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Protein

TBC1 domain family member 8

Gene

Tbc1d8

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

Functioni

May act as a GTPase-activating protein for Rab family protein(s).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei551 – 5511Arginine fingerBy similarity
Sitei590 – 5901Glutamine fingerBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 8
Alternative name(s):
BUB2-like protein 1
Vascular Rab-GAP/TBC-containing protein
Gene namesi
Name:Tbc1d8
Synonyms:Hblp1, Vrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1927225. Tbc1d8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11341134TBC1 domain family member 8PRO_0000208034Add
BLAST

Proteomic databases

MaxQBiQ9Z1A9.
PaxDbiQ9Z1A9.
PRIDEiQ9Z1A9.

PTM databases

iPTMnetiQ9Z1A9.
PhosphoSiteiQ9Z1A9.

Expressioni

Gene expression databases

BgeeiQ9Z1A9.
CleanExiMM_TBC1D8.
ExpressionAtlasiQ9Z1A9. baseline and differential.
GenevisibleiQ9Z1A9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049967.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1A9.
SMRiQ9Z1A9. Positions 457-721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 21268GRAM 1Add
BLAST
Domaini285 – 35369GRAM 2Add
BLAST
Domaini504 – 691188Rab-GAP TBCPROSITE-ProRule annotationAdd
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 2 GRAM domains.Curated
Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4347. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00760000119137.
HOGENOMiHOG000276905.
HOVERGENiHBG054142.
InParanoidiQ9Z1A9.
OMAiTYYSCCC.
OrthoDBiEOG7ZWD0Z.
PhylomeDBiQ9Z1A9.
TreeFamiTF313145.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR004182. GRAM.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF02893. GRAM. 2 hits.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLKPEEVLL KNALKLWVTQ KSSCYFVLQR RRGHGEGGGR LTGRLVGALD
60 70 80 90 100
AVLDSSARVA PFRILLQVPG SQVYSPIACG ATLEEINRHW DWLEQNLLHT
110 120 130 140 150
LSVFDNKDDI ASFVKGKVKA LIAEETSSRL AEQEEEPEKF REALVKFEAR
160 170 180 190 200
FNFPEAEKLV TYYSCCCWKG RVPRQGWLYL SINHLCFYSF FLGKELKLVI
210 220 230 240 250
PWVDIQKLER TSNVFLTDTI RITTQNKERD FSTFLNLDEV FKIMEQLADV
260 270 280 290 300
TLRRLLDNEV FDLDPDLQEP SQITKRDLEA RAQNEFFRAF FRLPREEKLH
310 320 330 340 350
AVADCSLWTP FSRCHTAGRI FSSDSYICFA SREDGCCNVV LPLREVVSIE
360 370 380 390 400
KMEDTSLLPN PIIVSIRSKM AFQFIELKDR ENLVEGLLLR LKQVHANHPV
410 420 430 440 450
HYETSPSDDD MASPVFYSAS ICTDKFGDLE MVASQSSEER EEKRPLPHPE
460 470 480 490 500
PLTAVFQQSG SQSPDSRLSR EQIKISLWND HFVEYGRTVC MFRTEKIRKL
510 520 530 540 550
VAMGIPESLR GRLWLLFSDA VTDLASHPGY YGNLVEQSLG RCCLVTEEIE
560 570 580 590 600
RDLHRSLPEH PAFQNETGIA ALRRVLTAYA HRNPKIGYCQ SMNILTSVLL
610 620 630 640 650
LYAKEEEAFW LLVAVCERML PDYFNHRVIG AQVDQSVFEE LIKEQLPELA
660 670 680 690 700
EHMSDLSALA SISLSWFLTL FLSIMPLESA VHVVDCFFYD GIKAIFQLGL
710 720 730 740 750
AVLEANAEEL CSSKDDGQAL MVLSRFLDHI KNEDSPGPPI GSHHAFFSDD
760 770 780 790 800
QEPYPVTDIA DLIRDSYEKF GNQSVEQIEH LRCKHRIRVL QGHEDTTKQN
810 820 830 840 850
VLRVVIPEVS ILPEDLEELY DLFKRAHMMS CYWEHHRPMA LRHDPSRPYA
860 870 880 890 900
EQYRIDARQF AHLFQLVSPW TCGVHTEILA ERLFRLLDDN MDQLIEFKAF
910 920 930 940 950
TSCLDIMYNG EMNEKIKLLY RLHIPPALTE NDRDSQSPLK NPLLSTSRPL
960 970 980 990 1000
VLGKPNGDTI DYQKQLKQMI KDLAKEKDKM EKELPKMSQR EFIQFCKTLY
1010 1020 1030 1040 1050
SMFHEDPEEN DLYQAIATVT TLLLQIGEVG QRGSSSGSCS QECEEPQASA
1060 1070 1080 1090 1100
PPEQDSVFAE AGKSPQAFPE TEGDWTVSLE HILASLLTEQ SLVNFFEKPL
1110 1120 1130
NIKSKLENAK LNQYSLKVLE MSHPPQAELK LNDL
Length:1,134
Mass (Da):130,057
Last modified:November 3, 2009 - v2
Checksum:i1F946A2523488158
GO

Sequence cautioni

The sequence AAD00658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH05421.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti349 – 3491I → F in BAE36878 (PubMed:16141072).Curated
Sequence conflicti705 – 7051A → D in BAE24715 (PubMed:16141072).Curated
Sequence conflicti824 – 8241K → N in BAE36878 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138630 mRNA. Translation: BAE23728.1.
AK141520 mRNA. Translation: BAE24715.1.
AK162371 mRNA. Translation: BAE36878.1.
CH466536 Genomic DNA. Translation: EDL14558.1.
BC065081 mRNA. Translation: AAH65081.1.
BC005421 mRNA. Translation: AAH05421.2. Different initiation.
U88873 mRNA. Translation: AAD00658.1. Different initiation.
CCDSiCCDS14905.1.
RefSeqiNP_061245.3. NM_018775.4.
UniGeneiMm.387293.

Genome annotation databases

EnsembliENSMUST00000054462; ENSMUSP00000049967; ENSMUSG00000003134.
GeneIDi54610.
KEGGimmu:54610.
UCSCiuc007atg.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138630 mRNA. Translation: BAE23728.1.
AK141520 mRNA. Translation: BAE24715.1.
AK162371 mRNA. Translation: BAE36878.1.
CH466536 Genomic DNA. Translation: EDL14558.1.
BC065081 mRNA. Translation: AAH65081.1.
BC005421 mRNA. Translation: AAH05421.2. Different initiation.
U88873 mRNA. Translation: AAD00658.1. Different initiation.
CCDSiCCDS14905.1.
RefSeqiNP_061245.3. NM_018775.4.
UniGeneiMm.387293.

3D structure databases

ProteinModelPortaliQ9Z1A9.
SMRiQ9Z1A9. Positions 457-721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049967.

PTM databases

iPTMnetiQ9Z1A9.
PhosphoSiteiQ9Z1A9.

Proteomic databases

MaxQBiQ9Z1A9.
PaxDbiQ9Z1A9.
PRIDEiQ9Z1A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054462; ENSMUSP00000049967; ENSMUSG00000003134.
GeneIDi54610.
KEGGimmu:54610.
UCSCiuc007atg.3. mouse.

Organism-specific databases

CTDi11138.
MGIiMGI:1927225. Tbc1d8.

Phylogenomic databases

eggNOGiKOG4347. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00760000119137.
HOGENOMiHOG000276905.
HOVERGENiHBG054142.
InParanoidiQ9Z1A9.
OMAiTYYSCCC.
OrthoDBiEOG7ZWD0Z.
PhylomeDBiQ9Z1A9.
TreeFamiTF313145.

Miscellaneous databases

PROiQ9Z1A9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1A9.
CleanExiMM_TBC1D8.
ExpressionAtlasiQ9Z1A9. baseline and differential.
GenevisibleiQ9Z1A9. MM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR004182. GRAM.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF02893. GRAM. 2 hits.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Tissue: Epididymis, Hippocampus 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. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Fetal brain and Mammary tumor.
  4. "The CHESS protein domain: a novel structural unit that is common among networks involved in cell signaling, chromatin metabolism and cell division."
    Guimaraes M.J., Bazan J.F.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-1134.
    Tissue: Hematopoietic.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiTBCD8_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1A9
Secondary accession number(s): Q3TRZ8
, Q3URH3, Q3UU99, Q6P1G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: November 3, 2009
Last modified: June 8, 2016
This is version 102 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.