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ZHANG_HUMAN
ID   ZHANG_HUMAN             Reviewed;         354 AA.
AC   Q9NS37; B2R8Q9; Q0P5U9; Q52LT3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=CREB/ATF bZIP transcription factor;
DE   AltName: Full=Host cell factor-binding transcription factor Zhangfei;
DE            Short=HCF-binding transcription factor Zhangfei;
GN   Name=CREBZF; Synonyms=ZF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAD28325.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HCFC1, TISSUE
RP   SPECIFICITY, MOTIF, AND MUTAGENESIS OF ASP-303; HIS-304 AND TYR-306.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10871379; DOI=10.1093/nar/28.12.2446;
RA   Lu R., Misra V.;
RT   "Zhangfei: a second cellular protein interacts with herpes simplex virus
RT   accessory factor HCF in a manner similar to Luman and VP16.";
RL   Nucleic Acids Res. 28:2446-2454(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Placenta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-354.
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 74-354.
RC   TISSUE=Bone marrow;
RA   Zhang J.W., Zhang X., Ma Y.N.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000305}
RP   FUNCTION AS A SUPPRESSOR OF CREB3 TRANSCRIPTIONAL ACTIVITY, INTERACTION
RP   WITH CREB3 AND HCFC1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-306.
RX   PubMed=15705566; DOI=10.1074/jbc.m500728200;
RA   Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P.;
RT   "Zhangfei is a potent and specific inhibitor of the host cell factor-
RT   binding transcription factor Luman.";
RL   J. Biol. Chem. 280:15257-15266(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Strongly activates transcription when bound to HCFC1.
CC       Suppresses the expression of HSV proteins in cells infected with the
CC       virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent
CC       transcriptional activation by CREB3 and reduces the amount of CREB3 in
CC       the cell. Able to down-regulate expression of some cellular genes in
CC       CREBZF-expressing cells. {ECO:0000269|PubMed:10871379,
CC       ECO:0000269|PubMed:15705566}.
CC   -!- SUBUNIT: Interacts with HCFC1; the interaction inhibits CREB3
CC       transcriptional activity (PubMed:10871379, PubMed:15705566). Interacts
CC       with CREB3; the interaction occurs only in combination with HCFC1
CC       (PubMed:15705566). {ECO:0000269|PubMed:10871379,
CC       ECO:0000269|PubMed:15705566}.
CC   -!- INTERACTION:
CC       Q9NS37; P14621: ACYP2; NbExp=3; IntAct=EBI-632965, EBI-10198377;
CC       Q9NS37; P18848: ATF4; NbExp=7; IntAct=EBI-632965, EBI-492498;
CC       Q9NS37; O43889: CREB3; NbExp=3; IntAct=EBI-632965, EBI-625002;
CC       Q9NS37; Q9NS37: CREBZF; NbExp=5; IntAct=EBI-632965, EBI-632965;
CC       Q9NS37; Q8WYA6: CTNNBL1; NbExp=3; IntAct=EBI-632965, EBI-748128;
CC       Q9NS37; P51610: HCFC1; NbExp=8; IntAct=EBI-632965, EBI-396176;
CC       Q9NS37; P51610-4: HCFC1; NbExp=3; IntAct=EBI-632965, EBI-18150048;
CC       Q9NS37; Q14494: NFE2L1; NbExp=3; IntAct=EBI-632965, EBI-2804436;
CC       Q9NS37; Q16236: NFE2L2; NbExp=5; IntAct=EBI-632965, EBI-2007911;
CC       Q9NS37; Q15311: RALBP1; NbExp=4; IntAct=EBI-632965, EBI-749285;
CC       Q9NS37; Q96EB6: SIRT1; NbExp=3; IntAct=EBI-632965, EBI-1802965;
CC       Q9NS37; O00268: TAF4; NbExp=2; IntAct=EBI-632965, EBI-1034261;
CC       Q9NS37; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-632965, EBI-6447954;
CC       Q9NS37; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-632965, EBI-9090990;
CC       Q9NS37; P17861: XBP1; NbExp=4; IntAct=EBI-632965, EBI-6942961;
CC       Q9NS37; P62509: Esrrg; Xeno; NbExp=3; IntAct=EBI-632965, EBI-5274019;
CC       Q9NS37; P0C746: HBZ; Xeno; NbExp=3; IntAct=EBI-632965, EBI-10890294;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15705566}.
CC       Note=Colocalizes in promyelocytic leukemia protein nuclear bodies (PML-
CC       NB) with CREB3 and HCFC1.
CC   -!- TISSUE SPECIFICITY: In adults, expressed most abundantly in heart,
CC       liver and skeletal muscle, moderately abundant in kidney and pancreas,
CC       and barely detectable in lung. In fetal tissues, expressed most
CC       abundantly in kidney and very low amounts in heart, lung and liver.
CC       {ECO:0000269|PubMed:10871379}.
CC   -!- MISCELLANEOUS: Named 'Zhangfei' after a legendary Chinese warrior who
CC       was contemporary with Luman in around 220 AD.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD28325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAD28325.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAZ42189.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG36256.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG36256.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF039942; AAD28325.1; ALT_SEQ; mRNA.
DR   EMBL; AP000642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060807; AAH60807.1; -; mRNA.
DR   EMBL; BC093796; AAH93796.2; -; mRNA.
DR   EMBL; BC093798; AAH93798.2; -; mRNA.
DR   EMBL; AK313471; BAG36256.1; ALT_SEQ; mRNA.
DR   EMBL; DQ128105; AAZ42189.1; ALT_INIT; mRNA.
DR   CCDS; CCDS41697.1; -.
DR   RefSeq; NP_001034707.1; NM_001039618.2.
DR   RefSeq; XP_011543497.1; XM_011545195.2.
DR   RefSeq; XP_016873577.1; XM_017018088.1.
DR   RefSeq; XP_016873578.1; XM_017018089.1.
DR   RefSeq; XP_016873579.1; XM_017018090.1.
DR   RefSeq; XP_016873580.1; XM_017018091.1.
DR   RefSeq; XP_016873581.1; XM_017018092.1.
DR   AlphaFoldDB; Q9NS37; -.
DR   SMR; Q9NS37; -.
DR   BioGRID; 121817; 23.
DR   ComplexPortal; CPX-6542; bZIP transcription factor complex, ATF4-CREBZF.
DR   ComplexPortal; CPX-6601; bZIP transcription factor complex, ATF6B-CREBZF.
DR   DIP; DIP-33934N; -.
DR   ELM; Q9NS37; -.
DR   IntAct; Q9NS37; 22.
DR   MINT; Q9NS37; -.
DR   STRING; 9606.ENSP00000433459; -.
DR   iPTMnet; Q9NS37; -.
DR   PhosphoSitePlus; Q9NS37; -.
DR   BioMuta; CREBZF; -.
DR   DMDM; 251757415; -.
DR   EPD; Q9NS37; -.
DR   jPOST; Q9NS37; -.
DR   MassIVE; Q9NS37; -.
DR   MaxQB; Q9NS37; -.
DR   PaxDb; Q9NS37; -.
DR   PeptideAtlas; Q9NS37; -.
DR   PRIDE; Q9NS37; -.
DR   ProteomicsDB; 82476; -.
DR   Antibodypedia; 31388; 203 antibodies from 27 providers.
DR   DNASU; 58487; -.
DR   Ensembl; ENST00000490820.2; ENSP00000434281.1; ENSG00000137504.15.
DR   Ensembl; ENST00000527447.2; ENSP00000433459.1; ENSG00000137504.15.
DR   GeneID; 58487; -.
DR   KEGG; hsa:58487; -.
DR   MANE-Select; ENST00000527447.2; ENSP00000433459.1; NM_001039618.4; NP_001034707.1.
DR   UCSC; uc001pas.3; human.
DR   CTD; 58487; -.
DR   DisGeNET; 58487; -.
DR   GeneCards; CREBZF; -.
DR   HGNC; HGNC:24905; CREBZF.
DR   HPA; ENSG00000137504; Low tissue specificity.
DR   MIM; 606444; gene.
DR   neXtProt; NX_Q9NS37; -.
DR   OpenTargets; ENSG00000137504; -.
DR   PharmGKB; PA162382821; -.
DR   VEuPathDB; HostDB:ENSG00000137504; -.
DR   eggNOG; ENOG502S3I0; Eukaryota.
DR   GeneTree; ENSGT00390000016589; -.
DR   InParanoid; Q9NS37; -.
DR   OMA; PEDMDFL; -.
DR   PhylomeDB; Q9NS37; -.
DR   TreeFam; TF336153; -.
DR   PathwayCommons; Q9NS37; -.
DR   SignaLink; Q9NS37; -.
DR   BioGRID-ORCS; 58487; 19 hits in 1085 CRISPR screens.
DR   ChiTaRS; CREBZF; human.
DR   GenomeRNAi; 58487; -.
DR   Pharos; Q9NS37; Tbio.
DR   PRO; PR:Q9NS37; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9NS37; protein.
DR   Bgee; ENSG00000137504; Expressed in sural nerve and 196 other tissues.
DR   ExpressionAtlas; Q9NS37; baseline and differential.
DR   Genevisible; Q9NS37; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0036500; P:ATF6-mediated unfolded protein response; IC:ComplexPortal.
DR   GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..354
FT                   /note="CREB/ATF bZIP transcription factor"
FT                   /id="PRO_0000076645"
FT   DOMAIN          204..267
FT                   /note="bZIP"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..226
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000250"
FT   REGION          232..267
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000250"
FT   MOTIF           303..306
FT                   /note="HCFC1-binding motif (HBM)"
FT                   /evidence="ECO:0000269|PubMed:10871379"
FT   COMPBIAS        8..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MUTAGEN         303
FT                   /note="D->A: Significantly reduced binding to HCFC1."
FT                   /evidence="ECO:0000269|PubMed:10871379"
FT   MUTAGEN         304
FT                   /note="H->A: Significantly reduced binding to HCFC1."
FT                   /evidence="ECO:0000269|PubMed:10871379"
FT   MUTAGEN         306
FT                   /note="Y->A: Does not interact with HCFC1 and is
FT                   inefficient at inhibiting CREB3 transcriptional activity.
FT                   Does not colocalize with CREB3 in promyelocytic leukemia
FT                   protein nuclear bodies (PML-NB)."
FT                   /evidence="ECO:0000269|PubMed:10871379,
FT                   ECO:0000269|PubMed:15705566"
FT   CONFLICT        16
FT                   /note="S -> F (in Ref. 3; AAH60807)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  37134 MW;  BE3AC77203216155 CRC64;
     MRHSLTKLLA ASGSNSPTRS ESPEPAATCS LPSDLTRAAA GEEETAAAGS PGRKQQFGDE
     GELEAGRGSR GGVAVRAPSP EEMEEEAIAS LPGEETEDMD FLSGLELADL LDPRQPDWHL
     DPGLSSPGPL SSSGGGSDSG GLWRGDDDDE AAAAEMQRFS DLLQRLLNGI GGCSSSSDSG
     SAEKRRRKSP GGGGGGGSGN DNNQAATKSP RKAAAAAARL NRLKKKEYVM GLESRVRGLA
     AENQELRAEN RELGKRVQAL QEESRYLRAV LANETGLARL LSRLSGVGLR LTTSLFRDSP
     AGDHDYALPV GKQKQDLLEE DDSAGGVCLH VDKDKVSVEF CSACARKASS SLKM
 
 
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