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Q15125

- EBP_HUMAN

UniProt

Q15125 - EBP_HUMAN

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Protein
3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
Gene
EBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.

Catalytic activityi

5-alpha-cholest-7-en-3-beta-ol = 5-alpha-cholest-8-en-3-beta-ol.

Pathwayi

GO - Molecular functioni

  1. C-8 sterol isomerase activity Source: Ensembl
  2. cholestenol delta-isomerase activity Source: UniProtKB-EC
  3. drug transmembrane transporter activity Source: ProtInc
  4. steroid delta-isomerase activity Source: ProtInc
  5. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. cholesterol biosynthetic process Source: Reactome
  2. cholesterol metabolic process Source: ProtInc
  3. drug transmembrane transport Source: GOC
  4. hemopoiesis Source: Ensembl
  5. signal transduction Source: GOC
  6. skeletal system development Source: ProtInc
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000147155-MONOMER.
BRENDAi5.3.3.5. 2681.
ReactomeiREACT_9405. Cholesterol biosynthesis.
SABIO-RKQ15125.
UniPathwayiUPA00063.

Names & Taxonomyi

Protein namesi
Recommended name:
3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC:5.3.3.5)
Alternative name(s):
Cholestenol Delta-isomerase
Delta(8)-Delta(7) sterol isomerase
Short name:
D8-D7 sterol isomerase
Emopamil-binding protein
Gene namesi
Name:EBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:3133. EBP.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4921Helical; Reviewed prediction
Add
BLAST
Transmembranei66 – 8621Helical; Reviewed prediction
Add
BLAST
Transmembranei121 – 14121Helical; Reviewed prediction
Add
BLAST
Transmembranei185 – 20521Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Chondrodysplasia punctata 2, X-linked dominant (CDPX2) [MIM:302960]: A clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. The key clinical features of CDPX2 are chondrodysplasia punctata, linear ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of defective cholesterol biosynthesis, biochemically characterized by an increased amount of 8-dehydrocholesterol and cholest-8(9)-en-3-beta-ol in the plasma and tissues.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801E → K in CDPX2. 1 Publication
Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
VAR_012105
Natural varianti110 – 1101R → Q in CDPX2. 1 Publication
VAR_012106
Natural varianti147 – 1471R → G in CDPX2. 1 Publication
VAR_012107
Natural varianti147 – 1471R → H in CDPX2. 2 Publications
Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
VAR_012108

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681W → A: Reduces catalytic activity to less than 35% of wild-type.
Mutagenesisi75 – 751I → A: Reduces catalytic activity to less than 35% of wild-type.
Mutagenesisi76 – 761H → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesisi80 – 801E → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesisi111 – 1111Y → W: Reduces catalytic activity to less than 2% of wild-type. 1 Publication
Mutagenesisi121 – 1211M → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi121 – 1211M → V: No effect on catalytic activity. 1 Publication
Mutagenesisi122 – 1221E → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesisi125 – 1251T → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesisi188 – 1881Y → A: Reduces catalytic activity to less than 35% of wild-type.
Mutagenesisi189 – 1891F → A: Reduces catalytic activity to less than 35% of wild-type. 1 Publication
Mutagenesisi189 – 1891F → L: No effect on catalytic activity. 1 Publication
Mutagenesisi193 – 1931N → A: Reduces catalytic activity to less than 10% of wild-type.
Mutagenesisi196 – 1961W → A: Reduces catalytic activity to less than 10% of wild-type.

Keywords - Diseasei

Cataract, Disease mutation, Dwarfism, Ichthyosis

Organism-specific databases

MIMi302960. phenotype.
Orphaneti35173. X-linked dominant chondrodysplasia punctata.
PharmGKBiPA27587.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 2302293-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
PRO_0000174342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15125.
PaxDbiQ15125.
PeptideAtlasiQ15125.
PRIDEiQ15125.

PTM databases

PhosphoSiteiQ15125.

Expressioni

Gene expression databases

ArrayExpressiQ15125.
BgeeiQ15125.
CleanExiHS_EBP.
GenevestigatoriQ15125.

Organism-specific databases

HPAiHPA003130.

Interactioni

Protein-protein interaction databases

BioGridi115921. 7 interactions.
IntActiQ15125. 2 interactions.
STRINGi9606.ENSP00000417052.

Structurei

3D structure databases

ProteinModelPortaliQ15125.

Family & Domainsi

Sequence similaritiesi

Belongs to the EBP family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG331138.
HOGENOMiHOG000204543.
HOVERGENiHBG018176.
InParanoidiQ15125.
KOiK01824.
OMAiFVIHHET.
PhylomeDBiQ15125.
TreeFamiTF314716.

Family and domain databases

InterProiIPR007905. EBP.
[Graphical view]
PANTHERiPTHR14207. PTHR14207. 1 hit.
PfamiPF05241. EBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15125-1 [UniParc]FASTAAdd to Basket

« Hide

MTTNAGPLHP YWPQHLRLDN FVPNDRPTWH ILAGLFSVTG VLVVTTWLLS    50
GRAAVVPLGT WRRLSLCWFA VCGFIHLVIE GWFVLYYEDL LGDQAFLSQL 100
WKEYAKGDSR YILGDNFTVC METITACLWG PLSLWVVIAF LRQHPLRFIL 150
QLVVSVGQIY GDVLYFLTEH RDGFQHGELG HPLYFWFYFV FMNALWLVLP 200
GVLVLDAVKH LTHAQSTLDA KATKAKSKKN 230
Length:230
Mass (Da):26,353
Last modified:January 23, 2007 - v3
Checksum:i3931A9DE3DBAFA04
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801E → K in CDPX2. 1 Publication
Corresponds to variant rs28936073 [ dbSNP | Ensembl ].
VAR_012105
Natural varianti110 – 1101R → Q in CDPX2. 1 Publication
VAR_012106
Natural varianti147 – 1471R → G in CDPX2. 1 Publication
VAR_012107
Natural varianti147 – 1471R → H in CDPX2. 2 Publications
Corresponds to variant rs28935174 [ dbSNP | Ensembl ].
VAR_012108

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1882FY → IF in CAG33096. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z37986 mRNA. Translation: CAA86068.1.
CR456815 mRNA. Translation: CAG33096.1.
CR542094 mRNA. Translation: CAG46891.1.
AF196969 Genomic DNA. No translation available.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50773.1.
BC001549 mRNA. Translation: AAH01549.1.
BC001572 mRNA. Translation: AAH01572.1.
BC046501 mRNA. Translation: AAH46501.1.
CCDSiCCDS14300.1.
PIRiB56122.
RefSeqiNP_006570.1. NM_006579.2.
UniGeneiHs.30619.

Genome annotation databases

EnsembliENST00000495186; ENSP00000417052; ENSG00000147155.
ENST00000598515; ENSP00000471792; ENSG00000268394.
GeneIDi10682.
KEGGihsa:10682.
UCSCiuc004djx.4. human.

Polymorphism databases

DMDMi17374795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z37986 mRNA. Translation: CAA86068.1 .
CR456815 mRNA. Translation: CAG33096.1 .
CR542094 mRNA. Translation: CAG46891.1 .
AF196969 Genomic DNA. No translation available.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50773.1 .
BC001549 mRNA. Translation: AAH01549.1 .
BC001572 mRNA. Translation: AAH01572.1 .
BC046501 mRNA. Translation: AAH46501.1 .
CCDSi CCDS14300.1.
PIRi B56122.
RefSeqi NP_006570.1. NM_006579.2.
UniGenei Hs.30619.

3D structure databases

ProteinModelPortali Q15125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115921. 7 interactions.
IntActi Q15125. 2 interactions.
STRINGi 9606.ENSP00000417052.

Chemistry

BindingDBi Q15125.
ChEMBLi CHEMBL612409.

PTM databases

PhosphoSitei Q15125.

Polymorphism databases

DMDMi 17374795.

Proteomic databases

MaxQBi Q15125.
PaxDbi Q15125.
PeptideAtlasi Q15125.
PRIDEi Q15125.

Protocols and materials databases

DNASUi 10682.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000495186 ; ENSP00000417052 ; ENSG00000147155 .
ENST00000598515 ; ENSP00000471792 ; ENSG00000268394 .
GeneIDi 10682.
KEGGi hsa:10682.
UCSCi uc004djx.4. human.

Organism-specific databases

CTDi 10682.
GeneCardsi GC0XP048380.
GeneReviewsi EBP.
HGNCi HGNC:3133. EBP.
HPAi HPA003130.
MIMi 300205. gene.
302960. phenotype.
neXtProti NX_Q15125.
Orphaneti 35173. X-linked dominant chondrodysplasia punctata.
PharmGKBi PA27587.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG331138.
HOGENOMi HOG000204543.
HOVERGENi HBG018176.
InParanoidi Q15125.
KOi K01824.
OMAi FVIHHET.
PhylomeDBi Q15125.
TreeFami TF314716.

Enzyme and pathway databases

UniPathwayi UPA00063 .
BioCyci MetaCyc:ENSG00000147155-MONOMER.
BRENDAi 5.3.3.5. 2681.
Reactomei REACT_9405. Cholesterol biosynthesis.
SABIO-RK Q15125.

Miscellaneous databases

GenomeRNAii 10682.
NextBioi 40611.
PROi Q15125.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15125.
Bgeei Q15125.
CleanExi HS_EBP.
Genevestigatori Q15125.

Family and domain databases

InterProi IPR007905. EBP.
[Graphical view ]
PANTHERi PTHR14207. PTHR14207. 1 hit.
Pfami PF05241. EBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning, tissue distribution, and heterologous expression."
    Hanner M., Moebius F.F., Weber F., Grabner M., Striessnig J., Glossmann H.
    J. Biol. Chem. 270:7551-7557(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix and Placenta.
  6. "Histidine77, glutamic acid81, glutamic acid123, threonine126, asparagine194, and tryptophan197 of the human emopamil binding protein are required for in vivo sterol delta 8-delta 7 isomerization."
    Moebius F.F., Soellner K.E.M., Fiechtner B., Huck C.W., Bonn G., Glossmann H.
    Biochemistry 38:1119-1127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "Cloning of an emopamil-binding protein (EBP)-like protein that lacks sterol delta8-delta7 isomerase activity."
    Moebius F.F., Fitzky B.U., Wietzorrek G., Haidekker A., Eder A., Glossmann H.
    Biochem. J. 374:229-237(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-111; MET-121 AND PHE-189.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Mutations in a delta(8)-delta(7) sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata."
    Derry J.M.J., Gormally E., Means G.D., Zhao W., Meindl A., Kelley R.I., Boyd Y., Herman G.E.
    Nat. Genet. 22:286-290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDPX2 GLN-110.
  11. "Mutations in the gene encoding 3-beta-hydroxysteroid-delta(8),delta(7)-isomerase cause X-linked dominant Conradi-Hunermann syndrome."
    Braverman N., Lin P., Moebius F.F., Obie C., Moser A., Glossmann H., Wilcox W.R., Rimoin D.L., Smith M., Kratz L., Kelley R.I., Valle D.
    Nat. Genet. 22:291-294(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDPX2 LYS-80 AND HIS-147.
  12. "The Conradi-Hunermann-Happle syndrome (CDPX2) and emopamil binding protein: novel mutations, and somatic and gonadal mosaicism."
    Has C., Bruckner-Tuderman L., Muller D., Floeth M., Folkers E., Donnai D., Traupe H.
    Hum. Mol. Genet. 9:1951-1955(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDPX2 HIS-147.
  13. "Identification of a novel mutation in 3beta-hydroxysteroid-Delta8-Delta7-isomerase in a case of Conradi-Hunermann-Happle syndrome."
    Becker K., Csikos M., Horvath A., Karpati S.
    Exp. Dermatol. 10:286-289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDPX2 GLY-147.

Entry informationi

Entry nameiEBP_HUMAN
AccessioniPrimary (citable) accession number: Q15125
Secondary accession number(s): Q6FGL3, Q6IBI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Binds to the phenylalkylamine calcium-ion antagonist emopamil, an anti-ischemic drug.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi