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AF1Q_MOUSE
ID   AF1Q_MOUSE              Reviewed;          90 AA.
AC   P97783;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Protein AF1q;
GN   Name=Mllt11; Synonyms=Af1q;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RA   Matsuo N., Kawamoto S., Okubo K., Matsubara K.;
RT   "Cloning of mouse AF1q homologue.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Koduru P.K., Tse W., Liu J., Broome J.D.;
RT   "AF1q in fetal mouse brain.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
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   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15530661; DOI=10.1016/j.molbrainres.2004.07.022;
RA   Lin H.J., Shaffer K.M., Sun Z., Jay G., He W.-W., Ma W.;
RT   "AF1q, a differentially expressed gene during neuronal differentiation,
RT   transforms HEK cells into neuron-like cells.";
RL   Brain Res. Mol. Brain Res. 131:126-130(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Cofactor for the transcription factor TCF7. Involved in
CC       regulation of lymphoid development by driving multipotent hematopoietic
CC       progenitor cells towards a T-cell fate. {ECO:0000250|UniProtKB:Q13015}.
CC   -!- SUBUNIT: Interacts with HSPA8 and LAMP2 isoform A; the interaction may
CC       target MLLT11 for degradation via chaperone-mediated autophagy.
CC       Interacts with TCF7. {ECO:0000250|UniProtKB:Q13015}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13015}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q13015}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q13015}.
CC       Note=Continuous nuclear export is followed by degradation.
CC       {ECO:0000250|UniProtKB:Q13015}.
CC   -!- TISSUE SPECIFICITY: Detected in embryonic brain cortex.
CC       {ECO:0000269|PubMed:15530661}.
CC   -!- INDUCTION: Up-regulated during neuronal differentiation (in vitro).
CC       {ECO:0000269|PubMed:15530661}.
CC   -!- PTM: Ubiquitinated, leading to degradation.
CC       {ECO:0000250|UniProtKB:Q13015}.
CC   -!- SIMILARITY: Belongs to the MLLT11 family. {ECO:0000305}.
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DR   EMBL; AB000733; BAA19173.1; -; mRNA.
DR   EMBL; U95498; AAD00803.1; -; mRNA.
DR   EMBL; BC022963; AAH22963.1; -; mRNA.
DR   CCDS; CCDS38544.1; -.
DR   RefSeq; NP_064298.1; NM_019914.4.
DR   RefSeq; XP_006501863.1; XM_006501800.3.
DR   RefSeq; XP_017175158.1; XM_017319669.1.
DR   RefSeq; XP_017175159.1; XM_017319670.1.
DR   RefSeq; XP_017175160.1; XM_017319671.1.
DR   AlphaFoldDB; P97783; -.
DR   SMR; P97783; -.
DR   STRING; 10090.ENSMUSP00000066448; -.
DR   iPTMnet; P97783; -.
DR   PhosphoSitePlus; P97783; -.
DR   PaxDb; P97783; -.
DR   PeptideAtlas; P97783; -.
DR   PRIDE; P97783; -.
DR   ProteomicsDB; 281947; -.
DR   Antibodypedia; 34047; 120 antibodies from 22 providers.
DR   DNASU; 56772; -.
DR   Ensembl; ENSMUST00000065482; ENSMUSP00000066448; ENSMUSG00000053192.
DR   Ensembl; ENSMUST00000196025; ENSMUSP00000143755; ENSMUSG00000053192.
DR   Ensembl; ENSMUST00000198948; ENSMUSP00000142604; ENSMUSG00000053192.
DR   GeneID; 56772; -.
DR   KEGG; mmu:56772; -.
DR   UCSC; uc008qit.2; mouse.
DR   CTD; 10962; -.
DR   MGI; MGI:1929671; Mllt11.
DR   VEuPathDB; HostDB:ENSMUSG00000053192; -.
DR   eggNOG; ENOG502S7MB; Eukaryota.
DR   GeneTree; ENSGT00390000009895; -.
DR   HOGENOM; CLU_2440320_0_0_1; -.
DR   InParanoid; P97783; -.
DR   OMA; FNYWKEP; -.
DR   OrthoDB; 1586302at2759; -.
DR   PhylomeDB; P97783; -.
DR   TreeFam; TF336906; -.
DR   BioGRID-ORCS; 56772; 0 hits in 74 CRISPR screens.
DR   ChiTaRS; Mllt11; mouse.
DR   PRO; PR:P97783; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P97783; protein.
DR   Bgee; ENSMUSG00000053192; Expressed in embryonic brain and 273 other tissues.
DR   ExpressionAtlas; P97783; baseline and differential.
DR   Genevisible; P97783; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISS:UniProtKB.
DR   GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR026778; MLLT11_fam.
DR   InterPro; IPR033461; WRNPLPNID.
DR   PANTHER; PTHR15404; PTHR15404; 1.
DR   Pfam; PF15017; WRNPLPNID; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..90
FT                   /note="Protein AF1q"
FT                   /id="PRO_0000064472"
FT   REGION          31..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..32
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q13015"
FT   COMPBIAS        36..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   90 AA;  10029 MW;  5A8BCE378D1922F2 CRC64;
     MRDPVSSQYS SFLFWRMPIP ELDLSELEGL GLSDTPTYES KDSSSVGKMN GQASGTEQKN
     PEGDPLLEYS TFNFWRAPIA SIHSVDLDLL
 
 
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