Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 49 (08 May 2019)
Sequence version 1 (25 Jan 2012)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi64Zinc 11
Metal bindingi64Zinc 21
Metal bindingi67Zinc 11
Metal bindingi74Zinc 11
Metal bindingi81Zinc 11
Metal bindingi81Zinc 21
Metal bindingi84Zinc 21
Metal bindingi93Zinc 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi64 – 93Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd BLAST30

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation
LigandHeme, Iron, Metal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Heme-responsive zinc finger transcription factor HAP1
Alternative name(s):
CYP1 activatory protein
Heme activator protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HAP1
Synonyms:CYP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4932 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi63S → R in CYP1-18; activates the expression of CYP3 (Iso-2) while reducing that of CYC1 (Iso-1). 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003920631 – 1483Heme-responsive zinc finger transcription factor HAP1Add BLAST1483

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P0CS82

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P0CS82

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
HSP82P028293EBI-5419,EBI-8659From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P0CS82, 4 interactors

Molecular INTeraction database

More...
MINTi
P0CS82

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11483
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0CS82

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati280 – 285HRM 16
Repeati299 – 304HRM 26
Repeati323 – 328HRM 36
Repeati347 – 352HRM 46
Repeati389 – 394HRM 56
Repeati415 – 420HRM 66
Repeati1192 – 1197HRM 76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni244 – 444Heme-responsive; required for HMC formationAdd BLAST201

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili105 – 134Sequence analysisAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi177 – 189Poly-GlnAdd BLAST13

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IGKM Eukaryota
ENOG4111QC2 LUCA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00067 GAL4, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
4.10.240.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007219 Transcription_factor_dom_fun
IPR001138 Zn2-C6_fun-type_DNA-bd
IPR036864 Zn2-C6_fun-type_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00172 Zn_clus, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00906 Fungal_trans, 1 hit
SM00066 GAL4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57701 SSF57701, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00463 ZN2_CY6_FUNGAL_1, 1 hit
PS50048 ZN2_CY6_FUNGAL_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i570ECA20E4ED71C6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti145T → I in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti323K → R in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti455S → N in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti508V → M in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti587N → K in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti883D → N in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti960H → S in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti1151D → N in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti1157S → P in AAA34662 (PubMed:2643482).Curated1
Sequence conflicti1305N → Y in AAA34662 (PubMed:2643482).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X13793 Genomic DNA Translation: CAA32032.1
J03152 Genomic DNA Translation: AAA34662.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S59400 RGBYH1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PDB 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[»]
SMRiP0CS82
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0CS82, 4 interactors
MINTiP0CS82

PTM databases

CarbonylDBiP0CS82

Proteomic databases

PRIDEiP0CS82

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IGKM Eukaryota
ENOG4111QC2 LUCA

Family and domain databases

CDDicd00067 GAL4, 1 hit
Gene3Di4.10.240.10, 1 hit
InterProiView protein in InterPro
IPR007219 Transcription_factor_dom_fun
IPR001138 Zn2-C6_fun-type_DNA-bd
IPR036864 Zn2-C6_fun-type_DNA-bd_sf
PfamiView protein in Pfam
PF00172 Zn_clus, 1 hit
SMARTiView protein in SMART
SM00906 Fungal_trans, 1 hit
SM00066 GAL4, 1 hit
SUPFAMiSSF57701 SSF57701, 1 hit
PROSITEiView protein in PROSITE
PS00463 ZN2_CY6_FUNGAL_1, 1 hit
PS50048 ZN2_CY6_FUNGAL_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHAP1_YEASX
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0CS82
Secondary accession number(s): P0CE42
, P12351, Q06574, Q6BD21
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: May 8, 2019
This is version 49 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again