Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Double-strand-break repair protein rad21 homolog

Gene

RAD21

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-BTA-2467813. Separation of Sister Chromatids.
R-BTA-2468052. Establishment of Sister Chromatid Cohesion.
R-BTA-2470946. Cohesin Loading onto Chromatin.
R-BTA-2500257. Resolution of Sister Chromatid Cohesion.
R-BTA-3108214. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-strand-break repair protein rad21 homolog
Gene namesi
Name:RAD21
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 14

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002454871 – 630Double-strand-break repair protein rad21 homologAdd BLAST630

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46PhosphoserineBy similarity1
Modified residuei153PhosphoserineBy similarity1
Modified residuei175PhosphoserineBy similarity1
Modified residuei249PhosphoserineBy similarity1
Modified residuei394PhosphothreonineBy similarity1
Modified residuei454PhosphoserineBy similarity1
Modified residuei544PhosphoserineBy similarity1
Modified residuei622PhosphothreonineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei172 – 173Cleavage; by ESPL1By similarity2
Sitei279 – 280Cleavage; by caspase-3 or caspase-7By similarity2
Sitei450 – 451Cleavage; by ESPL1By similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3SWX9.
PRIDEiQ3SWX9.

Expressioni

Gene expression databases

BgeeiENSBTAG00000007303.

Interactioni

Subunit structurei

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. Found in a complex with SMC1A, SMC3, CDCA5, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with PDS5B and WAPL; the interaction is direct. Interacts with SMC1A and SMC3. Interacts with DDX11.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009607.

Structurei

3D structure databases

ProteinModelPortaliQ3SWX9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni287 – 403Interaction with WAPL and PDS5BBy similarityAdd BLAST117
Regioni362 – 403Interaction with STAG1By similarityAdd BLAST42

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi468 – 509Pro-richAdd BLAST42

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

eggNOGiKOG1213. Eukaryota.
ENOG410XRB4. LUCA.
GeneTreeiENSGT00390000011606.
HOGENOMiHOG000233800.
HOVERGENiHBG059956.
InParanoidiQ3SWX9.
KOiK06670.
OMAiDEPIMEE.
OrthoDBiEOG091G03QW.
TreeFamiTF101215.

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.

Q3SWX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK
60 70 80 90 100
MALRTSGHLL LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN
110 120 130 140 150
REAAYNAITL PEEFHDFDQP LPDLDDIDVA QQFSLNQSRV EEITMREEVG
160 170 180 190 200
NISILQENDF GDFGMDDREI MREGSAFEDD DMLASTGASN LLLEPEQSTS
210 220 230 240 250
NLNEKINHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG IFDDPPALSE
260 270 280 290 300
AGVMLPEQPA HDDMDEDDNV SMGGPDSPDS VDPVEPMPTM TDQTTLVPNE
310 320 330 340 350
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT
360 370 380 390 400
LDLAPPTKKL MMWKETGGVE KLFSLPAQPL WNNRLLKLFT RCLTPLVPED
410 420 430 440 450
LRKRRKGGEA DNLDEFLKEF ENPEVPREDQ QQQHQQRDVI DEPILEEPSR
460 470 480 490 500
LQESMETSRT NLDESAMPPP PPQGVKRKAG QIDPEPMIPP QQAEQMEIPP
510 520 530 540 550
VELPPEEPPN ICQLIPELEL LPEKEKEKEK EKEDDEEEED EDASGGDQDQ
560 570 580 590 600
EERRWNKRTQ QMLHGLQRAL AKTGAESISL LELCRNTNRK QAAAKFYSFL
610 620 630
VLKKQQAIEL TQEEPYSDII ATPGPRFHII
Length:630
Mass (Da):71,514
Last modified:October 11, 2005 - v1
Checksum:iDC23DA37F757CD27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104612 mRNA. Translation: AAI04613.1.
RefSeqiNP_001029889.1. NM_001034717.1.
UniGeneiBt.15668.

Genome annotation databases

EnsembliENSBTAT00000009607; ENSBTAP00000009607; ENSBTAG00000007303.
GeneIDi540966.
KEGGibta:540966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104612 mRNA. Translation: AAI04613.1.
RefSeqiNP_001029889.1. NM_001034717.1.
UniGeneiBt.15668.

3D structure databases

ProteinModelPortaliQ3SWX9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009607.

Proteomic databases

PaxDbiQ3SWX9.
PRIDEiQ3SWX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009607; ENSBTAP00000009607; ENSBTAG00000007303.
GeneIDi540966.
KEGGibta:540966.

Organism-specific databases

CTDi5885.

Phylogenomic databases

eggNOGiKOG1213. Eukaryota.
ENOG410XRB4. LUCA.
GeneTreeiENSGT00390000011606.
HOGENOMiHOG000233800.
HOVERGENiHBG059956.
InParanoidiQ3SWX9.
KOiK06670.
OMAiDEPIMEE.
OrthoDBiEOG091G03QW.
TreeFamiTF101215.

Enzyme and pathway databases

ReactomeiR-BTA-2467813. Separation of Sister Chromatids.
R-BTA-2468052. Establishment of Sister Chromatid Cohesion.
R-BTA-2470946. Cohesin Loading onto Chromatin.
R-BTA-2500257. Resolution of Sister Chromatid Cohesion.
R-BTA-3108214. SUMOylation of DNA damage response and repair proteins.

Gene expression databases

BgeeiENSBTAG00000007303.

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_BOVIN
AccessioniPrimary (citable) accession number: Q3SWX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 11, 2005
Last modified: November 30, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.