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Q04183

- TR120_YEAST

UniProt

Q04183 - TR120_YEAST

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Protein

Trafficking protein particle complex II-specific subunit 120

Gene

TRS120

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS120 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS65 and TRS130.3 Publications

GO - Biological processi

  1. early endosome to Golgi transport Source: SGD
  2. intra-Golgi vesicle-mediated transport Source: SGD
  3. positive regulation of Rab GTPase activity Source: GOC
  4. regulation of Rab GTPase activity Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29951-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Trafficking protein particle complex II-specific subunit 120
Short name:
TRAPP II-specific subunit 120
Alternative name(s):
Transport protein particle 120 kDa subunit
Gene namesi
Name:TRS120
Ordered Locus Names:YDR407C
ORF Names:D9509.25, ESBP10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR407c.
SGDiS000002815. TRS120.

Subcellular locationi

Golgi apparatuscis-Golgi network 1 Publication

GO - Cellular componenti

  1. early endosome Source: SGD
  2. trans-Golgi network Source: SGD
  3. TRAPPII protein complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12891289Trafficking protein particle complex II-specific subunit 120PRO_0000076355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei379 – 3791Phosphoserine1 Publication
Modified residuei387 – 3871Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04183.
PaxDbiQ04183.
PeptideAtlasiQ04183.

Expressioni

Gene expression databases

GenevestigatoriQ04183.

Interactioni

Subunit structurei

Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS120 and TRS130. Interacts directly with TRS65.4 Publications

Protein-protein interaction databases

BioGridi32467. 22 interactions.
DIPiDIP-6461N.
IntActiQ04183. 4 interactions.
MINTiMINT-669053.
STRINGi4932.YDR407C.

Structurei

3D structure databases

ProteinModelPortaliQ04183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TRS120 family.Curated

Phylogenomic databases

eggNOGiNOG307918.
HOGENOMiHOG000142077.
InParanoidiQ04183.
OMAiETIMCDI.
OrthoDBiEOG7DRJBS.

Family and domain databases

InterProiIPR013935. TRAPP_II_complex_Trs120.
[Graphical view]
PfamiPF08626. TRAPPC9-Trs120. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04183-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNILKHFPSY VGPSKIRTLV IPIGHWTRKE FNNAVQKLSE FNEIHLSDVT
60 70 80 90 100
PIDSPIFTPQ GFPHGKLFFD FLTIDHDDAL ELFLYDFEPF RKTFVIIGLV
110 120 130 140 150
NDYSDPLTNL NFMKEKYPTL ISPNLVYASS TPTKELEQTI DTMENVFASS
160 170 180 190 200
PDMQKNIETI MCDIARNFLT ALNSYYSSYK HVTLRSPGAI GGNAVLKTTL
210 220 230 240 250
IRQNSYTSSS SSTPMSAVQS SVSSSSKAGS VTTASKRLSS FEMTTNSLKR
260 270 280 290 300
SASLKLATTL STSENRSQQK SLGRQMKILG NFQLLAGRYV DALNSFVDAI
310 320 330 340 350
TTLYKVRDYL WLGSALDGIS ICFLLLSYLG LSYQIPQIVS LICPVEKLNF
360 370 380 390 400
ESSSTGISPV DSNSKATAST TASSTPRNSI SIAAMQSPRN SIMSLSAPAL
410 420 430 440 450
NIDVENINLP LLIKCISDKV LYYYDLSLMH NSEYAPQVVY CEFLLKTLTF
460 470 480 490 500
MTSCYKSSEF SKDVLDNIVK NQHRALSDIP NSPMFPRFEV YFYSNKLFEL
510 520 530 540 550
QLKEMQVEAQ IKIYSTMAEV YRLLGYKRKQ LFVLRLLMVA LLATPNKIAW
560 570 580 590 600
HPDYRTLIDT IIELLNINES EAKINVDDPS QSTWLILQKK ILQLCIKVSR
610 620 630 640 650
KINDFEYVAK FSSILITKYT HLLNQSEQDA LFKEYIQPSI TNESITSYWD
660 670 680 690 700
PFILREVVIN RILDSDPTSN EIPLESDVSS LESLENRQKT QDINPQEVFN
710 720 730 740 750
PFKRVQPTSF VSNNSTKVPI LVFLVGDKAE FTCRVQNPFK FDFTINDIQL
760 770 780 790 800
DEEISEFCEI DRKAVSYSGP YNVKAESIRS ITLPLIIKKP TYKKIYEISC
810 820 830 840 850
LKISILKLPL QKFDIINDSR RSNPVEEEAE YSKCIYGKLK IKILPEQPQL
860 870 880 890 900
ELLSTSKMTR NSWMMLDGTK TDFHITVRNK SLSCAINHIK IIPMNNIEQM
910 920 930 940 950
LKPDYWKKMP PDDLYIMEKQ LDWLSKSCVR IIKLPTVIKP NETITFDLEL
960 970 980 990 1000
DNTAVPFNFT GFDLLIEYGM SATDESCIYL KKLSIPYEVT LRRTIEVPSM
1010 1020 1030 1040 1050
DIIPLNELFS SQVENVDWIE YVMSKIRAES NLHSRDFILL LLDFRNSWID
1060 1070 1080 1090 1100
GIKLNVQFED FTSNEYHVEA SHTSRIIVPI KKIDYKKYNF ENTPIPRIYP
1110 1120 1130 1140 1150
GRQFIQSGLN EEQTIEMRQK FWCREHIISK LKCNWKLTTD QSVTGSVDFN
1160 1170 1180 1190 1200
KFIEKFDHKM VYTIYPGRLF YGVQLLLDEP KVKVGEIINL KIITEPTSTC
1210 1220 1230 1240 1250
RRKQNSTVNF LDIVIFDSKT SKILPRSNRR ILYNGSLTKP ISTTKVSEIN
1260 1270 1280
LEIIPIEKGR YEFSVCISKS NNQDGIIQFD SENVILSVI
Length:1,289
Mass (Da):147,662
Last modified:November 1, 1996 - v1
Checksum:iA1B01959A5875E29
GO

Sequence cautioni

The sequence CAA59326.1 differs from that shown. Reason: Frameshift at position 61. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti435 – 4351A → C in CAA59326. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32274 Genomic DNA. Translation: AAB64847.1.
X84902 Genomic DNA. Translation: CAA59326.1. Sequence problems.
BK006938 Genomic DNA. Translation: DAA12249.1.
PIRiS69689.
RefSeqiNP_010695.1. NM_001180715.1.

Genome annotation databases

EnsemblFungiiYDR407C; YDR407C; YDR407C.
GeneIDi852016.
KEGGisce:YDR407C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32274 Genomic DNA. Translation: AAB64847.1 .
X84902 Genomic DNA. Translation: CAA59326.1 . Sequence problems.
BK006938 Genomic DNA. Translation: DAA12249.1 .
PIRi S69689.
RefSeqi NP_010695.1. NM_001180715.1.

3D structure databases

ProteinModelPortali Q04183.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32467. 22 interactions.
DIPi DIP-6461N.
IntActi Q04183. 4 interactions.
MINTi MINT-669053.
STRINGi 4932.YDR407C.

Proteomic databases

MaxQBi Q04183.
PaxDbi Q04183.
PeptideAtlasi Q04183.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR407C ; YDR407C ; YDR407C .
GeneIDi 852016.
KEGGi sce:YDR407C.

Organism-specific databases

CYGDi YDR407c.
SGDi S000002815. TRS120.

Phylogenomic databases

eggNOGi NOG307918.
HOGENOMi HOG000142077.
InParanoidi Q04183.
OMAi ETIMCDI.
OrthoDBi EOG7DRJBS.

Enzyme and pathway databases

BioCyci YEAST:G3O-29951-MONOMER.

Miscellaneous databases

NextBioi 970225.

Gene expression databases

Genevestigatori Q04183.

Family and domain databases

InterProi IPR013935. TRAPP_II_complex_Trs120.
[Graphical view ]
Pfami PF08626. TRAPPC9-Trs120. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Mai B., Lipp M.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-731.
  4. "TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion."
    Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L., Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S.
    EMBO J. 17:2494-2503(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TRAPP II COMPLEX.
  5. "TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport."
    Sacher M., Barrowman J., Wang W., Horecka J., Zhang Y., Pypaert M., Ferro-Novick S.
    Mol. Cell 7:433-442(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE TRAPP II COMPLEX, IDENTIFICATION IN THE TRAPP II COMPLEX, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "The role of Trs65 in the Ypt/Rab guanine nucleotide exchange factor function of the TRAPP II complex."
    Liang Y., Morozova N., Tokarev A.A., Mulholland J.W., Segev N.
    Mol. Biol. Cell 18:2533-2541(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRS65.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Molecular architecture of the TRAPPII complex and implications for vesicle tethering."
    Yip C.K., Berscheminski J., Walz T.
    Nat. Struct. Mol. Biol. 17:1298-1304(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TRAP II COMPLEX, FUNCTION OF THE TRAP II COMPLEX.

Entry informationi

Entry nameiTR120_YEAST
AccessioniPrimary (citable) accession number: Q04183
Secondary accession number(s): D6VT39, Q05731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 259 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3