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Protein

TBC1 domain family member 1

Gene

TBC1D1

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

Functioni

May act as a GTPase-activating protein for Rab family protein(s). May play a role in the cell cycle and differentiation of various tissues. Involved in the trafficking and translocation of GLUT4-containing vesicles and insulin-stimulated glucose uptake into cells (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
SIGNORiQ86TI0.

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 1
Gene namesi
Name:TBC1D1
Synonyms:KIAA1108
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11578. TBC1D1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi930 – 9301M → A: Substantially reduced RabGAP GTPase hydrolysis activity. 1 Publication
Mutagenesisi1019 – 10191L → A: Substantially reduced RabGAP GTPase hydrolysis activity. 1 Publication

Organism-specific databases

PharmGKBiPA36342.

Polymorphism and mutation databases

BioMutaiTBC1D1.
DMDMi116242816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11681168TBC1 domain family member 1PRO_0000208022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei235 – 2351Phosphoserine; by PKB/AKT1By similarity
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei503 – 5031PhosphoserineBy similarity
Modified residuei505 – 5051Phosphothreonine; by PKB/AKT1By similarity
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei525 – 5251PhosphoserineBy similarity
Modified residuei527 – 5271PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineCombined sources
Modified residuei566 – 5661PhosphoserineBy similarity
Modified residuei570 – 5701PhosphoserineCombined sources
Modified residuei571 – 5711PhosphoserineBy similarity
Modified residuei585 – 5851PhosphoserineCombined sources
Modified residuei596 – 5961PhosphothreonineBy similarity
Modified residuei614 – 6141PhosphoserineBy similarity
Modified residuei627 – 6271Phosphoserine; by PKB/AKT1By similarity
Modified residuei695 – 6951PhosphoserineBy similarity
Modified residuei941 – 9411PhosphoserineBy similarity
Modified residuei952 – 9521PhosphotyrosineBy similarity
Modified residuei1131 – 11311PhosphothreonineBy similarity

Post-translational modificationi

Insulin-stimulated phosphorylation by AKT family kinases stimulates SLC2A4/GLUT4 translocation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ86TI0.
MaxQBiQ86TI0.
PaxDbiQ86TI0.
PeptideAtlasiQ86TI0.
PRIDEiQ86TI0.

PTM databases

iPTMnetiQ86TI0.
PhosphoSiteiQ86TI0.

Expressioni

Gene expression databases

BgeeiQ86TI0.
CleanExiHS_TBC1D1.
ExpressionAtlasiQ86TI0. baseline and differential.
GenevisibleiQ86TI0. HS.

Organism-specific databases

HPAiHPA041816.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116823. 11 interactions.
IntActiQ86TI0. 8 interactions.
MINTiMINT-1193089.
STRINGi9606.ENSP00000261439.

Structurei

Secondary structure

1
1168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi751 – 7577Combined sources
Helixi768 – 77811Combined sources
Helixi783 – 7853Combined sources
Helixi790 – 7989Combined sources
Helixi803 – 8053Combined sources
Helixi806 – 82015Combined sources
Beta strandi825 – 8273Combined sources
Helixi834 – 8374Combined sources
Helixi845 – 8528Combined sources
Turni860 – 8623Combined sources
Helixi868 – 88316Combined sources
Turni885 – 8873Combined sources
Helixi893 – 9019Combined sources
Helixi906 – 91712Combined sources
Turni918 – 9203Combined sources
Helixi922 – 9265Combined sources
Helixi931 – 94717Combined sources
Helixi949 – 9579Combined sources
Helixi962 – 9643Combined sources
Helixi967 – 9715Combined sources
Turni973 – 9775Combined sources
Helixi980 – 99314Combined sources
Helixi997 – 100812Combined sources
Helixi1010 – 10145Combined sources
Helixi1019 – 102810Combined sources
Turni1029 – 10313Combined sources
Helixi1035 – 104713Combined sources
Helixi1051 – 106515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QYEX-ray2.20A/B746-1072[»]
ProteinModelPortaliQ86TI0.
SMRiQ86TI0. Positions 292-370, 750-1066.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini246 – 404159PIDPROSITE-ProRule annotationAdd
BLAST
Domaini800 – 994195Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4436. Eukaryota.
ENOG410YWJY. LUCA.
GeneTreeiENSGT00750000117238.
HOGENOMiHOG000090019.
HOVERGENiHBG059376.
InParanoidiQ86TI0.
KOiK18341.
OMAiCLIKEDA.
OrthoDBiEOG76T9QM.
PhylomeDBiQ86TI0.
TreeFamiTF317184.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
InterProiIPR021785. DUF3350.
IPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF11830. DUF3350. 1 hit.
PF00640. PID. 1 hit.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
SSF50729. SSF50729. 3 hits.
PROSITEiPS01179. PID. 1 hit.
PS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86TI0-1) [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
MEPITFTARK HLLSNEVSVD FGLQLVGSLP VHSLTTMPML PWVVAEVRRL
60 70 80 90 100
SRQSTRKEPV TKQVRLCVSP SGLRCEPEPG RSQQWDPLIY SSIFECKPQR
110 120 130 140 150
VHKLIHNSHD PSYFACLIKE DAVHRQSICY VFKADDQTKV PEIISSIRQA
160 170 180 190 200
GKIARQEELH CPSEFDDTFS KKFEVLFCGR VTVAHKKAPP ALIDECIEKF
210 220 230 240 250
NHVSGSRGSE SPRPNPPHAA PTGSQEPVRR PMRKSFSQPG LRSLAFRKEL
260 270 280 290 300
QDGGLRSSGF FSSFEESDIE NHLISGHNIV QPTDIEENRT MLFTIGQSEV
310 320 330 340 350
YLISPDTKKI ALEKNFKEIS FCSQGIRHVD HFGFICRESS GGGGFHFVCY
360 370 380 390 400
VFQCTNEALV DEIMMTLKQA FTVAAVQQTA KAPAQLCEGC PLQSLHKLCE
410 420 430 440 450
RIEGMNSSKT KLELQKHLTT LTNQEQATIF EEVQKLRPRN EQRENELIIS
460 470 480 490 500
FLRCLYEEKQ KEHIHIGEMK QTSQMAAENI GSELPPSATR FRLDMLKNKA
510 520 530 540 550
KRSLTESLES ILSRGNKARG LQEHSISVDL DSSLSSTLSN TSKEPSVCEK
560 570 580 590 600
EALPISESSF KLLGSSEDLS SDSESHLPEE PAPLSPQQAF RRRANTLSHF
610 620 630 640 650
PIECQEPPQP ARGSPGVSQR KLMRYHSVST ETPHERKDFE SKANHLGDSG
660 670 680 690 700
GTPVKTRRHS WRQQIFLRVA TPQKACDSSS RYEDYSELGE LPPRSPLEPV
710 720 730 740 750
CEDGPFGPPP EEKKRTSREL RELWQKAILQ QILLLRMEKE NQKLQASEND
760 770 780 790 800
LLNKRLKLDY EEITPCLKEV TTVWEKMLST PGRSKIKFDM EKMHSAVGQG
810 820 830 840 850
VPRHHRGEIW KFLAEQFHLK HQFPSKQQPK DVPYKELLKQ LTSQQHAILI
860 870 880 890 900
DLGRTFPTHP YFSAQLGAGQ LSLYNILKAY SLLDQEVGYC QGLSFVAGIL
910 920 930 940 950
LLHMSEEEAF KMLKFLMFDM GLRKQYRPDM IILQIQMYQL SRLLHDYHRD
960 970 980 990 1000
LYNHLEEHEI GPSLYAAPWF LTMFASQFPL GFVARVFDMI FLQGTEVIFK
1010 1020 1030 1040 1050
VALSLLGSHK PLILQHENLE TIVDFIKSTL PNLGLVQMEK TINQVFEMDI
1060 1070 1080 1090 1100
AKQLQAYEVE YHVLQEELID SSPLSDNQRM DKLEKTNSSL RKQNLDLLEQ
1110 1120 1130 1140 1150
LQVANGRIQS LEATIEKLLS SESKLKQAML TLELERSALL QTVEELRRRS
1160
AEPSDREPEC TQPEPTGD
Length:1,168
Mass (Da):133,084
Last modified:October 17, 2006 - v2
Checksum:i5EFEA168F04C88E0
GO
Isoform 2 (identifier: Q86TI0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     637-637: K → NVDPSPVGES...NTSDFMNTKR
     934-1036: Missing.

Note: No experimental confirmation available.
Show »
Length:1,159
Mass (Da):131,378
Checksum:iA7CE3F7ED898D87C
GO

Sequence cautioni

The sequence BAB55057.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti730 – 7301Q → K in AAH50321 (PubMed:15489334).Curated
Sequence conflicti1095 – 10951L → H in BAH12175 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141S → P.1 Publication
Corresponds to variant rs2279027 [ dbSNP | Ensembl ].
VAR_028089
Natural varianti55 – 551T → I.
Corresponds to variant rs4008480 [ dbSNP | Ensembl ].
VAR_028090
Natural varianti125 – 1251R → W May be associated with risk of familial obesity. 2 Publications
Corresponds to variant rs35859249 [ dbSNP | Ensembl ].
VAR_054392
Natural varianti228 – 2281V → G.
Corresponds to variant rs10501 [ dbSNP | Ensembl ].
VAR_028091
Natural varianti685 – 6851Y → S.
Corresponds to variant rs7677030 [ dbSNP | Ensembl ].
VAR_028092
Natural varianti1136 – 11361R → Q.
Corresponds to variant rs13110318 [ dbSNP | Ensembl ].
VAR_028093

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei637 – 6371K → NVDPSPVGESKHRPGQSSAP APPPRLNPSASSPNFFKYLK HNSSGEQSGNAVPKSISYRN ALRKKLHSSSSVPNFLKFLA PVDENNTSDFMNTKR in isoform 2. 1 PublicationVSP_044749
Alternative sequencei934 – 1036103Missing in isoform 2. 1 PublicationVSP_044750Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027355 mRNA. Translation: BAB55057.1. Different initiation.
AK295746 mRNA. Translation: BAH12175.1.
AC021106 Genomic DNA. No translation available.
AC098680 Genomic DNA. No translation available.
AC108933 Genomic DNA. No translation available.
BC050321 mRNA. Translation: AAH50321.3.
AB029031 mRNA. Translation: BAA83060.1.
CCDSiCCDS33972.1. [Q86TI0-1]
CCDS58897.1. [Q86TI0-2]
RefSeqiNP_001240841.1. NM_001253912.1. [Q86TI0-2]
NP_055988.2. NM_015173.3. [Q86TI0-1]
UniGeneiHs.176503.

Genome annotation databases

EnsembliENST00000261439; ENSP00000261439; ENSG00000065882. [Q86TI0-1]
ENST00000508802; ENSP00000423651; ENSG00000065882. [Q86TI0-2]
GeneIDi23216.
KEGGihsa:23216.
UCSCiuc003gtb.4. human. [Q86TI0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027355 mRNA. Translation: BAB55057.1. Different initiation.
AK295746 mRNA. Translation: BAH12175.1.
AC021106 Genomic DNA. No translation available.
AC098680 Genomic DNA. No translation available.
AC108933 Genomic DNA. No translation available.
BC050321 mRNA. Translation: AAH50321.3.
AB029031 mRNA. Translation: BAA83060.1.
CCDSiCCDS33972.1. [Q86TI0-1]
CCDS58897.1. [Q86TI0-2]
RefSeqiNP_001240841.1. NM_001253912.1. [Q86TI0-2]
NP_055988.2. NM_015173.3. [Q86TI0-1]
UniGeneiHs.176503.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QYEX-ray2.20A/B746-1072[»]
ProteinModelPortaliQ86TI0.
SMRiQ86TI0. Positions 292-370, 750-1066.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116823. 11 interactions.
IntActiQ86TI0. 8 interactions.
MINTiMINT-1193089.
STRINGi9606.ENSP00000261439.

PTM databases

iPTMnetiQ86TI0.
PhosphoSiteiQ86TI0.

Polymorphism and mutation databases

BioMutaiTBC1D1.
DMDMi116242816.

Proteomic databases

EPDiQ86TI0.
MaxQBiQ86TI0.
PaxDbiQ86TI0.
PeptideAtlasiQ86TI0.
PRIDEiQ86TI0.

Protocols and materials databases

DNASUi23216.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261439; ENSP00000261439; ENSG00000065882. [Q86TI0-1]
ENST00000508802; ENSP00000423651; ENSG00000065882. [Q86TI0-2]
GeneIDi23216.
KEGGihsa:23216.
UCSCiuc003gtb.4. human. [Q86TI0-1]

Organism-specific databases

CTDi23216.
GeneCardsiTBC1D1.
H-InvDBHIX0004155.
HGNCiHGNC:11578. TBC1D1.
HPAiHPA041816.
MIMi609850. gene.
neXtProtiNX_Q86TI0.
PharmGKBiPA36342.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4436. Eukaryota.
ENOG410YWJY. LUCA.
GeneTreeiENSGT00750000117238.
HOGENOMiHOG000090019.
HOVERGENiHBG059376.
InParanoidiQ86TI0.
KOiK18341.
OMAiCLIKEDA.
OrthoDBiEOG76T9QM.
PhylomeDBiQ86TI0.
TreeFamiTF317184.

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
SIGNORiQ86TI0.

Miscellaneous databases

ChiTaRSiTBC1D1. human.
GeneWikiiTBC1D1.
GenomeRNAii23216.
PROiQ86TI0.
SOURCEiSearch...

Gene expression databases

BgeeiQ86TI0.
CleanExiHS_TBC1D1.
ExpressionAtlasiQ86TI0. baseline and differential.
GenevisibleiQ86TI0. HS.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
InterProiIPR021785. DUF3350.
IPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF11830. DUF3350. 1 hit.
PF00640. PID. 1 hit.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
SSF50729. SSF50729. 3 hits.
PROSITEiPS01179. PID. 1 hit.
PS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-1168 (ISOFORM 1), VARIANT PRO-14.
    Tissue: Embryo and Hippocampus.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Brain.
  4. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1168 (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-565; SER-570 AND SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating protein (RabGAP) domains reveal critical elements for GLUT4 translocation."
    Park S.Y., Jin W., Woo J.R., Shoelson S.E.
    J. Biol. Chem. 286:18130-18138(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 750-1072, MUTAGENESIS OF MET-930 AND LEU-1019.
  10. Cited for: VARIANT TRP-125.
  11. "R125W coding variant in TBC1D1 confers risk for familial obesity and contributes to linkage on chromosome 4p14 in the French population."
    Meyre D., Farge M., Lecoeur C., Proenca C., Durand E., Allegaert F., Tichet J., Marre M., Balkau B., Weill J., Delplanque J., Froguel P.
    Hum. Mol. Genet. 17:1798-1802(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TRP-125.

Entry informationi

Entry nameiTBCD1_HUMAN
AccessioniPrimary (citable) accession number: Q86TI0
Secondary accession number(s): B7Z3D9
, E9PGH8, Q96K82, Q9UPP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 130 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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.