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Protein

TBC1 domain family member 7

Gene

TBC1D7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the TSC-TBC complex, that contains TBC1D7 in addition to the TSC1-TSC2 complex and consists of the functional complex possessing GTPase-activating protein (GAP) activity toward RHEB in response to alterations in specific cellular growth conditions. The small GTPase RHEB is a direct activator of the protein kinase activity of mTORC1 and the TSC-TBC complex acts as a negative regulator of mTORC1 signaling cascade by acting as a GAP for RHEB. Participates in the proper sensing of growth factors and glucose, but not amino acids, by mTORC1. It is unclear whether TBC1D7 acts as a GTPase-activating protein and additional studies are required to answer this question.1 Publication

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • activation of GTPase activity Source: UniProtKB
  • negative regulation of cilium assembly Source: UniProtKB
  • negative regulation of TOR signaling Source: UniProtKB
  • positive regulation of protein ubiquitination Source: UniProtKB
  • response to growth factor Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 7
Alternative name(s):
Cell migration-inducing protein 23
Gene namesi
Name:TBC1D7
Synonyms:TBC7
ORF Names:HSPC239
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21066. TBC1D7.

Subcellular locationi

GO - Cellular componenti

  • ciliary basal body Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Involvement in diseasei

Macrocephaly/megalencephaly syndrome, autosomal recessive (MGCPH)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by abnormal enlargement of the cerebral hemispheres, mental retardation, large head, optic atrophy and underdeveloped skeletal musculature. Head enlargement may be evident at birth or the head may become abnormally large in the early years of life. Additional clinical features include behavioral abnormalities, psychosis, learning difficulties, prognathism, myopia and astigmatism.
See also OMIM:248000

Organism-specific databases

MalaCardsiTBC1D7.
MIMi248000. phenotype.
Orphaneti268920. Isolated megalencephaly.
PharmGKBiPA134929978.

Polymorphism and mutation databases

BioMutaiTBC1D7.
DMDMi37538019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293TBC1 domain family member 7PRO_0000208031Add
BLAST

Proteomic databases

EPDiQ9P0N9.
MaxQBiQ9P0N9.
PaxDbiQ9P0N9.
PRIDEiQ9P0N9.
TopDownProteomicsiQ9P0N9-1. [Q9P0N9-1]

PTM databases

iPTMnetiQ9P0N9.
PhosphoSiteiQ9P0N9.

Expressioni

Tissue specificityi

Highly expressed in heart, and slightly in kidney, liver and placenta.1 Publication

Gene expression databases

BgeeiQ9P0N9.
CleanExiHS_TBC1D7.
ExpressionAtlasiQ9P0N9. baseline and differential.
GenevisibleiQ9P0N9. HS.

Organism-specific databases

HPAiHPA034748.

Interactioni

Subunit structurei

Component of the TSC-TBC complex (also named Rhebulator complex), composed of the TSC1-TSC2 heterodimer and TBC1D7. Interacts with TSC1 (via C-terminal half of the coiled-coil domain).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLZF1Q9H2G93EBI-3258000,EBI-2548012
HOOK1Q9UJC33EBI-3258000,EBI-746704
KRT19P087273EBI-3258000,EBI-742756
LDOC1O957513EBI-3258000,EBI-740738
LZTS2Q9BRK43EBI-3258000,EBI-741037
RPGRIP1Q96KN73EBI-3258000,EBI-1050213
SSNA1O438053EBI-3258000,EBI-2515299
TRAF4Q9BUZ43EBI-3258000,EBI-3650647

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119412. 24 interactions.
IntActiQ9P0N9. 14 interactions.
STRINGi9606.ENSP00000348813.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3110Combined sources
Beta strandi34 – 363Combined sources
Helixi39 – 4810Combined sources
Helixi53 – 6311Combined sources
Helixi71 – 733Combined sources
Helixi74 – 9421Combined sources
Helixi104 – 11613Combined sources
Helixi129 – 14416Combined sources
Helixi148 – 16316Combined sources
Turni164 – 1696Combined sources
Helixi170 – 1723Combined sources
Helixi173 – 18412Combined sources
Helixi186 – 1949Combined sources
Helixi198 – 2003Combined sources
Helixi203 – 2075Combined sources
Turni210 – 2145Combined sources
Helixi217 – 22812Combined sources
Helixi234 – 24512Combined sources
Helixi247 – 2526Combined sources
Helixi256 – 2638Combined sources
Helixi271 – 28616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QWLX-ray1.90A1-293[»]
5EJCX-ray3.10A/B18-293[»]
ProteinModelPortaliQ9P0N9.
SMRiQ9P0N9. Positions 21-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 231182Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IHB4. Eukaryota.
ENOG410YME8. LUCA.
GeneTreeiENSGT00390000009122.
HOGENOMiHOG000007897.
HOVERGENiHBG055235.
InParanoidiQ9P0N9.
OMAiISGSCKI.
OrthoDBiEOG7CVPZ2.
PhylomeDBiQ9P0N9.
TreeFamiTF323655.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P0N9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTEDSQRNFR SVYYEKVGFR GVEEKKSLEI LLKDDRLDTE KLCTFSQRFP
60 70 80 90 100
LPSMYRALVW KVLLGILPPH HESHAKVMMY RKEQYLDVLH ALKVVRFVSD
110 120 130 140 150
ATPQAEVYLR MYQLESGKLP RSPSFPLEPD DEVFLAIAKA MEEMVEDSVD
160 170 180 190 200
CYWITRRFVN QLNTKYRDSL PQLPKAFEQY LNLEDGRLLT HLRMCSAAPK
210 220 230 240 250
LPYDLWFKRC FAGCLPESSL QRVWDKVVSG SCKILVFVAV EILLTFKIKV
260 270 280 290
MALNSAEKIT KFLENIPQDS SDAIVSKAID LWHKHCGTPV HSS
Length:293
Mass (Da):33,972
Last modified:October 1, 2000 - v1
Checksum:iC2F35E10F10D00C2
GO
Isoform 2 (identifier: Q9P0N9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     38-64: Missing.

Show »
Length:266
Mass (Da):30,747
Checksum:i7F95E3AE0127D94B
GO
Isoform 3 (identifier: Q9P0N9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MTEDSQRNFR...LGILPPHHES → MEGASRNLASTPRV

Note: No experimental confirmation available.
Show »
Length:234
Mass (Da):26,787
Checksum:i0127CB9837D50624
GO
Isoform 4 (identifier: Q9P0N9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-172: Missing.

Note: No experimental confirmation available.
Show »
Length:247
Mass (Da):28,509
Checksum:iCDFF69668B48D871
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591V → I in BAD97165 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671L → W.
Corresponds to variant rs543580 [ dbSNP | Ensembl ].
VAR_052537
Natural varianti136 – 1361A → T.
Corresponds to variant rs9381921 [ dbSNP | Ensembl ].
VAR_052538

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373MTEDS…PHHES → MEGASRNLASTPRV in isoform 3. 1 PublicationVSP_044186Add
BLAST
Alternative sequencei38 – 6427Missing in isoform 2. 1 PublicationVSP_041480Add
BLAST
Alternative sequencei127 – 17246Missing in isoform 4. 1 PublicationVSP_044892Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449888 mRNA. Translation: BAH16631.1.
AY826820 mRNA. Translation: AAX18640.1.
AK057228 mRNA. Translation: BAB71389.1.
AF151073 mRNA. Translation: AAF36159.1.
AY542308 mRNA. Translation: AAT08177.1.
AK223445 mRNA. Translation: BAD97165.1.
AL008729 Genomic DNA. No translation available.
AL589984 Genomic DNA. Translation: CAI21569.1.
CH471087 Genomic DNA. Translation: EAW55325.1.
CH471087 Genomic DNA. Translation: EAW55323.1.
BC050465 mRNA. Translation: AAH50465.1.
BC007054 mRNA. Translation: AAH07054.1.
CCDSiCCDS4523.1. [Q9P0N9-1]
CCDS47376.1. [Q9P0N9-2]
CCDS58995.1. [Q9P0N9-4]
RefSeqiNP_001137436.1. NM_001143964.3. [Q9P0N9-1]
NP_001137437.1. NM_001143965.3. [Q9P0N9-1]
NP_001137438.1. NM_001143966.3. [Q9P0N9-2]
NP_001245386.1. NM_001258457.2. [Q9P0N9-4]
NP_001305734.1. NM_001318805.1. [Q9P0N9-1]
NP_001305738.1. NM_001318809.1. [Q9P0N9-1]
NP_057579.1. NM_016495.5. [Q9P0N9-1]
XP_005249220.1. XM_005249163.2. [Q9P0N9-1]
XP_005249223.1. XM_005249166.1. [Q9P0N9-2]
XP_005249224.1. XM_005249167.1. [Q9P0N9-2]
XP_011512954.1. XM_011514652.1. [Q9P0N9-1]
XP_011512955.1. XM_011514653.1. [Q9P0N9-2]
XP_011512956.1. XM_011514654.1. [Q9P0N9-4]
UniGeneiHs.484678.

Genome annotation databases

EnsembliENST00000343141; ENSP00000343100; ENSG00000145979. [Q9P0N9-4]
ENST00000356436; ENSP00000348813; ENSG00000145979. [Q9P0N9-1]
ENST00000379300; ENSP00000368602; ENSG00000145979. [Q9P0N9-1]
ENST00000379307; ENSP00000368609; ENSG00000145979. [Q9P0N9-2]
ENST00000606214; ENSP00000475727; ENSG00000145979. [Q9P0N9-1]
GeneIDi107080638.
51256.
KEGGihsa:51256.
UCSCiuc003nal.5. human. [Q9P0N9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449888 mRNA. Translation: BAH16631.1.
AY826820 mRNA. Translation: AAX18640.1.
AK057228 mRNA. Translation: BAB71389.1.
AF151073 mRNA. Translation: AAF36159.1.
AY542308 mRNA. Translation: AAT08177.1.
AK223445 mRNA. Translation: BAD97165.1.
AL008729 Genomic DNA. No translation available.
AL589984 Genomic DNA. Translation: CAI21569.1.
CH471087 Genomic DNA. Translation: EAW55325.1.
CH471087 Genomic DNA. Translation: EAW55323.1.
BC050465 mRNA. Translation: AAH50465.1.
BC007054 mRNA. Translation: AAH07054.1.
CCDSiCCDS4523.1. [Q9P0N9-1]
CCDS47376.1. [Q9P0N9-2]
CCDS58995.1. [Q9P0N9-4]
RefSeqiNP_001137436.1. NM_001143964.3. [Q9P0N9-1]
NP_001137437.1. NM_001143965.3. [Q9P0N9-1]
NP_001137438.1. NM_001143966.3. [Q9P0N9-2]
NP_001245386.1. NM_001258457.2. [Q9P0N9-4]
NP_001305734.1. NM_001318805.1. [Q9P0N9-1]
NP_001305738.1. NM_001318809.1. [Q9P0N9-1]
NP_057579.1. NM_016495.5. [Q9P0N9-1]
XP_005249220.1. XM_005249163.2. [Q9P0N9-1]
XP_005249223.1. XM_005249166.1. [Q9P0N9-2]
XP_005249224.1. XM_005249167.1. [Q9P0N9-2]
XP_011512954.1. XM_011514652.1. [Q9P0N9-1]
XP_011512955.1. XM_011514653.1. [Q9P0N9-2]
XP_011512956.1. XM_011514654.1. [Q9P0N9-4]
UniGeneiHs.484678.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QWLX-ray1.90A1-293[»]
5EJCX-ray3.10A/B18-293[»]
ProteinModelPortaliQ9P0N9.
SMRiQ9P0N9. Positions 21-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119412. 24 interactions.
IntActiQ9P0N9. 14 interactions.
STRINGi9606.ENSP00000348813.

PTM databases

iPTMnetiQ9P0N9.
PhosphoSiteiQ9P0N9.

Polymorphism and mutation databases

BioMutaiTBC1D7.
DMDMi37538019.

Proteomic databases

EPDiQ9P0N9.
MaxQBiQ9P0N9.
PaxDbiQ9P0N9.
PRIDEiQ9P0N9.
TopDownProteomicsiQ9P0N9-1. [Q9P0N9-1]

Protocols and materials databases

DNASUi51256.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343141; ENSP00000343100; ENSG00000145979. [Q9P0N9-4]
ENST00000356436; ENSP00000348813; ENSG00000145979. [Q9P0N9-1]
ENST00000379300; ENSP00000368602; ENSG00000145979. [Q9P0N9-1]
ENST00000379307; ENSP00000368609; ENSG00000145979. [Q9P0N9-2]
ENST00000606214; ENSP00000475727; ENSG00000145979. [Q9P0N9-1]
GeneIDi107080638.
51256.
KEGGihsa:51256.
UCSCiuc003nal.5. human. [Q9P0N9-1]

Organism-specific databases

CTDi51256.
GeneCardsiTBC1D7.
HGNCiHGNC:21066. TBC1D7.
HPAiHPA034748.
MalaCardsiTBC1D7.
MIMi248000. phenotype.
612655. gene.
neXtProtiNX_Q9P0N9.
Orphaneti268920. Isolated megalencephaly.
PharmGKBiPA134929978.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHB4. Eukaryota.
ENOG410YME8. LUCA.
GeneTreeiENSGT00390000009122.
HOGENOMiHOG000007897.
HOVERGENiHBG055235.
InParanoidiQ9P0N9.
OMAiISGSCKI.
OrthoDBiEOG7CVPZ2.
PhylomeDBiQ9P0N9.
TreeFamiTF323655.

Miscellaneous databases

ChiTaRSiTBC1D7. human.
GenomeRNAii51256.
NextBioi54410.
PROiQ9P0N9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0N9.
CleanExiHS_TBC1D7.
ExpressionAtlasiQ9P0N9. baseline and differential.
GenevisibleiQ9P0N9. HS.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity."
    Ishibashi K., Kanno E., Itoh T., Fukuda M.
    Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Identification of a migration-inducing gene."
    Kim J.W.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  5. "Identification of a human cell proliferation inducing gene."
    Kim J.W.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFPORMS 1 AND 2).
    Tissue: Eye and Kidney.
  10. "Identification of TBC7 having TBC domain as a novel binding protein to TSC1-TSC2 complex."
    Nakashima A., Yoshino K., Miyamoto T., Eguchi S., Oshiro N., Kikkawa U., Yonezawa K.
    Biochem. Biophys. Res. Commun. 361:218-223(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH TSC1.
  11. Cited for: FUNCTION, IDENTIFICATION IN THE TSC-TBC COMPLEX, INTERACTION WITH TSC1.
  12. Cited for: INVOLVEMENT IN MGCPH.
  13. "TBC1D7 mutations are associated with intellectual disability, macrocrania, patellar dislocation and celiac disease."
    Alfaiz A.A., Micale L., Mandriani B., Augello B., Pellico M.T., Chrast J., Xenarios I., Zelante L., Merla G., Reymond A.
    Hum. Mutat. 35:447-451(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MGCPH.
  14. "Crystal structure of human tbc1 domain family member 7."
    Structural genomics consortium (SGC)
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiTBCD7_HUMAN
AccessioniPrimary (citable) accession number: Q9P0N9
Secondary accession number(s): E7EV96
, Q2TU37, Q53F44, Q5SZL7, Q86VM8, Q96MB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was initially identified as a negative regulator of the TSC1-TSC2 complex (PubMed:17658474). However, it was later shown that TBC1D7 is part of the TSC-TBC complex and participates in GTPase-activating protein activity, leading to inhibition of the TOR signaling cascade (PubMed:22795129). The differences between 2 reports might be explained by experimental conditions in the initial report, in which they overexpressed the TBC1D7 subunit, possibly leading to disrupt the stoichiometric complex and its downstream functions.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.