TBD2A_HUMAN
ID TBD2A_HUMAN Reviewed; 928 AA.
AC Q9BYX2; B3KWD1; B4DQ05; B9A6J7; Q59EU0; Q5TBQ5; Q6IPC7; Q7L1K8; Q8WYT1;
AC Q9H6A2; Q9NSH4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=TBC1 domain family member 2A;
DE AltName: Full=Armus;
DE AltName: Full=Prostate antigen recognized and identified by SEREX 1;
DE Short=PARIS-1;
GN Name=TBC1D2; Synonyms=PARIS1, PP8997, TBC1D2A;
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 2), TISSUE SPECIFICITY, AND VARIANT
RP SER-253.
RX PubMed=11785977; DOI=10.1006/bbrc.2001.6257;
RA Zhou Y., Toth M., Hamman M.S., Monahan S.J., Lodge P.A., Boynton A.L.,
RA Salgaller M.L.;
RT "Serological cloning of PARIS-1: a new TBC domain-containing, immunogenic
RT tumor antigen from a prostate cancer cell line.";
RL Biochem. Biophys. Res. Commun. 290:830-838(2002).
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 [MRNA] (ISOFORM 3).
RA Jiang H.Q., Zhou X.M., Zhang P.P., Huang Y., Qin W.X., Zhao X.T., Wan D.F.,
RA Gu J.R.;
RT "Novel human cDNA clones with function of inhibiting cancer cell growth.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS
RP THR-241; SER-253 AND VAL-261.
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 MRNA] (ISOFORM 6).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-261.
RC TISSUE=Brain;
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-459, AND VARIANT VAL-261.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915 AND SER-920, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-920, 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 [12]
RP FUNCTION, INTERACTION WITH RAC1 AND CDH1, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20116244; DOI=10.1016/j.cub.2009.12.053;
RA Frasa M.A., Maximiano F.C., Smolarczyk K., Francis R.E., Betson M.E.,
RA Lozano E., Goldenring J., Seabra M.C., Rak A., Ahmadian M.R., Braga V.M.;
RT "Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin
RT degradation.";
RL Curr. Biol. 20:198-208(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
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).
RN [15]
RP STRUCTURE BY NMR OF 46-151.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of TBC1 domain family member 2 protein
RT from human.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB7A. Signal effector
CC acting as a linker between RAC1 and RAB7A, leading to RAB7A
CC inactivation and subsequent inhibition of cadherin degradation and
CC reduced cell-cell adhesion. {ECO:0000269|PubMed:20116244}.
CC -!- SUBUNIT: Interacts with activated RAC1 and CDH1.
CC {ECO:0000269|PubMed:20116244}.
CC -!- INTERACTION:
CC Q9BYX2-5; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-13560915, EBI-2511344;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20116244}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:20116244}. Cell junction
CC {ECO:0000269|PubMed:20116244}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=A variant C;
CC IsoId=Q9BYX2-1; Sequence=Displayed;
CC Name=2; Synonyms=PARIS-1;
CC IsoId=Q9BYX2-2; Sequence=VSP_039382;
CC Name=3; Synonyms=A;
CC IsoId=Q9BYX2-3; Sequence=VSP_039383;
CC Name=4;
CC IsoId=Q9BYX2-4; Sequence=VSP_039381;
CC Name=5;
CC IsoId=Q9BYX2-5; Sequence=VSP_039380;
CC Name=6;
CC IsoId=Q9BYX2-6; Sequence=VSP_039379;
CC -!- TISSUE SPECIFICITY: Expressed in a broad range of tissues, especially
CC in kidney, liver, lung and placenta. Also expressed in keratinocytes
CC and epithelia-containing organs. Isoform 2 is differentially expressed
CC in prostate normal and cancer cells (at protein level).
CC {ECO:0000269|PubMed:11785977, ECO:0000269|PubMed:20116244}.
CC -!- MISCELLANEOUS: 'Armus' means hinge, linker in Latin and ancient Greek.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB89247.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY026527; AAK07684.1; -; mRNA.
DR EMBL; AB449882; BAH16625.1; -; mRNA.
DR EMBL; AF318370; AAL55877.1; -; mRNA.
DR EMBL; AK026105; BAB15361.1; -; mRNA.
DR EMBL; AK124772; BAG54093.1; -; mRNA.
DR EMBL; AK298575; BAG60767.1; -; mRNA.
DR EMBL; AL353935; CAB89247.2; ALT_INIT; mRNA.
DR EMBL; AL137073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58882.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58884.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58887.1; -; Genomic_DNA.
DR EMBL; BC028918; AAH28918.1; -; mRNA.
DR EMBL; BC071978; AAH71978.1; -; mRNA.
DR EMBL; AB209721; BAD92958.1; -; mRNA.
DR CCDS; CCDS35080.1; -. [Q9BYX2-2]
DR CCDS; CCDS59137.1; -. [Q9BYX2-6]
DR CCDS; CCDS75865.1; -. [Q9BYX2-1]
DR PIR; JC7799; JC7799.
DR PIR; T48686; T48686.
DR RefSeq; NP_001254500.1; NM_001267571.1. [Q9BYX2-1]
DR RefSeq; NP_001254501.1; NM_001267572.1. [Q9BYX2-6]
DR RefSeq; NP_060891.3; NM_018421.3. [Q9BYX2-2]
DR RefSeq; XP_011517145.1; XM_011518843.1. [Q9BYX2-6]
DR PDB; 2DHK; NMR; -; A=46-151.
DR PDBsum; 2DHK; -.
DR AlphaFoldDB; Q9BYX2; -.
DR BMRB; Q9BYX2; -.
DR SMR; Q9BYX2; -.
DR BioGRID; 120637; 33.
DR IntAct; Q9BYX2; 9.
DR MINT; Q9BYX2; -.
DR STRING; 9606.ENSP00000481721; -.
DR iPTMnet; Q9BYX2; -.
DR PhosphoSitePlus; Q9BYX2; -.
DR BioMuta; TBC1D2; -.
DR DMDM; 300669706; -.
DR EPD; Q9BYX2; -.
DR jPOST; Q9BYX2; -.
DR MassIVE; Q9BYX2; -.
DR MaxQB; Q9BYX2; -.
DR PaxDb; Q9BYX2; -.
DR PeptideAtlas; Q9BYX2; -.
DR PRIDE; Q9BYX2; -.
DR ProteomicsDB; 79734; -. [Q9BYX2-1]
DR ProteomicsDB; 79735; -. [Q9BYX2-2]
DR ProteomicsDB; 79736; -. [Q9BYX2-3]
DR ProteomicsDB; 79737; -. [Q9BYX2-4]
DR ProteomicsDB; 79738; -. [Q9BYX2-5]
DR ProteomicsDB; 79739; -. [Q9BYX2-6]
DR Antibodypedia; 28952; 107 antibodies from 23 providers.
DR DNASU; 55357; -.
DR Ensembl; ENST00000342112.9; ENSP00000341567.5; ENSG00000095383.20. [Q9BYX2-4]
DR Ensembl; ENST00000375063.5; ENSP00000364203.1; ENSG00000095383.20. [Q9BYX2-6]
DR Ensembl; ENST00000375064.5; ENSP00000364205.1; ENSG00000095383.20. [Q9BYX2-3]
DR Ensembl; ENST00000375066.6; ENSP00000364207.5; ENSG00000095383.20. [Q9BYX2-2]
DR Ensembl; ENST00000465784.7; ENSP00000481721.1; ENSG00000095383.20. [Q9BYX2-1]
DR GeneID; 55357; -.
DR KEGG; hsa:55357; -.
DR MANE-Select; ENST00000465784.7; ENSP00000481721.1; NM_001267571.2; NP_001254500.1.
DR UCSC; uc004ayp.5; human. [Q9BYX2-1]
DR CTD; 55357; -.
DR DisGeNET; 55357; -.
DR GeneCards; TBC1D2; -.
DR HGNC; HGNC:18026; TBC1D2.
DR HPA; ENSG00000095383; Low tissue specificity.
DR MIM; 609871; gene.
DR neXtProt; NX_Q9BYX2; -.
DR OpenTargets; ENSG00000095383; -.
DR PharmGKB; PA38280; -.
DR VEuPathDB; HostDB:ENSG00000095383; -.
DR eggNOG; KOG2058; Eukaryota.
DR GeneTree; ENSGT00940000159937; -.
DR HOGENOM; CLU_578202_0_0_1; -.
DR InParanoid; Q9BYX2; -.
DR OMA; KTICNSR; -.
DR OrthoDB; 1162786at2759; -.
DR PhylomeDB; Q9BYX2; -.
DR TreeFam; TF317336; -.
DR PathwayCommons; Q9BYX2; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q9BYX2; -.
DR BioGRID-ORCS; 55357; 7 hits in 1081 CRISPR screens.
DR ChiTaRS; TBC1D2; human.
DR EvolutionaryTrace; Q9BYX2; -.
DR GenomeRNAi; 55357; -.
DR Pharos; Q9BYX2; Tbio.
DR PRO; PR:Q9BYX2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BYX2; protein.
DR Bgee; ENSG00000095383; Expressed in monocyte and 161 other tissues.
DR ExpressionAtlas; Q9BYX2; baseline and differential.
DR Genevisible; Q9BYX2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..928
FT /note="TBC1 domain family member 2A"
FT /id="PRO_0000208024"
FT DOMAIN 45..142
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 625..817
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..169
FT /note="Interaction with CADH1"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..433
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000269|PubMed:20116244"
FT COILED 298..416
FT /evidence="ECO:0000255"
FT COILED 875..913
FT /evidence="ECO:0000255"
FT COMPBIAS 25..39
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 MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..460
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_039379"
FT VAR_SEQ 1..435
FT /note="MEGAGENAPESSSSAPGSEESARDPQVPPPEEESGDCARSLEAVPKKLCGYL
FT SKFGGKGPIRGWKSRWFFYDERKCQLYYSRTAQDANPLDSIDLSSAVFDCKADAEEGIF
FT EIKTPSRVITLKAATKQAMLYWLQQLQMKRWEFHNSPPAPPATPDAALAGNGPVLHLEL
FT GQEEAELEEFLCPVKTPPGLVGVAAALQPFPALQNISLKHLGTEIQNTMHNIRGNKQAQ
FT GTGHEPPGEDSPQSGEPQREEQPLASDASTPGREPEDSPKPAPKPSLTISFAQKAKRQN
FT NTFPFFSEGITRNRTAQEKVAALEQQVLMLTKELKSQKELVKILHKALEAAQQEKRASS
FT AYLAAAEDKDRLELVRHKVRQIAELGRRVEALEQERESLAHTASLREQQVQELQQHVQL
FT LMDKNHAKQQVICKLSEKVTQDFTHPPDQ -> MPIPWTAST (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039380"
FT VAR_SEQ 1..218
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039381"
FT VAR_SEQ 820..830
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11785977"
FT /id="VSP_039382"
FT VAR_SEQ 861..928
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_039383"
FT VARIANT 241
FT /note="P -> T (in dbSNP:rs879368)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_046707"
FT VARIANT 253
FT /note="L -> S (in dbSNP:rs879369)"
FT /evidence="ECO:0000269|PubMed:11785977,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_046708"
FT VARIANT 261
FT /note="G -> V (in dbSNP:rs1573025)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15164053, ECO:0000269|Ref.9"
FT /id="VAR_046709"
FT CONFLICT 189..195
FT /note="Missing (in Ref. 4; BAG60767)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="D -> F (in Ref. 9; BAD92958)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="S -> F (in Ref. 1; AAK07684)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="V -> A (in Ref. 4; BAG54093)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="Q -> H (in Ref. 3; AAL55877)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="I -> T (in Ref. 4; BAG60767)"
FT /evidence="ECO:0000305"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:2DHK"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2DHK"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2DHK"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2DHK"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:2DHK"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2DHK"
SQ SEQUENCE 928 AA; 105414 MW; 08D7BC167B234CDA CRC64;
MEGAGENAPE SSSSAPGSEE SARDPQVPPP EEESGDCARS LEAVPKKLCG YLSKFGGKGP
IRGWKSRWFF YDERKCQLYY SRTAQDANPL DSIDLSSAVF DCKADAEEGI FEIKTPSRVI
TLKAATKQAM LYWLQQLQMK RWEFHNSPPA PPATPDAALA GNGPVLHLEL GQEEAELEEF
LCPVKTPPGL VGVAAALQPF PALQNISLKH LGTEIQNTMH NIRGNKQAQG TGHEPPGEDS
PQSGEPQREE QPLASDASTP GREPEDSPKP APKPSLTISF AQKAKRQNNT FPFFSEGITR
NRTAQEKVAA LEQQVLMLTK ELKSQKELVK ILHKALEAAQ QEKRASSAYL AAAEDKDRLE
LVRHKVRQIA ELGRRVEALE QERESLAHTA SLREQQVQEL QQHVQLLMDK NHAKQQVICK
LSEKVTQDFT HPPDQSPLRP DAANRDFLSQ QGKIEHLKDD MEAYRTQNCF LNSEIHQVTK
IWRKVAEKEK ALLTKCAYLQ ARNCQVESKY LAGLRRLQEA LGDEASECSE LLRQLVQEAL
QWEAGEASSD SIELSPISKY DEYGFLTVPD YEVEDLKLLA KIQALESRSH HLLGLEAVDR
PLRERWAALG DLVPSAELKQ LLRAGVPREH RPRVWRWLVH LRVQHLHTPG CYQELLSRGQ
AREHPAARQI ELDLNRTFPN NKHFTCPTSS FPDKLRRVLL AFSWQNPTIG YCQGLNRLAA
IALLVLEEEE SAFWCLVAIV ETIMPADYYC NTLTASQVDQ RVLQDLLSEK LPRLMAHLGQ
HHVDLSLVTF NWFLVVFADS LISNILLRVW DAFLYEGTKV VFRYALAIFK YNEKEILRLQ
NGLEIYQYLR FFTKTISNSR KLMNIAFNDM NPFRMKQLRQ LRMVHRERLE AELRELEQLK
AEYLERRASR RRAVSEGCAS EDEVEGEA
