Q04183 (TR120_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRS120
Ordered Locus Names:	YDR407C
ORF Names:	D9509.25, ESBP10

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1289 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.9 Ref.11
Subunit structure	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. Ref.4 Ref.5 Ref.9 Ref.11
Subcellular location	Golgi apparatus › cis-Golgi network Ref.5.
Miscellaneous	Present with 259 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the TRS120 family.
Sequence caution	The sequence CAA59326.1 differs from that shown. Reason: Frameshift at position 61.

Ontologies

Keywords
Biological process	Transport
Cellular component	Golgi apparatus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	early endosome to Golgi transport Inferred from mutant phenotype PubMed 16314430. Source: SGD intra-Golgi vesicle-mediated transport Inferred from mutant phenotype Ref.5. Source: SGD regulation of Rab GTPase activity Inferred from mutant phenotype PubMed 17041589. Source: SGD
Cellular_component	TRAPP complex Inferred from direct assay PubMed 10727015. Source: SGD early endosome Inferred from direct assay PubMed 16314430. Source: SGD trans-Golgi network Inferred from direct assay PubMed 16314430. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GYP6	P32806	2	EBI-32112,EBI-8013

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1289	1289	Trafficking protein particle complex II-specific subunit 120		PRO_0000076355
Amino acid modifications
	Modified residue	371	1	Phosphothreonine Ref.6
	Modified residue	374	1	Phosphoserine Ref.10
	Modified residue	375	1	Phosphothreonine Ref.6
	Modified residue	381	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	435	1	A → C in CAA59326. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q04183 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A1B01959A5875E29	FASTA	1,289	147,662
	10 20 30 40 50 60 MNILKHFPSY VGPSKIRTLV IPIGHWTRKE FNNAVQKLSE FNEIHLSDVT PIDSPIFTPQ 70 80 90 100 110 120 GFPHGKLFFD FLTIDHDDAL ELFLYDFEPF RKTFVIIGLV NDYSDPLTNL NFMKEKYPTL 130 140 150 160 170 180 ISPNLVYASS TPTKELEQTI DTMENVFASS PDMQKNIETI MCDIARNFLT ALNSYYSSYK 190 200 210 220 230 240 HVTLRSPGAI GGNAVLKTTL IRQNSYTSSS SSTPMSAVQS SVSSSSKAGS VTTASKRLSS 250 260 270 280 290 300 FEMTTNSLKR SASLKLATTL STSENRSQQK SLGRQMKILG NFQLLAGRYV DALNSFVDAI 310 320 330 340 350 360 TTLYKVRDYL WLGSALDGIS ICFLLLSYLG LSYQIPQIVS LICPVEKLNF ESSSTGISPV 370 380 390 400 410 420 DSNSKATAST TASSTPRNSI SIAAMQSPRN SIMSLSAPAL NIDVENINLP LLIKCISDKV 430 440 450 460 470 480 LYYYDLSLMH NSEYAPQVVY CEFLLKTLTF MTSCYKSSEF SKDVLDNIVK NQHRALSDIP 490 500 510 520 530 540 NSPMFPRFEV YFYSNKLFEL QLKEMQVEAQ IKIYSTMAEV YRLLGYKRKQ LFVLRLLMVA 550 560 570 580 590 600 LLATPNKIAW HPDYRTLIDT IIELLNINES EAKINVDDPS QSTWLILQKK ILQLCIKVSR 610 620 630 640 650 660 KINDFEYVAK FSSILITKYT HLLNQSEQDA LFKEYIQPSI TNESITSYWD PFILREVVIN 670 680 690 700 710 720 RILDSDPTSN EIPLESDVSS LESLENRQKT QDINPQEVFN PFKRVQPTSF VSNNSTKVPI 730 740 750 760 770 780 LVFLVGDKAE FTCRVQNPFK FDFTINDIQL DEEISEFCEI DRKAVSYSGP YNVKAESIRS 790 800 810 820 830 840 ITLPLIIKKP TYKKIYEISC LKISILKLPL QKFDIINDSR RSNPVEEEAE YSKCIYGKLK 850 860 870 880 890 900 IKILPEQPQL ELLSTSKMTR NSWMMLDGTK TDFHITVRNK SLSCAINHIK IIPMNNIEQM 910 920 930 940 950 960 LKPDYWKKMP PDDLYIMEKQ LDWLSKSCVR IIKLPTVIKP NETITFDLEL DNTAVPFNFT 970 980 990 1000 1010 1020 GFDLLIEYGM SATDESCIYL KKLSIPYEVT LRRTIEVPSM DIIPLNELFS SQVENVDWIE 1030 1040 1050 1060 1070 1080 YVMSKIRAES NLHSRDFILL LLDFRNSWID GIKLNVQFED FTSNEYHVEA SHTSRIIVPI 1090 1100 1110 1120 1130 1140 KKIDYKKYNF ENTPIPRIYP GRQFIQSGLN EEQTIEMRQK FWCREHIISK LKCNWKLTTD 1150 1160 1170 1180 1190 1200 QSVTGSVDFN KFIEKFDHKM VYTIYPGRLF YGVQLLLDEP KVKVGEIINL KIITEPTSTC 1210 1220 1230 1240 1250 1260 RRKQNSTVNF LDIVIFDSKT SKILPRSNRR ILYNGSLTKP ISTTKVSEIN LEIIPIEKGR 1270 1280 YEFSVCISKS NNQDGIIQFD SENVILSVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-371 AND THR-375, MASS SPECTROMETRY. Strain: 2124.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, MASS SPECTROMETRY. Strain: YAL6B.
[9]	"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.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U32274 Genomic DNA. Translation: AAB64847.1. X84902 Genomic DNA. Translation: CAA59326.1. Sequence problems. BK006938 Genomic DNA. Translation: DAA12249.1.
PIR	S69689.
RefSeq	NP_010695.1. NM_001180715.1.
3D structure databases
ProteinModelPortal	Q04183.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6461N.
IntAct	Q04183. 4 interactions.
MINT	MINT-669053.
STRING	4932.YDR407C.
Proteomic databases
PaxDb	Q04183.
PeptideAtlas	Q04183.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR407C; YDR407C; YDR407C.
GeneID	852016.
KEGG	sce:YDR407C.
Organism-specific databases
CYGD	YDR407c.
SGD	S000002815. TRS120.
Phylogenomic databases
eggNOG	NOG307918.
HOGENOM	HOG000142077.
OMA	REAFWYR.
OrthoDB	EOG4MPMZ9.
Gene expression databases
Genevestigator	Q04183.
GermOnline	YDR407C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013935. TRAPP_II_complex_Trs120. [Graphical view]
Pfam	PF08626. TRAPPC9-Trs120. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970225.

Entry information

Entry name

TR120_YEAST

Accession

Primary (citable) accession number: Q04183
Secondary accession number(s): D6VT39, Q05731

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program