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TBC1 domain family member 10A (EBP50-PDX interactor of 64 kDa) (EPI64 protein) (Rab27A-GAP-alpha)

 TB10A_HUMAN             Reviewed;         508 AA.
Q9BXI6; B3KXT8; O76053; Q20WK7; Q543A2;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=TBC1 domain family member 10A;
AltName: Full=EBP50-PDX interactor of 64 kDa;
Short=EPI64 protein;
AltName: Full=Rab27A-GAP-alpha;
Name=TBC1D10A; Synonyms=EPI64, TBC1D10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
MUTAGENESIS.
PubMed=11285285; DOI=10.1083/jcb.153.1.191;
Reczek D., Bretscher A.;
"Identification of EPI64, a TBC/rabGAP domain-containing microvillar
protein that binds to the first PDZ domain of EBP50 and E3KARP.";
J. Cell Biol. 153:191-206(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
Ishibashi K., Kanno E., Itoh T., Fukuda M.;
"Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
protein that possesses Rab3A-GAP activity.";
Genes Cells 14:41-52(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Mammary gland, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-157 AND
ARG-160.
PubMed=16923811; DOI=10.1074/jbc.M603808200;
Itoh T., Fukuda M.;
"Identification of EPI64 as a GTPase-activating protein specific for
Rab27A.";
J. Biol. Chem. 281:31823-31831(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Acts as GTPase-activating protein for RAB27A, but not
for RAB2A, RAB3A, nor RAB4A. {ECO:0000269|PubMed:16923811}.
-!- SUBUNIT: Binds to the first PDZ domain of SLC9A3R1 and SLC9A3R2.
-!- INTERACTION:
Q96AP0:ACD; NbExp=2; IntAct=EBI-7815040, EBI-717666;
Q9BXU3:TEX13A; NbExp=5; IntAct=EBI-7815040, EBI-10301068;
-!- SUBCELLULAR LOCATION: Cell projection, microvillus
{ECO:0000269|PubMed:16923811}. Note=Localizes to the microvilli-
rich region of the syncytiotrophoblast. In melanocytes, located at
the periphery of cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BXI6-1; Sequence=Displayed;
Name=2;
IsoId=Q9BXI6-2; Sequence=VSP_043119;
Note=No experimental confirmation available.;
-!- DOMAIN: The arginine and glutamine fingers are critical for the
GTPase-activating mechanism, they pull out Rab's 'switch 2'
glutamine and insert in Rab's active site. {ECO:0000250}.
-!- PTM: Exists in both phosphorylated and non-phosphorylated state.
-!- SEQUENCE CAUTION:
Sequence=AAC23434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF331038; AAK35048.1; -; mRNA.
EMBL; AB449894; BAH16637.1; -; mRNA.
EMBL; CT841514; CAJ86444.1; -; mRNA.
EMBL; AK074656; BAC11117.1; -; mRNA.
EMBL; AK127939; BAG54600.1; -; mRNA.
EMBL; AC004997; AAC23434.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471095; EAW59874.1; -; Genomic_DNA.
EMBL; CH471095; EAW59876.1; -; Genomic_DNA.
EMBL; BC136815; AAI36816.1; -; mRNA.
EMBL; BC142940; AAI42941.1; -; mRNA.
EMBL; BC150214; AAI50215.1; -; mRNA.
CCDS; CCDS13874.1; -. [Q9BXI6-1]
CCDS; CCDS56227.1; -. [Q9BXI6-2]
RefSeq; NP_001191169.1; NM_001204240.1. [Q9BXI6-2]
RefSeq; NP_114143.1; NM_031937.2. [Q9BXI6-1]
UniGene; Hs.655273; -.
ProteinModelPortal; Q9BXI6; -.
SMR; Q9BXI6; -.
BioGrid; 123787; 19.
IntAct; Q9BXI6; 4.
MINT; MINT-195567; -.
STRING; 9606.ENSP00000384996; -.
iPTMnet; Q9BXI6; -.
PhosphoSitePlus; Q9BXI6; -.
BioMuta; TBC1D10A; -.
DMDM; 20454903; -.
MaxQB; Q9BXI6; -.
PaxDb; Q9BXI6; -.
PeptideAtlas; Q9BXI6; -.
PRIDE; Q9BXI6; -.
Ensembl; ENST00000215790; ENSP00000215790; ENSG00000099992. [Q9BXI6-1]
Ensembl; ENST00000403477; ENSP00000384996; ENSG00000099992. [Q9BXI6-2]
GeneID; 83874; -.
KEGG; hsa:83874; -.
UCSC; uc003ahk.5; human. [Q9BXI6-1]
CTD; 83874; -.
EuPathDB; HostDB:ENSG00000099992.15; -.
GeneCards; TBC1D10A; -.
HGNC; HGNC:23609; TBC1D10A.
HPA; HPA007725; -.
HPA; HPA008142; -.
HPA; HPA076041; -.
MIM; 610020; gene.
neXtProt; NX_Q9BXI6; -.
OpenTargets; ENSG00000099992; -.
PharmGKB; PA134888210; -.
eggNOG; KOG2221; Eukaryota.
eggNOG; ENOG410XPSR; LUCA.
GeneTree; ENSGT00860000133698; -.
HOGENOM; HOG000007561; -.
HOVERGEN; HBG070028; -.
InParanoid; Q9BXI6; -.
KO; K19944; -.
OMA; CRSPPRL; -.
OrthoDB; EOG091G07CB; -.
PhylomeDB; Q9BXI6; -.
TreeFam; TF313293; -.
Reactome; R-HSA-8854214; TBC/RABGAPs.
ChiTaRS; TBC1D10A; human.
GeneWiki; TBC1D10A; -.
GenomeRNAi; 83874; -.
PRO; PR:Q9BXI6; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099992; -.
CleanEx; HS_TBC1D10A; -.
ExpressionAtlas; Q9BXI6; baseline and differential.
Genevisible; Q9BXI6; HS.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005902; C:microvillus; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0031338; P:regulation of vesicle fusion; IBA:GO_Central.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
InterPro; IPR000195; Rab-GTPase-TBC_dom.
InterPro; IPR035969; Rab-GTPase_TBC_sf.
Pfam; PF00566; RabGAP-TBC; 1.
SMART; SM00164; TBC; 1.
SUPFAM; SSF47923; SSF47923; 2.
PROSITE; PS50086; TBC_RABGAP; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Complete proteome;
Direct protein sequencing; GTPase activation;
Guanine-nucleotide releasing factor; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 508 TBC1 domain family member 10A.
/FTId=PRO_0000208035.
DOMAIN 111 299 Rab-GAP TBC. {ECO:0000255|PROSITE-
ProRule:PRU00163}.
REGION 505 508 Binding to the PDZ domain of EBP50.
SITE 156 156 Arginine finger. {ECO:0000250}.
SITE 197 197 Glutamine finger. {ECO:0000250}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P58802}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P58802}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 70 70 A -> APCPLLHR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043119.
VARIANT 411 411 R -> H (in dbSNP:rs4823086).
/FTId=VAR_052541.
MUTAGEN 157 157 D->A: Loss of activity. No effect on
subcellular location.
{ECO:0000269|PubMed:16923811}.
MUTAGEN 160 160 R->K: Loss of activity. No effect on
subcellular location.
{ECO:0000269|PubMed:16923811}.
MUTAGEN 508 508 L->LA: Loss of interaction with EBP50 and
impaired subcellular localization.
{ECO:0000269|PubMed:11285285}.
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


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CSB-EL019177DO Dog RAB27A, member RAS oncogene family (RAB27A) ELISA kit, Species Dog, Sample Type serum, plasma 96T
Y050697 Anti_TBC1D1(TBC1 domain family member 1) 100ug
ARP55029_P050 TBC1D22A(TBC1 domain family, member 22A) 50 µg
EH2275 TBC1 domain family member 1 Elisa Kit 96T


 

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