ZN326_PONAB
ID ZN326_PONAB Reviewed; 579 AA.
AC Q5RCA4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=DBIRD complex subunit ZNF326;
DE AltName: Full=Zinc finger protein 326;
DE AltName: Full=Zinc finger protein interacting with mRNPs;
GN Name=ZNF326; Synonyms=ZIRD;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. May play a role in neuronal
CC differentiation and is able to bind DNA and activate expression in
CC vitro (By similarity). {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01140}.
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DR EMBL; CR858374; CAH90603.1; -; mRNA.
DR RefSeq; NP_001125327.1; NM_001131855.1.
DR AlphaFoldDB; Q5RCA4; -.
DR PRIDE; Q5RCA4; -.
DR GeneID; 100172226; -.
DR KEGG; pon:100172226; -.
DR CTD; 284695; -.
DR InParanoid; Q5RCA4; -.
DR OrthoDB; 902224at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Metal-binding;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..579
FT /note="DBIRD complex subunit ZNF326"
FT /id="PRO_0000075388"
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 /evidence="ECO:0000250"
FT REGION 154..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 238..260
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 273..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
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:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 247
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BKZ1"
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"
SQ SEQUENCE 579 AA; 65254 MW; 7273A11097E1C525 CRC64;
MDFEDDYTHS ACRNTYQGFN GMDRDYGPGS YGGMDRDYGH GSYGGQRSMD SYLNQSYGMD
NHSGGGGGSR FGPYESYDSR SSLGGRDLYR SGYGFNEPEQ SRFGGSYGGR FESSYRNSLD
SFGGRNQGGS SWEAPYSRSK LRPGFMEDRG RENYSSYSSF SSPHMKPAPV GSRGRGTPAY
PESTFGSRNY DAFGGPSTGR GRGRGHMGDF GSIHRPGIVV DYQNKSTNVT VAAARGIKRK
MMQPFNKPSG TFIKKPKLAK PMEKISLSKS PTKTDPKNEE EEKRRIEARR EKQRRRREKN
SEKYGDGYRM AFTCSFCKFR TFEEKDIELH LESSSHQETL DHIQKQTKFD KVVMEFLHEC
MVNKFKKTSI RKQQTNNQTE VVKIIEKDVM EGVTADDHMM KVETVHCSAC SVYIPALHSS
VQQHLKSPDH IKGKQAYKEQ IKRESVLTAT SILNNPIVKA RYERFVKGEN PFEIQDHSQD
QQIEGDEEDE EKIDEPIEEE EDEDEEEEAE EVGEVEEVEE VEEVREGGIE GEGNIEGVGE
GGEVGVVGEV EGVGKVEEVE EETAKEEPAD FPVEQPEEN
