ZBT44_RAT
ID ZBT44_RAT Reviewed; 453 AA.
AC Q3SWU4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Zinc finger and BTB domain-containing protein 44;
DE AltName: Full=BTB/POZ domain-containing protein 15;
GN Name=Zbtb44; Synonyms=Btbd15;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-191 AND SER-194, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC104680; AAI04681.1; -; mRNA.
DR RefSeq; NP_001030114.1; NM_001034942.1.
DR AlphaFoldDB; Q3SWU4; -.
DR SMR; Q3SWU4; -.
DR STRING; 10116.ENSRNOP00000007539; -.
DR iPTMnet; Q3SWU4; -.
DR PhosphoSitePlus; Q3SWU4; -.
DR PaxDb; Q3SWU4; -.
DR GeneID; 363035; -.
DR KEGG; rno:363035; -.
DR UCSC; RGD:1308984; rat.
DR CTD; 29068; -.
DR RGD; 1308984; Zbtb44.
DR VEuPathDB; HostDB:ENSRNOG00000005578; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_034849_1_0_1; -.
DR InParanoid; Q3SWU4; -.
DR OMA; AHSQEML; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q3SWU4; -.
DR TreeFam; TF332673; -.
DR PRO; PR:Q3SWU4; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000005578; Expressed in liver and 18 other tissues.
DR ExpressionAtlas; Q3SWU4; baseline and differential.
DR Genevisible; Q3SWU4; RN.
DR GO; GO:0005634; C:nucleus; 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 Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..453
FT /note="Zinc finger and BTB domain-containing protein 44"
FT /id="PRO_0000274610"
FT DOMAIN 31..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 399..421
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..449
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCP5"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCP5"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCP5"
SQ SEQUENCE 453 AA; 50277 MW; 909F8C5082B7E87D CRC64;
MGVKTFTHSS SSHSQEMLGK LNMLRNDGHF CDITIRVQDR IFRAHKVVLA ACSDFFRTKL
VGQTEDENKN VLDLHHVTVT GFIPLLEYAY TATLSINTEN IIDVLAAASY MQMFSVASTC
SEFMKSSILW NTPNSQPEKG LDAGQENSSN CNFTSRDGSI SPVSSECSAV ERTIPVCRES
RRKRKSYIVM SPESPVKCST QTNSPQVLNS SASYAENRNQ PVDSSLAFPW TFPFGIDRRI
QPEKAKQAEN TRTLELPGPS EAGRRMADYV TCESTKTTLP LGTEEDVRVK VERLSDEEVH
EEVSQPVSAS QSSLSDQQTV PGSEPVQEDL LISPQSSSIG SVDEGVTEGL PTLQSTSSTN
AHADEDDRLE NVQYPYQLYI APSTSSTERP SPNGPDRPFQ CPTCGVRFTR IQNLKQHMLI
HSGIKPFQCD CCGKKFTRAY SLKMHRLKHE VIS
