AN13A_MOUSE
ID AN13A_MOUSE Reviewed; 588 AA.
AC Q80UP5; Q2VPQ7; Q6P7F2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ankyrin repeat domain-containing protein 13A;
GN Name=Ankrd13a; Synonyms=Ankrd13;
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 MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor, and Olfactory epithelium;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, 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: 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 (via the UIM 3 and 4 repeats) with EGFR
CC (ubiquitinated); the interaction is direct, inhibited by ANKRD13A
CC monoubiquitination and may regulate EGFR internalization.
CC {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 -!- DOMAIN: The UIM repeats 3 and 4 are required for binding to
CC ubiquitinated EGFR and 'Lys-63'-linked ubiquitin. {ECO:0000250}.
CC -!- PTM: Monoubiquitinated, inhibits interaction with ubiquitinated EGFR.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49187.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC049187; AAH49187.1; ALT_INIT; mRNA.
DR EMBL; BC061692; AAH61692.1; -; mRNA.
DR EMBL; BC108413; AAI08414.1; -; mRNA.
DR CCDS; CCDS19572.1; -.
DR RefSeq; NP_080994.2; NM_026718.2.
DR AlphaFoldDB; Q80UP5; -.
DR SMR; Q80UP5; -.
DR BioGRID; 212845; 1.
DR IntAct; Q80UP5; 1.
DR STRING; 10090.ENSMUSP00000099638; -.
DR iPTMnet; Q80UP5; -.
DR PhosphoSitePlus; Q80UP5; -.
DR EPD; Q80UP5; -.
DR MaxQB; Q80UP5; -.
DR PaxDb; Q80UP5; -.
DR PRIDE; Q80UP5; -.
DR ProteomicsDB; 282088; -.
DR Antibodypedia; 49620; 81 antibodies from 17 providers.
DR DNASU; 68420; -.
DR Ensembl; ENSMUST00000102578; ENSMUSP00000099638; ENSMUSG00000041870.
DR GeneID; 68420; -.
DR KEGG; mmu:68420; -.
DR UCSC; uc008zaf.1; mouse.
DR CTD; 88455; -.
DR MGI; MGI:1915670; Ankrd13a.
DR VEuPathDB; HostDB:ENSMUSG00000041870; -.
DR eggNOG; KOG0522; Eukaryota.
DR GeneTree; ENSGT00950000182928; -.
DR InParanoid; Q80UP5; -.
DR OMA; HSYEAQY; -.
DR OrthoDB; 425969at2759; -.
DR PhylomeDB; Q80UP5; -.
DR TreeFam; TF314176; -.
DR BioGRID-ORCS; 68420; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ankrd13a; mouse.
DR PRO; PR:Q80UP5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80UP5; protein.
DR Bgee; ENSMUSG00000041870; Expressed in granulocyte and 255 other tissues.
DR ExpressionAtlas; Q80UP5; baseline and differential.
DR Genevisible; Q80UP5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
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:1905667; P:negative regulation of protein localization to endosome; 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; PF13637; Ank_4; 1.
DR Pfam; PF11904; GPCR_chapero_1; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00726; UIM; 3.
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 ANK repeat; Cell membrane; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..588
FT /note="Ankyrin repeat domain-containing protein 13A"
FT /id="PRO_0000066910"
FT REPEAT 40..69
FT /note="ANK 1"
FT REPEAT 73..102
FT /note="ANK 2"
FT DOMAIN 481..500
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 517..536
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 547..566
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 572..588
FT /note="UIM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ07"
SQ SEQUENCE 588 AA; 67177 MW; 70F5B9E0588DECF9 CRC64;
MSSARDTSSR FPLHLLVWNN DYEQLEKELR DQNAEALDPR GRTLLHLAVS LGHLESARVL
LRHKADVTKE NGQGWTVLHE AVSTGDPEMV YTVLQHRDYH NTSMALEGVP ELLHKILEAP
DFYVQMKWEF TSWVPLVSRI CPNDVCRIWK SGAKLRVDIT LLGFENMSWI RGRRSFIFKG
GDNWAELMEV NHDDRVVTTE HFDLSQEMER LTLDLMKPKS REVERRLTSP VINTSLDTKN
VAFERTKSGF WGWRTDKAEV VNGYEAKVYS VNNVSVITRI RTEHLTEEEK KRYKEDRNPL
ESLLGTVEHQ FGAQGDLATE CATVNNPTAI TPDEYFDEDF DLKDRDIGRP KELTIRTQKF
KATLWMCEEF PLSLVEQVIP IIDLMARTSA HFARLRDFIK LDFPPGFPVK IEIPLFHVLN
ARITFGNVNG CSTADESQGV EGTPAEAVSE ATNFEVDQSV FEIPESYHIQ DNGRNVHLQD
EDYEIMQFAI QQSLLESSRS QDLSGPASNG GVSHTHSYEA QYERAIQESL LTNMEGRCPG
GLSESSRFDS DLQLAMELSA KELAERELRL QEEEAELQQV LQLSLTEK
