WDHD1_MOUSE
ID WDHD1_MOUSE Reviewed; 1117 AA.
AC P59328; Q6P408;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=WD repeat and HMG-box DNA-binding protein 1;
DE AltName: Full=Acidic nucleoplasmic DNA-binding protein 1;
DE Short=And-1;
GN Name=Wdhd1; Synonyms=And1;
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 MRNA] (ISOFORM 3).
RC TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-933 (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-819 AND SER-821, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and 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-664, 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 -!- FUNCTION: Acts as a replication initiation factor that brings together
CC the MCM2-7 helicase and the DNA polymerase alpha/primase complex in
CC order to initiate DNA replication. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the polymerase alpha catalytic subunit POLA1.
CC Interacts with MCM10. Interacts with DNA2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P59328-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59328-2; Sequence=VSP_006757, VSP_006758;
CC Name=3;
CC IsoId=P59328-3; Sequence=VSP_016898;
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DR EMBL; BC063740; AAH63740.1; -; mRNA.
DR EMBL; AK036390; BAC29408.1; -; mRNA.
DR EMBL; AK052690; BAC35097.1; -; mRNA.
DR RefSeq; NP_766186.2; NM_172598.3.
DR AlphaFoldDB; P59328; -.
DR SMR; P59328; -.
DR BioGRID; 230088; 2.
DR STRING; 10090.ENSMUSP00000107421; -.
DR iPTMnet; P59328; -.
DR PhosphoSitePlus; P59328; -.
DR EPD; P59328; -.
DR jPOST; P59328; -.
DR MaxQB; P59328; -.
DR PaxDb; P59328; -.
DR PeptideAtlas; P59328; -.
DR PRIDE; P59328; -.
DR ProteomicsDB; 297935; -. [P59328-1]
DR ProteomicsDB; 297936; -. [P59328-2]
DR ProteomicsDB; 297937; -. [P59328-3]
DR Antibodypedia; 44; 175 antibodies from 28 providers.
DR DNASU; 218973; -.
DR Ensembl; ENSMUST00000111790; ENSMUSP00000107420; ENSMUSG00000037572. [P59328-2]
DR GeneID; 218973; -.
DR KEGG; mmu:218973; -.
DR UCSC; uc007thu.2; mouse. [P59328-3]
DR UCSC; uc007thv.2; mouse. [P59328-1]
DR UCSC; uc007thw.2; mouse. [P59328-2]
DR CTD; 11169; -.
DR MGI; MGI:2443514; Wdhd1.
DR VEuPathDB; HostDB:ENSMUSG00000037572; -.
DR eggNOG; KOG1274; Eukaryota.
DR GeneTree; ENSGT00390000002030; -.
DR HOGENOM; CLU_004219_6_0_1; -.
DR InParanoid; P59328; -.
DR OMA; NAWFPIC; -.
DR PhylomeDB; P59328; -.
DR BioGRID-ORCS; 218973; 9 hits in 21 CRISPR screens.
DR ChiTaRS; Wdhd1; mouse.
DR PRO; PR:P59328; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P59328; protein.
DR Bgee; ENSMUSG00000037572; Expressed in otic placode and 185 other tissues.
DR ExpressionAtlas; P59328; baseline and differential.
DR Genevisible; P59328; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; IDA:MGI.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0140462; P:pericentric heterochromatin organization; IMP:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:MGI.
DR GO; GO:0006396; P:RNA processing; IMP:MGI.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR022100; Mcl1_mid.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12341; Mcl1_mid; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..1117
FT /note="WD repeat and HMG-box DNA-binding protein 1"
FT /id="PRO_0000051339"
FT REPEAT 11..50
FT /note="WD 1"
FT REPEAT 52..91
FT /note="WD 2"
FT REPEAT 93..131
FT /note="WD 3"
FT REPEAT 134..173
FT /note="WD 4"
FT REPEAT 184..223
FT /note="WD 5"
FT REPEAT 228..267
FT /note="WD 6"
FT REPEAT 271..310
FT /note="WD 7"
FT DNA_BIND 1004..1073
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 816..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 664
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 819
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT MOD_RES 953
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT CROSSLNK 1116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT CROSSLNK 1116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75717"
FT VAR_SEQ 314..350
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016898"
FT VAR_SEQ 630..641
FT /note="TPCYVDSEGCVR -> KIIFFLYIKDIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006757"
FT VAR_SEQ 642..1117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006758"
FT CONFLICT 54
FT /note="G -> V (in Ref. 2; BAC29408)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="S -> P (in Ref. 2; BAC29408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1117 AA; 124254 MW; 01F80C3012B39EA7 CRC64;
MPATQKPMRY GHTEGHTEVC FDDSGSYIVT CGSDGDVRMW EDLDDDDPKS VNVGEKAFSC
ALKNGKLVTA VSNNTVQVYT FPEGVPDGIL TRFTTNANHV VFNGAGNKIA AGSSDFLVKV
VDVMDNSQQQ TFRGHDAPVL SLSFDPKDIF LASASCDGTV RVWNISDQTC AVSWPVLQKS
NDVVNAKSIC RLAWQPKAGK LLAVPVEKSV KLYRRETWSN PFDLSDSSIS QTLNIVTWSP
CGQYLAAGAI NGLIVVWNVE TKDCMERVKH EKGYAICGLA WHPTCSRICY TDVEGNLGVL
ENVCDLSGKV SSNKVSSRVE KDYNDLFDGD DTSSAGDFLN DNAVEIPSFS KGIINEDDDN
DDIMLAADHD LGDDENSVDV TMLKADLSHK EEGDDDQARS IHNLPLIRPQ RPFYDGPMPT
PRQKPFQSSS TPLHLSHRFM VWNSVGIIRC YNDDQDSAID VEFHDTSIHH ATHLLNAFNY
TMGTLSHEAI LLACESADEL ASKLHCLHFS SWDSSKEWMV DMPQNEDIEA ICLGLGWAAA
ATTALLLRLF TIGGVQKEVF CLPGPVVSMA GHGEQLCIVY HRGTGFDGDQ CLGVQLLELG
RKKNQVLHGD PLPLTRKSYL TWLGFSAEGT PCYVDSEGCV RMLNRGLGNT WTPVCNIREH
CKGKSDHYWV VGIHENPQQL RCIPCKGSRF PPTLPRPAVA ILSFKLPYCQ TSTEKGQMEE
QFWHSVLFHN YLDYLAKNGY DYEESIKNQA VKEQQELLMK MLALSCKLER EFRCVELADL
MTQNAVHLAI KYASRSRKLI LAQKLSELAA EKAAELAETQ SEEEKEEDFR EKLNAGYSHT
TTEWSRPRVR SQVEDAEDRE DTVSEEKPES HNHGQNLFQS ANSSDTPALK SGAVFSSSQG
WVNPFKVVVS SKEPAVSANS TRSANILDSM NKSSRKSTSL NRMENNEKSP VIKPLTPKPR
SKQASAASYF QKRTPQADKT EEVKENPKSS SSDAPAVCLQ NSENQRPKTG FQMWLEENRS
QILSDNPDIS DETDIIKEGM IRFRVLSAEE RKAWTNKAKG ETASDGAEAK KRKRVVSEIC
ETENQEETVK ENLDLSKKQK ALNLPANQKL SAFAFKQ
