ID ZEP2_HUMAN Reviewed; 2446 AA. AC P31629; Q02646; Q5THT5; Q9NS05; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 05-MAY-2009, entry version 79. DE RecName: Full=Transcription factor HIVEP2; DE AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 2; DE Short=HIV-EP2; DE Short=MHC-binding protein 2; DE Short=MBP-2; GN Name=HIVEP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-1538. RX MEDLINE=91217105; PubMed=2022670; RA Nomura N., Zhao M.-J., Nagase T., Maekawa T., Ishizaki R., Tabata S., RA Ishii S.; RT "HIV-EP2, a new member of the gene family encoding the human RT immunodeficiency virus type 1 enhancer-binding protein. Comparison RT with HIV-EP1/PRDII-BF1/MBP-1."; RL J. Biol. Chem. 266:8590-8594(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-1538. RX MEDLINE=93028387; PubMed=1409593; DOI=10.1073/pnas.89.19.8971; RA Van't Veer L.J., Lutz P., Isselbacher K.J., Bernards R.; RT "Structure and expression of MBP-2: a 275 kDa zinc finger protein that RT binds to an enhancer of major histocompatibility complex class 1 RT genes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8971-8975(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-1538. RA Kukita Y., Komiya T., Tahira T., Asakawa S., Shimizu N., Suzuki Y., RA Sugano S., Hayashi K.; RT "Characterization of the human MBP-2/HIV-EP2 gene: identification of RT multiple promoters and alternative splicing of 5' untranslated RT region."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1797-1936. RX MEDLINE=91062349; PubMed=2247438; DOI=10.1073/pnas.87.22.8707; RA Rustgi A.K., Van't Veer L.J., Bernards R.; RT "Two genes encode factors with NF-kappa B- and H2TF1-like DNA-binding RT properties."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8707-8710(1990). RN [6] RP TISSUE SPECIFICITY. RC TISSUE=Brain; RX MEDLINE=99223602; PubMed=10207097; RA Doerflinger U., Pscherer A., Moser M., Ruemmele P., Schuele R., RA Buettner R.; RT "Specific activation of SSTR-2 promoter by SEF-2 and MIBP-1."; RL Mol. Cell. Biol. 19:3736-3747(1999). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2071 AND SER-2077, AND RP MASS SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [8] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-2092, AND MASS RP SPECTROMETRY. RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). CC -!- FUNCTION: This protein specifically binds to the DNA sequence 5'- CC GGGACTTTCC-3' which is found in the enhancer elements of numerous CC viral promoters such as those of SV40, CMV, or HIV1. In addition, CC related sequences are found in the enhancer elements of a number CC of cellular promoters, including those of the class I MHC, CC interleukin-2 receptor, somatostatin receptor II, and interferon- CC beta genes. It may act in T-cell activation. CC -!- SUBUNIT: Interacts with TCF4 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in brain and skeletal muscle. CC -!- INDUCTION: By mitogens and phorbol ester. CC -!- SIMILARITY: Contains 4 C2H2-type zinc fingers. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M60119; AAB88218.1; ALT_INIT; Genomic_DNA. DR EMBL; X65644; CAA46596.1; ALT_INIT; mRNA. DR EMBL; AF153836; AAF81365.1; -; Genomic_DNA. DR EMBL; AL023584; CAA19042.1; -; Genomic_DNA. DR EMBL; M61744; AAA36202.1; -; mRNA. DR IPI; IPI00144243; -. DR PIR; S26661; WMHUE2. DR RefSeq; NP_006725.3; -. DR UniGene; Hs.510172; -. DR HSSP; P15822; 1BBO. DR SMR; P31629; 1798-1854. DR PhosphoSite; P31629; -. DR PRIDE; P31629; -. DR Ensembl; ENSG00000010818; Homo sapiens. DR GeneID; 3097; -. DR KEGG; hsa:3097; -. DR GeneCards; GC06M143114; -. DR H-InvDB; HIX0032889; -. DR HGNC; HGNC:4921; HIVEP2. DR MIM; 143054; gene. DR PharmGKB; PA29298; -. DR HOGENOM; P31629; -. DR HOVERGEN; P31629; -. DR NextBio; 12289; -. DR ArrayExpress; P31629; -. DR Bgee; P31629; -. DR CleanEx; HS_HIVEP2; -. DR GermOnline; ENSG00000010818; Homo sapiens. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2. DR Pfam; PF00096; zf-C2H2; 4. DR SMART; SM00355; ZnF_C2H2; 4. 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; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Polymorphism; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1 2446 Transcription factor HIVEP2. FT /FTId=PRO_0000047371. FT REPEAT 2053 2056 1. FT REPEAT 2059 2062 2. FT REPEAT 2071 2074 3. FT REPEAT 2083 2086 4. FT REPEAT 2089 2092 5. FT REPEAT 2106 2109 6. FT REPEAT 2112 2115 7. FT REPEAT 2118 2121 8. FT REPEAT 2130 2133 9. FT REPEAT 2145 2148 10. FT ZN_FING 189 211 C2H2-type 1. FT ZN_FING 217 239 C2H2-type 2. FT ZN_FING 1799 1821 C2H2-type 3. FT ZN_FING 1827 1851 C2H2-type 4. FT REGION 2053 2148 10 X 4 AA tandem repeats of S-P-[RGMKC]- FT [RK]. FT MOTIF 937 943 Nuclear localization signal (Potential). FT COMPBIAS 950 982 Ser-rich. FT COMPBIAS 1510 1586 Ser-rich. FT COMPBIAS 1899 1923 Asp/Glu-rich (acidic). FT COMPBIAS 2073 2148 Arg-rich. FT MOD_RES 2071 2071 Phosphoserine. FT MOD_RES 2077 2077 Phosphoserine. FT CROSSLNK 2092 2092 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VARIANT 46 46 R -> Q (in dbSNP:rs17072013). FT /FTId=VAR_052754. FT VARIANT 1041 1041 A -> V (in dbSNP:rs34875559). FT /FTId=VAR_052755. FT VARIANT 1293 1293 L -> I (in dbSNP:rs35675714). FT /FTId=VAR_052756. FT VARIANT 1538 1538 L -> P (in dbSNP:rs109836). FT /FTId=VAR_052757. FT CONFLICT 2091 2091 R -> T (in Ref. 2; CAA46596). SQ SEQUENCE 2446 AA; 269053 MW; 482E2C577EF9449A CRC64; MDTGDTALGQ KATSRSGETD KASGRWRQEQ SAVIKMSTFG SHEGQRQPQI EPEQIGNTAS AQLFGSGKLA SPSEVVQQVA EKQYPPHRPS PYSCQHSLSF PQHSLPQGVM HSTKPHQSLE GPPWLFPGPL PSVASEDLFP FPIHGHSGGY PRKKISSLNP AYSQYSQKSI EQAEEAHKKE HKPKKPGKYI CPYCSRACAK PSVLKKHIRS HTGERPYPCI PCGFSFKTKS NLYKHRKSHA HAIKAGLVPF TESAVSKLDL EAGFIDVEAE IHSDGEQSTD TDEESSLFAE ASDKMSPGPP IPLDIASRGG YHGSLEESLG GPMKVPILII PKSGIPLPNE SSQYIGPDML PNPSLNTKAD DSHTVKQKLA LRLSEKKGQD SEPSLNLLSP HSKGSTDSGY FSRSESAEQQ ISPPNTNAKS YEEIIFGKYC RLSPRNALSV TTTSQERAAM GRKGIMEPLP HVNTRLDVKM FEDPVSQLIP SKGDVDPSQT SMLKSTKFNS ESRQPQIIPS SIRNEGKLYP ANFQGSNPVL LEAPVDSSPL IRSNSVPTSS ATNLTIPPSL RGSHSFDERM TGSDDVFYPG TVGIPPQRML RRQAAFELPS VQEGHVEVEH HGRMLKGISS SSLKEKKLSP GDRVGYDYDV CRKPYKKWED SETPKQNYRD ISCLSSLKHG GEYFMDPVVP LQGVPSMFGT TCENRKRRKE KSVGDEEDTP MICSSIVSTP VGIMASDYDP KLQMQEGVRS GFAMAGHENL SHGHTERFDP CRPQLQPGSP SLVSEESPSA IDSDKMSDLG GRKPPGNVIS VIQHTNSLSR PNSFERSESA ELVACTQDKA PSPSETCDSE ISEAPVSPEW APPGDGAESG GKPSPSQQVQ QQSYHTQPRL VRQHNIQVPE IRVTEEPDKP EKEKEAQSKE PEKPVEEFQW PQRSETLSQL PAEKLPPKKK RLRLADMEHS SGESSFESTG TGLSRSPSQE SNLSHSSSFS MSFEREETSK LSALPKQDEF GKHSEFLTVP AGSYSLSVPG HHHQKEMRRC SSEQMPCPHP AEVPEVRSKS FDYGNLSHAP VSGAAASTVS PSRERKKCFL VRQASFSGSP EISQGEVGMD QSVKQEQLEH LHAGLRSGWH HGPPAVLPPL QQEDPGKQVA GPCPPLSSGP LHLAQPQIMH MDSQESLRNP LIQPTSYMTS KHLPEQPHLF PHQETIPFSP IQNALFQFQY PTVCMVHLPA QQPPWWQAHF PHPFAQHPQK SYGKPSFQTE IHSSYPLEHV AEHTGKKPAE YAHTKEQTYP CYSGASGLHP KNLLPKFPSD QSSKSTETPS EQVLQEDFAS ANAGSLQSLP GTVVPVRIQT HVPSYGSVMY TSISQILGQN SPAIVICKVD ENMTQRTLVT NAAMQGIGFN IAQVLGQHAG LEKYPIWKAP QTLPLGLESS IPLCLPSTSD SVATLGGSKR MLSPASSLEL FMETKQQKRV KEEKMYGQIV EELSAVELTN SDIKKDLSRP QKPQLVRQGC ASEPKDGLQS GSSSFSSLSP SSSQDYPSVS PSSREPFLPS KEMLSGSRAP LPGQKSSGPS ESKESSDELD IDETASDMSM SPQSSSLPAG DGQLEEEGKG HKRPVGMLVR MASAPSGNVA DSTLLLTDMA DFQQILQFPS LRTTTTVSWC FLNYTKPNYV QQATFKSSVY ASWCISSCNP NPSGLNTKTT LALLRSKQKI TAEIYTLAAM HRPGTGKLTS SSAWKQFTQM KPDASFLFGS KLERKLVGNI LKERGKGDIH GDKDIGSKQT EPIRIKIFEG GYKSNEDYVY VRGRGRGKYI CEECGIRCKK PSMLKKHIRT HTDVRPYVCK LCNFAFKTKG NLTKHMKSKA HMKKCLELGV SMTSVDDTET EEAENLEDLH KAAEKHSMSS ISTDHQFSDA EESDGEDGDD NDDDDEDEDD FDDQGDLTPK TRSRSTSPQP PRFSSLPVNV GAVPHGVPSD SSLGHSSLIS YLVTLPSIRV TQLMTPSDSC EDTQMTEYQR LFQSKSTDSE PDKDRLDIPS CMDEECMLPS EPSSSPRDFS PSSHHSSPGY DSSPCRDNSP KRYLIPKGDL SPRRHLSPRR DLSPMRHLSP RKEAALRREM SQRDVSPRRH LSPRRPVSPG KDITARRDLS PRRERRYMTT IRAPSPRRAL YHNPPLSMGQ YLQAEPIVLG PPNLRRGLPQ VPYFSLYGDQ EGAYEHPGSS LFPEGPNDYV FSHLPLHSQQ QVRAPIPMVP VGGIQMVHSM PPALSSLHPS PTLPLPMEGF EEKKGASGES FSKDPYVLSK QHEKRGPHAL QSSGPPSTPS SPRLLMKQST SEDSLNATER EQEENIQTCT KAIASLRIAT EEAALLGPDQ PARVQEPHQN PLGSAHVSIR HFSRPEPGQP CTSATHPDLH DGEKDNFGTS QTPLAHSTFY SKSCVDDKQL DFHSSKELSS STEESKDPSS EKSQLH //