ID   ZBT7B_HUMAN             Reviewed;         539 AA.
AC   O15156; Q68DR2; Q96EP2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   05-OCT-2010, entry version 83.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 7B;
DE   AltName: Full=Krueppel-related zinc finger protein cKrox;
DE            Short=hcKrox;
DE   AltName: Full=T-helper-inducing POZ/Krueppel-like factor;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 15;
DE   AltName: Full=Zinc finger protein 67 homolog;
DE            Short=Zfp-67;
DE   AltName: Full=Zinc finger protein Th-POK;
GN   Name=ZBTB7B; Synonyms=ZBTB15, ZFP67;
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], AND FUNCTION.
RC   TISSUE=Skin fibroblast;
RX   MEDLINE=98036076; PubMed=9370309; DOI=10.1016/S0378-1119(97)00360-0;
RA   Widom R.L., Culic I., Lee J.Y., Korn J.H.;
RT   "Cloning and characterization of hcKrox, a transcriptional regulator
RT   of extracellular matrix gene expression.";
RL   Gene 198:407-420(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- FUNCTION: Transcription regulator that acts as a key regulator of
CC       lineage commitment of immature T-cell precursors. Necessary and
CC       sufficient for commitment of CD4 lineage, while its absence causes
CC       CD8 commitment. Development of immature T-cell precursors
CC       (thymocytes) to either the CD4 helper or CD8 killer T-cell
CC       lineages correlates precisely with their T-cell receptor
CC       specificity for major histocompatibility complex class II or class
CC       I molecules, respectively. Transcriptional repressor of the
CC       collagen COL1A1 and COL1A2 genes. May also function as a repressor
CC       of fibronectin and possibly other extracellular matrix genes (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH18158.1; Type=Erroneous initiation;
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DR   EMBL; AF007833; AAC51847.1; -; mRNA.
DR   EMBL; CR749303; CAH18158.1; ALT_INIT; mRNA.
DR   EMBL; AL451085; CAI13266.1; -; Genomic_DNA.
DR   EMBL; BC012070; AAH12070.1; -; mRNA.
DR   IPI; IPI00026277; -.
DR   RefSeq; NP_056956.2; -.
DR   RefSeq; XP_002345287.1; -.
DR   RefSeq; XP_002345288.1; -.
DR   UniGene; Hs.700874; -.
DR   ProteinModelPortal; O15156; -.
DR   SMR; O15156; 9-141, 344-450.
DR   IntAct; O15156; 2.
DR   MINT; MINT-1451723; -.
DR   STRING; O15156; -.
DR   PhosphoSite; O15156; -.
DR   PRIDE; O15156; -.
DR   Ensembl; ENST00000292176; ENSP00000292176; ENSG00000160685.
DR   Ensembl; ENST00000368426; ENSP00000357411; ENSG00000160685.
DR   Ensembl; ENST00000417934; ENSP00000406286; ENSG00000160685.
DR   GeneID; 100293130; -.
DR   GeneID; 51043; -.
DR   KEGG; hsa:100293130; -.
DR   KEGG; hsa:51043; -.
DR   UCSC; uc001fgj.2; human.
DR   CTD; 51043; -.
DR   GeneCards; GC01P154975; -.
DR   HGNC; HGNC:18668; ZBTB7B.
DR   HPA; HPA006811; -.
DR   HPA; HPA025820; -.
DR   MIM; 607646; gene.
DR   PharmGKB; PA38630; -.
DR   eggNOG; prNOG14380; -.
DR   HOVERGEN; HBG059461; -.
DR   InParanoid; O15156; -.
DR   PhylomeDB; O15156; -.
DR   NextBio; 53600; -.
DR   ArrayExpress; O15156; -.
DR   Bgee; O15156; -.
DR   CleanEx; HS_ZBTB7B; -.
DR   Genevestigator; O15156; -.
DR   GermOnline; ENSG00000160685; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0003704; F:specific RNA polymerase II transcription fa...; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007398; P:ectoderm development; TAS:ProtInc.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; Differentiation;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    539       Zinc finger and BTB domain-containing
FT                                protein 7B.
FT                                /FTId=PRO_0000047719.
FT   DOMAIN       34    115       BTB.
FT   ZN_FING     346    368       C2H2-type 1.
FT   ZN_FING     374    396       C2H2-type 2.
FT   ZN_FING     402    424       C2H2-type 3.
FT   ZN_FING     430    454       C2H2-type 4; atypical.
FT   COMPBIAS    181    196       Pro-rich.
FT   MOD_RES     369    369       Phosphothreonine.
FT   CONFLICT    437    437       K -> R (in Ref. 1; AAC51847).
FT   CONFLICT    480    480       S -> F (in Ref. 1; AAC51847).
FT   CONFLICT    509    510       GP -> WA (in Ref. 1; AAC51847).
SQ   SEQUENCE   539 AA;  58027 MW;  86B3616504B05B7E CRC64;
     MGSPEDDLIG IPFPDHSSEL LSCLNEQRQL GHLCDLTIRT QGLEYRTHRA VLAACSHYFK
     KLFTEGGGGA VMGAGGSGTA TGGAGAGVCE LDFVGPEALG ALLEFAYTAT LTTSSANMPA
     VLQAARLLEI PCVIAACMEI LQGSGLEAPS PDEDDCERAR QYLEAFATAT ASGVPNGEDS
     PPQVPLPPPP PPPPRPVARR SRKPRKAFLQ TKGARANHLV PEVPTVPAHP LTYEEEEVAG
     RVGSSGGSGP GDSYSPPTGT ASPPEGPQSY EPYEGEEEEE ELVYPPAYGL AQGGGPPLSP
     EELGSDEDAI DPDLMAYLSS LHQDNLAPGL DSQDKLVRKR RSQMPQECPV CHKIIHGAGK
     LPRHMRTHTG EKPFACEVCG VRFTRNDKLK IHMRKHTGER PYSCPHCPAR FLHSYDLKNH
     MHLHTGDRPY ECHLCHKAFA KEDHLQRHLK GQNCLEVRTR RRRKDDAPPH YPPPSTAAAS
     PAGLDLSNGH LDTFRLSLAR FWEQSAPTGP PVSTPGPPDD DEEEGAPTTP QAEGAMESS
//