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Protein

TBC1 domain family member 14

Gene

TBC1D14

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

Functioni

Negative regulator of starvation-induced autophagosome formation.1 Publication

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • protein kinase binding Source: BHF-UCL

GO - Biological processi

  • negative regulation of autophagy Source: BHF-UCL
  • recycling endosome to Golgi transport Source: UniProtKB
  • regulation of autophagosome assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 14
Gene namesi
Name:TBC1D14
Synonyms:KIAA1322
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:29246. TBC1D14.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: BHF-UCL
  • Golgi apparatus Source: UniProtKB-SubCell
  • recycling endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi472 – 4721R → A: Loss of inhibition of autophagosome formation; when associated with A-508. 1 Publication
Mutagenesisi508 – 5081Q → A: Loss of inhibition of autophagosome formation; when associated with A-472. 1 Publication

Organism-specific databases

PharmGKBiPA128394697.

Polymorphism and mutation databases

BioMutaiTBC1D14.
DMDMi172044690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 693693TBC1 domain family member 14PRO_0000208040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P2M4.
PaxDbiQ9P2M4.
PRIDEiQ9P2M4.

PTM databases

iPTMnetiQ9P2M4.
PhosphoSiteiQ9P2M4.

Expressioni

Gene expression databases

BgeeiQ9P2M4.
CleanExiHS_TBC1D14.
ExpressionAtlasiQ9P2M4. baseline and differential.
GenevisibleiQ9P2M4. HS.

Organism-specific databases

HPAiHPA036930.
HPA036931.

Interactioni

Subunit structurei

Interacts with ULK1. May interact with RAB11A and RAB11B, but does not exhibit any GTPase-activating activity toward these proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB11BQ159072EBI-2797718,EBI-722234
ULK1O753854EBI-2797718,EBI-908831

GO - Molecular functioni

  • protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi121592. 25 interactions.
IntActiQ9P2M4. 15 interactions.
MINTiMINT-4777056.
STRINGi9606.ENSP00000386921.

Structurei

Secondary structure

1
693
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi373 – 3797Combined sources
Helixi382 – 3843Combined sources
Helixi392 – 3998Combined sources
Helixi404 – 41512Combined sources
Helixi423 – 43614Combined sources
Helixi462 – 47110Combined sources
Helixi475 – 4773Combined sources
Beta strandi479 – 4813Combined sources
Helixi487 – 50014Combined sources
Turni502 – 5043Combined sources
Helixi510 – 52011Combined sources
Helixi523 – 53412Combined sources
Helixi537 – 5437Combined sources
Helixi548 – 56417Combined sources
Helixi566 – 5749Combined sources
Helixi579 – 5813Combined sources
Helixi583 – 5886Combined sources
Turni589 – 5946Combined sources
Helixi597 – 61014Combined sources
Helixi612 – 62514Combined sources
Helixi627 – 6315Combined sources
Helixi635 – 6439Combined sources
Helixi651 – 66010Combined sources
Helixi670 – 6789Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QQ8X-ray2.00A372-687[»]
ProteinModelPortaliQ9P2M4.
SMRiQ9P2M4. Positions 371-679.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P2M4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini401 – 611211Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2223. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00750000117238.
HOGENOMiHOG000016604.
HOVERGENiHBG061665.
InParanoidiQ9P2M4.
OMAiVQMQSRN.
OrthoDBiEOG786H3R.
PhylomeDBiQ9P2M4.
TreeFamiTF313318.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. 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: Q9P2M4-1) [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
MTDGKLSTST NGVAFMGILD GRPGNPLQNL QHVNLKAPRL LSAPEYGPKL
60 70 80 90 100
KLRALEDRHS LQSVDSGIPT LEIGNPEPVP CSAVHVRRKQ SDSDLIPERA
110 120 130 140 150
FQSACALPSC APPAPSSTER EQSVRKSSTF PRTGYDSVKL YSPTSKALTR
160 170 180 190 200
SDDVSVCSVS SLGTELSTTL SVSNEDILDL VVTSSSSAIV TLENDDDPQF
210 220 230 240 250
TNVTLSSIKE TRGLHQQDCV HEAEEGSKLK ILGPFSNFFA RNLLARKQSA
260 270 280 290 300
RLDKHNDLGW KLFGKAPLRE NAQKDSKRIQ KEYEDKAGRP SKPPSPKQNV
310 320 330 340 350
RKNLDFEPLS TTALILEDRP ANLPAKPAEE AQKHRQQYEE MVVQAKKREL
360 370 380 390 400
KEAQRRKKQL EERCRVEESI GNAVLTWNNE ILPNWETMWC SRKVRDLWWQ
410 420 430 440 450
GIPPSVRGKV WSLAIGNELN ITHELFDICL ARAKERWRSL STGGSEVENE
460 470 480 490 500
DAGFSAADRE ASLELIKLDI SRTFPNLCIF QQGGPYHDML HSILGAYTCY
510 520 530 540 550
RPDVGYVQGM SFIAAVLILN LDTADAFIAF SNLLNKPCQM AFFRVDHGLM
560 570 580 590 600
LTYFAAFEVF FEENLPKLFA HFKKNNLTPD IYLIDWIFTL YSKSLPLDLA
610 620 630 640 650
CRIWDVFCRD GEEFLFRTAL GILKLFEDIL TKMDFIHMAQ FLTRLPEDLP
660 670 680 690
AEELFASIAT IQMQSRNKKW AQVLTALQKD SREMEKGSPS LRH
Length:693
Mass (Da):78,137
Last modified:February 26, 2008 - v3
Checksum:i6E1332D236DE45BD
GO
Isoform 2 (identifier: Q9P2M4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-280: Missing.
     281-281: K → M

Note: No experimental confirmation available.
Show »
Length:413
Mass (Da):47,691
Checksum:iE3BF0E3B0730079C
GO

Sequence cautioni

The sequence AAH41167.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA92560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411L → V.2 Publications
Corresponds to variant rs34860182 [ dbSNP | Ensembl ].
VAR_067442
Natural varianti446 – 4461E → Q.
Corresponds to variant rs11731231 [ dbSNP | Ensembl ].
VAR_059856

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 280280Missing in isoform 2. CuratedVSP_041460Add
BLAST
Alternative sequencei281 – 2811K → M in isoform 2. CuratedVSP_041461

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449900 mRNA. Translation: BAH16643.1.
AB037743 mRNA. Translation: BAA92560.1. Different initiation.
AC092463 Genomic DNA. No translation available.
AC097382 Genomic DNA. No translation available.
AC106045 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82375.1.
CH471131 Genomic DNA. Translation: EAW82376.1.
CH471131 Genomic DNA. Translation: EAW82377.1.
BC041167 mRNA. Translation: AAH41167.1. Different initiation.
AL833868 mRNA. Translation: CAD38726.1.
CCDSiCCDS3394.2. [Q9P2M4-1]
CCDS47006.1. [Q9P2M4-2]
RefSeqiNP_001106832.1. NM_001113361.1. [Q9P2M4-1]
NP_001106834.1. NM_001113363.1. [Q9P2M4-2]
NP_001273734.1. NM_001286805.1.
NP_065824.2. NM_020773.2. [Q9P2M4-1]
XP_006713958.1. XM_006713895.2. [Q9P2M4-1]
UniGeneiHs.518611.

Genome annotation databases

EnsembliENST00000409757; ENSP00000386921; ENSG00000132405. [Q9P2M4-1]
ENST00000448507; ENSP00000404041; ENSG00000132405. [Q9P2M4-1]
ENST00000451522; ENSP00000388886; ENSG00000132405. [Q9P2M4-2]
GeneIDi57533.
KEGGihsa:57533.
UCSCiuc003gjs.5. human. [Q9P2M4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449900 mRNA. Translation: BAH16643.1.
AB037743 mRNA. Translation: BAA92560.1. Different initiation.
AC092463 Genomic DNA. No translation available.
AC097382 Genomic DNA. No translation available.
AC106045 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82375.1.
CH471131 Genomic DNA. Translation: EAW82376.1.
CH471131 Genomic DNA. Translation: EAW82377.1.
BC041167 mRNA. Translation: AAH41167.1. Different initiation.
AL833868 mRNA. Translation: CAD38726.1.
CCDSiCCDS3394.2. [Q9P2M4-1]
CCDS47006.1. [Q9P2M4-2]
RefSeqiNP_001106832.1. NM_001113361.1. [Q9P2M4-1]
NP_001106834.1. NM_001113363.1. [Q9P2M4-2]
NP_001273734.1. NM_001286805.1.
NP_065824.2. NM_020773.2. [Q9P2M4-1]
XP_006713958.1. XM_006713895.2. [Q9P2M4-1]
UniGeneiHs.518611.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QQ8X-ray2.00A372-687[»]
ProteinModelPortaliQ9P2M4.
SMRiQ9P2M4. Positions 371-679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121592. 25 interactions.
IntActiQ9P2M4. 15 interactions.
MINTiMINT-4777056.
STRINGi9606.ENSP00000386921.

PTM databases

iPTMnetiQ9P2M4.
PhosphoSiteiQ9P2M4.

Polymorphism and mutation databases

BioMutaiTBC1D14.
DMDMi172044690.

Proteomic databases

MaxQBiQ9P2M4.
PaxDbiQ9P2M4.
PRIDEiQ9P2M4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000409757; ENSP00000386921; ENSG00000132405. [Q9P2M4-1]
ENST00000448507; ENSP00000404041; ENSG00000132405. [Q9P2M4-1]
ENST00000451522; ENSP00000388886; ENSG00000132405. [Q9P2M4-2]
GeneIDi57533.
KEGGihsa:57533.
UCSCiuc003gjs.5. human. [Q9P2M4-1]

Organism-specific databases

CTDi57533.
GeneCardsiTBC1D14.
HGNCiHGNC:29246. TBC1D14.
HPAiHPA036930.
HPA036931.
MIMi614855. gene.
neXtProtiNX_Q9P2M4.
PharmGKBiPA128394697.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2223. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00750000117238.
HOGENOMiHOG000016604.
HOVERGENiHBG061665.
InParanoidiQ9P2M4.
OMAiVQMQSRN.
OrthoDBiEOG786H3R.
PhylomeDBiQ9P2M4.
TreeFamiTF313318.

Miscellaneous databases

ChiTaRSiTBC1D14. human.
EvolutionaryTraceiQ9P2M4.
GenomeRNAii57533.
NextBioi63944.
PROiQ9P2M4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2M4.
CleanExiHS_TBC1D14.
ExpressionAtlasiQ9P2M4. baseline and differential.
GenevisibleiQ9P2M4. HS.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. 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

« 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], VARIANT VAL-41.
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-41.
    Tissue: Brain.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-693.
    Tissue: Testis.
  7. "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."
    Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.
    J. Cell Biol. 197:659-675(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB11A; RAB11 AND ULK1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-472 AND GLN-508.
  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-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "First crystallographic models of human TBC domains in the context of a family-wide structural analysis."
    Tempel W., Tong Y., Dimov S., Bochkarev A., Park H.
    Proteins 71:497-502(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 372-672.

Entry informationi

Entry nameiTBC14_HUMAN
AccessioniPrimary (citable) accession number: Q9P2M4
Secondary accession number(s): B9A6L5
, D3DVT4, E9PAZ6, Q8IW15, Q8NDK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: February 26, 2008
Last modified: May 11, 2016
This is version 119 of the entry and version 3 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.