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Entry version 174 (16 Oct 2019)
Sequence version 1 (01 Nov 1997)
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Protein

Ceramide very long chain fatty acid hydroxylase SCS7

Gene

SCS7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (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

Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids (PubMed:9353282, PubMed:9368039, PubMed:26977056, PubMed:9559540, PubMed:16652392, PubMed:19074599). Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2 (PubMed:9368039, PubMed:26977056).6 Publications

Miscellaneous

Present with 3290 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit that likely form a catalytic dimetal center.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Sphingolipid metabolism

This protein is involved in Sphingolipid metabolism.7 Publications
View all proteins of this organism that are known to be involved in Sphingolipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi45Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi72Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi244Zinc 1; via tele nitrogen1 Publication1
Metal bindingi249Zinc 1; via tele nitrogen1 Publication1
Metal bindingi268Zinc 1; via tele nitrogen1 Publication1
Metal bindingi271Zinc 2; via tele nitrogen1 Publication1
Metal bindingi272Zinc 1; via tele nitrogen1 Publication1
Metal bindingi326Zinc 2; via tele nitrogen1 Publication1
Metal bindingi330Zinc 2; via tele nitrogen1 Publication1
Metal bindingi345Zinc 2; via tele nitrogen1 Publication1
Metal bindingi348Zinc 1; via tele nitrogen1 Publication1
Metal bindingi349Zinc 2; via tele nitrogen1 Publication1

<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

  • fatty acid alpha-hydroxylase activity Source: SGD
  • heme binding Source: InterPro
  • iron ion binding Source: InterPro
  • zinc ion binding Source: UniProtKB

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 functionOxidoreductase
Biological processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport
LigandHeme, Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YMR272C-MONOMER
YEAST:YMR272C-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1660661 Sphingolipid de novo biosynthesis

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001842

<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:
Ceramide very long chain fatty acid hydroxylase SCS71 Publication
Short name:
Ceramide VLCFA hydroxylase SCS71 Publication
Alternative name(s):
4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase SCS72 Publications (EC:1.14.18.62 Publications)
Dihydroceramide fatty acyl 2-hydroxylase SCS71 Publication (EC:1.14.18.71 Publication)
Sphingolipid alpha-hydroxylase1 Publication
Suppressor of calcium sensitivity 7
<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:SCS72 Publications
Synonyms:FAH11 Publication
Ordered Locus Names:YMR272C
ORF Names:YM8156.14C
<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 (strain ATCC 204508 / S288c) (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 identifieri559292 [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 subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YMR272C

Saccharomyces Genome Database

More...
SGDi
S000004885 SCS7

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 197CytoplasmicCuratedAdd BLAST197
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei198 – 216Helical; Name=TM11 PublicationAdd BLAST19
Topological domaini217 – 221LumenalCurated5
Transmembranei222 – 246Helical; Name=TM21 PublicationAdd BLAST25
Topological domaini247 – 284CytoplasmicCuratedAdd BLAST38
Transmembranei285 – 302Helical; Name=TM31 PublicationAdd BLAST18
Topological domaini303 – 304LumenalCurated2
Transmembranei305 – 328Helical; Name=TM41 PublicationAdd BLAST24
Topological domaini329 – 384CytoplasmicCuratedAdd BLAST56

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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>Mutagenesisi173H → A: Reduces the susceptibility to Syringomycin E, showing reduced catalytic activity. 1 Publication1
Mutagenesisi244H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi249H → A: Reduces the susceptibility to Syringomycin E, showing reduced catalytic activity. 1 Publication1
Mutagenesisi264H → A: Maintains the susceptibility to Syringomycin E, showing no effect on catalytic activity. 1 Publication1
Mutagenesisi268H → A: Reduces the susceptibility to Syringomycin E, showing reduced catalytic activity. 1 Publication1
Mutagenesisi271H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi272H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi319Y → A: Maintains the susceptibility to Syringomycin E, showing no effect on catalytic activity. 1 Publication1
Mutagenesisi322Y → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi323D → A: Reduces the susceptibility to Syringomycin E, showing reduced catalytic activity. 1 Publication1
Mutagenesisi326H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi330H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi331H → A: Maintains the susceptibility to Syringomycin E, showing no effect on catalytic activity. 1 Publication1
Mutagenesisi345H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi348H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1
Mutagenesisi349H → A: Confers resistance to Syringomycin E, showing impaired catalytic activity. 1 Publication1

<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_00001854071 – 384Ceramide very long chain fatty acid hydroxylase SCS7Add BLAST384

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q03529

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q03529

PRoteomics IDEntifications database

More...
PRIDEi
Q03529

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q03529

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35451, 1022 interactors

Protein interaction database and analysis system

More...
IntActi
Q03529, 35 interactors

Molecular INTeraction database

More...
MINTi
Q03529

STRING: functional protein association networks

More...
STRINGi
4932.YMR272C

<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

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q03529

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini9 – 90Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST82

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000023981

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q03529

KEGG Orthology (KO)

More...
KOi
K19703

Identification of Orthologs from Complete Genome Data

More...
OMAi
DMTHYFL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001199 Cyt_B5-like_heme/steroid-bd
IPR036400 Cyt_B5-like_heme/steroid_sf
IPR018506 Cyt_B5_heme-BS
IPR006694 Fatty_acid_hydroxylase
IPR014430 Scs7

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00173 Cyt-b5, 1 hit
PF04116 FA_hydroxylase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005149 IPC-B_HD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00363 CYTOCHROMEB5

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01117 Cyt-b5, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55856 SSF55856, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00191 CYTOCHROME_B5_1, 1 hit
PS50255 CYTOCHROME_B5_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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

Q03529-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTNTSKTLE LFSKKTVQEH NTANDCWVTY QNRKIYDVTR FLSEHPGGDE
60 70 80 90 100
SILDYAGKDI TEIMKDSDVH EHSDSAYEIL EDEYLIGYLA TDEEAARLLT
110 120 130 140 150
NKNHKVEVQL SADGTEFDST TFVKELPAEE KLSIATDYSN DYKKHKFLDL
160 170 180 190 200
NRPLLMQILR SDFKKDFYVD QIHRPRHYGK GSAPLFGNFL EPLTKTAWWV
210 220 230 240 250
VPVAWLPVVV YHMGVALKNM NQLFACFLFC VGVFVWTLIE YGLHRFLFHF
260 270 280 290 300
DDWLPESNIA FATHFLLHGC HHYLPMDKYR LVMPPTLFVI LCAPFYKLVF
310 320 330 340 350
ALLPLYWAYA GFAGGLFGYV CYDECHFFLH HSKLPPFMRK LKKYHLEHHY
360 370 380
KNYQLGFGVT SWFWDEVFGT YLGPDAPLSK MKYE
Length:384
Mass (Da):44,881
Last modified:November 1, 1997 - 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:iDF4BA5F2E0EA2218
GO

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
Z49260 Genomic DNA Translation: CAA89255.1
AY693150 Genomic DNA Translation: AAT93169.1
BK006946 Genomic DNA Translation: DAA10172.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S54484

NCBI Reference Sequences

More...
RefSeqi
NP_013999.1, NM_001182779.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR272C_mRNA; YMR272C; YMR272C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855315

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR272C

<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
Z49260 Genomic DNA Translation: CAA89255.1
AY693150 Genomic DNA Translation: AAT93169.1
BK006946 Genomic DNA Translation: DAA10172.1
PIRiS54484
RefSeqiNP_013999.1, NM_001182779.1

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
4ZR0X-ray3.80A/B1-384[»]
4ZR1X-ray2.60A/B96-384[»]
SMRiQ03529
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi35451, 1022 interactors
IntActiQ03529, 35 interactors
MINTiQ03529
STRINGi4932.YMR272C

Chemistry databases

SwissLipidsiSLP:000001842

PTM databases

iPTMnetiQ03529

Proteomic databases

MaxQBiQ03529
PaxDbiQ03529
PRIDEiQ03529

Genome annotation databases

EnsemblFungiiYMR272C_mRNA; YMR272C; YMR272C
GeneIDi855315
KEGGisce:YMR272C

Organism-specific databases

EuPathDBiFungiDB:YMR272C
SGDiS000004885 SCS7

Phylogenomic databases

HOGENOMiHOG000023981
InParanoidiQ03529
KOiK19703
OMAiDMTHYFL

Enzyme and pathway databases

BioCyciMetaCyc:YMR272C-MONOMER
YEAST:YMR272C-MONOMER
ReactomeiR-SCE-1660661 Sphingolipid de novo biosynthesis

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q03529

Family and domain databases

Gene3Di3.10.120.10, 1 hit
InterProiView protein in InterPro
IPR001199 Cyt_B5-like_heme/steroid-bd
IPR036400 Cyt_B5-like_heme/steroid_sf
IPR018506 Cyt_B5_heme-BS
IPR006694 Fatty_acid_hydroxylase
IPR014430 Scs7
PfamiView protein in Pfam
PF00173 Cyt-b5, 1 hit
PF04116 FA_hydroxylase, 1 hit
PIRSFiPIRSF005149 IPC-B_HD, 1 hit
PRINTSiPR00363 CYTOCHROMEB5
SMARTiView protein in SMART
SM01117 Cyt-b5, 1 hit
SUPFAMiSSF55856 SSF55856, 1 hit
PROSITEiView protein in PROSITE
PS00191 CYTOCHROME_B5_1, 1 hit
PS50255 CYTOCHROME_B5_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiSCS7_YEAST
<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: Q03529
Secondary accession number(s): D6W098
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 16, 2019
This is version 174 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, Complete proteome, Reference proteome

Documents

  1. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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