ID ZEP3_HUMAN Reviewed; 2406 AA. AC Q5T1R4; A7YY91; Q5T1R5; Q9BZS0; Q9HCL7; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 30-NOV-2010, entry version 66. DE RecName: Full=Transcription factor HIVEP3; DE AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3; DE AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein; DE AltName: Full=Kappa-binding protein 1; DE Short=KBP-1; DE AltName: Full=Zinc finger protein ZAS3; GN Name=HIVEP3; Synonyms=KBP1, KIAA1555, KRC, ZAS3; 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 [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE RP SPLICING, DOMAIN, AND VARIANTS ARG-575; PRO-2023; ALA-2109; ARG-2272 RP AND ALA-2339. RC TISSUE=Brain; RX MEDLINE=21100880; PubMed=11161801; DOI=10.1006/geno.2000.6425; RA Hicar M.D., Liu Y., Allen C.E., Wu L.-C.; RT "Structure of the human zinc finger protein HIVEP3: molecular cloning, RT expression, exon-intron structure, and comparison with paralogous RT genes HIVEP1 and HIVEP2."; RL Genomics 71:89-100(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS RP ARG-575; PRO-2023; ALA-2109 AND ALA-2339. RC TISSUE=Brain; RX MEDLINE=20450683; PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. RT XVIII. The complete sequences of 100 new cDNA clones from brain which RT code for large proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [3] RP SEQUENCE REVISION. RX MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS RP ARG-575; PRO-2023; ALA-2109 AND ALA-2339. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2037, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [7] RP VARIANT [LARGE SCALE ANALYSIS] MET-484. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role of transcription factor; binds to CC recognition signal sequences (Rss heptamer) for somatic CC recombination of immunoglobulin and T-cell receptor gene segments; CC Binds also to the kappa-B motif of gene such as S100A4, involved CC in cell progression and differentiation. Kappa-B motif is a gene CC regulatory element found in promoters and enhancers of genes CC involved in immunity, inflammation, and growth and that responds CC to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 CC in cell growth is strengthened by the fact that its down- CC regulation promotes cell cycle progression with ultimate formation CC of multinucleated giant cells. Strongly inhibits TNF-alpha-induced CC NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B CC by several mechanisms: as transcription factor, by competing for CC Kappa-B motif and by repressing transcription in the nucleus; CC Trough non transcriptional process, by inhibiting nuclear CC translocation of RELA by association with TRAF2, an adapter CC molecule in the tumor necrosis factor signaling, which blocks the CC formation of IKK complex. Interaction with TRAF proteins inhibits CC both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated CC responses that include apoptosis and proinflammatory cytokine gene CC expression. Positively regulates the expression of IL2 in T-cell. CC Essential regulator of adult bone formation. CC -!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms CC a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms can be generated by alternative CC splicing or polyadenylation. HIVEP3L transcript may lack exon 7 CC leading to a premature codon stop; CC Name=1; Synonyms=HIVEP3S; CC IsoId=Q5T1R4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5T1R4-2; Sequence=VSP_033279; CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13 acetate (TPA). CC -!- DOMAIN: The ZAS2 domain binds DNA as dimers, tetramers, and CC multiple of tetramers and readily forms highly ordred DNA-protein CC structures (By similarity). CC -!- PTM: Phosphorylated on threonine and serine residues (By CC similarity). CC -!- SIMILARITY: Contains 5 C2H2-type zinc fingers. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13381.2; Type=Erroneous initiation; 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; AF278765; AAK01082.1; -; mRNA. DR EMBL; AB046775; BAB13381.2; ALT_INIT; mRNA. DR EMBL; AL445933; CAI14537.1; -; Genomic_DNA. DR EMBL; AL445933; CAI14538.1; -; Genomic_DNA. DR EMBL; BC152563; AAI52564.1; -; mRNA. DR IPI; IPI00328089; -. DR IPI; IPI00641105; -. DR RefSeq; NP_001121186.1; NM_001127714.1. DR RefSeq; NP_078779.2; NM_024503.3. DR UniGene; Hs.648369; -. DR HSSP; P15822; 1BBO. DR ProteinModelPortal; Q5T1R4; -. DR SMR; Q5T1R4; 191-247, 1753-1809. DR STRING; Q5T1R4; -. DR PRIDE; Q5T1R4; -. DR Ensembl; ENST00000247584; ENSP00000247584; ENSG00000127124. DR Ensembl; ENST00000372583; ENSP00000361664; ENSG00000127124. DR GeneID; 59269; -. DR KEGG; hsa:59269; -. DR NMPDR; fig|9606.3.peg.957; -. DR UCSC; uc001cgz.2; human. DR UCSC; uc001cha.2; human. DR CTD; 59269; -. DR GeneCards; GC01M042003; -. DR HGNC; HGNC:13561; HIVEP3. DR HPA; HPA005728; -. DR MIM; 606649; gene. DR PharmGKB; PA29299; -. DR HOGENOM; HBG283020; -. DR HOVERGEN; HBG095595; -. DR InParanoid; Q5T1R4; -. DR OMA; MERIPGE; -. DR PhylomeDB; Q5T1R4; -. DR NextBio; 65146; -. DR ArrayExpress; Q5T1R4; -. DR Bgee; Q5T1R4; -. DR CleanEx; HS_HIVEP3; -. DR Genevestigator; Q5T1R4; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016563; F:transcription activator activity; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. 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; 4. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; KW Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 2406 Transcription factor HIVEP3. FT /FTId=PRO_0000331627. FT REPEAT 1964 1967 1. FT REPEAT 1970 1973 2. FT REPEAT 1993 1996 3. FT REPEAT 1998 2001 4. FT REPEAT 2067 2070 5. FT REPEAT 2079 2082 6. FT ZN_FING 192 214 C2H2-type 1. FT ZN_FING 220 242 C2H2-type 2. FT ZN_FING 643 665 C2H2-type 3; degenerate. FT ZN_FING 1754 1776 C2H2-type 4. FT ZN_FING 1782 1806 C2H2-type 5. FT REGION 192 242 ZAS1. FT REGION 211 1074 No DNA binding activity or FT transactivation activity, but complete FT prevention of TRAF-dependent NF-Kappa-B FT activation; associates with TRAF2 and JUN FT (By similarity). FT REGION 264 287 Acidic 1. FT REGION 862 883 Acidic 2. FT REGION 1754 1806 ZAS2. FT REGION 1817 1872 Acidic 3. FT REGION 2053 2148 6 X 4 AA tandem repeats of S-P-X-[RK]. FT COILED 1442 1466 Potential. FT MOTIF 903 909 Nuclear localization signal (Potential). FT COMPBIAS 308 334 Ser-rich. FT COMPBIAS 378 414 Ser-rich. FT COMPBIAS 797 819 Ser-rich. FT COMPBIAS 844 880 Glu/Pro-rich. FT COMPBIAS 916 948 Ser-rich. FT COMPBIAS 1907 1936 Ser-rich. FT MOD_RES 2037 2037 Phosphothreonine. FT VAR_SEQ 2136 2136 Missing (in isoform 2). FT /FTId=VSP_033279. FT VARIANT 35 35 V -> I (in dbSNP:rs2146315). FT /FTId=VAR_042910. FT VARIANT 484 484 V -> M (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_042911. FT VARIANT 575 575 H -> R (in dbSNP:rs2810566). FT /FTId=VAR_042912. FT VARIANT 1087 1087 Q -> H (in dbSNP:rs17363472). FT /FTId=VAR_042913. FT VARIANT 2023 2023 A -> P (in dbSNP:rs2483689). FT /FTId=VAR_042914. FT VARIANT 2109 2109 D -> A (in dbSNP:rs2991344). FT /FTId=VAR_042915. FT VARIANT 2272 2272 G -> R (in dbSNP:rs11809423). FT /FTId=VAR_042916. FT VARIANT 2339 2339 T -> A (in dbSNP:rs9439043). FT /FTId=VAR_042917. FT CONFLICT 44 44 A -> P (in Ref. 1; AAK01082). FT CONFLICT 94 95 QL -> HV (in Ref. 1; AAK01082). FT CONFLICT 123 123 D -> S (in Ref. 1; AAK01082). FT CONFLICT 127 127 P -> L (in Ref. 1; AAK01082). FT CONFLICT 133 134 FV -> LL (in Ref. 1; AAK01082). FT CONFLICT 589 589 R -> P (in Ref. 1; AAK01082). FT CONFLICT 901 901 L -> A (in Ref. 1; AAK01082). FT CONFLICT 961 961 S -> D (in Ref. 1; AAK01082). FT CONFLICT 1034 1035 RV -> GE (in Ref. 1; AAK01082). FT CONFLICT 1048 1049 QA -> SP (in Ref. 1; AAK01082). FT CONFLICT 1110 1110 P -> A (in Ref. 1; AAK01082). FT CONFLICT 1180 1180 P -> L (in Ref. 2; BAB13381 and 5; FT AAI52564). FT CONFLICT 1279 1279 T -> Q (in Ref. 1; AAK01082). FT CONFLICT 1524 1524 T -> Q (in Ref. 1; AAK01082). FT CONFLICT 2376 2376 P -> S (in Ref. 1; AAK01082). SQ SEQUENCE 2406 AA; 259465 MW; AFCCFDAF87014A7D CRC64; MDPEQSVKGT KKAEGSPRKR LTKGEAIQTS VSSSVPYPGS GTAATQESPA QELLAPQPFP GPSSVLREGS QEKTGQQQKP PKRPPIEASV HISQLPQHPL TPAFMSPGKP EHLLEGSTWQ LVDPMRPGPS GSFVAPGLHP QSQLLPSHAS IIPPEDLPGV PKVFVPRPSQ VSLKPTEEAH KKERKPQKPG KYICQYCSRP CAKPSVLQKH IRSHTGERPY PCGPCGFSFK TKSNLYKHRK SHAHRIKAGL ASGMGGEMYP HGLEMERIPG EEFEEPTEGE STDSEEETSA TSGHPAELSP RPKQPLLSSG LYSSGSHSSS HERCSLSQSS TAQSLEDPPP FVEPSSEHPL SHKPEDTHTI KQKLALRLSE RKKVIDEQAF LSPGSKGSTE SGYFSRSESA EQQVSPPNTN AKSYAEIIFG KCGRIGQRTA MLTATSTQPL LPLSTEDKPS LVPLSVPRTQ VIEHITKLIT INEAVVDTSE IDSVKPRRSS LSRRSSMESP KSSLYREPLS SHSEKTKPEQ SLLSLQHPPS TAPPVPLLRS HSMPSAACTI STPHHPFRGS YSFDDHITDS EALSHSSHVF TSHPRMLKRQ PAIELPLGGE YSSEEPGPSS KDTASKPSDE VEPKESELTK KTKKGLKTKG VIYECNICGA RYKKRDNYEA HKKYYCSELQ IAKPISAGTH TSPEAEKSQI EHEPWSQMMH YKLGTTLELT PLRKRRKEKS LGDEEEPPAF ESTKSQFGSP GPSDAARNLP LESTKSPAEP SKSVPSLEGP TGFQPRTPKP GSGSESGKER RTTSKEISVI QHTSSFEKSD SLEQPSGLEG EDKPLAQFPS PPPAPHGRSA HSLQPKLVRQ PNIQVPEILV TEEPDRPDTE PEPPPKEPEK TEEFQWPQRS QTLAQLPAEK LPPKKKRLRL AEMAQSSGES SFESSVPLSR SPSQESNVSL SGSSRSASFE RDDHGKAEAP SPSSDMRPKP LGTHMLTVPS HHPHAREMRR SASEQSPNVS HSAHMTETRS KSFDYGSLSL TGPSAPAPVA PPARVAPPER RKCFLVRQAS LSRPPESELE VAPKGRQESE EPQPSSSKPS AKSSLSQISS AATSHGGPPG GKGPGQDRPP LGPTVPYTEA LQVFHHPVAQ TPLHEKPYLP PPVSLFSFQH LVQHEPGQSP EFFSTQAMSS LLSSPYSMPP LPPSLFQAPP LPLQPTVLHP GQLHLPQLMP HPANIPFRQP PSFLPMPYPT SSALSSGFFL PLQSQFALQL PGDVESHLPQ IKTSLAPLAT GSAGLSPSTE YSSDIRLPPV APPASSSAPT SAPPLALPAC PDTMVSLVVP VRVQTNMPSY GSAMYTTLSQ ILVTQSQGSS ATVALPKFEE PPSKGTTVCG ADVHEVGPGP SGLSEEQSRA FPTPYLRVPV TLPERKGTSL SSESILSLEG SSSTAGGSKR VLSPAGSLEL TMETQQQKRV KEEEASKADE KLELVKPCSV VLTSTEDGKR PEKSHLGNQG QGRRELEMLS SLSSDPSDTK EIPPLPHPAL SHGTAPGSEA LKEYPQPSGK PHRRGLTPLS VKKEDSKEQP DLPSLAPPSS LPLSETSSRP AKSQEGTDSK KVLQFPSLHT TTNVSWCYLN YIKPNHIQHA DRRSSVYAGW CISLYNPNLP GVSTKAALSL LRSKQKVSKE TYTMATAPHP EAGRLVPSSS RKPRMTEVHL PSLVSPEGQK DLARVEKEEE RRGEPEEDAP ASQRGEPARI KIFEGGYKSN EEYVYVRGRG RGKYVCEECG IRCKKPSMLK KHIRTHTDVR PYVCKHCHFA FKTKGNLTKH MKSKAHSKKC QETGVLEELE AEEGTSDDLF QDSEGREGSE AVEEHQFSDL EDSDSDSDLD EDEDEDEEES QDELSRPSSE APPPGPPHAL RADSSPILGP QPPDAPASGT EATRGSSVSE AERLTASSCS MSSQSMPGLP WLGPAPLGSV EKDTGSALSY KPVSPRRPWS PSKEAGSRPP LARKHSLTKN DSSPQRCSPA REPQASAPSP PGLHVDPGRG MGALPCGSPR LQLSPLTLCP LGRELAPRAH VLSKLEGTTD PGLPRYSPTR RWSPGQAESP PRSAPPGKWA LAGPGSPSAG EHGPGLGLDP RVLFPPAPLP HKLLSRSPET CASPWQKAES RSPSCSPGPA HPLSSRPFSA LHDFHGHILA RTEENIFSHL PLHSQHLTRA PCPLIPIGGI QMVQARPGAH PTLLPGPTAA WVSGFSGGGS DLTGAREAQE RGRWSPTESS SASVSPVAKV SKFTLSSELE GGDYPKERER TGGGPGRPPD WTPHGTGAPA EPTPTHSPCT PPDTLPRPPQ GRRAAQSWSP RLESPRAPTN PEPSATPPLD RSSSVGCLAE ASARFPARTR NLSGEPRTRQ DSPKPSGSGE PRAHPHQPED RVPPNA //