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Double-strand-break repair protein rad21 homolog (hHR21) (Nuclear matrix protein 1) (NXP-1) (SCC1 homolog)

 RAD21_HUMAN             Reviewed;         631 AA.
O60216; A8K0E0; Q15001; Q99568;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 2.
05-DEC-2018, entry version 175.
RecName: Full=Double-strand-break repair protein rad21 homolog;
Short=hHR21;
AltName: Full=Nuclear matrix protein 1;
Short=NXP-1;
AltName: Full=SCC1 homolog;
Name=RAD21; Synonyms=HR21, KIAA0078, NXP1, SCC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=8812457; DOI=10.1006/geno.1996.0466;
McKay M.J., Troelstra C., van der Spek P., Kanaar R., Smit B.,
Hagemeijer A., Bootsma D., Hoeijmakers J.H.J.;
"Sequence conservation of the rad21 Schizosaccharomyces pombe DNA
double-strand break repair gene in human and mouse.";
Genomics 36:305-315(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=10623634; DOI=10.1006/bbrc.1999.1969;
Sadano H., Sugimoto H., Sakai F., Nomura N., Osumi T.;
"NXP-1, a human protein related to Rad21/Scc1/Mcd1, is a component of
the nuclear matrix.";
Biochem. Biophys. Res. Commun. 267:418-422(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 406-418, AND IDENTIFICATION IN A COHESIN COMPLEX
WITH SMC1A; SMC3; STAG1 OR STAG2.
PubMed=11590136; DOI=10.1074/jbc.M103364200;
Gregson H.C., Schmiesing J.A., Kim J.-S., Kobayashi T., Zhou S.,
Yokomori K.;
"A potential role for human cohesin in mitotic spindle aster
assembly.";
J. Biol. Chem. 276:47575-47582(2001).
[9]
PROTEIN SEQUENCE OF 275-279 (60 KDA PRODUCT), PROTEIN SEQUENCE OF
280-286 (64 KDA C-TERMINAL PRODUCT), CLEAVAGE BY CASPASE-3, FUNCTION,
AND MUTAGENESIS OF ASP-279.
PubMed=12417729; DOI=10.1128/MCB.22.23.8267-8277.2002;
Pati D., Zhang N., Plon S.E.;
"Linking sister chromatid cohesion and apoptosis: role of rad21.";
Mol. Cell. Biol. 22:8267-8277(2002).
[10]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
PubMed=11073952; DOI=10.1074/jbc.M007809200;
Hoque M.T., Ishikawa F.;
"Human chromatid cohesin component hRad21 is phosphorylated in M phase
and associated with metaphase centromeres.";
J. Biol. Chem. 276:5059-5067(2001).
[11]
CLEAVAGE BY ESPL1, AND MUTAGENESIS OF ARG-172 AND ARG-450.
PubMed=11509732; DOI=10.1126/science.1061376;
Hauf S., Waizenegger I.C., Peters J.-M.;
"Cohesin cleavage by separase required for anaphase and cytokinesis in
human cells.";
Science 293:1320-1323(2001).
[12]
FUNCTION, CLEAVAGE BY CASPASE-3, AND MUTAGENESIS OF ASP-279.
PubMed=11875078; DOI=10.1074/jbc.M201322200;
Chen F., Kamradt M., Mulcahy M., Byun Y., Xu H., McKay M.J.,
Cryns V.L.;
"Caspase proteolysis of the cohesin component RAD21 promotes
apoptosis.";
J. Biol. Chem. 277:16775-16781(2002).
[13]
IDENTIFICATION IN A COMPLEX WITH SMC1A; SMC3; CDCA5; PDS5A AND PDS5B.
PubMed=15837422; DOI=10.1016/j.molcel.2005.03.017;
Rankin S., Ayad N.G., Kirschner M.W.;
"Sororin, a substrate of the anaphase-promoting complex, is required
for sister chromatid cohesion in vertebrates.";
Mol. Cell 18:185-200(2005).
[14]
ERRATUM.
Rankin S., Ayad N.G., Kirschner M.W.;
Mol. Cell 18:609-609(2005).
[15]
INTERACTION WITH DDX11.
PubMed=17105772; DOI=10.1242/jcs.03262;
Parish J.L., Rosa J., Wang X., Lahti J.M., Doxsey S.J., Androphy E.J.;
"The DNA helicase ChlR1 is required for sister chromatid cohesion in
mammalian cells.";
J. Cell Sci. 119:4857-4865(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-175, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
INTERACTION WITH PDS5B; STAG1 AND WAPL.
PubMed=19696148; DOI=10.1101/gad.1844309;
Shintomi K., Hirano T.;
"Releasing cohesin from chromosome arms in early mitosis: opposing
actions of Wapl-Pds5 and Sgo1.";
Genes Dev. 23:2224-2236(2009).
[18]
POLYMORPHISM, AND VARIANT ARG-481.
PubMed=11483345; DOI=10.1016/S0360-3016(01)01608-X;
Severin D.M., Leong T., Cassidy B., Elsaleh H., Peters L., Venter D.,
Southey M., McKay M.;
"Novel DNA sequence variants in the hHR21 DNA repair gene in
radiosensitive cancer patients.";
Int. J. Radiat. Oncol. Biol. Phys. 50:1323-1331(2001).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-175, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-153, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A; SMC3 AND STAG1.
PubMed=22628566; DOI=10.1073/pnas.1206840109;
Bermudez V.P., Farina A., Higashi T.L., Du F., Tappin I.,
Takahashi T.S., Hurwitz J.;
"In vitro loading of human cohesin on DNA by the human Scc2-Scc4
loader complex.";
Proc. Natl. Acad. Sci. U.S.A. 109:9366-9371(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394; SER-454; SER-545
AND THR-623, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-249, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-216 AND LYS-418, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
VARIANTS CDLS4 ARG-376 AND ARG-585.
PubMed=22633399; DOI=10.1016/j.ajhg.2012.04.019;
Deardorff M.A., Wilde J.J., Albrecht M., Dickinson E., Tennstedt S.,
Braunholz D., Monnich M., Yan Y., Xu W., Gil-Rodriguez M.C., Clark D.,
Hakonarson H., Halbach S., Michelis L.D., Rampuria A., Rossier E.,
Spranger S., Van Maldergem L., Lynch S.A., Gillessen-Kaesbach G.,
Ludecke H.J., Ramsay R.G., McKay M.J., Krantz I.D., Xu H.,
Horsfield J.A., Kaiser F.J.;
"RAD21 mutations cause a human cohesinopathy.";
Am. J. Hum. Genet. 90:1014-1027(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11875078,
ECO:0000269|PubMed:12417729}.
-!- SUBUNIT: 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 (PubMed:11590136). Found in a complex
with SMC1A, SMC3, CDCA5, PDS5A/SCC-112 and PDS5B/APRIN
(PubMed:15837422). Interacts with PDS5B and WAPL; the interaction
is direct (PubMed:19696148). Interacts with SMC1A and SMC3 (By
similarity). Interacts with DDX11 (PubMed:17105772). Found in a
cohesin complex with SMC1A, SMC3 and STAG1 (PubMed:22628566).
{ECO:0000250|UniProtKB:Q61550, ECO:0000269|PubMed:11590136,
ECO:0000269|PubMed:15837422, ECO:0000269|PubMed:17105772,
ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:22628566}.
-!- INTERACTION:
Q13643:FHL3; NbExp=3; IntAct=EBI-80739, EBI-741101;
Q29RF7:PDS5A; NbExp=4; IntAct=EBI-80739, EBI-1175454;
Q9NTI5:PDS5B; NbExp=4; IntAct=EBI-80739, EBI-1175604;
Q14683:SMC1A; NbExp=14; IntAct=EBI-80739, EBI-80690;
Q9UQE7:SMC3; NbExp=15; IntAct=EBI-80739, EBI-80718;
Q9NP77:SSU72; NbExp=9; IntAct=EBI-80739, EBI-2515416;
Q8N3U4:STAG2; NbExp=13; IntAct=EBI-80739, EBI-1057252;
Q7Z5K2:WAPL; NbExp=15; IntAct=EBI-80739, EBI-1022242;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10623634}.
Chromosome {ECO:0000269|PubMed:11073952}. Chromosome, centromere
{ECO:0000269|PubMed:11073952}. Note=Associates with chromatin.
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 by
separase/ESPL1, leading to the dissociation of the complex from
chromosomes, allowing chromosome separation. Once cleaved by
caspase-3, the C-terminal 64 kDa cleavage product translocates to
the cytoplasm, where it may trigger apoptosis.
{ECO:0000269|PubMed:11073952}.
-!- DOMAIN: The C-terminal part associates with the head of SMC1A,
while the N-terminal part binds to the head of SMC3.
{ECO:0000250}.
-!- PTM: 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.
{ECO:0000269|PubMed:11509732, ECO:0000269|PubMed:11875078,
ECO:0000269|PubMed:12417729}.
-!- PTM: 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.
{ECO:0000269|PubMed:11073952}.
-!- POLYMORPHISM: Some radiosensitive cancer patients seem to have
Arg-481 instead of the conserved Gly-481. It may be that this
mutation could contribute to radiosensitivity.
{ECO:0000269|PubMed:11483345}.
-!- DISEASE: Cornelia de Lange syndrome 4 (CDLS4) [MIM:614701]: A form
of Cornelia de Lange syndrome, a clinically heterogeneous
developmental disorder associated with malformations affecting
multiple systems. It is characterized by facial dysmorphisms,
abnormal hands and feet, growth delay, cognitive retardation,
hirsutism, gastroesophageal dysfunction and cardiac,
ophthalmologic and genitourinary anomalies.
{ECO:0000269|PubMed:22633399}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA07554.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rad21/";
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EMBL; X98294; CAA66940.1; -; mRNA.
EMBL; D38551; BAA07554.2; ALT_INIT; mRNA.
EMBL; AY675320; AAT70725.1; -; Genomic_DNA.
EMBL; AK289505; BAF82194.1; -; mRNA.
EMBL; CH471060; EAW91963.1; -; Genomic_DNA.
EMBL; BC050381; AAH50381.1; -; mRNA.
CCDS; CCDS6321.1; -.
RefSeq; NP_006256.1; NM_006265.2.
UniGene; Hs.81848; -.
PDB; 4PJU; X-ray; 3.05 A; B=281-420.
PDB; 4PJW; X-ray; 2.85 A; B=281-420.
PDB; 4PK7; X-ray; 2.95 A; B=281-420.
PDBsum; 4PJU; -.
PDBsum; 4PJW; -.
PDBsum; 4PK7; -.
ProteinModelPortal; O60216; -.
SMR; O60216; -.
BioGrid; 111822; 278.
CORUM; O60216; -.
DIP; DIP-29201N; -.
ELM; O60216; -.
IntAct; O60216; 36.
MINT; O60216; -.
STRING; 9606.ENSP00000297338; -.
iPTMnet; O60216; -.
PhosphoSitePlus; O60216; -.
SwissPalm; O60216; -.
BioMuta; RAD21; -.
EPD; O60216; -.
MaxQB; O60216; -.
PaxDb; O60216; -.
PeptideAtlas; O60216; -.
PRIDE; O60216; -.
ProteomicsDB; 49246; -.
Ensembl; ENST00000297338; ENSP00000297338; ENSG00000164754.
GeneID; 5885; -.
KEGG; hsa:5885; -.
UCSC; uc003yod.4; human.
CTD; 5885; -.
DisGeNET; 5885; -.
EuPathDB; HostDB:ENSG00000164754.12; -.
GeneCards; RAD21; -.
GeneReviews; RAD21; -.
HGNC; HGNC:9811; RAD21.
HPA; CAB022065; -.
HPA; HPA020044; -.
MalaCards; RAD21; -.
MIM; 606462; gene.
MIM; 614701; phenotype.
neXtProt; NX_O60216; -.
OpenTargets; ENSG00000164754; -.
Orphanet; 199; Cornelia de Lange syndrome.
PharmGKB; PA34170; -.
eggNOG; KOG1213; Eukaryota.
eggNOG; ENOG410XRB4; LUCA.
GeneTree; ENSGT00940000154655; -.
HOGENOM; HOG000233800; -.
HOVERGEN; HBG059956; -.
InParanoid; O60216; -.
KO; K06670; -.
OMA; ENMGYDQ; -.
OrthoDB; EOG091G03QW; -.
PhylomeDB; O60216; -.
TreeFam; TF101215; -.
BioCyc; MetaCyc:ENSG00000164754-MONOMER; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
Reactome; R-HSA-2470946; Cohesin Loading onto Chromatin.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SIGNOR; O60216; -.
ChiTaRS; RAD21; human.
GeneWiki; RAD21; -.
GenomeRNAi; 5885; -.
PMAP-CutDB; O60216; -.
PRO; PR:O60216; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164754; Expressed in 249 organ(s), highest expression level in cerebral cortex.
CleanEx; HS_RAD21; -.
ExpressionAtlas; O60216; baseline and differential.
Genevisible; O60216; HS.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0005694; C:chromosome; TAS:Reactome.
GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
GO; GO:0008278; C:cohesin complex; IDA:UniProtKB.
GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030893; C:meiotic cohesin complex; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IMP:UniProtKB.
GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
InterPro; IPR039781; Rad21/Rec8-like.
InterPro; IPR006909; Rad21/Rec8_C_eu.
InterPro; IPR006910; Rad21_Rec8_N.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12585; PTHR12585; 1.
Pfam; PF04824; Rad21_Rec8; 1.
Pfam; PF04825; Rad21_Rec8_N; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Cell cycle; Cell division; Centromere;
Chromosome; Chromosome partition; Complete proteome;
Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
Isopeptide bond; Mental retardation; Mitosis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 631 Double-strand-break repair protein rad21
homolog.
/FTId=PRO_0000097872.
REGION 287 403 Interaction with WAPL and PDS5B.
{ECO:0000269|PubMed:19696148}.
REGION 362 403 Interaction with STAG1.
{ECO:0000269|PubMed:19696148}.
COMPBIAS 469 510 Pro-rich.
SITE 172 173 Cleavage; by ESPL1.
SITE 279 280 Cleavage; by caspase-3 or caspase-7.
SITE 450 451 Cleavage; by ESPL1.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 623 623 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 216 216 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 418 418 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 376 376 P -> R (in CDLS4; dbSNP:rs387907212).
{ECO:0000269|PubMed:22633399}.
/FTId=VAR_068691.
VARIANT 481 481 G -> R (in dbSNP:rs755168088).
{ECO:0000269|PubMed:11483345}.
/FTId=VAR_014281.
VARIANT 585 585 C -> R (in CDLS4; dbSNP:rs387907213).
{ECO:0000269|PubMed:22633399}.
/FTId=VAR_068692.
MUTAGEN 172 172 R->A: Abolishes first cleavage by ESPL1.
{ECO:0000269|PubMed:11509732}.
MUTAGEN 279 279 D->A: Abolishes cleavage by caspase-3.
{ECO:0000269|PubMed:11875078,
ECO:0000269|PubMed:12417729}.
MUTAGEN 450 450 R->A: Abolishes second cleavage by ESPL1.
{ECO:0000269|PubMed:11509732}.
CONFLICT 136 136 N -> I (in Ref. 1; CAA66940).
{ECO:0000305}.
HELIX 334 342 {ECO:0000244|PDB:4PJW}.
HELIX 345 347 {ECO:0000244|PDB:4PK7}.
HELIX 358 366 {ECO:0000244|PDB:4PJW}.
HELIX 369 372 {ECO:0000244|PDB:4PJW}.
HELIX 383 390 {ECO:0000244|PDB:4PJW}.
TURN 391 393 {ECO:0000244|PDB:4PK7}.
SEQUENCE 631 AA; 71690 MW; 7D4A6EA6392BE73D CRC64;
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP
LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD
DMLVSTTTSN LLLESEQSTS NLNEKINHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG
IFDDPPALSE AGVMLPEQPA HDDMDEDDNV SMGGPDSPDS VDPVEPMPTM TDQTTLVPNE
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL
MMWKETGGVE KLFSLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF
ENPEVPREDQ QQQHQQRDVI DEPIIEEPSR LQESVMEASR TNIDESAMPP PPPQGVKRKA
GQIDPEPVMP PQQVEQMEIP PVELPPEEPP NICQLIPELE LLPEKEKEKE KEKEDDEEEE
DEDASGGDQD QEERRWNKRT QQMLHGLQRA LAKTGAESIS LLELCRNTNR KQAAAKFYSF
LVLKKQQAIE LTQEEPYSDI IATPGPRFHI I


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