TB10A_HUMAN
ID TB10A_HUMAN Reviewed; 508 AA.
AC Q9BXI6; B3KXT8; O76053; Q20WK7; Q543A2;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=TBC1 domain family member 10A;
DE AltName: Full=EBP50-PDX interactor of 64 kDa;
DE Short=EPI64 protein;
DE AltName: Full=Rab27A-GAP-alpha;
GN Name=TBC1D10A; Synonyms=EPI64, TBC1D10;
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 [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP MUTAGENESIS.
RX PubMed=11285285; DOI=10.1083/jcb.153.1.191;
RA Reczek D., Bretscher A.;
RT "Identification of EPI64, a TBC/rabGAP domain-containing microvillar
RT protein that binds to the first PDZ domain of EBP50 and E3KARP.";
RL J. Cell Biol. 153:191-206(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland, and Synovium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-157 AND ARG-160.
RX PubMed=16923811; DOI=10.1074/jbc.m603808200;
RA Itoh T., Fukuda M.;
RT "Identification of EPI64 as a GTPase-activating protein specific for
RT Rab27A.";
RL J. Biol. Chem. 281:31823-31831(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP 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 [11]
RP IDENTIFICATION BY MASS 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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP 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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB27A, but not for
CC RAB2A, RAB3A, nor RAB4A. {ECO:0000269|PubMed:16923811}.
CC -!- SUBUNIT: Binds to the first PDZ domain of SLC9A3R1 and SLC9A3R2.
CC -!- INTERACTION:
CC Q9BXI6; Q96AP0: ACD; NbExp=2; IntAct=EBI-7815040, EBI-717666;
CC Q9BXI6; Q9BXU3: TEX13A; NbExp=6; IntAct=EBI-7815040, EBI-10301068;
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus
CC {ECO:0000269|PubMed:16923811}. Note=Localizes to the microvilli-rich
CC region of the syncytiotrophoblast. In melanocytes, located at the
CC periphery of cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXI6-2; Sequence=VSP_043119;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- PTM: Exists in both phosphorylated and non-phosphorylated state.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF331038; AAK35048.1; -; mRNA.
DR EMBL; AB449894; BAH16637.1; -; mRNA.
DR EMBL; CT841514; CAJ86444.1; -; mRNA.
DR EMBL; AK074656; BAC11117.1; -; mRNA.
DR EMBL; AK127939; BAG54600.1; -; mRNA.
DR EMBL; AC004997; AAC23434.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471095; EAW59874.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59876.1; -; Genomic_DNA.
DR EMBL; BC136815; AAI36816.1; -; mRNA.
DR EMBL; BC142940; AAI42941.1; -; mRNA.
DR EMBL; BC150214; AAI50215.1; -; mRNA.
DR CCDS; CCDS13874.1; -. [Q9BXI6-1]
DR CCDS; CCDS56227.1; -. [Q9BXI6-2]
DR RefSeq; NP_001191169.1; NM_001204240.1. [Q9BXI6-2]
DR RefSeq; NP_114143.1; NM_031937.2. [Q9BXI6-1]
DR AlphaFoldDB; Q9BXI6; -.
DR SMR; Q9BXI6; -.
DR BioGRID; 123787; 30.
DR IntAct; Q9BXI6; 13.
DR MINT; Q9BXI6; -.
DR STRING; 9606.ENSP00000384996; -.
DR iPTMnet; Q9BXI6; -.
DR PhosphoSitePlus; Q9BXI6; -.
DR BioMuta; TBC1D10A; -.
DR DMDM; 20454903; -.
DR EPD; Q9BXI6; -.
DR jPOST; Q9BXI6; -.
DR MassIVE; Q9BXI6; -.
DR MaxQB; Q9BXI6; -.
DR PaxDb; Q9BXI6; -.
DR PeptideAtlas; Q9BXI6; -.
DR PRIDE; Q9BXI6; -.
DR ProteomicsDB; 79427; -. [Q9BXI6-1]
DR ProteomicsDB; 79428; -. [Q9BXI6-2]
DR Antibodypedia; 220; 129 antibodies from 22 providers.
DR DNASU; 83874; -.
DR Ensembl; ENST00000215790.12; ENSP00000215790.8; ENSG00000099992.16. [Q9BXI6-1]
DR Ensembl; ENST00000403477.7; ENSP00000384996.3; ENSG00000099992.16. [Q9BXI6-2]
DR GeneID; 83874; -.
DR KEGG; hsa:83874; -.
DR MANE-Select; ENST00000215790.12; ENSP00000215790.8; NM_031937.3; NP_114143.1.
DR UCSC; uc003ahk.5; human. [Q9BXI6-1]
DR CTD; 83874; -.
DR DisGeNET; 83874; -.
DR GeneCards; TBC1D10A; -.
DR HGNC; HGNC:23609; TBC1D10A.
DR HPA; ENSG00000099992; Low tissue specificity.
DR MIM; 610020; gene.
DR neXtProt; NX_Q9BXI6; -.
DR OpenTargets; ENSG00000099992; -.
DR PharmGKB; PA134888210; -.
DR VEuPathDB; HostDB:ENSG00000099992; -.
DR eggNOG; KOG2221; Eukaryota.
DR GeneTree; ENSGT00940000157386; -.
DR InParanoid; Q9BXI6; -.
DR OMA; KWLYMID; -.
DR PhylomeDB; Q9BXI6; -.
DR TreeFam; TF313293; -.
DR PathwayCommons; Q9BXI6; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q9BXI6; -.
DR BioGRID-ORCS; 83874; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; TBC1D10A; human.
DR GeneWiki; TBC1D10A; -.
DR GenomeRNAi; 83874; -.
DR Pharos; Q9BXI6; Tbio.
DR PRO; PR:Q9BXI6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9BXI6; protein.
DR Bgee; ENSG00000099992; Expressed in nasal cavity epithelium and 164 other tissues.
DR ExpressionAtlas; Q9BXI6; baseline and differential.
DR Genevisible; Q9BXI6; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Direct protein sequencing;
KW GTPase activation; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..508
FT /note="TBC1 domain family member 10A"
FT /id="PRO_0000208035"
FT DOMAIN 111..299
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..508
FT /note="Binding to the PDZ domain of EBP50"
FT COMPBIAS 21..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 156
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58802"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58802"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 70
FT /note="A -> APCPLLHR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043119"
FT VARIANT 411
FT /note="R -> H (in dbSNP:rs4823086)"
FT /id="VAR_052541"
FT MUTAGEN 157
FT /note="D->A: Loss of activity. No effect on subcellular
FT location."
FT /evidence="ECO:0000269|PubMed:16923811"
FT MUTAGEN 160
FT /note="R->K: Loss of activity. No effect on subcellular
FT location."
FT /evidence="ECO:0000269|PubMed:16923811"
FT MUTAGEN 508
FT /note="L->LA: Loss of interaction with EBP50 and impaired
FT subcellular localization."
FT /evidence="ECO:0000269|PubMed:11285285"
SQ SEQUENCE 508 AA; 57118 MW; 17BFAA85BE86DE84 CRC64;
MAKSNGENGP RAPAAGESLS GTRESLAQGP DAATTDELSS LGSDSEANGF AERRIDKFGF
IVGSQGAEGA LEEVPLEVLR QRESKWLDML NNWDKWMAKK HKKIRLRCQK GIPPSLRGRA
WQYLSGGKVK LQQNPGKFDE LDMSPGDPKW LDVIERDLHR QFPFHEMFVS RGGHGQQDLF
RVLKAYTLYR PEEGYCQAQA PIAAVLLMHM PAEQAFWCLV QICEKYLPGY YSEKLEAIQL
DGEILFSLLQ KVSPVAHKHL SRQKIDPLLY MTEWFMCAFS RTLPWSSVLR VWDMFFCEGV
KIIFRVGLVL LKHALGSPEK VKACQGQYET IERLRSLSPK IMQEAFLVQE VVELPVTERQ
IEREHLIQLR RWQETRGELQ CRSPPRLHGA KAILDAEPGP RPALQPSPSI RLPLDAPLPG
SKAKPKPPKQ AQKEQRKQMK GRGQLEKPPA PNQAMVVAAA GDACPPQHVP PKDSAPKDSA
PQDLAPQVSA HHRSQESLTS QESEDTYL
