AN13D_MOUSE
ID AN13D_MOUSE Reviewed; 605 AA.
AC Q6PD24; G3X9A8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ankyrin repeat domain-containing protein 13D;
GN Name=Ankrd13d;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Ubiquitin-binding protein that specifically recognizes and
CC binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked
CC ubiquitin. Positively regulates the internalization of ligand-activated
CC EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell
CC membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EGFR (ubiquitinated); the interaction is direct
CC and may regulate EGFR internalization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Late endosome. Note=Interaction
CC with EGFR may enhance association with the cell membrane.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58982.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC140073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466612; EDL33042.1; -; Genomic_DNA.
DR EMBL; BC058982; AAH58982.1; ALT_INIT; mRNA.
DR CCDS; CCDS50351.1; -.
DR RefSeq; NP_080996.2; NM_026720.2.
DR AlphaFoldDB; Q6PD24; -.
DR SMR; Q6PD24; -.
DR BioGRID; 212847; 5.
DR IntAct; Q6PD24; 1.
DR STRING; 10090.ENSMUSP00000053783; -.
DR iPTMnet; Q6PD24; -.
DR PhosphoSitePlus; Q6PD24; -.
DR MaxQB; Q6PD24; -.
DR PaxDb; Q6PD24; -.
DR PeptideAtlas; Q6PD24; -.
DR PRIDE; Q6PD24; -.
DR ProteomicsDB; 281977; -.
DR Antibodypedia; 44541; 52 antibodies from 16 providers.
DR Ensembl; ENSMUST00000056888; ENSMUSP00000053783; ENSMUSG00000005986.
DR GeneID; 68423; -.
DR KEGG; mmu:68423; -.
DR UCSC; uc008fzr.1; mouse.
DR CTD; 338692; -.
DR MGI; MGI:1915673; Ankrd13d.
DR VEuPathDB; HostDB:ENSMUSG00000005986; -.
DR eggNOG; KOG0522; Eukaryota.
DR GeneTree; ENSGT00950000182928; -.
DR HOGENOM; CLU_026137_2_0_1; -.
DR InParanoid; Q6PD24; -.
DR OMA; RICAPQE; -.
DR OrthoDB; 425969at2759; -.
DR PhylomeDB; Q6PD24; -.
DR TreeFam; TF314176; -.
DR BioGRID-ORCS; 68423; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ankrd13d; mouse.
DR PRO; PR:Q6PD24; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6PD24; protein.
DR Bgee; ENSMUSG00000005986; Expressed in granulocyte and 198 other tissues.
DR ExpressionAtlas; Q6PD24; baseline and differential.
DR Genevisible; Q6PD24; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0140036; F:ubiquitin-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR021832; ANKRD13.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12447; PTHR12447; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF11904; GPCR_chapero_1; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00726; UIM; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..605
FT /note="Ankyrin repeat domain-containing protein 13D"
FT /id="PRO_0000240652"
FT DOMAIN 482..501
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 528..547
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 564..583
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 589..605
FT /note="UIM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 538..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 605 AA; 68076 MW; DD5D44F3969A46D9 CRC64;
MAGLGPTFPL HRLVWANRHR ELEAALHSRK HDIEQEDPQG RTPLELAVTL GNLESVRVLL
RHNANVGKES HQGWAVLQEA VSTGDPEMVQ LVLQYRDFQR ATQRLAGIPE LLNKLRQAPD
FYVEMKWEFT SWVPLVSKMC PSDVYRVWKR GESLRVDTSL LGFEHMTWQR GRRSFIFRGQ
EAGALVMEVD HDRQVVHTET LAPALHEPEA LLAAMRPSEE HVASRLTSPI VSTHLDTRNV
AFERNKCGIW GWRSEKMESV SGYEAKVYSA TNVELVTRTR TEHLSDQDKL RNKGGKTPFQ
SFLGMAQQHS SHTLAPVQQA ASPTNPTAIS AEEYFDPSFS LESRNIGRPI EMSSKVQRFK
ATLWLSEEHP LSLGDQVTPI IDLMAISNAH FAKLRDFITL RLPPGFPVKI EIPLFHVLNA
RITFSNLCGC DEPVSSVCVP NSSSAISASG SPFPCEVDPT VFEVPEGYSV LGAERSEPLR
DEDDDLLQFA IQQSLLEAGT EAEQVTVWEA LTNTRPGIHP PPRVTVFEEQ LQLEQALQES
LQLSTESRGP ESPQKTPPSP APPSFEEQLR LALELSSREQ EELERRGQQE EDDLQRILQL
SLTEH