TB22B_HUMAN
ID TB22B_HUMAN Reviewed; 505 AA.
AC Q9NU19; A8KA28; Q32MQ8; Q5VUK9; Q6P4C3; Q7Z6P7; Q9BPV6; Q9BUT5; Q9NXB6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=TBC1 domain family member 22B;
GN Name=TBC1D22B; Synonyms=C6orf197;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shan Y.X., Huang C.Q., Guo Z.K., Ye M.G., Yu L.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, Lung, and Uterus;
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 [7]
RP PROTEIN SEQUENCE OF 2-293; 346-421 AND 454-505, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-154, INTERACTION
RP WITH ACBD3; ARFGEF1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ,
RP MUTAGENESIS OF SER-58; 88-LEU--SER-90; 91-LYS-VAL-92; 94-LEU--THR-96;
RP GLN-99; 100-VAL-LEU-101; 102-GLU--HIS-104; SER-114; 116-SER--SER-119;
RP 140-SER-SER-141; THR-143 AND SER-168, AND MASS SPECTROMETRY.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-116 AND SER-154, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [10]
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-505.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the RabGAP domain of human TBC1D22B.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACBD3 and ARFGEF1. Interacts with YWHAB, YWHAE,
CC YWHAG, YWHAH, YWHAQ and YWHAZ. {ECO:0000269|PubMed:23572552}.
CC -!- INTERACTION:
CC Q9NU19; Q9H3P7: ACBD3; NbExp=6; IntAct=EBI-8787464, EBI-1791792;
CC Q9NU19; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-8787464, EBI-11978055;
CC Q9NU19; O43307: ARHGEF9; NbExp=3; IntAct=EBI-8787464, EBI-3447299;
CC Q9NU19; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-8787464, EBI-2548012;
CC Q9NU19; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-8787464, EBI-739580;
CC Q9NU19; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-8787464, EBI-3866279;
CC Q9NU19; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-8787464, EBI-2808286;
CC Q9NU19; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-8787464, EBI-347573;
CC Q9NU19; Q01850: CDR2; NbExp=4; IntAct=EBI-8787464, EBI-1181367;
CC Q9NU19; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-8787464, EBI-11522539;
CC Q9NU19; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-8787464, EBI-739624;
CC Q9NU19; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-8787464, EBI-3866319;
CC Q9NU19; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-8787464, EBI-742054;
CC Q9NU19; Q05D60: DEUP1; NbExp=4; IntAct=EBI-8787464, EBI-748597;
CC Q9NU19; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-8787464, EBI-2349927;
CC Q9NU19; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-8787464, EBI-742102;
CC Q9NU19; Q13643: FHL3; NbExp=3; IntAct=EBI-8787464, EBI-741101;
CC Q9NU19; P51114-2: FXR1; NbExp=3; IntAct=EBI-8787464, EBI-11022345;
CC Q9NU19; P51116: FXR2; NbExp=5; IntAct=EBI-8787464, EBI-740459;
CC Q9NU19; P14136: GFAP; NbExp=3; IntAct=EBI-8787464, EBI-744302;
CC Q9NU19; Q08379: GOLGA2; NbExp=5; IntAct=EBI-8787464, EBI-618309;
CC Q9NU19; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-8787464, EBI-740641;
CC Q9NU19; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-8787464, EBI-748420;
CC Q9NU19; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-8787464, EBI-10961706;
CC Q9NU19; Q9BPX1: HSD17B14; NbExp=7; IntAct=EBI-8787464, EBI-742664;
CC Q9NU19; Q9UKT9: IKZF3; NbExp=9; IntAct=EBI-8787464, EBI-747204;
CC Q9NU19; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-8787464, EBI-14069005;
CC Q9NU19; O76011: KRT34; NbExp=3; IntAct=EBI-8787464, EBI-1047093;
CC Q9NU19; Q6A162: KRT40; NbExp=4; IntAct=EBI-8787464, EBI-10171697;
CC Q9NU19; Q68G74: LHX8; NbExp=3; IntAct=EBI-8787464, EBI-8474075;
CC Q9NU19; P48059-3: LIMS1; NbExp=3; IntAct=EBI-8787464, EBI-12864460;
CC Q9NU19; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-8787464, EBI-10172526;
CC Q9NU19; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-8787464, EBI-11522433;
CC Q9NU19; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-8787464, EBI-79165;
CC Q9NU19; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-8787464, EBI-949255;
CC Q9NU19; Q96PV4: PNMA5; NbExp=4; IntAct=EBI-8787464, EBI-10171633;
CC Q9NU19; P98175: RBM10; NbExp=3; IntAct=EBI-8787464, EBI-721525;
CC Q9NU19; Q5RL73: RBM48; NbExp=3; IntAct=EBI-8787464, EBI-473821;
CC Q9NU19; Q04864-2: REL; NbExp=3; IntAct=EBI-8787464, EBI-10829018;
CC Q9NU19; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-8787464, EBI-747107;
CC Q9NU19; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-8787464, EBI-10269374;
CC Q9NU19; O60504: SORBS3; NbExp=4; IntAct=EBI-8787464, EBI-741237;
CC Q9NU19; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-8787464, EBI-744066;
CC Q9NU19; Q9Y6A5: TACC3; NbExp=7; IntAct=EBI-8787464, EBI-2554984;
CC Q9NU19; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-8787464, EBI-11139477;
CC Q9NU19; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-8787464, EBI-742397;
CC Q9NU19; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-8787464, EBI-10175039;
CC Q9NU19; P36406: TRIM23; NbExp=8; IntAct=EBI-8787464, EBI-740098;
CC Q9NU19; P14373: TRIM27; NbExp=4; IntAct=EBI-8787464, EBI-719493;
CC Q9NU19; Q9BYV2: TRIM54; NbExp=5; IntAct=EBI-8787464, EBI-2130429;
CC Q9NU19; Q15654: TRIP6; NbExp=3; IntAct=EBI-8787464, EBI-742327;
CC Q9NU19; Q8N1B4: VPS52; NbExp=7; IntAct=EBI-8787464, EBI-2799833;
CC Q9NU19; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-8787464, EBI-11419867;
CC Q9NU19; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-8787464, EBI-11962468;
CC Q9NU19; P36508: ZNF76; NbExp=3; IntAct=EBI-8787464, EBI-7254550;
CC Q9NU19; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-8787464, EBI-7252920;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB449909; BAH16652.1; -; mRNA.
DR EMBL; AY313781; AAQ72548.1; -; mRNA.
DR EMBL; AK000344; BAA91099.1; ALT_INIT; mRNA.
DR EMBL; AK292893; BAF85582.1; -; mRNA.
DR EMBL; AL096712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03939.1; -; Genomic_DNA.
DR EMBL; BC000291; AAH00291.2; -; mRNA.
DR EMBL; BC000743; AAH00743.2; -; mRNA.
DR EMBL; BC001927; AAH01927.1; -; mRNA.
DR EMBL; BC002720; AAH02720.2; -; mRNA.
DR EMBL; BC063523; AAH63523.1; -; mRNA.
DR EMBL; BC109026; AAI09027.1; -; mRNA.
DR EMBL; BC109027; AAI09028.1; -; mRNA.
DR CCDS; CCDS4832.1; -.
DR RefSeq; NP_060242.2; NM_017772.3.
DR PDB; 6D0S; X-ray; 2.30 A; A=178-505.
DR PDBsum; 6D0S; -.
DR AlphaFoldDB; Q9NU19; -.
DR SMR; Q9NU19; -.
DR BioGRID; 120772; 192.
DR IntAct; Q9NU19; 152.
DR MINT; Q9NU19; -.
DR STRING; 9606.ENSP00000362590; -.
DR GlyGen; Q9NU19; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NU19; -.
DR MetOSite; Q9NU19; -.
DR PhosphoSitePlus; Q9NU19; -.
DR BioMuta; TBC1D22B; -.
DR DMDM; 47117913; -.
DR EPD; Q9NU19; -.
DR jPOST; Q9NU19; -.
DR MassIVE; Q9NU19; -.
DR MaxQB; Q9NU19; -.
DR PaxDb; Q9NU19; -.
DR PeptideAtlas; Q9NU19; -.
DR PRIDE; Q9NU19; -.
DR ProteomicsDB; 82648; -.
DR Antibodypedia; 29804; 24 antibodies from 9 providers.
DR DNASU; 55633; -.
DR Ensembl; ENST00000373491.3; ENSP00000362590.3; ENSG00000065491.8.
DR GeneID; 55633; -.
DR KEGG; hsa:55633; -.
DR MANE-Select; ENST00000373491.3; ENSP00000362590.3; NM_017772.4; NP_060242.2.
DR UCSC; uc003onn.3; human.
DR CTD; 55633; -.
DR DisGeNET; 55633; -.
DR GeneCards; TBC1D22B; -.
DR HGNC; HGNC:21602; TBC1D22B.
DR HPA; ENSG00000065491; Low tissue specificity.
DR MIM; 616880; gene.
DR neXtProt; NX_Q9NU19; -.
DR OpenTargets; ENSG00000065491; -.
DR PharmGKB; PA134867087; -.
DR VEuPathDB; HostDB:ENSG00000065491; -.
DR eggNOG; KOG1092; Eukaryota.
DR GeneTree; ENSGT00940000157472; -.
DR HOGENOM; CLU_018687_6_0_1; -.
DR InParanoid; Q9NU19; -.
DR OMA; YVCAVFL; -.
DR OrthoDB; 750722at2759; -.
DR PhylomeDB; Q9NU19; -.
DR TreeFam; TF314211; -.
DR PathwayCommons; Q9NU19; -.
DR SignaLink; Q9NU19; -.
DR BioGRID-ORCS; 55633; 21 hits in 1079 CRISPR screens.
DR EvolutionaryTrace; Q9NU19; -.
DR GenomeRNAi; 55633; -.
DR Pharos; Q9NU19; Tbio.
DR PRO; PR:Q9NU19; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NU19; protein.
DR Bgee; ENSG00000065491; Expressed in lower esophagus mucosa and 142 other tissues.
DR Genevisible; Q9NU19; HS.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
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 3D-structure; Acetylation; Direct protein sequencing; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23572552"
FT CHAIN 2..505
FT /note="TBC1 domain family member 22B"
FT /id="PRO_0000208054"
FT DOMAIN 210..434
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 105..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:23572552"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23572552,
FT ECO:0007744|PubMed:23186163"
FT MUTAGEN 58
FT /note="S->E: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 88..90
FT /note="LNS->AAA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 91..92
FT /note="KV->AA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 94..96
FT /note="LAT->AAA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 99
FT /note="Q->A: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 100..101
FT /note="VL->AA: Almost complete loss of ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 102..104
FT /note="ENH->AAA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 114
FT /note="S->E: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 116..119
FT /note="STTS->EEEE: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 140..141
FT /note="SS->EE: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 143
FT /note="T->E: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 168
FT /note="S->E: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT CONFLICT 376..378
FT /note="KVK -> HEE (in Ref. 6; AAH00291)"
FT /evidence="ECO:0000305"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:6D0S"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:6D0S"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 285..301
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 341..360
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 371..387
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:6D0S"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 453..457
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:6D0S"
FT HELIX 479..495
FT /evidence="ECO:0007829|PDB:6D0S"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6D0S"
SQ SEQUENCE 505 AA; 59081 MW; C0093770BE04AA4D CRC64;
MAAENSKQFW KRSAKLPGSI QPVYGAQHPP LDPRLTKNFI KERSKVNTVP LKNKKASSFH
EFARNTSDAW DIGDDEEEDF SSPSFQTLNS KVALATAAQV LENHSKLRVK PERSQSTTSD
VPANYKVIKS SSDAQLSRNS SDTCLRNPLH KQQSLPLRPI IPLVARISDQ NASGAPPMTV
REKTRLEKFR QLLSSQNTDL DELRKCSWPG VPREVRPITW RLLSGYLPAN TERRKLTLQR
KREEYFGFIE QYYDSRNEEH HQDTYRQIHI DIPRTNPLIP LFQQPLVQEI FERILFIWAI
RHPASGYVQG INDLVTPFFV VFLSEYVEED VENFDVTNLS QDMLRSIEAD SFWCMSKLLD
GIQDNYTFAQ PGIQKKVKAL EELVSRIDEQ VHNHFRRYEV EYLQFAFRWM NNLLMRELPL
RCTIRLWDTY QSEPEGFSHF HLYVCAAFLI KWRKEILDEE DFQGLLMLLQ NLPTIHWGNE
EIGLLLAEAY RLKYMFADAP NHYRR
