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Protein

TBC1 domain family member 17

Gene

Tbc1d17

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable GTPase-activating protein for Rab8; its transient association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated endocytic trafficking, such as of transferrin receptor (TfR) and reduces Rab8 recruitnment to tubules emanating from the endocytic recycling compartment (ERC). Involved in regulation of autophagy. Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-50; the function requires its catalytic activity, however, the involved Rab is not known (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei377 – 3771Arginine fingerBy similarity
Sitei418 – 4181Glutamine fingerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Autophagy, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 17
Gene namesi
Name:Tbc1d17
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2449973. Tbc1d17.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 645645TBC1 domain family member 17PRO_0000208046Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei602 – 6021PhosphoserineBy similarity
Modified residuei604 – 6041PhosphoserineBy similarity
Modified residuei608 – 6081PhosphoserineBy similarity
Modified residuei615 – 6151PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BYH7.
MaxQBiQ8BYH7.
PaxDbiQ8BYH7.
PRIDEiQ8BYH7.

PTM databases

iPTMnetiQ8BYH7.
PhosphoSiteiQ8BYH7.

Expressioni

Gene expression databases

BgeeiQ8BYH7.
ExpressionAtlasiQ8BYH7. baseline and differential.
GenevisibleiQ8BYH7. MM.

Interactioni

Subunit structurei

Interacts with OPTN.

Protein-protein interaction databases

BioGridi231386. 1 interaction.
STRINGi10090.ENSMUSP00000048260.

Structurei

3D structure databases

ProteinModelPortaliQ8BYH7.
SMRiQ8BYH7. Positions 276-568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini310 – 520211Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 30993Required for interaction with OPTNBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi597 – 63135Pro-richAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2197. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00550000074386.
HOVERGENiHBG057668.
InParanoidiQ8BYH7.
KOiK19945.
OMAiREYLAVM.
OrthoDBiEOG7HTHHR.
TreeFamiTF314296.

Family and domain databases

InterProiIPR021935. DUF3548.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF12068. DUF3548. 1 hit.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BYH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGSSYRVVF EKGGVYLHTS ARKHQDPDSL IAGVIRVVEK DSDVFLHWAP
60 70 80 90 100
VEEAGDPTQI LFKKDPSRGE PSTSEEEPTF DPGYEPDWAV ISTVRPQPHL
110 120 130 140 150
AEPRKGAEPS SSRSSWAFSV SLGELKSIRR SKPGLSWAYL VLVTQAGGSL
160 170 180 190 200
PALHFHRGGT RALLRVLSRY LLLASSPQDS RLYLVFPQDP SALSDSFHHL
210 220 230 240 250
QLFDQDSSNV VSRFLQDPYS TTFSSFSRVT NFFRGALQPH PEGASSPNLP
260 270 280 290 300
PLPDDEPEPG FEVISCVELG QRPTVERAPP VTEEEWNRYV GPEGRLQNVP
310 320 330 340 350
ELKNRIFSGG LSPGLRREAW KFLLGYLSWE SSAEEHKAHV RKKTDEYFRM
360 370 380 390 400
KLQWKSVSAE QERRNSLLHG YRSLIERDVS RTDRTNKFYE GPENPGLSLL
410 420 430 440 450
HDILLTYCMY HFDLGYVQGM SDLLSPILFV VQNEVDAFWC FCGFMELVHG
460 470 480 490 500
NFEESQETMK RQLGQLLLLL RVLDQPLCDF LDSQDSGSLC FCFRWLLIWF
510 520 530 540 550
KREFPFPDVL RLWEVLWTGL PGPNLHLLVA CAILDMERDT LMLSGFGSNE
560 570 580 590 600
ILKHINELTM KLSVEDVLTR AEALYRQLTA CPELPHNVQE ILGLAQPEEP
610 620 630 640
SSPSPPVSPM PLSPTRAPLP PPLPEEVIPQ PDSSLEILPE DEDGA
Length:645
Mass (Da):72,860
Last modified:July 27, 2011 - v2
Checksum:iB0C3FC3C0F4A27E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751E → Q in BAC30387 (PubMed:16141072).Curated
Sequence conflicti608 – 6081S → F in BAC30387 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK136705 mRNA. Translation: BAE23103.1.
AK170821 mRNA. Translation: BAE42052.1.
AK039566 mRNA. Translation: BAC30387.1.
CH466603 Genomic DNA. Translation: EDL22756.1.
CCDSiCCDS39944.1.
RefSeqiNP_001036120.1. NM_001042655.1.
UniGeneiMm.27567.

Genome annotation databases

EnsembliENSMUST00000047085; ENSMUSP00000048260; ENSMUSG00000038520.
GeneIDi233204.
KEGGimmu:233204.
UCSCiuc009grc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK136705 mRNA. Translation: BAE23103.1.
AK170821 mRNA. Translation: BAE42052.1.
AK039566 mRNA. Translation: BAC30387.1.
CH466603 Genomic DNA. Translation: EDL22756.1.
CCDSiCCDS39944.1.
RefSeqiNP_001036120.1. NM_001042655.1.
UniGeneiMm.27567.

3D structure databases

ProteinModelPortaliQ8BYH7.
SMRiQ8BYH7. Positions 276-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231386. 1 interaction.
STRINGi10090.ENSMUSP00000048260.

PTM databases

iPTMnetiQ8BYH7.
PhosphoSiteiQ8BYH7.

Proteomic databases

EPDiQ8BYH7.
MaxQBiQ8BYH7.
PaxDbiQ8BYH7.
PRIDEiQ8BYH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047085; ENSMUSP00000048260; ENSMUSG00000038520.
GeneIDi233204.
KEGGimmu:233204.
UCSCiuc009grc.1. mouse.

Organism-specific databases

CTDi79735.
MGIiMGI:2449973. Tbc1d17.

Phylogenomic databases

eggNOGiKOG2197. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00550000074386.
HOVERGENiHBG057668.
InParanoidiQ8BYH7.
KOiK19945.
OMAiREYLAVM.
OrthoDBiEOG7HTHHR.
TreeFamiTF314296.

Miscellaneous databases

ChiTaRSiTbc1d17. mouse.
PROiQ8BYH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BYH7.
ExpressionAtlasiQ8BYH7. baseline and differential.
GenevisibleiQ8BYH7. MM.

Family and domain databases

InterProiIPR021935. DUF3548.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF12068. DUF3548. 1 hit.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Epididymis and Spinal cord.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTBC17_MOUSE
AccessioniPrimary (citable) accession number: Q8BYH7
Secondary accession number(s): Q3TCA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.