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ZN692_HUMAN
ID   ZN692_HUMAN             Reviewed;         519 AA.
AC   Q9BU19; B4DXZ0; Q5SRA5; Q5SRA6; Q9HBC9; Q9NW93; Q9NWY6; Q9UF97;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Zinc finger protein 692 {ECO:0000305};
DE   AltName: Full=AICAR responsive element binding protein {ECO:0000303|PubMed:17097062};
GN   Name=ZNF692;
GN   Synonyms=AREBP {ECO:0000303|PubMed:17097062},
GN   ZFP692 {ECO:0000250|UniProtKB:Q3U381};
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, MUTAGENESIS OF THR-62;
RP   SER-63; THR-386; SER-402; THR-442 AND SER-470, PHOSPHORYLATION AT SER-470,
RP   AND FUNCTION.
RX   PubMed=17097062; DOI=10.1016/j.bbrc.2006.10.124;
RA   Inoue E., Yamauchi J.;
RT   "AMP-activated protein kinase regulates PEPCK gene expression by direct
RT   phosphorylation of a novel zinc finger transcription factor.";
RL   Biochem. Biophys. Res. Commun. 351:793-799(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANT
RP   ARG-230.
RC   TISSUE=Carcinoma, Embryo, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Testis;
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., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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 1).
RC   TISSUE=Lung;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 221-519.
RC   TISSUE=Parathyroid adenoma;
RA   Pryor J.S., Sullivan L., Dial M., May K., Morgan M., Smith C., Buford D.,
RA   Kirklin S., Williams D., Pugh M.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION.
RX   PubMed=21910974; DOI=10.1016/j.bbrc.2011.08.120;
RA   Shirai T., Inoue E., Ishimi Y., Yamauchi J.;
RT   "AICAR response element binding protein (AREBP), a key modulator of hepatic
RT   glucose production regulated by AMPK in vivo.";
RL   Biochem. Biophys. Res. Commun. 414:287-291(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-231, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   STRUCTURE BY NMR OF 328-481.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of ZF-C2H2 domains of zinc finger protein 692.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: May act as an transcriptional repressor for PCK1 gene
CC       expression, in turn may participate in the hepatic gluconeogenesis
CC       regulation through the activated AMPK signaling pathway.
CC       {ECO:0000269|PubMed:17097062, ECO:0000269|PubMed:21910974}.
CC   -!- INTERACTION:
CC       Q9BU19; Q92993: KAT5; NbExp=3; IntAct=EBI-12076976, EBI-399080;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9BU19-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BU19-2; Sequence=VSP_018188;
CC       Name=3;
CC         IsoId=Q9BU19-3; Sequence=VSP_018186;
CC       Name=4;
CC         IsoId=Q9BU19-4; Sequence=VSP_018185, VSP_018187;
CC       Name=5;
CC         IsoId=Q9BU19-5; Sequence=VSP_043025;
CC   -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:17097062). Highly expressed in
CC       brain, thymus and spleen (PubMed:17097062).
CC       {ECO:0000269|PubMed:17097062}.
CC   -!- PTM: Phosphorylation at Ser-470 results in loss of DNA-binding
CC       activity. {ECO:0000269|PubMed:17097062}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AK000538; BAA91239.1; -; mRNA.
DR   EMBL; AK001070; BAA91490.1; -; mRNA.
DR   EMBL; AK302187; BAG63552.1; -; mRNA.
DR   EMBL; AL133100; CAB61410.2; -; mRNA.
DR   EMBL; AL672291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002948; AAH02948.1; -; mRNA.
DR   EMBL; AF256175; AAG15327.1; -; Transcribed_RNA.
DR   CCDS; CCDS31127.1; -. [Q9BU19-1]
DR   CCDS; CCDS44348.1; -. [Q9BU19-5]
DR   CCDS; CCDS53487.1; -. [Q9BU19-2]
DR   PIR; T42682; T42682.
DR   RefSeq; NP_001129508.1; NM_001136036.2. [Q9BU19-5]
DR   RefSeq; NP_001180257.1; NM_001193328.1. [Q9BU19-2]
DR   RefSeq; NP_060335.2; NM_017865.3. [Q9BU19-1]
DR   RefSeq; XP_011542524.1; XM_011544222.1. [Q9BU19-1]
DR   PDB; 2D9H; NMR; -; A=417-481.
DR   PDB; 2DLK; NMR; -; A=328-393.
DR   PDB; 6H0G; X-ray; 4.25 A; C/F=416-441.
DR   PDBsum; 2D9H; -.
DR   PDBsum; 2DLK; -.
DR   PDBsum; 6H0G; -.
DR   AlphaFoldDB; Q9BU19; -.
DR   SMR; Q9BU19; -.
DR   BioGRID; 120789; 39.
DR   IntAct; Q9BU19; 29.
DR   STRING; 9606.ENSP00000391200; -.
DR   iPTMnet; Q9BU19; -.
DR   PhosphoSitePlus; Q9BU19; -.
DR   BioMuta; ZNF692; -.
DR   DMDM; 74761262; -.
DR   EPD; Q9BU19; -.
DR   jPOST; Q9BU19; -.
DR   MassIVE; Q9BU19; -.
DR   MaxQB; Q9BU19; -.
DR   PaxDb; Q9BU19; -.
DR   PeptideAtlas; Q9BU19; -.
DR   PRIDE; Q9BU19; -.
DR   ProteomicsDB; 79040; -. [Q9BU19-1]
DR   ProteomicsDB; 79041; -. [Q9BU19-2]
DR   ProteomicsDB; 79042; -. [Q9BU19-3]
DR   ProteomicsDB; 79044; -. [Q9BU19-5]
DR   TopDownProteomics; Q9BU19-3; -. [Q9BU19-3]
DR   Antibodypedia; 54395; 45 antibodies from 15 providers.
DR   DNASU; 55657; -.
DR   Ensembl; ENST00000306601.9; ENSP00000305483.5; ENSG00000171163.16. [Q9BU19-1]
DR   Ensembl; ENST00000366471.7; ENSP00000355427.3; ENSG00000171163.16. [Q9BU19-2]
DR   Ensembl; ENST00000451251.5; ENSP00000391200.1; ENSG00000171163.16. [Q9BU19-5]
DR   Ensembl; ENST00000463519.5; ENSP00000436308.1; ENSG00000171163.16. [Q9BU19-4]
DR   GeneID; 55657; -.
DR   KEGG; hsa:55657; -.
DR   MANE-Select; ENST00000306601.9; ENSP00000305483.5; NM_017865.4; NP_060335.2.
DR   UCSC; uc001ifc.3; human. [Q9BU19-1]
DR   CTD; 55657; -.
DR   DisGeNET; 55657; -.
DR   GeneCards; ZNF692; -.
DR   HGNC; HGNC:26049; ZNF692.
DR   HPA; ENSG00000171163; Low tissue specificity.
DR   MIM; 617758; gene.
DR   neXtProt; NX_Q9BU19; -.
DR   OpenTargets; ENSG00000171163; -.
DR   PharmGKB; PA142670491; -.
DR   VEuPathDB; HostDB:ENSG00000171163; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161175; -.
DR   HOGENOM; CLU_045687_1_0_1; -.
DR   InParanoid; Q9BU19; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9BU19; -.
DR   TreeFam; TF332664; -.
DR   PathwayCommons; Q9BU19; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9BU19; -.
DR   SIGNOR; Q9BU19; -.
DR   BioGRID-ORCS; 55657; 128 hits in 1102 CRISPR screens.
DR   ChiTaRS; ZNF692; human.
DR   EvolutionaryTrace; Q9BU19; -.
DR   GenomeRNAi; 55657; -.
DR   Pharos; Q9BU19; Tbio.
DR   PRO; PR:Q9BU19; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9BU19; protein.
DR   Bgee; ENSG00000171163; Expressed in right hemisphere of cerebellum and 192 other tissues.
DR   ExpressionAtlas; Q9BU19; baseline and differential.
DR   Genevisible; Q9BU19; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; IMP:UniProtKB.
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; 5.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..519
FT                   /note="Zinc finger protein 692"
FT                   /id="PRO_0000234014"
FT   ZN_FING         328..353
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         359..383
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         389..411
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         417..439
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         448..471
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          123..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..207
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         470
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   VAR_SEQ         1
FT                   /note="M -> MPLVHM (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043025"
FT   VAR_SEQ         61..96
FT                   /note="YTSSGCVLCAGPEPLPPKGLQYLVLLSHAHSRECSL -> ACPAALFHPQVS
FT                   HFTRTACVTCGLRGSCSPPHGLSE (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_018185"
FT   VAR_SEQ         88..259
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_018186"
FT   VAR_SEQ         97..519
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_018187"
FT   VAR_SEQ         175..220
FT                   /note="RRVGPPPETFPPPGEEEGEEEEDNDEDEEEMLSDASLWTYSSSPDD -> S
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_018188"
FT   VARIANT         230
FT                   /note="P -> R (in dbSNP:rs13313088)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_033590"
FT   MUTAGEN         62
FT                   /note="T->A: Does not affect phosphorylation by AMPK."
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   MUTAGEN         63
FT                   /note="S->A: Does not affect phosphorylation by AMPK."
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   MUTAGEN         386
FT                   /note="T->A: Does not affect phosphorylation by AMPK."
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   MUTAGEN         402
FT                   /note="S->A: Does not affect phosphorylation by AMPK."
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   MUTAGEN         442
FT                   /note="T->A: Does not affect phosphorylation by AMPK."
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   MUTAGEN         470
FT                   /note="S->A: Reduces phosphorylation by AMPK. Does not
FT                   affect DNA binding. Does not repress transcription of
FT                   PCK1."
FT                   /evidence="ECO:0000269|PubMed:17097062"
FT   CONFLICT        373
FT                   /note="K -> R (in Ref. 2; BAA91490)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="S -> G (in Ref. 2; BAA91239)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        435
FT                   /note="H -> R (in Ref. 2; BAA91490)"
FT                   /evidence="ECO:0000305"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   STRAND          338..341
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   HELIX           342..351
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   HELIX           352..354
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   TURN            364..366
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   STRAND          369..372
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   HELIX           373..384
FT                   /evidence="ECO:0007829|PDB:2DLK"
FT   STRAND          420..422
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   STRAND          425..428
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   HELIX           429..442
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   TURN            443..445
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   TURN            451..453
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   STRAND          456..459
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   HELIX           460..469
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   TURN            472..474
FT                   /evidence="ECO:0007829|PDB:2D9H"
FT   STRAND          479..481
FT                   /evidence="ECO:0007829|PDB:2D9H"
SQ   SEQUENCE   519 AA;  56968 MW;  DEFAEF73C910619E CRC64;
     MASSPAVDVS CRRREKRRQL DARRSKCRIR LGGHMEQWCL LKERLGFSLH SQLAKFLLDR
     YTSSGCVLCA GPEPLPPKGL QYLVLLSHAH SRECSLVPGL RGPGGQDGGL VWECSAGHTF
     SWGPSLSPTP SEAPKPASLP HTTRRSWCSE ATSGQELADL ESEHDERTQE ARLPRRVGPP
     PETFPPPGEE EGEEEEDNDE DEEEMLSDAS LWTYSSSPDD SEPDAPRLLP SPVTCTPKEG
     ETPPAPAALS SPLAVPALSA SSLSSRAPPP AEVRVQPQLS RTPQAAQQTE ALASTGSQAQ
     SAPTPAWDED TAQIGPKRIR KAAKRELMPC DFPGCGRIFS NRQYLNHHKK YQHIHQKSFS
     CPEPACGKSF NFKKHLKEHM KLHSDTRDYI CEFCARSFRT SSNLVIHRRI HTGEKPLQCE
     ICGFTCRQKA SLNWHQRKHA ETVAALRFPC EFCGKRFEKP DSVAAHRSKS HPALLLAPQE
     SPSGPLEPCP SISAPGPLGS SEGSRPSASP QAPTLLPQQ
 
 
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