Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Restriction of telomere capping protein 1

Gene

RTC1

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

Functioni

Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in a process influencing telomere capping.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1293 – 133543RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • positive regulation of TORC1 signaling Source: SGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33531-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Restriction of telomere capping protein 1
Alternative name(s):
SEH-associated protein 2
Gene namesi
Name:RTC1
Synonyms:SEA2
Ordered Locus Names:YOL138C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL138C.
SGDiS000005498. RTC1.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of fungal-type vacuolar membrane Source: SGD
  • Seh1-associated complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

Leads to short telomeres.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13411341Restriction of telomere capping protein 1PRO_0000223528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1036 – 10361PhosphoserineCombined sources
Modified residuei1080 – 10801PhosphoserineCombined sources
Modified residuei1087 – 10871PhosphoserineCombined sources
Modified residuei1089 – 10891PhosphoserineCombined sources
Modified residuei1123 – 11231PhosphoserineCombined sources
Modified residuei1133 – 11331PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08281.

PTM databases

iPTMnetiQ08281.

Interactioni

Subunit structurei

Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1. Interacts with ribosomes.2 Publications

Protein-protein interaction databases

BioGridi34238. 19 interactions.
IntActiQ08281. 42 interactions.
MINTiMINT-4502222.

Structurei

3D structure databases

ProteinModelPortaliQ08281.
SMRiQ08281. Positions 203-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati207 – 24842WD 1Add
BLAST
Repeati256 – 29641WD 2Add
BLAST
Repeati305 – 34238WD 3Add
BLAST
Repeati367 – 40640WD 4Add
BLAST
Repeati439 – 48648WD 5Add
BLAST
Repeati489 – 52739WD 6Add
BLAST
Repeati843 – 88341WD 7Add
BLAST
Repeati1129 – 116941WD 8Add
BLAST
Repeati1216 – 125540WD 9Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi753 – 76513Poly-AspAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat RTC1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 9 WD repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1293 – 133543RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, WD repeat, Zinc-finger

Phylogenomic databases

InParanoidiQ08281.
OMAiGGRDGKC.
OrthoDBiEOG718KMV.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 2 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSPHVENA SIPKGSTPIP KNRNVSSIGK GEFLGSSSSN NSSFRMNHYS
60 70 80 90 100
NSGQPSVLDS IRRPNLTPTF SYSNGVYMPE SHRTSSFNDS YLPYDKNPYA
110 120 130 140 150
KTTGSMSNKS NMKIKTKKNA INTNTRKSSG LIYTTKVDKE LSSIDKVNDP
160 170 180 190 200
NINGLVCAGK THLGLYKFSP SDRSIKCVHD FITPNSNTST RGTTSLLPKL
210 220 230 240 250
SKRTRQNKFS TIADVKTGFN NYKNCIAVCN NSTAISIYDL NKSSSIDNPL
260 270 280 290 300
ITSLCEHTRS INSFDFNMVE SNLIISGGQD SCVKIWDLRS NKSKSSNRSD
310 320 330 340 350
ISINTASDSI RDVKWMPGYN FASKNDQGSS TYGNLKSGYK FASIHDSGYL
360 370 380 390 400
LKFDLRQPAQ YEKKLNAHTG PGLCLNWHPN QEYIATGGRD GKCCLWFVGD
410 420 430 440 450
NANAAENTVL NYGNSPSLHA PNTSLNNSGS LAFPKLTINT GYPVTKLKFK
460 470 480 490 500
PAYSSNIYNS LLGISSMGDE AEVRIYSLAR KYIPKHVLLS ETPSLGLVWW
510 520 530 540 550
DENLIFNIDK GTRINGWDIN KEPTVLENLS KNTTTWRDLD GNGLLSVDQE
560 570 580 590 600
IGSYEVVEPE LQPTSSTTCK KHPGTIKNPK NGNPENQGII GGIKKGFSHT
610 620 630 640 650
GLTSFTPERP PTLKAGPTFS TKSLTLASGA SSFNSSSASL TSLTPQTENR
660 670 680 690 700
EEIAIEPPCI ITLDIPQIFN NIRLTKIAHS RKKNVISESS SMKNSPVEKF
710 720 730 740 750
KYLARQLKFS YIREHNVSDS ADTAYKNDIE NIDVVKNATE THGDNTTTTN
760 770 780 790 800
NNDDGDDDDD DDDDDKIIES HLLKKYNFPE NNTWATLMNE KVNNKKSKRN
810 820 830 840 850
SSSSREFDEK DVRSSISSIS ASRQSHDRAR KIDKNVEAEL QEKIQTLVDL
860 870 880 890 900
ISIATHNASV YLSIDDLTNF KIWILIRDSL LWDLKWMTSS QISSDNASNM
910 920 930 940 950
DANESSDFEA GENLKTGKEF PEEDGAGTSG AESLVEERPQ AFRANSDEPS
960 970 980 990 1000
DAEKKPVSKL KEQLKNTEII PYAQPNEDSD EVLTKLKELQ NQRLESRTKM
1010 1020 1030 1040 1050
GETVSDDVII EEDEHEHQEE EQPHDSPTKS AQFHASPIAK SIPILQKREH
1060 1070 1080 1090 1100
RKSFIDTFML HSPNGYNGDT DIGNEDDNIS PRFTYNSVSP RSKVSSLQSY
1110 1120 1130 1140 1150
ATTTSQLETF KKLSSHTAPI IGSPRHAPSR PDSIGREQLS SSLTKKLAKC
1160 1170 1180 1190 1200
KKIIADPPWD TKKLIKQLYN QATETGNVVL TVNILFLFQT IYQITEIDIA
1210 1220 1230 1240 1250
KDAIAHFLLL LHRYELFGIA ADVLKYCPFE DIMGSEGDQS SIRLFCERCG
1260 1270 1280 1290 1300
ELITNESSKE KLRAEAQQTG NKKIMDKFGY WYCDSCKKKN TSCVLCERPL
1310 1320 1330 1340
KKLTMVILPC GHEGHFQCIQ EWFLDENEQE CPGGCPGVAF I
Length:1,341
Mass (Da):149,344
Last modified:September 21, 2011 - v2
Checksum:i45B62E3D341397AA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti393 – 3931C → S in CAA64732 (PubMed:8896270).Curated
Sequence conflicti393 – 3931C → S in CAA99159 (PubMed:9169874).Curated
Sequence conflicti548 – 5481D → G in CAA64732 (PubMed:8896270).Curated
Sequence conflicti548 – 5481D → G in CAA99159 (PubMed:9169874).Curated
Sequence conflicti1222 – 12221D → DV in CAA64732 (PubMed:8896270).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95465 Genomic DNA. Translation: CAA64732.1.
Z74880 Genomic DNA. Translation: CAA99159.1.
BK006948 Genomic DNA. Translation: DAA10647.2.
PIRiS66835.
RefSeqiNP_014503.2. NM_001183392.2.

Genome annotation databases

EnsemblFungiiYOL138C; YOL138C; YOL138C.
GeneIDi853982.
KEGGisce:YOL138C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95465 Genomic DNA. Translation: CAA64732.1.
Z74880 Genomic DNA. Translation: CAA99159.1.
BK006948 Genomic DNA. Translation: DAA10647.2.
PIRiS66835.
RefSeqiNP_014503.2. NM_001183392.2.

3D structure databases

ProteinModelPortaliQ08281.
SMRiQ08281. Positions 203-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34238. 19 interactions.
IntActiQ08281. 42 interactions.
MINTiMINT-4502222.

PTM databases

iPTMnetiQ08281.

Proteomic databases

MaxQBiQ08281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL138C; YOL138C; YOL138C.
GeneIDi853982.
KEGGisce:YOL138C.

Organism-specific databases

EuPathDBiFungiDB:YOL138C.
SGDiS000005498. RTC1.

Phylogenomic databases

InParanoidiQ08281.
OMAiGGRDGKC.
OrthoDBiEOG718KMV.

Enzyme and pathway databases

BioCyciYEAST:G3O-33531-MONOMER.

Miscellaneous databases

NextBioi975449.
PROiQ08281.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 2 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 12 801 bp fragment of the left arm of yeast chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene for a possible glycophospholipid-anchored surface protein and six other open reading frames."
    Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L., Arino J., Herrero E.
    Yeast 12:1053-1058(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 393 AND 548.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length."
    Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C., Krauskopf A., Kupiec M., McEachern M.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
    Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
    Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RIBOSOMES.
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036 AND SER-1123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae."
    Addinall S.G., Downey M., Yu M., Zubko M.K., Dewar J., Leake A., Hallinan J., Shaw O., James K., Wilkinson D.J., Wipat A., Durocher D., Lydall D.
    Genetics 180:2251-2266(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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-1036; SER-1080; SER-1087; SER-1089; SER-1123 AND SER-1133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-1036; SER-1080; SER-1089 AND SER-1123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae."
    Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P., Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C., Rout M.P., Dargemont C.
    Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, FUNCTION.

Entry informationi

Entry nameiRTC1_YEAST
AccessioniPrimary (citable) accession number: Q08281
Secondary accession number(s): D6W1T1, Q92271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: September 21, 2011
Last modified: May 11, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 606 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.