RHNO1
entrez
83695
canonical
uniprot
Q9BSD3
canonical
ensembl
ENSG00000171792
resolver
ensp
ENSP00000438590
resolver
ensp
ENSP00000438828
resolver
ensp
ENSP00000479598
resolver
genesymbol
RHNO1
resolver
genesymbol_syn
C12orf32
resolver
genesymbol_syn
RHINO
resolver
hgnc
HGNC:28206
resolver
uniprot
B7Z989
resolver
uniprot_entry
RHNO1_HUMAN
resolver
uniprot_sec
B7Z989
resolver
amino_acid_sequence
MPPRKKRRQPSQKAPLLFHQQPLEGPKHSCASTQLPITHTRQVPSKPIDHSTITSWVSPDFDTAAGSLFPAYQKHQNRARHSSRKPTTSKFPHLTFESPQSSSSETLGIPLIRECPSESEKDVSRRPLVPVLSPQSCGNMSVQALQSLPYVFIPPDIQTPESSSVKEELIPQDQKENSLLSCTLHTGTPNSPEPGPVLVKDTPEDKYGIKVTWRRRQHLLAYLRERGKLSRSQFLVKS
uniprot
proteins
function
FUNCTION: Involved in microhomology-mediated end-joining (MMEJ) DNA repair by promoting recruitment of polymerase theta (POLQ) to DNA damage sites during mitosis (PubMed:37440612). MMEJ is an alternative non-homologous end-joining (NHEJ) machinery that takes place during mitosis to repair double-strand breaks in DNA that originate in S-phase (PubMed:37440612). Accumulates in M-phase; following phosphorylation by PLK1, interacts with POLQ, enabling its recruitment to double-strand breaks for subsequent repair (PubMed:37440612). Also involved in the DNA damage response (DDR) signaling in response to genotoxic stresses such as ionizing radiation (IR) during the S phase (PubMed:21659603, PubMed:25602520). Recruited to sites of DNA damage through interaction with the 9-1-1 cell-cycle checkpoint response complex and TOPBP1 in a ATR-dependent manner (PubMed:21659603, PubMed:25602520). Required for the progression of the G1 to S phase transition (PubMed:21659603). Plays a role in the stimulation of CHEK1 phosphorylation (PubMed:21659603). {ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:25602520, ECO:0000269|PubMed:37440612}.
uniprot
proteins
mass_dalton
26709
uniprot
proteins
mutagenesis
MUTAGEN 51..52; /note="ST->AA: In RHINO-PLK1S/T(7A) mutant; abolished phosphorylation leading to decreased interaction with POLQ; when associated with A-141, 162-A--A-164 and A-178."; /evidence="ECO:0000269|PubMed:37440612"; MUTAGEN 51; /note="S->A: Abolished phosphorylation by PLK1, leading to decreased interaction with POLQ."; /evidence="ECO:0000269|PubMed:37440612"; MUTAGEN 55..61; /note="SWVSPDF->AAAAAAA: Inhibits binding to the 9-1-1 complex. Does not inhibit interaction with TOPBP1. Inhibits localizion to sites of DNA damage."; /evidence="ECO:0000269|PubMed:21659603"; MUTAGEN 125..132; /note="Missing: Abolished degradation following mitosis; when associated with 174-Missing-178."; /evidence="ECO:0000269|PubMed:37440612"; MUTAGEN 141; /note="S->A: In RHINO-PLK1S/T(7A) mutant; abolished phosphorylation leading to decreased interaction with POLQ; when associated with 51-A-A-52, 162-A--A-164 and A-178."; /evidence="ECO:0000269|PubMed:37440612"; MUTAGEN 162..164; /note="SSS->AAA: In RHINO-PLK1S/T(7A) mutant; abolished phosphorylation leading to decreased interaction with POLQ; when associated with 51-A-A-52, A-141 and A-178."; /evidence="ECO:0000269|PubMed:37440612"; MUTAGEN 174..178; /note="Missing: Abolished degradation following mitosis; when associated with 125-Missing-132."; /evidence="ECO:0000269|PubMed:37440612"; MUTAGEN 178; /note="S->A: In RHINO-PLK1S/T(7A) mutant; abolished phosphorylation leading to decreased interaction with POLQ; when associated with 51-A-A-52, 162-A--A-164 and A-141."; /evidence="ECO:0000269|PubMed:37440612
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-51 by PLK1, promoting interaction with polymerase theta (POLQ). {ECO:0000269|PubMed:37440612}.; PTM: Ubiquitinated and degraded by the APC/C complex upon mitotic exit. {ECO:0000269|PubMed:37440612}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15221005
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
20811708
uniprot
proteins
pubmed
21659603
uniprot
proteins
pubmed
25602520
uniprot
proteins
pubmed
31776186
uniprot
proteins
pubmed
37440612
uniprot
proteins
sequence_length
238
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20811708}. Chromosome {ECO:0000269|PubMed:20811708, ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:25602520, ECO:0000269|PubMed:37440612}. Note=Localizes to sites of DNA damage in a H2AX-independent manner. {ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:37440612}.
uniprot
proteins