TBC9B_MOUSE
ID TBC9B_MOUSE Reviewed; 1263 AA.
AC Q5SVR0; Q3UGF5; Q6A019; Q6P1G9; Q6PDP2; Q80ZU6; Q8C7K9; Q8CBR7; Q8CCW2;
AC Q9CSQ2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=TBC1 domain family member 9B;
GN Name=Tbc1d9b; Synonyms=Kiaa0676;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Hippocampus, Medulla oblongata, Melanocyte, and
RC Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 797-1263 (ISOFORM 1).
RC TISSUE=Brain, Eye, and Olfactory epithelium;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SVR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SVR0-2; Sequence=VSP_025700;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172999; BAD32277.1; ALT_INIT; mRNA.
DR EMBL; AK012224; BAB28107.1; -; mRNA.
DR EMBL; AK031992; BAC27640.1; ALT_INIT; mRNA.
DR EMBL; AK035457; BAC29068.1; -; mRNA.
DR EMBL; AK049999; BAC34024.2; -; mRNA.
DR EMBL; AK147964; BAE28254.1; -; mRNA.
DR EMBL; AL627187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048085; AAH48085.1; -; mRNA.
DR EMBL; BC058596; AAH58596.1; -; mRNA.
DR EMBL; BC062928; AAH62928.1; -; mRNA.
DR EMBL; BC065080; AAH65080.1; -; mRNA.
DR CCDS; CCDS36146.1; -. [Q5SVR0-2]
DR CCDS; CCDS70175.1; -. [Q5SVR0-1]
DR RefSeq; NP_001277688.1; NM_001290759.1.
DR RefSeq; NP_001277689.1; NM_001290760.1. [Q5SVR0-1]
DR RefSeq; NP_084021.2; NM_029745.2. [Q5SVR0-2]
DR AlphaFoldDB; Q5SVR0; -.
DR SMR; Q5SVR0; -.
DR BioGRID; 218320; 5.
DR IntAct; Q5SVR0; 2.
DR MINT; Q5SVR0; -.
DR STRING; 10090.ENSMUSP00000090825; -.
DR iPTMnet; Q5SVR0; -.
DR PhosphoSitePlus; Q5SVR0; -.
DR EPD; Q5SVR0; -.
DR jPOST; Q5SVR0; -.
DR MaxQB; Q5SVR0; -.
DR PaxDb; Q5SVR0; -.
DR PeptideAtlas; Q5SVR0; -.
DR PRIDE; Q5SVR0; -.
DR ProteomicsDB; 254655; -. [Q5SVR0-1]
DR ProteomicsDB; 254656; -. [Q5SVR0-2]
DR Antibodypedia; 50209; 64 antibodies from 14 providers.
DR Ensembl; ENSMUST00000093138; ENSMUSP00000090825; ENSMUSG00000036644. [Q5SVR0-2]
DR Ensembl; ENSMUST00000101270; ENSMUSP00000098828; ENSMUSG00000036644. [Q5SVR0-1]
DR GeneID; 76795; -.
DR KEGG; mmu:76795; -.
DR UCSC; uc007irp.2; mouse. [Q5SVR0-1]
DR UCSC; uc007irq.1; mouse. [Q5SVR0-2]
DR CTD; 23061; -.
DR MGI; MGI:1924045; Tbc1d9b.
DR VEuPathDB; HostDB:ENSMUSG00000036644; -.
DR eggNOG; KOG4347; Eukaryota.
DR GeneTree; ENSGT00940000158554; -.
DR HOGENOM; CLU_003535_0_1_1; -.
DR InParanoid; Q5SVR0; -.
DR OMA; KLLNCCD; -.
DR OrthoDB; 450360at2759; -.
DR PhylomeDB; Q5SVR0; -.
DR TreeFam; TF313145; -.
DR BioGRID-ORCS; 76795; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tbc1d9b; mouse.
DR PRO; PR:Q5SVR0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SVR0; protein.
DR Bgee; ENSMUSG00000036644; Expressed in ear vesicle and 224 other tissues.
DR Genevisible; Q5SVR0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR CDD; cd13351; PH-GRAM1_TCB1D9_TCB1D9B; 1.
DR CDD; cd13354; PH-GRAM2_TCB1D9_TCB1D9B; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR036014; TCB1D9/TCB1D9B_PH-GRAM1.
DR InterPro; IPR036017; TCB1D9/TCB1D9B_PH-GRAM2.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1263
FT /note="TBC1 domain family member 9B"
FT /id="PRO_0000288502"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 142..209
FT /note="GRAM 1"
FT DOMAIN 288..356
FT /note="GRAM 2"
FT DOMAIN 509..696
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 880..915
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 397..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 556
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 595
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66K14"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K14"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K14"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K14"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K14"
FT VAR_SEQ 957..973
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025700"
FT CONFLICT 73
FT /note="I -> T (in Ref. 1; BAD32277)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..163
FT /note="SCN -> PCT (in Ref. 1; BAD32277)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="D -> A (in Ref. 1; BAD32277)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="Missing (in Ref. 1; BAD32277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1225
FT /note="V -> M (in Ref. 2; BAE28254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1263 AA; 141779 MW; 2D12CE5E297D723E CRC64;
MWLGPEEVLV ANALWVTERA NPFFVLQRRR GHGKGGGLTG LLVGTLDVVL DSSARVAPYR
ILHQTQDSQV YWIVACGSSR KEITKHWEWL ENNLLQTLSI FDNEEDITTF VKGKIHGIIA
EENKNLQPQG DEDPGKFKEA ELKMRKQFGM PEGEKLVNYY SCNFWKGRVP RQGWLYLTVN
HLCFYSFLLG KEVSLVVQWV DVTRLEKNAT LLFPESIRVD TRDQELFFSM FLNIGETFKL
MEQLANLAMR QLLDSEGFLE DKALPRPIRP HKNISALKRD LDARAKNECY RATFRLPKDE
RLDGHTGCTL WTPFNKLHIP GQMFISNNYI CFASKEEDAC RLIIPLREVT IVEKADSSSV
LPSPLSISTK SKMTFLFANL KDRDFLVQRI SDFLQKTPSK QTGSSIGGTK ASVSDPAPES
LPTPQEASEP PASPSSPLSS PPSFSTQEIP TTSQGLLKVF QKNSPMEDLG AKGAKEKMKE
ESWNIHFFEY GRGMCMYRTA KTRELVLKGI PESLRGELWL LFSGAWNEMV THPGYYAELV
EKSLGKYSLA TEEIERDLHR SMPEHPAFQN ELGIAALRRV LTAYAFRNPT IGYCQAMNIV
TSVLLLYGSE EEAFWLLVAL CERMLPDYYN TRVVGALVDQ GIFEELTRDV LPRLSEKMQE
LGVISSISLS WFLTLFLSVM PFESAVVIVD CFFYEGIKVI LQVALAVLDA NVEQLLDCND
EGEAMTVLGR YLDNVVNKQS ISPPIPHLHA LLTSGDDPPV EVDIFDLLRV SYEKFSNLRA
DDIEQMRFKQ RLKVIQSLED TAKRSVVRAI PGDIGFSIEE LEDLYMVFKA KHLASQYWGG
NRSAAVHRDP SLPYLEQYRI DASQFRELFA SLTPWACGSH TPVLAGRMFR LLDQNKDSLI
NFKEFVTGMS GMYHGDLTEK LKALYKLHLP PALIPEEAES ALEAAHYFTE DSSSEASPLA
SDLDLFLPWE AQALLQEQQE GSGNEDTPER REEKGTSPPD YRHYLRMWAK EKEAQKETIK
DLPKMNQEQF IELCKTLYNM FSEDPMEQDL YHAIATVASL LLRIGEVGKK FSALTTKKPR
DGAHSGDPNS ATEEDEPPTP KLHQDPTQEC QPPAAGDRQA KASGDMHLGK ALQDSHVIVE
GGSGEGQGSP SLLLSDDETK DDMSMSSYSV VSTGSLQCED LTEDTVLVGG GACSPTATSR
AGGTVDTDWC ISFEQILASI LTESVLVNFF EKRVDIGLKI KDQKKVERQF STSSDHEPPG
VLG
