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Protein

Heme-responsive zinc finger transcription factor HAP1

Gene

HAP1

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

Functioni

Regulation of oxygen dependent gene expression. It modulates the expression of Iso-1 (CYP1) and Iso-2 (CYP3) cytochrome c. In response to heme, promotes transcription of genes encoding functions required for respiration, controlling oxidative damage and repression of anaerobic genes. Binds to the sequence 5'-CGGNNNTNNCGG-3'. Is non-functional in terms of iso-1 cytochrome c expression in strain S288c and its derivatives.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Zinc 1
Metal bindingi64 – 641Zinc 2
Metal bindingi67 – 671Zinc 1
Metal bindingi74 – 741Zinc 1
Metal bindingi81 – 811Zinc 1
Metal bindingi81 – 811Zinc 2
Metal bindingi84 – 841Zinc 2
Metal bindingi93 – 931Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi64 – 9330Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Heme, Iron, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Heme-responsive zinc finger transcription factor HAP1
Alternative name(s):
CYP1 activatory protein
Heme activator protein 1
Gene namesi
Name:HAP1
Synonyms:CYP1
OrganismiSaccharomyces cerevisiae (Baker's yeast)
Taxonomic identifieri4932 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631S → R in CYP1-18; activates the expression of CYP3 (Iso-2) while reducing that of CYC1 (Iso-1). 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14831483Heme-responsive zinc finger transcription factor HAP1PRO_0000392063Add
BLAST

Proteomic databases

PaxDbiP0CS82.

Interactioni

Subunit structurei

Binds DNA as a homodimer. Interacts with SRO9 and YDJ1. In the absence of heme, binds to at least four cellular proteins, including YDJ1 and SRO9, forming a high-molecular-weight complex (HMC) which results in repression of its activity and dictates its DNA-binding specificity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP82P028293EBI-5419,EBI-8659From a different organism.

Protein-protein interaction databases

IntActiP0CS82. 4 interactions.
STRINGi4932.YLR256W.

Structurei

Secondary structure

1
1483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 706Combined sources
Beta strandi78 – 803Combined sources
Helixi82 – 876Combined sources
Helixi90 – 923Combined sources
Helixi100 – 12526Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HWTX-ray2.50C/D/G/H55-135[»]
1PYCNMR-A56-126[»]
1QP9X-ray2.80A/B/C/D55-130[»]
2HAPX-ray2.50C/D55-135[»]
ProteinModelPortaliP0CS82.
SMRiP0CS82. Positions 55-128.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati280 – 2856HRM 1
Repeati299 – 3046HRM 2
Repeati323 – 3286HRM 3
Repeati347 – 3526HRM 4
Repeati389 – 3946HRM 5
Repeati415 – 4206HRM 6
Repeati1192 – 11976HRM 7

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 444201Heme-responsive; required for HMC formationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili105 – 13430Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi177 – 18913Poly-GlnAdd
BLAST

Sequence similaritiesi

Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IGKM. Eukaryota.
ENOG4111QC2. LUCA.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR033287. Hap1.
IPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PANTHERiPTHR31405:SF6. PTHR31405:SF6. 3 hits.
PfamiPF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CS82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTPYNSSV PSIASMTQSS VSRSPNMHTA TTPGANTSSN SPPLHMSSDS
60 70 80 90 100
SKIKRKRNRI PLSCTICRKR KVKCDKLRPH CQQCTKTGVA HLCHYMEQTW
110 120 130 140 150
AEEAEKELLK DNELKKLRER VKSLEKTLSK VHSSPSSNSL KSYNTPESSN
160 170 180 190 200
LFMGSDEHTT LVNANTGSAS SASHMHQQQQ QQQQQEQQQD FSRSANANAN
210 220 230 240 250
SSSLSISNKY DNDELDLTKD FDLLHIKSNG TIHLGATHWL SIMKGDPYLK
260 270 280 290 300
LLWGHIFAMR EKLNEWYYQK NSYSKLKSSK CPINHAQAPP SAAAAATRKC
310 320 330 340 350
PVDHSAFSSG MVAPKEETPL PRKCPVDHTM FSSGMIPPRE DTSSQKRCPV
360 370 380 390 400
DHTMYSAGMM PPKDETPSPF STKAMIDHNK HTMNPPQSKC PVDHRNYMKD
410 420 430 440 450
YPSDMANSSS NPASRCPIDH SSMKNTAALP ASTHNTIPHH QPQSGSHARS
460 470 480 490 500
HPAQSRKHDS YMTESEVLAT LCEMLPPKRV IALFIEKFFK HLYPAIPILD
510 520 530 540 550
EQNFKNHVNQ MLSLSSMNPT VNNFGMSMPS SSTLENQPIT QINLPKLSDS
560 570 580 590 600
CNLGILIIIL RLTWLSIPSN SCEVDLGEES GSFLVPNESS NMSASALTSM
610 620 630 640 650
AKEESLLLKH ETPVEALELC QKYLIKFDEL SSISNNNVNL TTVQFAIFYN
660 670 680 690 700
FYMKSASNDL TTLTNTNNTG MANPGHDSES HQILLSNITQ MAFSCGLHRD
710 720 730 740 750
PDNFPQLNAT IPATSQDVSN NGSKKANPST NPTLNNNMSA ATTNSSSRSG
760 770 780 790 800
SADSRSGSNP VNKKENQVSI ERFKHTWRKI WYYIVSMDVN QSLSLGSPRL
810 820 830 840 850
LRNLRDFSDT KLPSASRIDY VRDIKELIIV KNFTLFFQID LCIIAVLNHI
860 870 880 890 900
LNVSLARSVR KFELDSLINL LKNLTYGTEN VNDVVSSLIN KGLLPTSEGG
910 920 930 940 950
SVDSNNDEIY GLPKLPDILN HGQHNQNLYA DGRNTSSSDI DKKLDLPHES
960 970 980 990 1000
TTRALFFSKH MTIRMLLYLL NYILFTHYEP MGSEDPGTNI LAKEYAQEAL
1010 1020 1030 1040 1050
NFAMDGYRNC MIFFNNIRNT NSLFDYMNVI LSYPCLDIGH RSLQFIVCLI
1060 1070 1080 1090 1100
LRAKCGPLTG MRESSIITNG TSSGFNSSVE DEDVKVKQES SDELKKDDFM
1110 1120 1130 1140 1150
KDVNLDSGDS LAEILMSRML LFQKLTKQLS KKYNYAIRMN KSTGFFVSLL
1160 1170 1180 1190 1200
DTPSKKSDSK SGGSSFMLGN WKHPKVSNMS GFLAGDKDQL QKCPVYQDAL
1210 1220 1230 1240 1250
GFVSPTGANE GSAPMQGMSL QGSTARMGGT QLPPIRSYKP ITYTSSNLRR
1260 1270 1280 1290 1300
MNETGEAEAK RRRFNDGYID NNSNNDIPRG ISPKPSNGLS SVQPLLSSFS
1310 1320 1330 1340 1350
MNQLNGGTIP TVPSLTNITS QMGALPSLDR ITTNQINLPD PSRDEAFDNS
1360 1370 1380 1390 1400
IKQMTPMTSA FMNANTTIPS STLNGNMNMN GAGTANTDTS ANGSALSTLT
1410 1420 1430 1440 1450
SPQGSDLASN SATQYKPDLE DFLMQNSNFN GLMINPSSLV EVVGGYNDPN
1460 1470 1480
NLGRNDAVDF LPVDNVEIDG LVDFYRADFP IWE
Length:1,483
Mass (Da):164,151
Last modified:January 25, 2012 - v1
Checksum:i570ECA20E4ED71C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451T → I in AAA34662 (PubMed:2643482).Curated
Sequence conflicti323 – 3231K → R in AAA34662 (PubMed:2643482).Curated
Sequence conflicti455 – 4551S → N in AAA34662 (PubMed:2643482).Curated
Sequence conflicti508 – 5081V → M in AAA34662 (PubMed:2643482).Curated
Sequence conflicti587 – 5871N → K in AAA34662 (PubMed:2643482).Curated
Sequence conflicti883 – 8831D → N in AAA34662 (PubMed:2643482).Curated
Sequence conflicti960 – 9601H → S in AAA34662 (PubMed:2643482).Curated
Sequence conflicti1151 – 11511D → N in AAA34662 (PubMed:2643482).Curated
Sequence conflicti1157 – 11571S → P in AAA34662 (PubMed:2643482).Curated
Sequence conflicti1305 – 13051N → Y in AAA34662 (PubMed:2643482).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13793 Genomic DNA. Translation: CAA32032.1.
J03152 Genomic DNA. Translation: AAA34662.1.
PIRiS59400. RGBYH1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13793 Genomic DNA. Translation: CAA32032.1.
J03152 Genomic DNA. Translation: AAA34662.1.
PIRiS59400. RGBYH1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HWTX-ray2.50C/D/G/H55-135[»]
1PYCNMR-A56-126[»]
1QP9X-ray2.80A/B/C/D55-130[»]
2HAPX-ray2.50C/D55-135[»]
ProteinModelPortaliP0CS82.
SMRiP0CS82. Positions 55-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0CS82. 4 interactions.
STRINGi4932.YLR256W.

Proteomic databases

PaxDbiP0CS82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IGKM. Eukaryota.
ENOG4111QC2. LUCA.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR033287. Hap1.
IPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PANTHERiPTHR31405:SF6. PTHR31405:SF6. 3 hits.
PfamiPF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast. I. Overall organization of the protein sequence displays several novel structural domains."
    Creusot F., Verdiere J., Gaisne M., Slonimski P.P.
    J. Mol. Biol. 204:263-276(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF SER-63.
  2. "Functional dissection and sequence of yeast HAP1 activator."
    Pfeifer K., Kim K.-S., Kogan S., Guarente L.
    Cell 56:291-301(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC MYA-3516 / BWG1-7A.
  3. "HAP1 is nuclear but is bound to a cellular factor in the absence of heme."
    Zhang L., Guarente L.
    J. Biol. Chem. 269:14643-14647(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  4. "The C6 zinc cluster dictates asymmetric binding by HAP1."
    Zhang L., Guarente L.
    EMBO J. 15:4676-4681(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  5. "Regulation of hypoxic gene expression in yeast."
    Zitomer R.S., Carrico P., Deckert J.
    Kidney Int. 51:507-513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "A 'natural' mutation in Saccharomyces cerevisiae strains derived from S288c affects the complex regulatory gene HAP1 (CYP1)."
    Gaisne M., Becam A.-M., Verdiere J., Herbert C.J.
    Curr. Genet. 36:195-200(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION OF STRAIN-SPECIFIC DEFECTIVE TY1 INSERTION.
  7. "The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme."
    Hon T., Lee H.C., Hach A., Johnson J.L., Craig E.A., Erdjument-Bromage H., Tempst P., Zhang L.
    Mol. Cell. Biol. 21:7923-7932(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain."
    Timmerman J., Vuidepot A.-L., Bontems F., Lallemand J.-Y., Gervais M., Shechter E., Guiard B.
    J. Mol. Biol. 259:792-804(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 60-100.
  9. "Structure of HAP1-18-DNA implicates direct allosteric effect of protein-DNA interactions on transcriptional activation."
    King D.A., Zhang L., Guarente L., Marmorstein R.
    Nat. Struct. Biol. 6:22-27(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 55-135 OF MUTANT HAP1-18 COMPLEXED WITH DNA.
  10. "Structure of a HAP1-DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein."
    King D.A., Zhang L., Guarente L., Marmorstein R.
    Nat. Struct. Biol. 6:64-71(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 56-135 IN COMPLEX WITH DNA.
  11. "Structure of HAP1-PC7 bound to DNA: implications for DNA recognition and allosteric effects of DNA-binding on transcriptional activation."
    Lukens A.K., King D.A., Marmorstein R.
    Nucleic Acids Res. 28:3853-3863(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 55-135 OF MUTANT HAP1-PC7 COMPLEXED WITH DNA.
  12. "CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast. II. Missense mutation suggests alternative Zn fingers as discriminating agents of gene control."
    Verdiere J., Gaisne M., Guiard B., Defranoux N., Slonimski P.P.
    J. Mol. Biol. 204:277-282(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-63.

Entry informationi

Entry nameiHAP1_YEASX
AccessioniPrimary (citable) accession number: P0CS82
Secondary accession number(s): P0CE42
, P12351, Q06574, Q6BD21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: July 6, 2016
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Heme is an effector molecule for CYP1/HAP1. The HRM repeat region mediates heme induction by masking the DNA-binding domain in the absence of inducer.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.