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Protein

Double-strand-break repair protein rad21 homolog

Gene

rad21

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Double-strand-break repair protein rad21 homolog
Alternative name(s):
SCC1 homolog
Gene namesi
Name:rad21
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity
  • Chromosomecentromere By similarity

  • 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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 629629Double-strand-break repair protein rad21 homologPRO_0000097874Add
BLAST

Post-translational modificationi

Cleaved by separase/espl1 after the Arg residue at the at the onset of anaphase.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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei172 – 1732Cleavage; by ESPL1By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with separase/espl1, which cleaves it. Cohesin complexes are composed of the smc1 and smc3 heterodimer attached via their hinge domain, rad21 which link them, and one STAG protein (stag1 or stag2), which interacts with rad21.2 Publications

Protein-protein interaction databases

BioGridi100454. 4 interactions.
IntActiO93310. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliO93310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi463 – 51149Pro-richAdd
BLAST
Compositional biasi479 – 55173Glu-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

HOVERGENiHBG059956.
KOiK06670.

Family and domain databases

Gene3Di1.10.10.580. 1 hit.
InterProiIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

O93310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIICPKVK
60 70 80 90 100
MALRTSGHLL LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN
110 120 130 140 150
REAAYNAITL PEEFHDFDQP LPDLDDIDVA QQFSLNQSRV EEITMREEVS
160 170 180 190 200
NINILQDNDF GDFGMDDREM MREGSAFEDD MLTTNASNLK LEPEQSTSQL
210 220 230 240 250
NEKSNHLEYD DQYKDDNFGE GNEGGILDDK LLSNDAGGIF DDPPAMPEEG
260 270 280 290 300
VAMPEQPVHD DLDDDDNVSM GAPDSPDSVD PVEPLPTMTD QTTLVPNEEE
310 320 330 340 350
AFALEPIDIT VKETKAKRKR KLIVDSVKEL DSKTIRAQLS DYSDIVTTLD
360 370 380 390 400
LAPPTKKLMM WKETGGVEKL FSLPAQPLWN TRLLKLFTRC LTPLVLDDLR
410 420 430 440 450
KRRKGGEADN LDEFLKEFEN PEVPREELRP QDVIDQPILE EASHLQESLM
460 470 480 490 500
EGSRTHLDDT IMPPPPPKQG VKRDSLQMEP EPMPMMQEAE PQIEMPPPPL
510 520 530 540 550
PPPLELPPEE PQSISDLIPE LNLLPEKEKE KDEEEEEEEE DTTGTEQDQE
560 570 580 590 600
ERRWNKRTQQ MLHGLQRVLA KTGAESISLL DLCRNTNRKQ AAAKFYSFLV
610 620
LKKQQAIELT QREPYSDIVA TPGPRFHTV
Length:629
Mass (Da):71,555
Last modified:November 1, 1998 - v1
Checksum:i0FCD268C712FF2C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051786 mRNA. Translation: AAC26809.1.
RefSeqiNP_001083807.1. NM_001090338.1.
UniGeneiXl.53864.

Genome annotation databases

GeneIDi399129.
KEGGixla:399129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051786 mRNA. Translation: AAC26809.1.
RefSeqiNP_001083807.1. NM_001090338.1.
UniGeneiXl.53864.

3D structure databases

ProteinModelPortaliO93310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi100454. 4 interactions.
IntActiO93310. 6 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399129.
KEGGixla:399129.

Organism-specific databases

CTDi5885.

Phylogenomic databases

HOVERGENiHBG059956.
KOiK06670.

Family and domain databases

Gene3Di1.10.10.580. 1 hit.
InterProiIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRAD21_XENLA
AccessioniPrimary (citable) accession number: O93310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: November 1, 1998
Last modified: January 20, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.