AHDC1_MOUSE
ID AHDC1_MOUSE Reviewed; 1594 AA.
AC Q6PAL7; Q5U5N7; Q8C4Y6; Q8VCU7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=AT-hook DNA-binding motif-containing protein 1;
GN Name=Ahdc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Mammary tumor, and Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1457-1594.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-842; SER-892; SER-1180;
RP SER-1315; SER-1317; SER-1392; THR-1394; SER-1396 AND SER-1540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19130.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL627184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019130; AAH19130.1; ALT_INIT; mRNA.
DR EMBL; BC042621; AAH42621.1; -; mRNA.
DR EMBL; BC060231; AAH60231.1; -; mRNA.
DR EMBL; AK080410; BAC37907.1; -; mRNA.
DR CCDS; CCDS38900.1; -.
DR RefSeq; NP_666267.3; NM_146155.3.
DR RefSeq; XP_006538797.1; XM_006538734.1.
DR RefSeq; XP_006538799.1; XM_006538736.2.
DR RefSeq; XP_006538800.1; XM_006538737.1.
DR RefSeq; XP_006538801.1; XM_006538738.3.
DR RefSeq; XP_006538802.1; XM_006538739.1.
DR RefSeq; XP_006538803.1; XM_006538740.1.
DR RefSeq; XP_006538804.1; XM_006538741.3.
DR RefSeq; XP_006538805.1; XM_006538742.1.
DR RefSeq; XP_011248533.1; XM_011250231.1.
DR RefSeq; XP_017175648.1; XM_017320159.1.
DR AlphaFoldDB; Q6PAL7; -.
DR BioGRID; 231029; 5.
DR STRING; 10090.ENSMUSP00000101536; -.
DR iPTMnet; Q6PAL7; -.
DR PhosphoSitePlus; Q6PAL7; -.
DR EPD; Q6PAL7; -.
DR jPOST; Q6PAL7; -.
DR MaxQB; Q6PAL7; -.
DR PaxDb; Q6PAL7; -.
DR PeptideAtlas; Q6PAL7; -.
DR PRIDE; Q6PAL7; -.
DR ProteomicsDB; 282045; -.
DR Antibodypedia; 30793; 19 antibodies from 8 providers.
DR Ensembl; ENSMUST00000044521; ENSMUSP00000047113; ENSMUSG00000037692.
DR Ensembl; ENSMUST00000105914; ENSMUSP00000101534; ENSMUSG00000037692.
DR Ensembl; ENSMUST00000105915; ENSMUSP00000101535; ENSMUSG00000037692.
DR Ensembl; ENSMUST00000105916; ENSMUSP00000101536; ENSMUSG00000037692.
DR GeneID; 230793; -.
DR KEGG; mmu:230793; -.
DR UCSC; uc008vcc.1; mouse.
DR CTD; 27245; -.
DR MGI; MGI:2444218; Ahdc1.
DR VEuPathDB; HostDB:ENSMUSG00000037692; -.
DR eggNOG; ENOG502QSFA; Eukaryota.
DR GeneTree; ENSGT00390000018883; -.
DR HOGENOM; CLU_004578_0_0_1; -.
DR InParanoid; Q6PAL7; -.
DR OMA; TEWAGDK; -.
DR OrthoDB; 61471at2759; -.
DR PhylomeDB; Q6PAL7; -.
DR TreeFam; TF332128; -.
DR BioGRID-ORCS; 230793; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ahdc1; mouse.
DR PRO; PR:Q6PAL7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PAL7; protein.
DR Bgee; ENSMUSG00000037692; Expressed in embryonic brain and 175 other tissues.
DR Genevisible; Q6PAL7; MM.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR039225; AHDC1.
DR InterPro; IPR032757; DUF4683.
DR PANTHER; PTHR15617; PTHR15617; 1.
DR Pfam; PF15735; DUF4683; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1594
FT /note="AT-hook DNA-binding motif-containing protein 1"
FT /id="PRO_0000313825"
FT DNA_BIND 395..407
FT /note="A.T hook 1"
FT DNA_BIND 541..553
FT /note="A.T hook 2"
FT REGION 19..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 887
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1394
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 606
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT CROSSLNK 1402
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5TGY3"
FT CONFLICT 431
FT /note="L -> LP (in Ref. 2; AAH42621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1594 AA; 168081 MW; 2DC06E3D70D75DC4 CRC64;
MRVKPQGLVV TSSAVCSSPD YLREPKYYPG GPPTPRPLLP TRPPASPPDK AFSTHTFSEN
PRPPPRRDPS SRRPPVLAKG DDLLPPRAAR PVSQAHCPSP APDNSSLRHW DNGRVNLRPV
VQLIDIMKDL TRLSQDLQHS GVHLDCGGLR LSRPPAPPPG DLQYSFFSSP SLANSIRSPE
ERANPHTKSE RPSHPLYEPE PEPRDSPQPG QGHGPGAAAT ATGLPPEPEP DGPDYSELAD
ADILSELASL TCPEAQLLEA QALEPPSPQP EPQLLDPQPR FLDPQALEPL GEGLELPPLQ
PLADPLGLPS LTLQALDTLP DSLESQLLDP QALDPLPKLL DVPGRRLEPQ QSLGHCQLAE
PLRLDLCSPH GPPGPEGHPK YALRRTDRPK ILCRRRKAGR GRKADSGPEG RLLPLPMPTG
LAAALAEPPP LPPPPPPTLS GPGPVPELEP ESSQTPMVPT RKGKCRGVRR MVVKMAKIPV
SLGRRNKTTY KVSSLSSSLS VEGKELGLRV SSEPTPLLKM KNNGRNVVVV FPPGEMPIIL
KRKRGRPPKN LLLGPGKPKE PTVVAAEAAT VTAATMAMPE VKKRRRRKQK LASPQPSYAA
DANDSKAEYS DVLAKLAFLN RQSQCAGRCS PPRCWTPSEP ESVHQAPDTQ SISQFLHRVQ
GFRRRGGKTG GFGGRGGGHA AKAARCSFSD FFEGIGKKKK VVAVAAPGLV GPGLTELGHP
RKRGRGEVDA VTGKPKRKRR SRKNGTLFPE QVPSGPGFGE AGAEWVGDKG GGWAPHHGHP
GGQAGRNCGF QGTEARAFAS TGLESGASGR GSYYAGAPSG QTELSQERQN LFTGYFRSLL
DSDDSSDLLD FALSASRPES RKASGTYAGP PSSALPAQRG LATFPSRGAK ASPVAVGSSG
AGADPSFQPV LPSRQTFPPG RATSYGITPA TSDCRAAETF PKLAPPPSAV ARSPTTHPPA
NTYPPQYGGY GAGQSVFASA KPFSGQDCAN SKDCSFAYGS GNSLPASPSS AHSAGYAPPP
TGGPCLPPSK ASFFNSSEGG PFSGSAPTPL RCDSRASTVS PGGYMVPKGT TASAASVASS
SSSSFQPSPE NCRQFVGASQ WPFRQGYGGL DWASEAFSQL YNPNFDCHGS EPNVILDISN
YTPQKVKQQT AVSETFSESS SDSTQFSQPV GGGGFRRANS EASSSEGQSS LSSLEKLMMD
WNEASSAPGY NWNQSVLFQS SSKPGRGRRK KVDLFEASHL GFSTSTSATA SGYPSKRSTG
PRQPRGGRGS GACSAKKERG GTAAKAKFIP KPQPVNPLFQ DSPDLGLDYY SGDSSMSPLP
SQSRAFGVGE RDPCDFMGPY SMNPSTPSDG TFGQGFHCDS PSLGAAELDG KHFPPLAHPP
TVFDAGLQKA YSPTCSPTLG FKEELRPPPS KLTACEPLKH GLQGASLSHA AQAHLSCRDL
PLGQPHYDSP SCKGTAYWYP PGSAARSPPY EGKVGSGLLA DFLGRTEAVC LSAPHLASPP
ATPKADKEPL EMARPPGPPR GPAAATAGYG CPLLSDLTLS PVPRDSLLPL QDTAYRYPGF
MPQAHPGLGG GPKSGFLGPM AEPHPEDTFT VTSL
