AN13B_HUMAN
ID AN13B_HUMAN Reviewed; 626 AA.
AC Q86YJ7; Q8N7S9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ankyrin repeat domain-containing protein 13B;
GN Name=ANKRD13B;
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 2).
RC TISSUE=Testis;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22298428}. Late
CC endosome {ECO:0000269|PubMed:22298428}. Early endosome
CC {ECO:0000269|PubMed:22298428}. Note=Interaction with EGFR may enhance
CC association with the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YJ7-2; Sequence=VSP_019404;
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DR EMBL; AK097716; BAC05148.1; -; mRNA.
DR EMBL; AC104564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032554; AAH32554.3; -; mRNA.
DR CCDS; CCDS11251.1; -. [Q86YJ7-1]
DR RefSeq; NP_689558.4; NM_152345.4. [Q86YJ7-1]
DR AlphaFoldDB; Q86YJ7; -.
DR SMR; Q86YJ7; -.
DR BioGRID; 125900; 11.
DR IntAct; Q86YJ7; 6.
DR STRING; 9606.ENSP00000378328; -.
DR iPTMnet; Q86YJ7; -.
DR PhosphoSitePlus; Q86YJ7; -.
DR BioMuta; ANKRD13B; -.
DR DMDM; 269849747; -.
DR jPOST; Q86YJ7; -.
DR MassIVE; Q86YJ7; -.
DR MaxQB; Q86YJ7; -.
DR PaxDb; Q86YJ7; -.
DR PeptideAtlas; Q86YJ7; -.
DR PRIDE; Q86YJ7; -.
DR ProteomicsDB; 70426; -. [Q86YJ7-1]
DR ProteomicsDB; 70427; -. [Q86YJ7-2]
DR Antibodypedia; 26768; 59 antibodies from 18 providers.
DR DNASU; 124930; -.
DR Ensembl; ENST00000394859.8; ENSP00000378328.3; ENSG00000198720.13. [Q86YJ7-1]
DR Ensembl; ENST00000488766.5; ENSP00000431958.1; ENSG00000198720.13. [Q86YJ7-1]
DR Ensembl; ENST00000614878.4; ENSP00000481530.1; ENSG00000198720.13. [Q86YJ7-1]
DR GeneID; 124930; -.
DR KEGG; hsa:124930; -.
DR MANE-Select; ENST00000394859.8; ENSP00000378328.3; NM_152345.5; NP_689558.4.
DR UCSC; uc002hei.4; human. [Q86YJ7-1]
DR CTD; 124930; -.
DR DisGeNET; 124930; -.
DR GeneCards; ANKRD13B; -.
DR HGNC; HGNC:26363; ANKRD13B.
DR HPA; ENSG00000198720; Low tissue specificity.
DR MIM; 615124; gene.
DR neXtProt; NX_Q86YJ7; -.
DR OpenTargets; ENSG00000198720; -.
DR PharmGKB; PA142672616; -.
DR VEuPathDB; HostDB:ENSG00000198720; -.
DR eggNOG; KOG0522; Eukaryota.
DR GeneTree; ENSGT00950000182928; -.
DR HOGENOM; CLU_026137_2_0_1; -.
DR InParanoid; Q86YJ7; -.
DR OMA; GYMKKIF; -.
DR OrthoDB; 425969at2759; -.
DR PhylomeDB; Q86YJ7; -.
DR TreeFam; TF314176; -.
DR PathwayCommons; Q86YJ7; -.
DR SignaLink; Q86YJ7; -.
DR BioGRID-ORCS; 124930; 20 hits in 1080 CRISPR screens.
DR GenomeRNAi; 124930; -.
DR Pharos; Q86YJ7; Tdark.
DR PRO; PR:Q86YJ7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q86YJ7; protein.
DR Bgee; ENSG00000198720; Expressed in right hemisphere of cerebellum and 157 other tissues.
DR ExpressionAtlas; Q86YJ7; baseline and differential.
DR Genevisible; Q86YJ7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
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; 3.
DR SMART; SM00726; UIM; 2.
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 Acetylation; Alternative splicing; ANK repeat; Cell membrane; Endosome;
KW Membrane; Reference proteome; Repeat.
FT CHAIN 1..626
FT /note="Ankyrin repeat domain-containing protein 13B"
FT /id="PRO_0000240643"
FT REPEAT 47..76
FT /note="ANK 1"
FT REPEAT 80..109
FT /note="ANK 2"
FT DOMAIN 503..522
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 585..604
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 610..626
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 442..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019404"
FT CONFLICT 126
FT /note="A -> P (in Ref. 3; AAH32554)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="Q -> H (in Ref. 3; AAH32554)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> E (in Ref. 1; BAC05148)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="Q -> R (in Ref. 1; BAC05148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 70205 MW; 8807A784A21F395C CRC64;
MIPANASARK GPEGKYPLHY LVWHNRHREL EKEVRAGQVD IEQLDPRGRT PLHLATTLGH
LECARVLLAH GADVGRENRS GWTVLQEAVS TRDLELVQLV LRYRDYQRVV KRLAGIPVLL
EKLRKAQDFY VEMKWEFTSW VPLVSKICPS DTYKVWKSGQ NLRVDTTLLG FDHMTWQRGN
RSFVFRGQDT SAVVMEIDHD RRVVYTETLA LAGQDRELLL AAAQPTEEQV LSRLTAPVVT
TQLDTKNISF ERNKTGILGW RSEKTEMVNG YEAKVYGASN VELITRTRTE HLSEQHKGKV
KGCKTPLQSF LGIAEQHGGP QNGTLITQTL SQANPTAITA EEYFNPNFEL GNRDMGRPME
LTTKTQKFKA KLWLCEEHPL SLCEQVAPII DLMAVSNALF AKLRDFITLR LPPGFPVKIE
IPIFHILNAR ITFGNLNGCD EPVPSVRGSP SSETPSPGSD SSSVSSSSST TSCRGCEISP
ALFEAPRGYS MMGGQREAAT RDDDDDLLQF AIQQSLLEAG SEYDQVTIWE ALTNSKPGTH
PMSYEGRRQD RSAPPTPQRQ PAPPASVPSP RPSSGPGSGG HVFRSYDEQL RLAMELSAQE
QEERRRRARQ EEEELERILR LSLTEQ
