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Q61550

- RAD21_MOUSE

UniProt

Q61550 - RAD21_MOUSE

Protein

Double-strand-break repair protein rad21 homolog

Gene

Rad21

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei172 – 1732Cleavage; by ESPL1By similarity
    Sitei279 – 2802Cleavage; by caspase-3 or caspase-7By similarity
    Sitei454 – 4552Cleavage; by ESPL1By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. chromosome segregation Source: UniProtKB-KW
    3. DNA repair 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

    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.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 635635Double-strand-break repair protein rad21 homologPRO_0000097873Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461PhosphoserineBy similarity
    Modified residuei153 – 1531PhosphoserineBy similarity
    Modified residuei175 – 1751PhosphoserineBy 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.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.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.By similarity1 Publication

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ61550.
    SMRiQ61550. Positions 562-628.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni287 – 403117Interaction with WAPAL and PDS5BBy similarityAdd
    BLAST
    Regioni362 – 40342Interaction with STAG1By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi473 – 51442Pro-richAdd
    BLAST
    Compositional biasi499 – 55759Glu-richAdd
    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.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471E → G in BAB23527. (PubMed:16141072)Curated
    Sequence conflicti205 – 2051K → E in BAB23527. (PubMed:16141072)Curated
    Sequence conflicti374 – 3741F → S in BAA08408. (PubMed:8521526)Curated
    Sequence conflicti374 – 3741F → S in AAK56113. (PubMed:11471062)Curated
    Sequence conflicti374 – 3741F → S in AAK56114. (PubMed:11471062)Curated
    Sequence conflicti544 – 5441Missing in BAA08408. (PubMed:8521526)Curated

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 118 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