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Q61550 (RAD21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length635 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with PDS5B and WAPAL; the interaction is direct 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. Ref.6

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 635635Double-strand-break repair protein rad21 homolog
PRO_0000097873

Regions

Region287 – 403117Interaction with WAPAL and PDS5B By similarity
Region362 – 40342Interaction with STAG1 By similarity
Compositional bias473 – 51442Pro-rich
Compositional bias499 – 55759Glu-rich

Sites

Site172 – 1732Cleavage; by ESPL1 By similarity
Site279 – 2802Cleavage; by caspase-3 or caspase-7 By similarity
Site454 – 4552Cleavage; by ESPL1 By similarity

Amino acid modifications

Modified residue461Phosphoserine By similarity
Modified residue1531Phosphoserine By similarity
Modified residue1751Phosphoserine By similarity

Experimental info

Sequence conflict1471E → G in BAB23527. Ref.4
Sequence conflict2051K → E in BAB23527. Ref.4
Sequence conflict3741F → S in BAA08408. Ref.1
Sequence conflict3741F → S in AAK56113. Ref.3
Sequence conflict3741F → S in AAK56114. Ref.3
Sequence conflict5441Missing in BAA08408. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61550 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 2EC1AC08E358E9CE

FASTA63572,083
        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 KLFFLPAQPL 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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[6]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3 AND SMC1A.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AK163992 mRNA. Translation: BAE37576.1.
BC043032 mRNA. Translation: AAH43032.2.
CCDSCCDS27463.1.
PIRJC4248.
RefSeqNP_033035.3. NM_009009.4.
XP_006520707.1. XM_006520644.1.
XP_006520708.1. XM_006520645.1.
UniGeneMm.182628.

3D structure databases

ProteinModelPortalQ61550.
SMRQ61550. Positions 562-628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202560. 17 interactions.
DIPDIP-56655N.
IntActQ61550. 14 interactions.
MINTMINT-4131622.

PTM databases

PhosphoSiteQ61550.

Proteomic databases

MaxQBQ61550.
PaxDbQ61550.
PRIDEQ61550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022927; ENSMUSP00000022927; ENSMUSG00000022314.
GeneID19357.
KEGGmmu:19357.
UCSCuc007vrd.2. mouse.

Organism-specific databases

CTD5885.
MGIMGI:108016. Rad21.

Phylogenomic databases

eggNOGNOG249424.
GeneTreeENSGT00390000011606.
HOGENOMHOG000233800.
HOVERGENHBG059956.
InParanoidQ810A8.
KOK06670.
OMAVPREEQQ.
OrthoDBEOG7B31N3.
TreeFamTF101215.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressQ61550.
BgeeQ61550.
CleanExMM_RAD21.
GenevestigatorQ61550.

Family and domain databases

Gene3D1.10.10.580. 1 hit.
InterProIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view]
PfamPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD21. mouse.
NextBio296405.
PROQ61550.
SOURCESearch...

Entry information

Entry nameRAD21_MOUSE
AccessionPrimary (citable) accession number: Q61550
Secondary accession number(s): P70219 expand/collapse secondary AC list , Q3TQ09, Q810A8, Q91VB9, Q9DBU4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot