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Database: UniProt
Entry: AN13A_MOUSE
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Original site: 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   27-MAR-2024, entry version 140.
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; 2.
DR   IntAct; Q80UP5; 1.
DR   STRING; 10090.ENSMUSP00000099638; -.
DR   iPTMnet; Q80UP5; -.
DR   PhosphoSitePlus; Q80UP5; -.
DR   EPD; Q80UP5; -.
DR   MaxQB; Q80UP5; -.
DR   PaxDb; 10090-ENSMUSP00000099638; -.
DR   ProteomicsDB; 282088; -.
DR   Pumba; Q80UP5; -.
DR   Antibodypedia; 49620; 107 antibodies from 18 providers.
DR   DNASU; 68420; -.
DR   Ensembl; ENSMUST00000102578.11; ENSMUSP00000099638.5; ENSMUSG00000041870.18.
DR   GeneID; 68420; -.
DR   KEGG; mmu:68420; -.
DR   UCSC; uc008zaf.1; mouse.
DR   AGR; MGI:1915670; -.
DR   CTD; 88455; -.
DR   MGI; MGI:1915670; Ankrd13a.
DR   VEuPathDB; HostDB:ENSMUSG00000041870; -.
DR   eggNOG; KOG0522; Eukaryota.
DR   GeneTree; ENSGT00950000182928; -.
DR   InParanoid; Q80UP5; -.
DR   OMA; INQTHAY; -.
DR   OrthoDB; 20116at2759; -.
DR   PhylomeDB; Q80UP5; -.
DR   TreeFam; TF314176; -.
DR   BioGRID-ORCS; 68420; 3 hits in 77 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 259 other cell types or 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; Ankyrin repeat-containing domain; 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; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13; 1.
DR   PANTHER; PTHR12447:SF4; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13A; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF11904; GPCR_chapero_1; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00726; UIM; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 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
//
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