AUNIP_RAT
ID AUNIP_RAT Reviewed; 347 AA.
AC D3ZUC4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Aurora kinase A and ninein-interacting protein {ECO:0000305};
GN Name=Aunip {ECO:0000312|RGD:1589922};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: DNA-binding protein that accumulates at DNA double-strand
CC breaks (DSBs) following DNA damage and promotes DNA resection and
CC homologous recombination. Serves as a sensor of DNA damage: binds DNA
CC with a strong preference for DNA substrates that mimic structures
CC generated at stalled replication forks, and anchors RBBP8/CtIP to DSB
CC sites to promote DNA end resection and ensuing homologous recombination
CC repair. Inhibits non-homologous end joining (NHEJ). Required for the
CC dynamic movement of AURKA at the centrosomes and spindle apparatus
CC during the cell cycle. {ECO:0000250|UniProtKB:Q9H7T9}.
CC -!- SUBUNIT: Interacts (via C-terminus) with AURKA (via C-terminus).
CC Interacts (via N-terminus) with NIN; this interaction blocks NIN
CC phosphorylation by both AURKA and GSK3B. Identified in a complex with
CC NIN and AURKA. Interacts with RBBP8/CtIP.
CC {ECO:0000250|UniProtKB:Q9H7T9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7T9}.
CC Chromosome {ECO:0000250|UniProtKB:Q9H7T9}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9H7T9}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9H7T9}. Note=Accumulates at sites of DNA damage
CC by binding to DNA substrates that mimick structures generated at
CC stalled replication forks. Localizes to the centrosome in interphase
CC and to the spindle pole in metaphase. {ECO:0000250|UniProtKB:Q9H7T9}.
CC -!- SIMILARITY: Belongs to the AUNIP family. {ECO:0000305}.
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DR EMBL; AABR06040351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001071529.1; XM_001071529.4.
DR RefSeq; XP_002726684.1; XM_002726638.4.
DR AlphaFoldDB; D3ZUC4; -.
DR STRING; 10116.ENSRNOP00000032347; -.
DR PhosphoSitePlus; D3ZUC4; -.
DR PaxDb; D3ZUC4; -.
DR PRIDE; D3ZUC4; -.
DR Ensembl; ENSRNOT00000039322; ENSRNOP00000032347; ENSRNOG00000022030.
DR GeneID; 689656; -.
DR KEGG; rno:689656; -.
DR UCSC; RGD:1589922; rat.
DR CTD; 79000; -.
DR RGD; 1589922; Aunip.
DR eggNOG; ENOG502SFBZ; Eukaryota.
DR GeneTree; ENSGT00390000003280; -.
DR HOGENOM; CLU_835590_0_0_1; -.
DR InParanoid; D3ZUC4; -.
DR OMA; HHRMGTP; -.
DR OrthoDB; 1235123at2759; -.
DR PhylomeDB; D3ZUC4; -.
DR TreeFam; TF337334; -.
DR PRO; PR:D3ZUC4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000022030; Expressed in testis and 14 other tissues.
DR Genevisible; D3ZUC4; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR InterPro; IPR029286; AUNIP.
DR PANTHER; PTHR14526; PTHR14526; 1.
DR Pfam; PF15334; AIB; 1.
PE 3: Inferred from homology;
KW Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..347
FT /note="Aurora kinase A and ninein-interacting protein"
FT /id="PRO_0000419631"
FT REGION 182..347
FT /note="Interaction with AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9H7T9"
FT REGION 273..347
FT /note="Interaction with RBBP8/CtIP"
FT /evidence="ECO:0000250|UniProtKB:Q9H7T9"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7T9"
SQ SEQUENCE 347 AA; 38244 MW; B3858257513440F1 CRC64;
MSRRGPEEEA CGVWLDAAAL KRQKMQTHLL KLGTKMLTLL PGERKPSIPF TQRRATRQTS
ITSFVTSQPG MANGGNQKNA SSLKENQINR ECKSRSQLDC LDQGLEDDCL VSPLATSTPA
DIREAGHSPQ SSQISGCQSL ETTSLTMMSF PQPVVLMGTG ESKAPLASSF TQFLERSCLL
DQREAKRKRE GLCGSKTDCP GMGSHIRPPG GKCHQPLDKA KVEKRATAKE NRQAPVHLQT
YRFGSHSGKK TLLVTKSPCP LSVFSWDIDR KDRDSWSQLF TEDSQGHQVI AHSTKMPFQD
VTNARNQGSG QFPDSPQAQG QDGPTLLHLQ PHLLFTQDSE GNRVIRH
