TBC12_HUMAN
ID TBC12_HUMAN Reviewed; 775 AA.
AC O60347; Q5VYA6; Q8WX26; Q8WX59; Q9UG83;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=TBC1 domain family member 12;
GN Name=TBC1D12; Synonyms=KIAA0608;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-775.
RC TISSUE=Fetal brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747 AND THR-748, AND
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP 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 [8]
RP INTERACTION WITH RAB11A, AND SUBCELLULAR LOCATION.
RX PubMed=28384198; DOI=10.1371/journal.pone.0174883;
RA Oguchi M.E., Noguchi K., Fukuda M.;
RT "TBC1D12 is a novel Rab11-binding protein that modulates neurite outgrowth
RT of PC12 cells.";
RL PLoS ONE 12:E0174883-E0174883(2017).
CC -!- FUNCTION: RAB11A-binding protein that plays a role in neurite
CC outgrowth. {ECO:0000250|UniProtKB:M0R7T9}.
CC -!- SUBUNIT: Interacts with RAB11A; this interaction recruits TBC1D12 to
CC RAB11A-positive recycling endosomes. {ECO:0000269|PubMed:28384198}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:28384198}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB43225.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB011180; BAA25534.1; ALT_INIT; mRNA.
DR EMBL; AL138759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049956; CAB43225.2; ALT_INIT; mRNA.
DR CCDS; CCDS41553.1; -.
DR PIR; T08683; T08683.
DR RefSeq; NP_056003.1; NM_015188.1.
DR AlphaFoldDB; O60347; -.
DR SMR; O60347; -.
DR BioGRID; 116837; 11.
DR IntAct; O60347; 2.
DR MINT; O60347; -.
DR STRING; 9606.ENSP00000225235; -.
DR iPTMnet; O60347; -.
DR PhosphoSitePlus; O60347; -.
DR BioMuta; TBC1D12; -.
DR EPD; O60347; -.
DR jPOST; O60347; -.
DR MassIVE; O60347; -.
DR MaxQB; O60347; -.
DR PaxDb; O60347; -.
DR PeptideAtlas; O60347; -.
DR PRIDE; O60347; -.
DR ProteomicsDB; 49377; -.
DR Antibodypedia; 48752; 21 antibodies from 8 providers.
DR DNASU; 23232; -.
DR Ensembl; ENST00000225235.5; ENSP00000225235.4; ENSG00000108239.9.
DR GeneID; 23232; -.
DR KEGG; hsa:23232; -.
DR MANE-Select; ENST00000225235.5; ENSP00000225235.4; NM_015188.2; NP_056003.1.
DR UCSC; uc001kjr.3; human.
DR CTD; 23232; -.
DR DisGeNET; 23232; -.
DR GeneCards; TBC1D12; -.
DR HGNC; HGNC:29082; TBC1D12.
DR HPA; ENSG00000108239; Tissue enhanced (brain).
DR neXtProt; NX_O60347; -.
DR OpenTargets; ENSG00000108239; -.
DR PharmGKB; PA134891743; -.
DR VEuPathDB; HostDB:ENSG00000108239; -.
DR eggNOG; KOG2223; Eukaryota.
DR GeneTree; ENSGT00940000156410; -.
DR HOGENOM; CLU_015133_0_0_1; -.
DR InParanoid; O60347; -.
DR OMA; GQSARDH; -.
DR OrthoDB; 798837at2759; -.
DR PhylomeDB; O60347; -.
DR TreeFam; TF313318; -.
DR PathwayCommons; O60347; -.
DR SignaLink; O60347; -.
DR BioGRID-ORCS; 23232; 3 hits in 1073 CRISPR screens.
DR ChiTaRS; TBC1D12; human.
DR GenomeRNAi; 23232; -.
DR Pharos; O60347; Tdark.
DR PRO; PR:O60347; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O60347; protein.
DR Bgee; ENSG00000108239; Expressed in C1 segment of cervical spinal cord and 176 other tissues.
DR Genevisible; O60347; HS.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:2000785; P:regulation of autophagosome assembly; 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 Acetylation; Coiled coil; Endosome; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..775
FT /note="TBC1 domain family member 12"
FT /id="PRO_0000208037"
FT DOMAIN 484..692
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 409..452
FT /evidence="ECO:0000255"
FT COMPBIAS 48..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Polar 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 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A039"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 748
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CONFLICT 51..56
FT /note="Missing (in Ref. 1; BAA25534)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="Q -> G (in Ref. 3; CAB43225)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="F -> Y (in Ref. 3; CAB43225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 85626 MW; 106CD6E788C4C44E CRC64;
MVGPEDAGAC SGRNPKLLPV PAPDPVGQDR KVIRATGGFG GGVGAVEPPE EADEEEEADE
EEETPPRQLL QRYLAAAGEQ LEPGLCYCPL PAGQAGAPPP SAAPRSDACL LGSGSKHRGA
EVADGRAPRH EGMTNGDSGF LPGRDCRDLE EARGLARAGG RESRRRRPYG RLRLEGPGDE
DADGAGSPSD WASPLEDPLR SCCLVAADAQ EPEGAGSDSG DSPASSCSSS EDSEQRGVGA
GGPEEGAPPA TSAERTNGGA EPRLGFSDIH FNSRNTFQVS RGQSARDHLP PAGPPVPLPA
AEQGPAGASA RARRSGGFAD FFTRNLFPKR TKELKSVVHS APGWKLFGKV PPRENLQKTS
KIIQQEYEAR TGRTCKPPPQ SSRRKNFEFE PLSTTALILE DRPSNLPAKS VEEALRHRQE
YDEMVAEAKK REIKEAHKRK RIMKERFKQE ENIASAMVIW INEILPNWEV MRSTRRVREL
WWQGLPPSVR GKVWSLAVGN ELNITPELYE IFLSRAKERW KSFSETSSEN DTEGVSVADR
EASLELIKLD ISRTFPSLYI FQKGGPYHDV LHSILGAYTC YRPDVGYVQG MSFIAAVLIL
NLEEADAFIA FANLLNKPCQ LAFFRVDHSM MLKYFATFEV FFEENLSKLF LHFKSYSLTP
DIYLIDWIFT LYSKSLPLDL ACRVWDVFCR DGEEFLFRTG LGILRLYEDI LLQMDFIHIA
QFLTKLPEDI TSEKLFSCIA AIQMQNSTKK WTQVFASVMK DIKEGDKNSS PALKS
