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Q61550

- RAD21_MOUSE

UniProt

Q61550 - RAD21_MOUSE

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Protein
Double-strand-break repair protein rad21 homolog
Gene
Rad21, Hr21
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei172 – 1732Cleavage; by ESPL1 By similarity
Sitei279 – 2802Cleavage; by caspase-3 or caspase-7 By similarity
Sitei454 – 4552Cleavage; by ESPL1 By similarity

GO - Molecular functioni

  1. protein binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. apoptotic process Source: UniProtKB-KW
  3. chromosome segregation Source: UniProtKB-KW
  4. mitotic nuclear division Source: UniProtKB-KW
  5. protein localization to chromatin Source: UniProtKB
  6. regulation of transcription from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Chromosome partition, DNA damage, DNA repair, Mitosis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_196614. Establishment of Sister Chromatid Cohesion.
REACT_196634. Cohesin Loading onto Chromatin.
REACT_198626. Meiotic synapsis.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-strand-break repair protein rad21 homolog
Alternative name(s):
Pokeweed agglutinin-binding protein 29
Short name:
PW29
SCC1 homolog
Gene namesi
Name:Rad21
Synonyms:Hr21
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:108016. Rad21.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-SubCell
  2. cohesin complex Source: MGI
  3. nuclear meiotic cohesin complex Source: MGI
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Double-strand-break repair protein rad21 homolog
PRO_0000097873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine By similarity
Modified residuei153 – 1531Phosphoserine By similarity
Modified residuei175 – 1751Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61550.
PaxDbiQ61550.
PRIDEiQ61550.

PTM databases

PhosphoSiteiQ61550.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis, brain, kidney, heart and thymus. Lowest levels in skeletal muscle.1 Publication

Developmental stagei

Abundance does not change during cell cycle.

Gene expression databases

ArrayExpressiQ61550.
BgeeiQ61550.
CleanExiMM_RAD21.
GenevestigatoriQ61550.

Interactioni

Subunit structurei

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 RAD21.1 Publication

Protein-protein interaction databases

BioGridi202560. 17 interactions.
DIPiDIP-56655N.
IntActiQ61550. 14 interactions.
MINTiMINT-4131622.

Structurei

3D structure databases

ProteinModelPortaliQ61550.
SMRiQ61550. Positions 562-628.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 403117Interaction with WAPAL and PDS5B By similarity
Add
BLAST
Regioni362 – 40342Interaction with STAG1 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi473 – 51442Pro-rich
Add
BLAST
Compositional biasi499 – 55759Glu-rich
Add
BLAST

Domaini

The C-terminal part associates with the head of SMC1A, while the N-terminal part binds to the head of SMC3 By similarity.

Sequence similaritiesi

Belongs to the rad21 family.

Phylogenomic databases

eggNOGiNOG249424.
GeneTreeiENSGT00390000011606.
HOGENOMiHOG000233800.
HOVERGENiHBG059956.
InParanoidiQ810A8.
KOiK06670.
OMAiVPREEQQ.
OrthoDBiEOG7B31N3.
TreeFamiTF101215.

Family and domain databases

Gene3Di1.10.10.580. 1 hit.
InterProiIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view]
PfamiPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61550-1 [UniParc]FASTAAdd to Basket

« Hide

MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK    50
MALRTSGHLL LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN 100
REAAYNAITL PEEFHDFDQP LPDLDDIDVA QQFSLNQSRV EEITMREEVG 150
NISILQENDF GDFGMDDREI MREGSAFEDD DMLVSTSASN LLLEPEQSTS 200
NLNEKMNHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG IFDDPPALSE 250
AGVMLPEQPA HDDMDEDDNG SLGGPDSPDS VDPVEPMPTM TDQTTLVPNE 300
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT 350
LDLAPPTKKL MMWKETGGVE KLFFLPAQPL WNNRLLKLFT RCLTPLVPED 400
LRKRRKGGEA DNLDEFLKEF ENPEVPREEQ QPQQQQPQPQ RDVIDEPIIE 450
EPSRLQDSVM EASRTTIEES AMPPPPPQGV KRKAGQIDPE PSIPPQQVEQ 500
MEIPPVELPP EEPPNICQLI PELELLPEKE KEKEKEKEEE EEEEDEDASG 550
GDQDQEERRW NKRTQQMLHG LQRALAKTGA ESISLLELCR NTNRKQAAAK 600
FYSFLVLKKQ QAIELTQEEP YSDIIATPGP RFHII 635
Length:635
Mass (Da):72,083
Last modified:July 27, 2011 - v3
Checksum:i2EC1AC08E358E9CE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471E → G in BAB23527. 1 Publication
Sequence conflicti205 – 2051K → E in BAB23527. 1 Publication
Sequence conflicti374 – 3741F → S in BAA08408. 1 Publication
Sequence conflicti374 – 3741F → S in AAK56113. 1 Publication
Sequence conflicti374 – 3741F → S in AAK56114. 1 Publication
Sequence conflicti544 – 5441Missing in BAA08408. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS27463.1.
PIRiJC4248.
RefSeqiNP_033035.3. NM_009009.4.
XP_006520707.1. XM_006520644.1.
XP_006520708.1. XM_006520645.1.
UniGeneiMm.182628.

Genome annotation databases

EnsembliENSMUST00000022927; ENSMUSP00000022927; ENSMUSG00000022314.
GeneIDi19357.
KEGGimmu:19357.
UCSCiuc007vrd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS27463.1.
PIRi JC4248.
RefSeqi NP_033035.3. NM_009009.4.
XP_006520707.1. XM_006520644.1.
XP_006520708.1. XM_006520645.1.
UniGenei Mm.182628.

3D structure databases

ProteinModelPortali Q61550.
SMRi Q61550. Positions 562-628.
ModBasei Search...

Protein-protein interaction databases

BioGridi 202560. 17 interactions.
DIPi DIP-56655N.
IntActi Q61550. 14 interactions.
MINTi MINT-4131622.

PTM databases

PhosphoSitei Q61550.

Proteomic databases

MaxQBi Q61550.
PaxDbi Q61550.
PRIDEi Q61550.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022927 ; ENSMUSP00000022927 ; ENSMUSG00000022314 .
GeneIDi 19357.
KEGGi mmu:19357.
UCSCi uc007vrd.2. mouse.

Organism-specific databases

CTDi 5885.
MGIi MGI:108016. Rad21.

Phylogenomic databases

eggNOGi NOG249424.
GeneTreei ENSGT00390000011606.
HOGENOMi HOG000233800.
HOVERGENi HBG059956.
InParanoidi Q810A8.
KOi K06670.
OMAi VPREEQQ.
OrthoDBi EOG7B31N3.
TreeFami TF101215.

Enzyme and pathway databases

Reactomei REACT_196614. Establishment of Sister Chromatid Cohesion.
REACT_196634. Cohesin Loading onto Chromatin.
REACT_198626. Meiotic synapsis.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

ChiTaRSi RAD21. mouse.
NextBioi 296405.
PROi Q61550.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61550.
Bgeei Q61550.
CleanExi MM_RAD21.
Genevestigatori Q61550.

Family and domain databases

Gene3Di 1.10.10.580. 1 hit.
InterProi IPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view ]
Pfami PF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRAD21_MOUSE
AccessioniPrimary (citable) accession number: Q61550
Secondary accession number(s): P70219
, Q3TQ09, Q810A8, Q91VB9, Q9DBU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Seems to bind calcium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi