ZN326_MOUSE
ID ZN326_MOUSE Reviewed; 580 AA.
AC O88291; Q05DP5; Q3TRI9; Q3UJI3; Q8BSJ5; Q8K1X9; Q9CYG9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DBIRD complex subunit ZNF326;
DE AltName: Full=Zinc finger protein 326;
DE AltName: Full=Zinc finger protein interacting with mRNPs;
DE AltName: Full=Zinc finger protein-associated with nuclear matrix of 75 kDa;
GN Name=Znf326; Synonyms=Zan75, Zfp326, Zird;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9809746; DOI=10.1089/dna.1998.17.849;
RA Lee J.-Y., Kambe M., Hayashi M., Takenaga K.;
RT "Cloning and characterization of a novel zinc finger protein that
RT associates with nuclear matrix.";
RL DNA Cell Biol. 17:849-858(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Thymus, and Wolffian duct;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-277 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, BIPARTITE NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=10798446; DOI=10.1089/104454900314492;
RA Lee J.-Y., Nakane Y., Koshikawa N., Nakayama K., Hayashi M., Takenaga K.;
RT "Characterization of a zinc finger protein ZAN75: nuclear localization
RT signal, transcriptional activator activity, and expression during neuronal
RT differentiation of P19 cells.";
RL DNA Cell Biol. 19:227-234(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-235, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Core component of the DBIRD complex, a multiprotein complex
CC that acts at the interface between core mRNP particles and RNA
CC polymerase II (RNAPII) and integrates transcript elongation with the
CC regulation of alternative splicing: the DBIRD complex affects local
CC transcript elongation rates and alternative splicing of a large set of
CC exons embedded in (A + T)-rich DNA regions (By similarity). May also
CC play a role in neuronal differentiation. Able to bind DNA and activate
CC expression in vitro. {ECO:0000250, ECO:0000269|PubMed:10798446}.
CC -!- SUBUNIT: Component of the DBIRD complex. Interacts with CCAR2; the
CC interaction is direct (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10798446,
CC ECO:0000269|PubMed:9809746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O88291-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88291-2; Sequence=VSP_014957;
CC Name=3;
CC IsoId=O88291-3; Sequence=VSP_014958, VSP_014959;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues. Highly
CC expressed in neuronal tissues such as brain and neural tube.
CC {ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed during 9.5 dpc and 10.5 dpc,
CC expressed at highest level in 11.5 dpc and gradually decreases
CC thereafter. During the cell cycle, it is weakly expressed in G0 and G1
CC phases. It increases during G1, S, G2 and M phases.
CC {ECO:0000269|PubMed:10798446, ECO:0000269|PubMed:9809746}.
CC -!- INDUCTION: Upon retinoic acid treatment. {ECO:0000269|PubMed:10798446}.
CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01140}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05567.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB012725; BAA31522.1; -; mRNA.
DR EMBL; AK017693; BAB30878.1; -; mRNA.
DR EMBL; AK032801; BAC28029.1; -; mRNA.
DR EMBL; AK146438; BAE27172.1; -; mRNA.
DR EMBL; AK162729; BAE37040.1; -; mRNA.
DR EMBL; BC037055; AAH37055.1; -; mRNA.
DR EMBL; BC005567; AAH05567.1; ALT_SEQ; mRNA.
DR CCDS; CCDS19496.1; -. [O88291-1]
DR RefSeq; NP_061229.2; NM_018759.2.
DR AlphaFoldDB; O88291; -.
DR SMR; O88291; -.
DR BioGRID; 207624; 12.
DR DIP; DIP-58947N; -.
DR IntAct; O88291; 3.
DR MINT; O88291; -.
DR STRING; 10090.ENSMUSP00000031227; -.
DR iPTMnet; O88291; -.
DR PhosphoSitePlus; O88291; -.
DR EPD; O88291; -.
DR jPOST; O88291; -.
DR MaxQB; O88291; -.
DR PaxDb; O88291; -.
DR PeptideAtlas; O88291; -.
DR PRIDE; O88291; -.
DR ProteomicsDB; 275073; -. [O88291-2]
DR ProteomicsDB; 275074; -. [O88291-3]
DR DNASU; 54367; -.
DR GeneID; 54367; -.
DR KEGG; mmu:54367; -.
DR UCSC; uc008ylj.3; mouse. [O88291-1]
DR CTD; 54367; -.
DR MGI; MGI:1927246; Zfp326.
DR eggNOG; ENOG502QUAZ; Eukaryota.
DR InParanoid; O88291; -.
DR OrthoDB; 902224at2759; -.
DR PhylomeDB; O88291; -.
DR TreeFam; TF105407; -.
DR BioGRID-ORCS; 54367; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp326; mouse.
DR PRO; PR:O88291; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88291; protein.
DR GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR007071; AKAP95.
DR InterPro; IPR034736; ZF_C2H2_AKAP95.
DR PANTHER; PTHR12190; PTHR12190; 1.
DR Pfam; PF04988; AKAP95; 1.
DR PROSITE; PS51799; ZF_C2H2_AKAP95; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..580
FT /note="DBIRD complex subunit ZNF326"
FT /id="PRO_0000075387"
FT ZN_FING 314..336
FT /note="C2H2 AKAP95-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT ZN_FING 407..430
FT /note="C2H2 AKAP95-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT REGION 1..124
FT /note="Mediates transcriptional activation"
FT REGION 156..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 238..260
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 273..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 173
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 235
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 247
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 264
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT VAR_SEQ 1..206
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014957"
FT VAR_SEQ 35..67
FT /note="DRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGG -> AFKDIYLKILLLSAS
FT KGEQHLIFFFLNSYRAGS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014958"
FT VAR_SEQ 68..580
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014959"
FT CONFLICT 55
FT /note="Q -> R (in Ref. 2; BAE27172)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="D -> G (in Ref. 2; BAB30878/BAE37040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 65225 MW; EF9672513D0FFC70 CRC64;
MDFEDDYVHS TCRGAYQDFN GMDRDYGPGS YGGLDRDYGH GSYGGQRSMD SYLNQSYGMD
NHSGGGGGSR FGPYESYDSR SSLGGRDLYR SGYGFNEPEQ TRFGGSYGGR FESSYRNSLD
SFGGRNQGGS SWEAPYSRSK LRPGFMEDRG RENYSSYSSF SSPHMKPAPV GSRGRGTPAY
PESTFGSRSY DAFGGPSTGR GRGRGHMGDF GSFHRPGIIV DYQNKPANVT IATARGIKRK
MMQIFIKPGG AFIKKPKLAK PMDKMNLSKS PTKTDPKNEE EEKRRIEARR EKQRRRREKN
SEKYGDGYRM AFTCSFCKFR TFEEKDIELH LESSSHQETL DHIQKQTKFD KVVMEFLHEC
MVNKFKKASI RKQQTLNHPE AYKIIEKDIM EGVTADDHMM KVETVHCSAC SVYIPALHSS
VQLHLKSPDH SKGKQAYKEQ IKRESVLTAT SILNNPIVKA RYERFVKGEN PFEIQDHPQD
QQIEGDEEDE EKIDEPIEEE EEEEEEEEEE GEEAGSVEEE GDVEGEEGTA EAAAAGEADA
VGEAEGAGEA EEAEEEEEEE GTQEFAAQAC ATEQCEHRQM
