ZEP2_RAT
ID ZEP2_RAT Reviewed; 2437 AA.
AC Q00900; Q63725;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 23-FEB-2022, entry version 142.
DE RecName: Full=Human immunodeficiency virus type I enhancer-binding protein 2 homolog;
DE AltName: Full=Angiotensinogen gene-inducible enhancer-binding protein 1;
DE AltName: Full=DNA-binding protein AGIE-BP1;
DE AltName: Full=Myc intron-binding protein 1;
DE Short=MIBP-1;
GN Name=Hivep2; Synonyms=Agie-bp1, Mibp1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7838722; DOI=10.1093/nar/22.25.5679;
RA Makino R., Akiyama K., Yasuda J., Mashiyama S., Honda S., Sekiya T.,
RA Hayashi K.;
RT "Cloning and characterization of a c-myc intron binding protein (MIBP1).";
RL Nucleic Acids Res. 22:5679-5685(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1522-2437.
RC TISSUE=Liver;
RX PubMed=2017183; DOI=10.1128/mcb.11.5.2887-2895.1991;
RA Ron D., Brasier A.R., Habener J.F.;
RT "Angiotensinogen gene-inducible enhancer-binding protein 1, a member of a
RT new family of large nuclear proteins that recognize nuclear factor kappa B-
RT binding sites through a zinc finger motif.";
RL Mol. Cell. Biol. 11:2887-2895(1991).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816 AND SER-1438, 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 -!- FUNCTION: Binds to DNA at the acute-phase response element of the
CC angiotensinogen gene and related nuclear factor kappa-B binding sites
CC through a zinc-finger motif.
CC -!- SUBUNIT: Interacts with TCF4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in brain, spleen, kidney, muscle and to a
CC lower extent in liver. {ECO:0000269|PubMed:7838722}.
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DR EMBL; D37951; BAA07168.1; -; mRNA.
DR EMBL; M65251; AAA40698.1; -; mRNA.
DR PIR; S53611; S53611.
DR RefSeq; NP_077051.1; NM_024137.1.
DR IntAct; Q00900; 2.
DR MINT; Q00900; -.
DR STRING; 10116.ENSRNOP00000015131; -.
DR iPTMnet; Q00900; -.
DR PhosphoSitePlus; Q00900; -.
DR PaxDb; Q00900; -.
DR PRIDE; Q00900; -.
DR GeneID; 29721; -.
DR KEGG; rno:29721; -.
DR UCSC; RGD:61988; rat.
DR CTD; 3097; -.
DR RGD; 61988; Hivep2.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q00900; -.
DR OrthoDB; 212048at2759; -.
DR PhylomeDB; Q00900; -.
DR PRO; PR:Q00900; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2437
FT /note="Human immunodeficiency virus type I enhancer-binding
FT protein 2 homolog"
FT /id="PRO_0000047373"
FT REPEAT 2044..2047
FT /note="1"
FT REPEAT 2050..2053
FT /note="2"
FT REPEAT 2062..2065
FT /note="3"
FT REPEAT 2074..2077
FT /note="4"
FT REPEAT 2080..2083
FT /note="5"
FT REPEAT 2097..2100
FT /note="6"
FT REPEAT 2103..2106
FT /note="7"
FT REPEAT 2109..2112
FT /note="8"
FT REPEAT 2121..2124
FT /note="9"
FT REPEAT 2136..2139
FT /note="10"
FT ZN_FING 189..211
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 217..239
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1790..1812
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1818..1842
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1993..2125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2044..2139
FT /note="10 X 4 AA tandem repeats of S-P-[RGMKC]-[RK]"
FT REGION 2233..2316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2364..2437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 934..940
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 6..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1915
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1997..2012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2017..2045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2058..2102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2111..2125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2281..2304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 2109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31629"
FT MOD_RES 2288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31629"
FT MOD_RES 2292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31629"
FT MOD_RES 2420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 2422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT CONFLICT 1522
FT /note="H -> I (in Ref. 2; AAA40698)"
FT /evidence="ECO:0000305"
FT CONFLICT 2264
FT /note="Q -> K (in Ref. 2; AAA40698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2437 AA; 267426 MW; BD5C21358D3A1F5B CRC64;
MDTGDTALGQ KATSRSGETD SVSGRWRQEQ SAGLKMSTFS SQEGQRQPQI DPDQIGNVAS
AQLFGSGKLA SPGEGVHQVT EKQYPPHRPS PYPCQHSLSF PQHSLPQGMM HSNKPHQSLE
GPPWLFSGPL PSVASEDLFP FPMHGHSSGY PRKKISSLNP AYSQYSQKSI EQAEDAHKKE
HKPKKPGKYI CPYCSRACAK PSVLKKHIRS HTGERPYPCI PCGFSFKTKS NLYKHRKSHA
HAIKAGLVPF TESSVSKLDL EAGFIDVEAE IHSDGEQSTD TDEESSLFAE ASDKVSPGPP
IPLDIASRGG YPGSLEESLG GPMKVPILII PKSGIPLPNE GSQYLGPDML PNPSLNAKAD
DSHTVKQKLA LRLSEKKGQD SEPSLNLLSP HSKGSTDSGY FSRSESAEQQ ISPPNTNAKS
YEEIIFGKYC RLSPRNTLSV TPTGQERTAM GRRGLVEPLP HVNTRLEVKM FEDPITQLIP
SKGEMDPSQV NMLKTTKFNS ECRQPQAMAA SVRNEGKPYP GSFPGSNPIL LEAPVDSSPL
IRSNSMPTSS ATNLSIPPSL RGSHSFDERM TGSDDVFYPG TVGIPPQRML RRQAAFELPS
VQEGHMEFEH PARVPKILAG SSLKEKKLVP GDRSGYDYDA CRKPYKKWED PETPKQSYRD
ISCLSTFKHG GEYFMDPSVP LPGVPTMFGT TCENRKRRKE KSVGDEEDTP MICGGMGSAP
GSMMSSEYDS KLQDGGRSGF TMTGHESLPH GYSDRLDLAR PQLPSRSPSL GSEDLPSAGD
PDKMTDLGKK PPGNVISVIQ HTNSLSRPNS FERSESTEMA VSTQDKTPSP SEMGDSEVLE
GPVSPEWAPP GDGAESGSRP TPSQQVPQHS YHGQPRLVRQ HNIQVPEIRV TEEPDKPEKE
KEAPTKEPEK PVEEFQWPQR SETLSQLPAE KLPPKKKRLR LADMEHSSGE SSFESTGTGL
SRSPSQESNL SHSSSFSMSF DRDETVKLTA PPKQDESGKH SEFLTVPAGS YSLSVPGHHH
QKEMRRCSSE QMPCPHPTEV PEIRSKSFDY GNLSHAPVAG ASPSTLSPSR ERKKCFLVRQ
ASFSGSPEIA QGEAGMDPSV KQEQLEQLHA GLRAAWTTVL PPLPGDDPGK QVVGPCGQLS
SGPPLHLAQQ QIMHMDSQES LRNPLIQPTS YMTGKHLPEQ PHLFPHQDAV PFSPIQNALF
QFQYPTVCMV HLPAQQPPWW QAHFPHPFTP HPQNSYSKPP FQADIHSSYS LEHVAEHTGK
KSADYPHAKE QTYPCYSGAS GLHSKNLPPK FPSDPGSKST EAPPTEQLLR EDFASENAGP
LQSLPGTVVP VRIQTHVPSY GSVMYTSISQ ILGQNSPAIV ICKVDENMTQ RTLVTNAAMQ
GIGFNIAQVL GQRTGLEKYP LWKVPQTLPL GLESSIPLCL PSTSDSAASL GGSKRMLSPA
SSLELFMETK QQKRVKEEKM YGQIVEELSA VELTNSDIKK GLSRPQKPQL VRQGCASEPK
DGSSQSRSSS FSSLSPSSSQ DHPAASGPFP PNREILSGSR APPRRKFSGP SESRESSDEL
DIDETSSDMS MSPQSSSLPT GGSQQEDEGK ARKLPVSMLV HMASGPGGNV ANSTLLFTDV
ADFQQILQFP SLRTTTTVSW CFLNYTKPNF VQQATFKSSV YASWCISSCN PNPSGLNTKT
TLALLRSKQK ITAEIYTLAA MHRPGTGKLT SSSAWKQFAQ MKPDAPFLFG NKLERKLGGN
VLKERGKGEI HGDKDLGSKQ TEPIRIKIFE GGYKSNEDYV YVRGRGRGKY ICEECGIRCK
KPSMLKKHIR THTDVRPYVC KLCNFAFKTK GNLTKHMKSK AHMKKCLELG VSMTSVDETE
TEEAENMEDL HKTSEKHSMS GISTDHQFSD AEESDGEDGD DNDEDDEDDD DFDDQGDLTP
KTRSRSTSPQ PPRFSSLPVN VGAVAHGVPS DSSLGHSSLI SYLVTLPSIQ VTQLMTPSDS
CEDTQMTEYQ RLFQSKSTDS EPDKDRLDIP SSMDEEAMLS SEPSSSPRDF SPSSYRSSPG
YDSSPCRDNS PKRYLIPKGD LSPRRHLSPR RDLSPMRHLS PRKEAALRRE MSQGDASPRR
HLSPRRPLSP GKDITTRRDL SPRRERRYMT TIRAPSPRRA LYHNPPLPMG QYLQTEPIVL
GPPNLRRGLP QVPYFSLYGD QEGAYEHHGS SLFPEGPTDY VFSHLPLHSQ QQVRAPIPMV
PVGGIQMVHS LPPAISGLHP PPTLPLPTEG SEEKKGAPGE ALTQDPYTLS RRHEKQAPHV
LQSSGLPSSP SSPRLLMKQS TSEDSLNSTE REQEENIQTC TKAIASLRIA TEEAALLGAD
QPTWVQESPQ KPLESAHISI RHFSGPEPGQ LCTSAAHPDL HDGEKDTFGT SQTAVAHPTF
YSKGSVDEKQ VDFQSSKELS LSTEEGNEPS SEKNRLH
