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F264_HUMAN
ID   F264_HUMAN              Reviewed;         469 AA.
AC   Q16877; Q5S3G5; Q5XLC2; Q64EX5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 6.
DT   03-AUG-2022, entry version 195.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4;
DE            Short=6PF-2-K/Fru-2,6-P2ase 4;
DE            Short=PFK/FBPase 4;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ase testis-type isozyme;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   Name=PFKFB4;
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] (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING.
RX   PubMed=15474002; DOI=10.1016/j.febslet.2004.08.053;
RA   Minchenko O., Opentanova I., Minchenko D., Ogura T., Esumi H.;
RT   "Hypoxia induces transcription of 6-phosphofructo-2-kinase/fructose-2,6-
RT   biphosphatase-4 gene via hypoxia-inducible factor-1alpha activation.";
RL   FEBS Lett. 576:14-20(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Sakakibara R.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RA   Minchenko O.H., Opentanova I.L., Minchenko D.O., Kurashima Y., Esumi H.;
RT   "Alternative splicing of human 6-phosphofructo-2-kinase/fructose-2,6-
RT   phosphatase 4 in melanoma cells.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=10095107; DOI=10.1016/s0378-1119(99)00037-2;
RA   Manzano A., Perez J.X., Nadal M., Estivill X., Lange A., Bartrons R.;
RT   "Cloning, expression and chromosomal localization of a human testis 6-
RT   phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene.";
RL   Gene 229:83-89(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15642344; DOI=10.1016/j.febslet.2004.11.096;
RA   Gomez M., Manzano A., Navarro-Sabate A., Duran J., Obach M., Perales J.C.,
RA   Bartrons R.;
RT   "Specific expression of pfkfb4 gene in spermatogonia germ cells and
RT   analysis of its 5'-flanking region.";
RL   FEBS Lett. 579:357-362(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=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   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 357-469 (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=8830046; DOI=10.1093/oxfordjournals.jbchem.a021270;
RA   Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.;
RT   "Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-
RT   kinase/fructose 2,6-bisphosphatase from human placenta.";
RL   J. Biochem. 119:506-511(1996).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] LYS-181.
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., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579,
CC         ChEBI:CHEBI:456216; EC=2.7.1.105;
CC   -!- ACTIVITY REGULATION: The most important regulatory mechanism of these
CC       opposing activities is by phosphorylation and dephosphorylation of the
CC       enzyme. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q16877; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-764534, EBI-10171570;
CC       Q16877; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-764534, EBI-396137;
CC       Q16877; Q96L50: LRR1; NbExp=3; IntAct=EBI-764534, EBI-2510106;
CC       Q16877; P16118: PFKFB1; NbExp=5; IntAct=EBI-764534, EBI-709807;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q16877-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q16877-2; Sequence=VSP_056530;
CC       Name=3;
CC         IsoId=Q16877-3; Sequence=VSP_056621;
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase family. {ECO:0000305}.
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DR   EMBL; AY756062; AAV28717.1; -; mRNA.
DR   EMBL; AY756064; AAV28719.1; -; mRNA.
DR   EMBL; D49818; BAA18921.1; -; mRNA.
DR   EMBL; AY714243; AAU14998.1; -; mRNA.
DR   EMBL; AF108765; AAD09427.1; -; mRNA.
DR   EMBL; AY786551; AAV65753.1; -; Genomic_DNA.
DR   EMBL; AC134772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64890.1; -; Genomic_DNA.
DR   EMBL; BC010269; AAH10269.1; -; mRNA.
DR   CCDS; CCDS2771.1; -. [Q16877-1]
DR   CCDS; CCDS82769.1; -. [Q16877-2]
DR   PIR; JC5871; JC5871.
DR   RefSeq; NP_001304063.1; NM_001317134.1.
DR   RefSeq; NP_001304064.1; NM_001317135.1.
DR   RefSeq; NP_001304065.1; NM_001317136.1.
DR   RefSeq; NP_001304066.1; NM_001317137.1. [Q16877-2]
DR   RefSeq; NP_001304067.1; NM_001317138.1.
DR   RefSeq; NP_004558.1; NM_004567.3. [Q16877-1]
DR   AlphaFoldDB; Q16877; -.
DR   SMR; Q16877; -.
DR   BioGRID; 111231; 32.
DR   ComplexPortal; CPX-1996; 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 complex.
DR   IntAct; Q16877; 13.
DR   MINT; Q16877; -.
DR   STRING; 9606.ENSP00000232375; -.
DR   BindingDB; Q16877; -.
DR   ChEMBL; CHEMBL3721311; -.
DR   DrugBank; DB04493; Fructose-6-phosphate.
DR   DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR   DEPOD; PFKFB4; -.
DR   iPTMnet; Q16877; -.
DR   PhosphoSitePlus; Q16877; -.
DR   BioMuta; PFKFB4; -.
DR   DMDM; 6226609; -.
DR   EPD; Q16877; -.
DR   jPOST; Q16877; -.
DR   MassIVE; Q16877; -.
DR   MaxQB; Q16877; -.
DR   PaxDb; Q16877; -.
DR   PeptideAtlas; Q16877; -.
DR   PRIDE; Q16877; -.
DR   ProteomicsDB; 61116; -. [Q16877-1]
DR   ProteomicsDB; 65838; -.
DR   ProteomicsDB; 65916; -.
DR   Antibodypedia; 30130; 193 antibodies from 24 providers.
DR   DNASU; 5210; -.
DR   Ensembl; ENST00000232375.8; ENSP00000232375.3; ENSG00000114268.12. [Q16877-1]
DR   Ensembl; ENST00000383734.6; ENSP00000373240.2; ENSG00000114268.12. [Q16877-2]
DR   GeneID; 5210; -.
DR   KEGG; hsa:5210; -.
DR   MANE-Select; ENST00000232375.8; ENSP00000232375.3; NM_004567.4; NP_004558.1.
DR   UCSC; uc003ctv.4; human. [Q16877-1]
DR   CTD; 5210; -.
DR   DisGeNET; 5210; -.
DR   GeneCards; PFKFB4; -.
DR   HGNC; HGNC:8875; PFKFB4.
DR   HPA; ENSG00000114268; Tissue enhanced (testis).
DR   MIM; 605320; gene.
DR   neXtProt; NX_Q16877; -.
DR   OpenTargets; ENSG00000114268; -.
DR   PharmGKB; PA33214; -.
DR   VEuPathDB; HostDB:ENSG00000114268; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   GeneTree; ENSGT00950000182835; -.
DR   HOGENOM; CLU_006383_1_1_1; -.
DR   InParanoid; Q16877; -.
DR   OMA; IACMNGR; -.
DR   OrthoDB; 392001at2759; -.
DR   PhylomeDB; Q16877; -.
DR   TreeFam; TF313541; -.
DR   BioCyc; MetaCyc:HS03750-MON; -.
DR   BRENDA; 2.7.1.105; 2681.
DR   BRENDA; 3.1.3.46; 2681.
DR   PathwayCommons; Q16877; -.
DR   Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR   SignaLink; Q16877; -.
DR   SIGNOR; Q16877; -.
DR   BioGRID-ORCS; 5210; 21 hits in 1075 CRISPR screens.
DR   ChiTaRS; PFKFB4; human.
DR   GeneWiki; PFKFB4; -.
DR   GenomeRNAi; 5210; -.
DR   Pharos; Q16877; Tchem.
DR   PRO; PR:Q16877; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q16877; protein.
DR   Bgee; ENSG00000114268; Expressed in blood and 118 other tissues.
DR   ExpressionAtlas; Q16877; baseline and differential.
DR   Genevisible; Q16877; HS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR10606; PTHR10606; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Hydrolase; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..469
FT                   /note="6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
FT                   4"
FT                   /id="PRO_0000179970"
FT   REGION          1..249
FT                   /note="6-phosphofructo-2-kinase"
FT   REGION          250..469
FT                   /note="Fructose-2,6-bisphosphatase"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        257
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   ACT_SITE        326
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         46..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         79
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         103
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         131
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         137
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         168..173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         173
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         194
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         198
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         256
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         263
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         269
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         306
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         337
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         348..351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         351
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         355
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         366
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         392..396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         392
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         396
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         428
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   SITE            391
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00950"
FT   MOD_RES         444
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15474002, ECO:0000303|Ref.3"
FT                   /id="VSP_056621"
FT   VAR_SEQ         330..364
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15474002"
FT                   /id="VSP_056530"
FT   VARIANT         181
FT                   /note="N -> K (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036075"
SQ   SEQUENCE   469 AA;  54040 MW;  7E190C3C0A197D9F CRC64;
     MASPRELTQN PLKKIWMPYS NGRPALHACQ RGVCMTNCPT LIVMVGLPAR GKTYISKKLT
     RYLNWIGVPT REFNVGQYRR DVVKTYKSFE FFLPDNEEGL KIRKQCALAA LRDVRRFLSE
     EGGHVAVFDA TNTTRERRAT IFNFGEQNGY KTFFVESICV DPEVIAANIV QVKLGSPDYV
     NRDSDEATED FMRRIECYEN SYESLDEDLD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY
     YLMNIHVTPR SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FAKSLAQFIS DQNIKDLKVW
     TSQMKRTIQT AEALGVPYEQ WKVLNEIDAG VCEEMTYEEI QDNYPLEFAL RDQDKYRYRY
     PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA YFLDKAAEQL PYLKCPLHTV
     LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ NVDISRPPEE ALVTVPAHQ
 
 
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