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Protein

TBC1 domain family member 25

Gene

TBC1D25

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

Functioni

Acts as a GTPase-activating protein specific for RAB33B. Involved in the regulation of autophagosome maturation, the process in which autophagosomes fuse with endosomes and lysosomes.1 Publication

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

SIGNORiQ3MII6.

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 25
Gene namesi
Name:TBC1D25
Synonyms:OATL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8092. TBC1D25.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmic vesicleautophagosome 1 Publication

  • Note: It is dispersed in the cytoplasm under nutrient-rich conditions. Localizes at autophagosomes under cell starving conditions.

GO - Cellular componenti

  • autophagosome Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • endomembrane system Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi134 – 1352ED → AA: Severely affects interaction with GABARAP. Does not localize at autophagosomes. 1 Publication
Mutagenesisi136 – 1361W → A: Abolishes interaction with GABARAP. Does not localize at autophagosomes. 1 Publication

Organism-specific databases

PharmGKBiPA162405201.

Polymorphism and mutation databases

BioMutaiTBC1D25.
DMDMi296452922.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 688688TBC1 domain family member 25PRO_0000288508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei160 – 1601PhosphothreonineBy similarity
Modified residuei506 – 5061PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3MII6.
MaxQBiQ3MII6.
PaxDbiQ3MII6.
PRIDEiQ3MII6.

PTM databases

iPTMnetiQ3MII6.
PhosphoSiteiQ3MII6.

Expressioni

Gene expression databases

BgeeiQ3MII6.
CleanExiHS_TBC1D25.
ExpressionAtlasiQ3MII6. baseline and differential.
GenevisibleiQ3MII6. HS.

Organism-specific databases

HPAiHPA029197.

Interactioni

Subunit structurei

Interacts (via N-terminus) with MAP1LC3B, GABARAP and GABARAPL2.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110997. 10 interactions.
STRINGi9606.ENSP00000365962.

Structurei

3D structure databases

ProteinModelPortaliQ3MII6.
SMRiQ3MII6. Positions 202-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini228 – 434207Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 287Poly-Ala
Compositional biasi29 – 346Poly-Glu
Compositional biasi494 – 4996Poly-Gly
Compositional biasi559 – 5646Poly-Ser

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2197. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00550000074386.
HOVERGENiHBG103222.
InParanoidiQ3MII6.
OMAiEHRDHIM.
PhylomeDBiQ3MII6.
TreeFamiTF323518.

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. 3 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: Q3MII6-1) [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
MATASGASDL SGSGAPPPGV GAQAAAAAEE EEREVVRVRV KKCESFLPPE
60 70 80 90 100
FRSFAVDPQI TSLDVLQHIL IRAFDLSGKK NFGISYLGRD RLGQEVYLSL
110 120 130 140 150
LSDWDLSTAF ATASKPYLQL RVDIRPSEDS PLLEDWDIIS PKDVIGSDVL
160 170 180 190 200
LAEKRSSLTT AALPFTQSIL TQVGRTLSKV QQVLSWSYGE DVKPFKPPLS
210 220 230 240 250
DAEFHTYLNH EGQLSRPEEL RLRIYHGGVE PSLRKVVWRY LLNVYPDGLT
260 270 280 290 300
GRERMDYMKR KSREYEQLKS EWAQRANPED LEFIRSTVLK DVLRTDRAHP
310 320 330 340 350
YYAGPEDGPH LRALHDLLTT YAVTHPQVSY CQGMSDLASP ILAVMDHEGH
360 370 380 390 400
AFVCFCGIMK RLAANFHPDG RAMATKFAHL KLLLRHADPD FYQYLQEAGA
410 420 430 440 450
DDLFFCYRWL LLELKREFAF DDALRMLEVT WSSLPPDPPE HEVELVGPPS
460 470 480 490 500
QVADAGFGGH RGWPVRQRHM LRPAGGGGST FEDAVDHLAT ASQGPGGGGR
510 520 530 540 550
LLRQASLDGL QQLRDNMGSR RDPLVQLPHP AALISSKSLS EPLLNSPDPL
560 570 580 590 600
LSSFSHPDSP SSSSPPSTQE ASPTGDMAVG SPLMQEVGSP KDPGKSLPPV
610 620 630 640 650
PPMGLPPPQE FGRGNPFMLF LCLAILLEHR DHIMRNGLDY NELAMHFDRL
660 670 680
VRKHHLGRVL RRARALFADY LQSEVWDSEE GAEATAAS
Length:688
Mass (Da):76,327
Last modified:May 18, 2010 - v2
Checksum:i5B070FE11D78D0A4
GO
Isoform 2 (identifier: Q3MII6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-100: KKNFGISYLGRDRLGQEVYLSL → PIARRLGHNQPQRCHWLRRVAG
     101-688: Missing.

Note: No experimental confirmation available.
Show »
Length:100
Mass (Da):10,757
Checksum:i552B53E4E93159B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti455 – 4551A → T in AAI01818 (PubMed:15489334).Curated
Sequence conflicti455 – 4551A → T in AAI01820 (PubMed:15489334).Curated
Sequence conflicti455 – 4551A → T in AAI25089 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771N → S.1 Publication
Corresponds to variant rs2293948 [ dbSNP | Ensembl ].
VAR_057345

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 10022KKNFG…VYLSL → PIARRLGHNQPQRCHWLRRV AG in isoform 2. 1 PublicationVSP_025703Add
BLAST
Alternative sequencei101 – 688588Missing in isoform 2. 1 PublicationVSP_025704Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC115618 Genomic DNA. No translation available.
AF196969 Genomic DNA. No translation available.
BC026050 mRNA. Translation: AAH26050.1.
BC101817 mRNA. Translation: AAI01818.1.
BC101819 mRNA. Translation: AAI01820.1.
BC125088 mRNA. Translation: AAI25089.1.
BC125089 mRNA. Translation: AAI25090.2.
CCDSiCCDS35242.1. [Q3MII6-1]
RefSeqiNP_002527.1. NM_002536.2. [Q3MII6-1]
UniGeneiHs.694353.

Genome annotation databases

EnsembliENST00000376771; ENSP00000365962; ENSG00000068354. [Q3MII6-1]
ENST00000481090; ENSP00000476787; ENSG00000068354. [Q3MII6-2]
GeneIDi4943.
KEGGihsa:4943.
UCSCiuc004dka.2. human. [Q3MII6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC115618 Genomic DNA. No translation available.
AF196969 Genomic DNA. No translation available.
BC026050 mRNA. Translation: AAH26050.1.
BC101817 mRNA. Translation: AAI01818.1.
BC101819 mRNA. Translation: AAI01820.1.
BC125088 mRNA. Translation: AAI25089.1.
BC125089 mRNA. Translation: AAI25090.2.
CCDSiCCDS35242.1. [Q3MII6-1]
RefSeqiNP_002527.1. NM_002536.2. [Q3MII6-1]
UniGeneiHs.694353.

3D structure databases

ProteinModelPortaliQ3MII6.
SMRiQ3MII6. Positions 202-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110997. 10 interactions.
STRINGi9606.ENSP00000365962.

PTM databases

iPTMnetiQ3MII6.
PhosphoSiteiQ3MII6.

Polymorphism and mutation databases

BioMutaiTBC1D25.
DMDMi296452922.

Proteomic databases

EPDiQ3MII6.
MaxQBiQ3MII6.
PaxDbiQ3MII6.
PRIDEiQ3MII6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376771; ENSP00000365962; ENSG00000068354. [Q3MII6-1]
ENST00000481090; ENSP00000476787; ENSG00000068354. [Q3MII6-2]
GeneIDi4943.
KEGGihsa:4943.
UCSCiuc004dka.2. human. [Q3MII6-1]

Organism-specific databases

CTDi4943.
GeneCardsiTBC1D25.
HGNCiHGNC:8092. TBC1D25.
HPAiHPA029197.
MIMi311240. gene.
neXtProtiNX_Q3MII6.
PharmGKBiPA162405201.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2197. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00550000074386.
HOVERGENiHBG103222.
InParanoidiQ3MII6.
OMAiEHRDHIM.
PhylomeDBiQ3MII6.
TreeFamiTF323518.

Enzyme and pathway databases

SIGNORiQ3MII6.

Miscellaneous databases

GenomeRNAii4943.
PROiQ3MII6.
SOURCEiSearch...

Gene expression databases

BgeeiQ3MII6.
CleanExiHS_TBC1D25.
ExpressionAtlasiQ3MII6. baseline and differential.
GenevisibleiQ3MII6. 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. 3 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] (ISOFORMS 1 AND 2), VARIANT SER-277.
    Tissue: Brain and Pancreas.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  5. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation."
    Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.
    J. Cell Biol. 192:839-853(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP1LC3B; GABARAP AND GABARAPL2, MUTAGENESIS OF 134-GLU-ASP-135 AND TRP-136.
  7. "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-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTBC25_HUMAN
AccessioniPrimary (citable) accession number: Q3MII6
Secondary accession number(s): Q08AN9, Q3MII4, Q8TAR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 88 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. 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.