P39521 (FHL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pre-rRNA-processing protein FHL1

Gene names

Name:	FHL1
Ordered Locus Names:	YPR104C
ORF Names:	P8283.15

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	936 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Controls the pre-rRNA processing machinery in conjunction with IFH1. Presumably acts as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator.
Subcellular location	Nucleus Probable.
Miscellaneous	Present with 639 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Contains 1 FHA domain. Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD positive regulation of ribosomal protein gene transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD regulation of sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	nuclear chromatin Inferred from direct assay. Source: SGD nucleolus Inferred from direct assay. Source: SGD transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome repressing transcription factor binding Inferred from physical interaction. Source: SGD sequence-specific DNA binding Inferred from direct assay. Source: SGD sequence-specific distal enhancer binding RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 936	936	Pre-rRNA-processing protein FHL1		PRO_0000091901
Regions
	Domain	300 – 357	58	FHA
	DNA binding	460 – 552	93	Fork-head
	Compositional bias	816 – 862	47	Ser-rich
Amino acid modifications
	Modified residue	44	1	Phosphoserine Ref.5 Ref.6 Ref.8
	Modified residue	46	1	Phosphothreonine Ref.8
	Modified residue	47	1	Phosphoserine Ref.8
	Modified residue	264	1	Phosphoserine Ref.8
	Modified residue	391	1	Phosphoserine Ref.7 Ref.8
	Modified residue	393	1	Phosphoserine Ref.7 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P39521 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 2FC02DFC0DFFF503	FASTA	936	103,502
	10 20 30 40 50 60 MDGEMAIIES SNHVGTSSPT TETQFTIDSS ALKDQETKES ITNSPTSEVP IETKLPKSSD 70 80 90 100 110 120 IVTEEKHPQN TTTDIENEVE NPVTDDNGNL KLELPDNLDN ADFSKLLEFD AKNDEALFNS 130 140 150 160 170 180 NELLSHTMDP VNNIDLTHDH SREVSSKEDI NIEPVNPDED EREKTQDNTA AVKTEGIRNS 190 200 210 220 230 240 EDTSIQKDEP TADAIYTDVH KLSVNKDTET LPTLVDEKNN MLHMRNNSIT PIMFQQHELV 250 260 270 280 290 300 GQPPQNTVTE NNSTDAETTQ RKLSEPIDAS LPLPNEQPTI FAYARLDFQS FTFYVQTLHA 310 320 330 340 350 360 IIGRRSENDF SHKVDVNLGP SKSISRRHAQ IFYNFGTGRF ELSIIGKNGA FVDDIFVEKG 370 380 390 400 410 420 NTVPLRNKTK IQIGQIPFQF ILPEQERNDD SKSPENADIA ESEINTRNLK KNEPKSKKKI 430 440 450 460 470 480 TTGAKPKKAQ TKPAVKKEKK PPKIPKKVYT LEEIPVEYRT KPTVSYSAML TTCIRKYSTA 490 500 510 520 530 540 KGMSLSEIYA GIRELFPYYK YCPDGWQSSV RHNLSLNKSF RKVSKEGKGW LWGLDEEYIA 550 560 570 580 590 600 ERERQKKKQS EIAVAKAQAA QLKLEQQQHK LQQVPQRGKK DIVSQRSNVN ARKQNISQTL 610 620 630 640 650 660 AANRAASNRK NTASDNQRTM KYLQEQLVIL TRDRKGLSKQ VIAAILTQAL AMTINQVTQA 670 680 690 700 710 720 AKNKGITGNP LTALMDKNPQ HLNLILAAAV NAATAKVTKG EVKQLVNPET TAAAALAAKA 730 740 750 760 770 780 QHSKPIRQPI VQTPHVPDRP PSQLSASASS HPNNYLHDKQ PGSFDPSSLS RFFQPRQNAR 790 800 810 820 830 840 ATSSVAATSV PAAASQNVDA QPKPKPAQDN DLESESGTSS SSSSSSESGS ESDSGSDDGS 850 860 870 880 890 900 ASGSGDNSST SSESESESDS GSEVDEKNNK NEKIDSESIK NNESKDDIPS KDENSSNDNR 910 920 930 EISKTDEEGH DSKRRKVSED INEGITEVNV SLEEKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding for a fork head protein involved in rRNA processing." Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P. Mol. Cell. Biol. 14:2905-2913(1994) [PubMed: 8164651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, MASS SPECTROMETRY. Strain: YAL6B.
[6]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-393, MASS SPECTROMETRY.
[8]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; THR-46; SER-47; SER-264; SER-391 AND SER-393, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z28348 Genomic DNA. Translation: CAA82202.1. U32445 Genomic DNA. Translation: AAB68074.1. BK006949 Genomic DNA. Translation: DAA11518.1.
PIR	S43738.
RefSeq	NP_015429.1. NM_001184201.1.
3D structure databases
ProteinModelPortal	P39521.
SMR	P39521. Positions 291-383, 460-544.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3821N.
IntAct	P39521. 4 interactions.
MINT	MINT-495767.
STRING	P39521.
Proteomic databases
PeptideAtlas	P39521.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPR104C; YPR104C; YPR104C.
GeneID	856219.
KEGG	sce:YPR104C.
NMPDR	fig|4932.3.peg.6565.
Organism-specific databases
CYGD	YPR104c.
SGD	S000006308. FHL1.
Phylogenomic databases
eggNOG	fuNOG10650.
GeneTree	EFGT00050000000171.
HOGENOM	HBG203985.
OMA	ICEWIAN.
OrthoDB	EOG4JDMGH.
Gene expression databases
ArrayExpress	P39521.
Genevestigator	P39521.
GermOnline	YPR104C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000253. FHA_dom. IPR008984. SMAD_FHA_domain. IPR001766. TF_fork_head. IPR018122. TF_fork_head_CS. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:2.60.200.20. FHA. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF00498. FHA. 1 hit. PF00250. Fork_head. 1 hit. [Graphical view]
PRINTS	PR00053. FORKHEAD.
SMART	SM00339. FH. 1 hit. SM00240. FHA. 1 hit. [Graphical view]
SUPFAM	SSF49879. SMAD_FHA. 1 hit.
PROSITE	PS50006. FHA_DOMAIN. 1 hit. PS00657. FORK_HEAD_1. 1 hit. PS00658. FORK_HEAD_2. 1 hit. PS50039. FORK_HEAD_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	981444.

Entry information

Entry name

FHL1_YEAST

Accession

Primary (citable) accession number: P39521
Secondary accession number(s): D6W4A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program