AN13D_HUMAN
ID AN13D_HUMAN Reviewed; 605 AA.
AC Q6ZTN6; D6RCN6; Q0VAK0; Q0VGC3; Q6ZVD0; Q86SU1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ankyrin repeat domain-containing protein 13D;
GN Name=ANKRD13D;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Blood, and Lung;
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=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP FUNCTION, INTERACTION WITH EGFR, UBIQUITIN-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22298428; DOI=10.1091/mbc.e11-09-0817;
RA Tanno H., Yamaguchi T., Goto E., Ishido S., Komada M.;
RT "The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor
RT endocytosis from the plasma membrane.";
RL Mol. Biol. Cell 23:1343-1353(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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. {ECO:0000269|PubMed:22298428}.
CC -!- SUBUNIT: Interacts with EGFR (ubiquitinated); the interaction is direct
CC and may regulate EGFR internalization. {ECO:0000269|PubMed:22298428}.
CC -!- INTERACTION:
CC Q6ZTN6-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-25840993, EBI-25840379;
CC Q6ZTN6-2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-25840993, EBI-12593112;
CC Q6ZTN6-2; P04792: HSPB1; NbExp=3; IntAct=EBI-25840993, EBI-352682;
CC Q6ZTN6-2; O43464: HTRA2; NbExp=3; IntAct=EBI-25840993, EBI-517086;
CC Q6ZTN6-2; P42858: HTT; NbExp=9; IntAct=EBI-25840993, EBI-466029;
CC Q6ZTN6-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25840993, EBI-1055254;
CC Q6ZTN6-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25840993, EBI-10975473;
CC Q6ZTN6-2; O14901: KLF11; NbExp=3; IntAct=EBI-25840993, EBI-948266;
CC Q6ZTN6-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-25840993, EBI-21251460;
CC Q6ZTN6-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25840993, EBI-396669;
CC Q6ZTN6-2; P37840: SNCA; NbExp=3; IntAct=EBI-25840993, EBI-985879;
CC Q6ZTN6-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25840993, EBI-5235340;
CC Q6ZTN6-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-25840993, EBI-372899;
CC Q6ZTN6-2; O76024: WFS1; NbExp=3; IntAct=EBI-25840993, EBI-720609;
CC Q6ZTN6-3; Q8IV28: NID2; NbExp=3; IntAct=EBI-13057940, EBI-10261509;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22298428}. Late
CC endosome {ECO:0000269|PubMed:22298428}. Note=Interaction with EGFR may
CC enhance association with the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q6ZTN6-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6ZTN6-1; Sequence=VSP_061476;
CC Name=2;
CC IsoId=Q6ZTN6-2; Sequence=VSP_061475;
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DR EMBL; AK124721; BAC85932.1; -; mRNA.
DR EMBL; AK126438; BAC86550.1; -; mRNA.
DR EMBL; AP001885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044239; AAH44239.1; -; mRNA.
DR EMBL; BC110419; AAI10420.1; -; mRNA.
DR EMBL; BC121024; AAI21025.1; -; mRNA.
DR EMBL; BC121025; AAI21026.1; -; mRNA.
DR CCDS; CCDS31616.2; -. [Q6ZTN6-3]
DR CCDS; CCDS86220.1; -. [Q6ZTN6-3]
DR RefSeq; NP_001334830.1; NM_001347901.1. [Q6ZTN6-1]
DR RefSeq; NP_997237.2; NM_207354.2. [Q6ZTN6-3]
DR AlphaFoldDB; Q6ZTN6; -.
DR SMR; Q6ZTN6; -.
DR BioGRID; 130781; 58.
DR IntAct; Q6ZTN6; 39.
DR STRING; 9606.ENSP00000427130; -.
DR iPTMnet; Q6ZTN6; -.
DR PhosphoSitePlus; Q6ZTN6; -.
DR BioMuta; ANKRD13D; -.
DR DMDM; 109940208; -.
DR EPD; Q6ZTN6; -.
DR jPOST; Q6ZTN6; -.
DR MassIVE; Q6ZTN6; -.
DR MaxQB; Q6ZTN6; -.
DR PaxDb; Q6ZTN6; -.
DR PeptideAtlas; Q6ZTN6; -.
DR PRIDE; Q6ZTN6; -.
DR ProteomicsDB; 68279; -. [Q6ZTN6-1]
DR ProteomicsDB; 68280; -. [Q6ZTN6-2]
DR ProteomicsDB; 68281; -. [Q6ZTN6-3]
DR Antibodypedia; 44541; 52 antibodies from 16 providers.
DR DNASU; 338692; -.
DR Ensembl; ENST00000511455.7; ENSP00000427130.2; ENSG00000172932.16. [Q6ZTN6-3]
DR GeneID; 338692; -.
DR KEGG; hsa:338692; -.
DR MANE-Select; ENST00000511455.7; ENSP00000427130.2; NM_207354.3; NP_997237.2.
DR UCSC; uc001okc.3; human. [Q6ZTN6-3]
DR CTD; 338692; -.
DR GeneCards; ANKRD13D; -.
DR HGNC; HGNC:27880; ANKRD13D.
DR HPA; ENSG00000172932; Low tissue specificity.
DR MIM; 615126; gene.
DR neXtProt; NX_Q6ZTN6; -.
DR OpenTargets; ENSG00000172932; -.
DR PharmGKB; PA142672618; -.
DR VEuPathDB; HostDB:ENSG00000172932; -.
DR eggNOG; KOG0522; Eukaryota.
DR GeneTree; ENSGT00950000182928; -.
DR HOGENOM; CLU_026137_2_0_1; -.
DR InParanoid; Q6ZTN6; -.
DR OMA; RICAPQE; -.
DR OrthoDB; 425969at2759; -.
DR PhylomeDB; Q6ZTN6; -.
DR TreeFam; TF314176; -.
DR PathwayCommons; Q6ZTN6; -.
DR SignaLink; Q6ZTN6; -.
DR BioGRID-ORCS; 338692; 13 hits in 1044 CRISPR screens.
DR ChiTaRS; ANKRD13D; human.
DR GenomeRNAi; 338692; -.
DR Pharos; Q6ZTN6; Tdark.
DR PRO; PR:Q6ZTN6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6ZTN6; protein.
DR Bgee; ENSG00000172932; Expressed in granulocyte and 164 other tissues.
DR ExpressionAtlas; Q6ZTN6; baseline and differential.
DR Genevisible; Q6ZTN6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140036; F:ubiquitin-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0002091; P:negative regulation of receptor internalization; IMP: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; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Endosome; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..605
FT /note="Ankyrin repeat domain-containing protein 13D"
FT /id="PRO_0000240651"
FT REPEAT 39..68
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 72..101
FT /note="ANK 2"
FT /evidence="ECO:0000255"
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 306..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Pro 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:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..357
FT /note="MAGPGPTFPLHRLVWANRHRELEAALHSHQHDIEQEDPRGRTPLELAVSLGN
FT LESVRVLLRHNANVGKENRQGWAVLQEAVSTGDPEMVQLVLQYRDYQRATQRLAGIPEL
FT LNKLRQAPDFYVEMKWEFTSWVPLVSKMCPSDVYRVWKRGESLRVDTSLLGFEHMTWQR
FT GRRSFIFKGQEAGALVMEVDHDRQVVHVETLGLTLQEPETLLAAMRPSEEHVASRLTSP
FT IVSTHLDTRNVAFERNKCGIWGWRSEKMETVSGYEAKVYSATNVELVTRTRTEHLSDQD
FT KSRSKAGKTPFQSFLGMAQQHSSHTGAPVQQAASPTNPTAISPEEYFDPNFSLESRNIG
FT RPIEMSSKVQ -> MSCGRLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_061475"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_061476"
FT CONFLICT 166
FT /note="M -> V (in Ref. 1; BAC85932)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="G -> R (in Ref. 1; BAC86550)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="P -> S (in Ref. 1; BAC86550)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="L -> F (in Ref. 3; AAI10420)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="D -> Y (in Ref. 1; BAC86550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 68172 MW; 27F91C1518642550 CRC64;
MAGPGPTFPL HRLVWANRHR ELEAALHSHQ HDIEQEDPRG RTPLELAVSL GNLESVRVLL
RHNANVGKEN RQGWAVLQEA VSTGDPEMVQ LVLQYRDYQR ATQRLAGIPE LLNKLRQAPD
FYVEMKWEFT SWVPLVSKMC PSDVYRVWKR GESLRVDTSL LGFEHMTWQR GRRSFIFKGQ
EAGALVMEVD HDRQVVHVET LGLTLQEPET LLAAMRPSEE HVASRLTSPI VSTHLDTRNV
AFERNKCGIW GWRSEKMETV SGYEAKVYSA TNVELVTRTR TEHLSDQDKS RSKAGKTPFQ
SFLGMAQQHS SHTGAPVQQA ASPTNPTAIS PEEYFDPNFS LESRNIGRPI EMSSKVQRFK
ATLWLSEEHP LSLGDQVTPI IDLMAISNAH FAKLRDFITL RLPPGFPVKI EIPLFHVLNA
RITFSNLCGC DEPLSSVWVP APSSAVAASG NPFPCEVDPT VFEVPNGYSV LGMERNEPLR
DEDDDLLQFA IQQSLLEAGT EAEQVTVWEA LTNTRPGARP PPQATVYEEQ LQLERALQES
LQLSTEPRGP GSPPRTPPAP GPPSFEEQLR LALELSSREQ EERERRGQQE EEDLQRILQL
SLTEH
