AUNIP_HUMAN
ID AUNIP_HUMAN Reviewed; 357 AA.
AC Q9H7T9; C9EI59; Q53F70;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Aurora kinase A and ninein-interacting protein {ECO:0000303|PubMed:20596670};
DE Short=AIBp {ECO:0000303|PubMed:20596670};
GN Name=AUNIP {ECO:0000303|PubMed:29042561, ECO:0000312|HGNC:HGNC:28363};
GN Synonyms=C1orf135 {ECO:0000312|HGNC:HGNC:28363};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION,
RP INDUCTION, AND INTERACTION WITH AURKA AND NIN.
RX PubMed=20596670; DOI=10.3892/ijo_00000691;
RA Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y.,
RA Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.;
RT "Functional characterization of AIBp, a novel Aurora-A binding protein in
RT centrosome structure and spindle formation.";
RL Int. J. Oncol. 37:429-436(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-82.
RC TISSUE=Kidney epithelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 AND SER-292, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBBP8, AND DNA-BINDING.
RX PubMed=29042561; DOI=10.1038/s41467-017-01151-w;
RA Lou J., Chen H., Han J., He H., Huen M.S.Y., Feng X.H., Liu T., Huang J.;
RT "AUNIP/C1orf135 directs DNA double-strand breaks towards the homologous
RT recombination repair pathway.";
RL Nat. Commun. 8:985-985(2017).
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 (PubMed:29042561). Serves as a sensor of DNA
CC damage: binds DNA with a strong preference for DNA substrates that
CC mimic structures generated at stalled replication forks, and anchors
CC RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing
CC homologous recombination repair (PubMed:29042561). Inhibits non-
CC homologous end joining (NHEJ) (PubMed:29042561). Required for the
CC dynamic movement of AURKA at the centrosomes and spindle apparatus
CC during the cell cycle (PubMed:20596670). {ECO:0000269|PubMed:20596670,
CC ECO:0000269|PubMed:29042561}.
CC -!- SUBUNIT: Interacts (via C-terminus) with AURKA (via C-terminus)
CC (PubMed:20596670). Interacts (via N-terminus) with NIN; this
CC interaction blocks NIN phosphorylation by both AURKA and GSK3B
CC (PubMed:20596670). Identified in a complex with NIN and AURKA
CC (PubMed:20596670). Interacts with RBBP8/CtIP (PubMed:29042561).
CC {ECO:0000269|PubMed:20596670, ECO:0000269|PubMed:29042561}.
CC -!- INTERACTION:
CC Q9H7T9; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-10693257, EBI-725606;
CC Q9H7T9; Q01658: DR1; NbExp=3; IntAct=EBI-10693257, EBI-750300;
CC Q9H7T9; P22607: FGFR3; NbExp=3; IntAct=EBI-10693257, EBI-348399;
CC Q9H7T9; P06396: GSN; NbExp=3; IntAct=EBI-10693257, EBI-351506;
CC Q9H7T9; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-10693257, EBI-1054873;
CC Q9H7T9; P01112: HRAS; NbExp=3; IntAct=EBI-10693257, EBI-350145;
CC Q9H7T9; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-10693257, EBI-398874;
CC Q9H7T9; O43741: PRKAB2; NbExp=3; IntAct=EBI-10693257, EBI-1053424;
CC Q9H7T9; Q9Y649; NbExp=3; IntAct=EBI-10693257, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29042561}. Chromosome
CC {ECO:0000269|PubMed:29042561}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:20596670}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:20596670}.
CC Note=Accumulates at sites of DNA damage by binding to DNA substrates
CC that mimick structures generated at stalled replication forks
CC (PubMed:29042561). Localizes to the centrosome in interphase and to the
CC spindle pole in metaphase (PubMed:20596670).
CC {ECO:0000269|PubMed:20596670, ECO:0000269|PubMed:29042561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H7T9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7T9-2; Sequence=VSP_044288;
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscles, placenta and
CC testis.
CC -!- INDUCTION: Overexpressed in brain tumors.
CC {ECO:0000269|PubMed:20596670}.
CC -!- SIMILARITY: Belongs to the AUNIP family. {ECO:0000305}.
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DR EMBL; GQ844687; ACV90488.1; -; mRNA.
DR EMBL; AK024326; BAB14886.1; -; mRNA.
DR EMBL; AK223419; BAD97139.1; -; mRNA.
DR EMBL; AL020996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000209; AAH00209.1; -; mRNA.
DR CCDS; CCDS266.1; -. [Q9H7T9-1]
DR CCDS; CCDS72731.1; -. [Q9H7T9-2]
DR RefSeq; NP_001274419.1; NM_001287490.1. [Q9H7T9-2]
DR RefSeq; NP_076942.1; NM_024037.2. [Q9H7T9-1]
DR AlphaFoldDB; Q9H7T9; -.
DR BioGRID; 122471; 15.
DR IntAct; Q9H7T9; 13.
DR STRING; 9606.ENSP00000443647; -.
DR iPTMnet; Q9H7T9; -.
DR PhosphoSitePlus; Q9H7T9; -.
DR BioMuta; AUNIP; -.
DR DMDM; 74733700; -.
DR MassIVE; Q9H7T9; -.
DR MaxQB; Q9H7T9; -.
DR PaxDb; Q9H7T9; -.
DR PeptideAtlas; Q9H7T9; -.
DR PRIDE; Q9H7T9; -.
DR ProteomicsDB; 7615; -.
DR ProteomicsDB; 81147; -. [Q9H7T9-1]
DR Antibodypedia; 50871; 58 antibodies from 13 providers.
DR DNASU; 79000; -.
DR Ensembl; ENST00000374298.4; ENSP00000363416.4; ENSG00000127423.11. [Q9H7T9-1]
DR Ensembl; ENST00000538789.5; ENSP00000443647.1; ENSG00000127423.11. [Q9H7T9-2]
DR GeneID; 79000; -.
DR KEGG; hsa:79000; -.
DR MANE-Select; ENST00000374298.4; ENSP00000363416.4; NM_024037.3; NP_076942.1.
DR UCSC; uc001bkw.3; human. [Q9H7T9-1]
DR CTD; 79000; -.
DR DisGeNET; 79000; -.
DR GeneCards; AUNIP; -.
DR HGNC; HGNC:28363; AUNIP.
DR HPA; ENSG00000127423; Group enriched (bone marrow, testis).
DR neXtProt; NX_Q9H7T9; -.
DR OpenTargets; ENSG00000127423; -.
DR PharmGKB; PA142672453; -.
DR VEuPathDB; HostDB:ENSG00000127423; -.
DR eggNOG; ENOG502SFBZ; Eukaryota.
DR GeneTree; ENSGT00390000003280; -.
DR HOGENOM; CLU_835590_0_0_1; -.
DR InParanoid; Q9H7T9; -.
DR OMA; HHRMGTP; -.
DR OrthoDB; 1235123at2759; -.
DR PhylomeDB; Q9H7T9; -.
DR TreeFam; TF337334; -.
DR PathwayCommons; Q9H7T9; -.
DR SignaLink; Q9H7T9; -.
DR BioGRID-ORCS; 79000; 25 hits in 1088 CRISPR screens.
DR ChiTaRS; AUNIP; human.
DR GenomeRNAi; 79000; -.
DR Pharos; Q9H7T9; Tbio.
DR PRO; PR:Q9H7T9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H7T9; protein.
DR Bgee; ENSG00000127423; Expressed in oocyte and 108 other tissues.
DR Genevisible; Q9H7T9; HS.
DR GO; GO:0005813; C:centrosome; IDA: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; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR InterPro; IPR029286; AUNIP.
DR PANTHER; PTHR14526; PTHR14526; 1.
DR Pfam; PF15334; AIB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..357
FT /note="Aurora kinase A and ninein-interacting protein"
FT /id="PRO_0000284572"
FT REGION 71..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..357
FT /note="Interaction with AURKA"
FT /evidence="ECO:0000269|PubMed:20596670"
FT REGION 281..357
FT /note="Interaction with RBBP8/CtIP"
FT /evidence="ECO:0000269|PubMed:29042561"
FT COMPBIAS 71..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 349..357
FT /note="GNQVIRHQF -> VQALACQQDCCRRSILKRQKHLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20596670"
FT /id="VSP_044288"
FT VARIANT 82
FT /note="K -> T (in dbSNP:rs34449716)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_031776"
SQ SEQUENCE 357 AA; 40253 MW; 8080DCF2E3CAB569 CRC64;
MRRTGPEEEA CGVWLDAAAL KRRKVQTHLI KPGTKMLTLL PGERKANIYF TQRRAPSTGI
HQRSIASFFT LQPGKTNGSD QKSVSSHTES QINKESKKNA TQLDHLIPGL AHDCMASPLA
TSTTADIQEA GLSPQSLQTS GHHRMKTPFS TELSLLQPDT PDCAGDSHTP LAFSFTEDLE
SSCLLDRKEE KGDSARKWEW LHESKKNYQS MEKHTKLPGD KCCQPLGKTK LERKVSAKEN
RQAPVLLQTY RESWNGENIE SVKQSRSPVS VFSWDNEKND KDSWSQLFTE DSQGQRVIAH
NTRAPFQDVT NNWNWDLGPF PNSPWAQCQE DGPTQNLKPD LLFTQDSEGN QVIRHQF
