550.
Bgee	Q61550.
CleanEx	MM_RAD21.
GermOnline	ENSMUSG00000022314. Mus musculus.
Family and domain databases
InterPro	IPR006909. Rad21/Rec8_C. IPR006910. Rad21_Rec8_N. [Graphical view]
Pfam	PF04824. Rad21_Rec8. 1 hit. PF04825. Rad21_Rec8_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	296405.
SOURCE	Search...

Entry information

Entry name

RAD21_MOUSE

Accession

Primary (citable) accession number: Q61550
Secondary accession number(s): P70219, Q91VB9, Q9DBU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 15, 2002
Last modified:	March 3, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)