TB22A_HUMAN
ID TB22A_HUMAN Reviewed; 517 AA.
AC Q8WUA7; B0QYI2; B0QYI3; B9A6M3; Q5TE47; Q6ZUH2; Q92680; Q9BVD6; Q9UGG0;
AC Q9UGT2; Q9UGU6; Q9UH25; Q9Y4W5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=TBC1 domain family member 22A;
GN Name=TBC1D22A; Synonyms=C22orf4;
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).
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Esophagus;
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=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 [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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cervix, Lung, Testis, 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 2-304; 370-433; 438-463 AND 504-517, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION, INTERACTION
RP WITH ACBD3; ARFGEF1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ,
RP MUTAGENESIS OF 90-ASN--GLU-92; 92-GLU-VAL-93; 93-VAL--GLU-96;
RP 96-GLU-THR-97; 99-ASN-ARG-100; 101-VAL-LEU-102; 103-ARG--HIS-105; SER-132;
RP SER-165; 165-SER--SER-167; SER-167; 149-THR-SER-150 AND GLN-320, AND MASS
RP 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-517.
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 191-517, AND SUBUNIT.
RX PubMed=18186464; DOI=10.1002/prot.21885;
RA Tempel W., Tong Y., Dimov S., Bochkarev A., Park H.;
RT "First crystallographic models of human TBC domains in the context of a
RT family-wide structural analysis.";
RL Proteins 71:497-502(2008).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (PubMed:18186464). Interacts with ACBD3 and ARFGEF1.
CC Interacts with YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ
CC (PubMed:23572552). {ECO:0000269|PubMed:18186464,
CC ECO:0000269|PubMed:23572552}.
CC -!- INTERACTION:
CC Q8WUA7; Q9H3P7: ACBD3; NbExp=13; IntAct=EBI-2821276, EBI-1791792;
CC Q8WUA7-2; P49821: NDUFV1; NbExp=3; IntAct=EBI-21575846, EBI-748312;
CC Q8WUA7-2; O43933: PEX1; NbExp=3; IntAct=EBI-21575846, EBI-988601;
CC Q8WUA7-2; P02766: TTR; NbExp=3; IntAct=EBI-21575846, EBI-711909;
CC Q8WUA7-2; O76024: WFS1; NbExp=3; IntAct=EBI-21575846, EBI-720609;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8WUA7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUA7-2; Sequence=VSP_010382, VSP_010383;
CC Name=3;
CC IsoId=Q8WUA7-3; Sequence=VSP_015142, VSP_015143, VSP_015144;
CC Name=4;
CC IsoId=Q8WUA7-4; Sequence=VSP_015142;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB46628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB449908; BAH16651.1; -; mRNA.
DR EMBL; CR456412; CAG30298.1; -; mRNA.
DR EMBL; AK125705; BAC86253.1; -; mRNA.
DR EMBL; AK127653; BAG54543.1; -; mRNA.
DR EMBL; U51561; AAD12228.1; -; Genomic_DNA.
DR EMBL; AL023733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL118516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP325331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z79999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z80896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73443.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73445.1; -; Genomic_DNA.
DR EMBL; BC001292; AAH01292.2; -; mRNA.
DR EMBL; BC002743; AAH02743.2; -; mRNA.
DR EMBL; BC020976; AAH20976.2; -; mRNA.
DR EMBL; BC029897; AAH29897.1; -; mRNA.
DR EMBL; AL096779; CAB46628.1; ALT_INIT; mRNA.
DR CCDS; CCDS14078.1; -. [Q8WUA7-1]
DR CCDS; CCDS63511.1; -. [Q8WUA7-2]
DR CCDS; CCDS63512.1; -. [Q8WUA7-4]
DR RefSeq; NP_001271232.1; NM_001284303.1. [Q8WUA7-2]
DR RefSeq; NP_001271234.1; NM_001284305.1. [Q8WUA7-4]
DR RefSeq; NP_055161.1; NM_014346.3. [Q8WUA7-1]
DR RefSeq; XP_016884233.1; XM_017028744.1. [Q8WUA7-4]
DR PDB; 2QFZ; X-ray; 2.10 A; A/B=191-517.
DR PDBsum; 2QFZ; -.
DR AlphaFoldDB; Q8WUA7; -.
DR SMR; Q8WUA7; -.
DR BioGRID; 117308; 32.
DR IntAct; Q8WUA7; 33.
DR STRING; 9606.ENSP00000336724; -.
DR iPTMnet; Q8WUA7; -.
DR PhosphoSitePlus; Q8WUA7; -.
DR BioMuta; TBC1D22A; -.
DR DMDM; 25008319; -.
DR EPD; Q8WUA7; -.
DR jPOST; Q8WUA7; -.
DR MassIVE; Q8WUA7; -.
DR MaxQB; Q8WUA7; -.
DR PaxDb; Q8WUA7; -.
DR PeptideAtlas; Q8WUA7; -.
DR PRIDE; Q8WUA7; -.
DR ProteomicsDB; 2648; -.
DR ProteomicsDB; 74649; -. [Q8WUA7-1]
DR ProteomicsDB; 74650; -. [Q8WUA7-2]
DR ProteomicsDB; 74651; -. [Q8WUA7-3]
DR Antibodypedia; 242; 164 antibodies from 21 providers.
DR DNASU; 25771; -.
DR Ensembl; ENST00000337137.9; ENSP00000336724.4; ENSG00000054611.14. [Q8WUA7-1]
DR Ensembl; ENST00000355704.7; ENSP00000347932.3; ENSG00000054611.14. [Q8WUA7-2]
DR Ensembl; ENST00000406733.1; ENSP00000385634.1; ENSG00000054611.14. [Q8WUA7-4]
DR Ensembl; ENST00000441162.5; ENSP00000406214.1; ENSG00000054611.14. [Q8WUA7-3]
DR GeneID; 25771; -.
DR KEGG; hsa:25771; -.
DR MANE-Select; ENST00000337137.9; ENSP00000336724.4; NM_014346.5; NP_055161.1.
DR UCSC; uc003bib.5; human. [Q8WUA7-1]
DR CTD; 25771; -.
DR DisGeNET; 25771; -.
DR GeneCards; TBC1D22A; -.
DR HGNC; HGNC:1309; TBC1D22A.
DR HPA; ENSG00000054611; Low tissue specificity.
DR MIM; 616879; gene.
DR neXtProt; NX_Q8WUA7; -.
DR OpenTargets; ENSG00000054611; -.
DR PharmGKB; PA25888; -.
DR VEuPathDB; HostDB:ENSG00000054611; -.
DR eggNOG; KOG1092; Eukaryota.
DR GeneTree; ENSGT00940000159840; -.
DR InParanoid; Q8WUA7; -.
DR OMA; TACWGDE; -.
DR OrthoDB; 750722at2759; -.
DR PhylomeDB; Q8WUA7; -.
DR TreeFam; TF314211; -.
DR PathwayCommons; Q8WUA7; -.
DR SignaLink; Q8WUA7; -.
DR BioGRID-ORCS; 25771; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; TBC1D22A; human.
DR EvolutionaryTrace; Q8WUA7; -.
DR GenomeRNAi; 25771; -.
DR Pharos; Q8WUA7; Tbio.
DR PRO; PR:Q8WUA7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8WUA7; protein.
DR Bgee; ENSG00000054611; Expressed in pancreatic ductal cell and 181 other tissues.
DR ExpressionAtlas; Q8WUA7; baseline and differential.
DR Genevisible; Q8WUA7; 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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; Alternative splicing; Direct protein sequencing;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23572552"
FT CHAIN 2..517
FT /note="TBC1 domain family member 22A"
FT /id="PRO_0000208051"
FT DOMAIN 222..446
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 103..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..191
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 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5A6"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5A6"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015142"
FT VAR_SEQ 22..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010382"
FT VAR_SEQ 154..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010383"
FT VAR_SEQ 339..371
FT /note="EAEEVDTVDVSGVPAEVLCNIEADTYWCMSKLL -> AFPGCGRPQIPILAV
FT IWRDEPYPRTDEQIILRR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015143"
FT VAR_SEQ 372..517
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015144"
FT MUTAGEN 90..92
FT /note="NSE->AAA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 92..93
FT /note="EV->AA: No effect on interaction with ACBD3, nor
FT with 14-3-3 proteins."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 93..96
FT /note="VVME->AAAA: Decreased ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 96..97
FT /note="ET->AA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 99..100
FT /note="NR->AA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 101..102
FT /note="VL->AA: Drastically decreased ACBD3-binding. No
FT effect on binding to 14-3-3 protein."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 103..105
FT /note="RNH->AAA: No effect on ACBD3-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 132
FT /note="S->A: No effect on 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 149..150
FT /note="TS->EE: Decreased 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 165..167
FT /note="SQS->AQA: Complete loss of 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 165..167
FT /note="SQS->EQE: Complete loss of 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 165
FT /note="S->A: No effect on interaction with ACBD3. Decreased
FT 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 165
FT /note="S->E: Complete loss of 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 167
FT /note="S->E: Complete loss of 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT MUTAGEN 320
FT /note="Q->A: Decreased 14-3-3 protein-binding."
FT /evidence="ECO:0000269|PubMed:23572552"
FT CONFLICT 92
FT /note="E -> K (in Ref. 6; AAH01292)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..345
FT /note="EAEEVDT -> GKISCKH (in Ref. 4; AAD12228)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="G -> C (in Ref. 6; AAH01292)"
FT /evidence="ECO:0000305"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:2QFZ"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 353..372
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 383..399
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:2QFZ"
FT TURN 424..429
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:2QFZ"
FT TURN 446..451
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:2QFZ"
FT HELIX 491..507
FT /evidence="ECO:0007829|PDB:2QFZ"
SQ SEQUENCE 517 AA; 59121 MW; 865A3CDCDA0C5543 CRC64;
MASDGARKQF WKRSNSKLPG SIQHVYGAQH PPFDPLLHGT LLRSTAKMPT TPVKAKRVST
FQEFESNTSD AWDAGEDDDE LLAMAAESLN SEVVMETANR VLRNHSQRQG RPTLQEGPGL
QQKPRPEAEP PSPPSGDLRL VKSVSESHTS CPAESASDAA PLQRSQSLPH SATVTLGGTS
DPSTLSSSAL SEREASRLDK FKQLLAGPNT DLEELRRLSW SGIPKPVRPM TWKLLSGYLP
ANVDRRPATL QRKQKEYFAF IEHYYDSRND EVHQDTYRQI HIDIPRMSPE ALILQPKVTE
IFERILFIWA IRHPASGYVQ GINDLVTPFF VVFICEYIEA EEVDTVDVSG VPAEVLCNIE
ADTYWCMSKL LDGIQDNYTF AQPGIQMKVK MLEELVSRID EQVHRHLDQH EVRYLQFAFR
WMNNLLMREV PLRCTIRLWD TYQSEPDGFS HFHLYVCAAF LVRWRKEILE EKDFQELLLF
LQNLPTAHWD DEDISLLLAE AYRLKFAFAD APNHYKK
