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O60427

- FADS1_HUMAN

UniProt

O60427 - FADS1_HUMAN

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Protein
Fatty acid desaturase 1
Gene
FADS1, FADSD5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Isoform 2 does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity By similarity. Isoform 1 is a component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the desaturation of dihomo-gamma-linoleic acid (DHGLA) (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid (EPA)(20:5n-3), respectively.2 Publications

Pathwayi

GO - Molecular functioni

  1. C-5 sterol desaturase activity Source: ProtInc
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro
  4. oxidoreductase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. aging Source: Ensembl
  2. alpha-linolenic acid metabolic process Source: Reactome
  3. arachidonic acid metabolic process Source: Ensembl
  4. cell-cell signaling Source: UniProtKB
  5. cellular lipid metabolic process Source: Reactome
  6. cellular response to starvation Source: UniProtKB
  7. icosanoid biosynthetic process Source: UniProtKB
  8. linoleic acid metabolic process Source: Reactome
  9. phospholipid biosynthetic process Source: UniProtKB
  10. regulation of cell differentiation Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB
  12. response to insulin Source: Ensembl
  13. response to organic cyclic compound Source: Ensembl
  14. response to sucrose Source: Ensembl
  15. response to vitamin A Source: Ensembl
  16. small molecule metabolic process Source: Reactome
  17. unsaturated fatty acid biosynthetic process Source: UniProtKB
  18. unsaturated fatty acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS07617-MONOMER.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
UniPathwayiUPA00658.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid desaturase 1 (EC:1.14.19.-)
Alternative name(s):
Delta(5) fatty acid desaturase
Short name:
D5D
Short name:
Delta(5) desaturase
Short name:
Delta-5 desaturase
Gene namesi
Name:FADS1
Synonyms:FADSD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3574. FADS1.

Subcellular locationi

Isoform 1 : Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Mitochondrion 1 Publication
Isoform 2 : Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 121121Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei122 – 14221Helical; Reviewed prediction
Add
BLAST
Topological domaini143 – 1453Lumenal Reviewed prediction
Transmembranei146 – 17025Helical; Reviewed prediction
Add
BLAST
Topological domaini171 – 26797Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei268 – 28821Helical; Reviewed prediction
Add
BLAST
Topological domaini289 – 30517Lumenal Reviewed prediction
Add
BLAST
Transmembranei306 – 32621Helical; Reviewed prediction
Add
BLAST
Topological domaini327 – 444118Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: UniProtKB
  4. membrane Source: UniProtKB
  5. mitochondrion Source: UniProtKB-SubCell
  6. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27973.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Fatty acid desaturase 1
PRO_0000307096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO60427.
PaxDbiO60427.
PRIDEiO60427.

PTM databases

PhosphoSiteiO60427.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in liver, brain, adrenal gland and heart. Highly expressed in fetal liver and brain.3 Publications

Inductioni

Strongly down-regulated upon differentiation in a neuroblastoma cell line (at protein level).1 Publication

Gene expression databases

ArrayExpressiO60427.
BgeeiO60427.
GenevestigatoriO60427.

Organism-specific databases

HPAiHPA042705.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DHCR7Q9UBM71EBI-1055473,EBI-1054468
PAAF1Q9BRP41EBI-1055473,EBI-1056358

Protein-protein interaction databases

BioGridi110180. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliO60427.
SMRiO60427. Positions 19-107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9478Cytochrome b5 heme-binding
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi179 – 1835Histidine box-1
Motifi216 – 2205Histidine box-2
Motifi382 – 3865Histidine box-3

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5274.
HOVERGENiHBG002839.
InParanoidiO60427.
KOiK10224.
OrthoDBiEOG7G1V6P.
PhylomeDBiO60427.
TreeFamiTF313604.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid/sphinglp_desaturase.
IPR005804. Fatty_acid_desaturase-1.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60427-1) [UniParc]FASTAAdd to Basket

Also known as: FADS1CS

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAPDPVAAET AAQGPTPRYF TWDEVAQRSG CEERWLVIDR KVYNISEFTR    50
RHPGGSRVIS HYAGQDATDP FVAFHINKGL VKKYMNSLLI GELSPEQPSF 100
EPTKNKELTD EFRELRATVE RMGLMKANHV FFLLYLLHIL LLDGAAWLTL 150
WVFGTSFLPF LLCAVLLSAV QAQAGWLQHD FGHLSVFSTS KWNHLLHHFV 200
IGHLKGAPAS WWNHMHFQHH AKPNCFRKDP DINMHPFFFA LGKILSVELG 250
KQKKKYMPYN HQHKYFFLIG PPALLPLYFQ WYIFYFVIQR KKWVDLAWMI 300
TFYVRFFLTY VPLLGLKAFL GLFFIVRFLE SNWFVWVTQM NHIPMHIDHD 350
RNMDWVSTQL QATCNVHKSA FNDWFSGHLN FQIEHHLFPT MPRHNYHKVA 400
PLVQSLCAKH GIEYQSKPLL SAFADIIHSL KESGQLWLDA YLHQ 444
Length:444
Mass (Da):51,964
Last modified:December 11, 2013 - v3
Checksum:iCC3C28D82AA49BF2
GO
Isoform 2 (identifier: O60427-2) [UniParc]FASTAAdd to Basket

Also known as: FADS1AT1

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Note: No experimental confirmation available.

Show »
Length:360
Mass (Da):42,474
Checksum:iCD55B8317E4BF21E
GO

Sequence cautioni

The sequence BAC11182.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAC11229.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721P → S.1 Publication
Corresponds to variant rs17856235 [ dbSNP | Ensembl ].
VAR_035340

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8484Missing in isoform 2.
VSP_047521Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61V → L in AAF29378. 1 Publication
Sequence conflicti9 – 91E → G in BAB55103. 1 Publication
Sequence conflicti15 – 151P → L in AAF29378. 1 Publication
Sequence conflicti100 – 1001F → L in BAC11182. 1 Publication
Sequence conflicti143 – 1431D → E in BAC11182. 1 Publication
Sequence conflicti180 – 1801D → G in BAD96626. 1 Publication
Sequence conflicti212 – 2121W → R in BAB55173. 1 Publication
Sequence conflicti213 – 2131N → S in BAC11182. 1 Publication
Sequence conflicti255 – 2551K → N in AAF29378. 1 Publication
Sequence conflicti319 – 3191F → L in BAB55103. 1 Publication
Sequence conflicti361 – 3611Q → L in AAF70457. 1 Publication
Sequence conflicti381 – 3811F → S in BAC11229. 1 Publication
Sequence conflicti410 – 4101H → R in AAF70457. 1 Publication
Sequence conflicti431 – 4311K → E in BAC11229. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK027427 mRNA. Translation: BAB55103.1.
AK027522 mRNA. Translation: BAB55173.1.
AK074754 mRNA. Translation: BAC11182.1. Different initiation.
AK074819 mRNA. Translation: BAC11229.1. Different initiation.
AK096275 mRNA. Translation: BAG53244.1.
AK289552 mRNA. Translation: BAF82241.1.
AK314199 mRNA. Translation: BAG36877.1.
AC004770 Genomic DNA. Translation: AAC23397.1.
AP002380 Genomic DNA. No translation available.
AF084558 mRNA. Translation: AAG23120.1.
AL512760 mRNA. Translation: CAC21679.1.
AL834479 mRNA. Translation: CAD39138.1.
AK222906 mRNA. Translation: BAD96626.1.
BC007846 mRNA. Translation: AAH07846.1.
AF199596 mRNA. Translation: AAF29378.1.
AF226273 mRNA. Translation: AAF70457.1.
RefSeqiNP_037534.3. NM_013402.4.
UniGeneiHs.503546.

Genome annotation databases

EnsembliENST00000433932; ENSP00000405087; ENSG00000149485. [O60427-2]
ENST00000542506; ENSP00000441403; ENSG00000149485. [O60427-2]
GeneIDi3992.
KEGGihsa:3992.
UCSCiuc001nsh.3. human. [O60427-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK027427 mRNA. Translation: BAB55103.1 .
AK027522 mRNA. Translation: BAB55173.1 .
AK074754 mRNA. Translation: BAC11182.1 . Different initiation.
AK074819 mRNA. Translation: BAC11229.1 . Different initiation.
AK096275 mRNA. Translation: BAG53244.1 .
AK289552 mRNA. Translation: BAF82241.1 .
AK314199 mRNA. Translation: BAG36877.1 .
AC004770 Genomic DNA. Translation: AAC23397.1 .
AP002380 Genomic DNA. No translation available.
AF084558 mRNA. Translation: AAG23120.1 .
AL512760 mRNA. Translation: CAC21679.1 .
AL834479 mRNA. Translation: CAD39138.1 .
AK222906 mRNA. Translation: BAD96626.1 .
BC007846 mRNA. Translation: AAH07846.1 .
AF199596 mRNA. Translation: AAF29378.1 .
AF226273 mRNA. Translation: AAF70457.1 .
RefSeqi NP_037534.3. NM_013402.4.
UniGenei Hs.503546.

3D structure databases

ProteinModelPortali O60427.
SMRi O60427. Positions 19-107.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110180. 4 interactions.

Chemistry

BindingDBi O60427.
ChEMBLi CHEMBL5840.
DrugBanki DB00132. Alpha-Linolenic Acid.
DB00159. Icosapent.

PTM databases

PhosphoSitei O60427.

Proteomic databases

MaxQBi O60427.
PaxDbi O60427.
PRIDEi O60427.

Protocols and materials databases

DNASUi 3992.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000433932 ; ENSP00000405087 ; ENSG00000149485 . [O60427-2 ]
ENST00000542506 ; ENSP00000441403 ; ENSG00000149485 . [O60427-2 ]
GeneIDi 3992.
KEGGi hsa:3992.
UCSCi uc001nsh.3. human. [O60427-1 ]

Organism-specific databases

CTDi 3992.
GeneCardsi GC11M061567.
HGNCi HGNC:3574. FADS1.
HPAi HPA042705.
MIMi 606148. gene.
neXtProti NX_O60427.
PharmGKBi PA27973.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5274.
HOVERGENi HBG002839.
InParanoidi O60427.
KOi K10224.
OrthoDBi EOG7G1V6P.
PhylomeDBi O60427.
TreeFami TF313604.

Enzyme and pathway databases

UniPathwayi UPA00658 .
BioCyci MetaCyc:HS07617-MONOMER.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.

Miscellaneous databases

ChiTaRSi FADS1. human.
GeneWikii FADS1.
GenomeRNAii 3992.
NextBioi 15660.
PROi O60427.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60427.
Bgeei O60427.
Genevestigatori O60427.

Family and domain databases

Gene3Di 3.10.120.10. 1 hit.
InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid/sphinglp_desaturase.
IPR005804. Fatty_acid_desaturase-1.
[Graphical view ]
Pfami PF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view ]
PIRSFi PIRSF015921. FA_sphinglp_des. 1 hit.
PRINTSi PR00363. CYTOCHROMEB5.
SUPFAMi SSF55856. SSF55856. 1 hit.
PROSITEi PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and fatty acid regulation of the human Delta-5 desaturase."
    Cho H.P., Nakamura M., Clarke S.D.
    J. Biol. Chem. 274:37335-37339(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid."
    Leonard A.E., Kelder B., Bobik E.G., Chuang L.-T., Parker-Barnes J.M., Thurmond J.M., Kroeger P.E., Kopchick J.J., Huang Y.-S., Mukerji P.
    Biochem. J. 347:719-724(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Liver.
  3. "cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family."
    Marquardt A., Stoehr H., White K., Weber B.H.
    Genomics 66:175-183(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Retina.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum, Neuroblastoma and Teratocarcinoma.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Melanoma.
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney epithelium.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1), VARIANT SER-272.
    Tissue: Brain.
  9. "A novel FADS1 isoform potentiates FADS2-mediated production of eicosanoid precursor fatty acids."
    Park W.J., Kothapalli K.S., Reardon H.T., Lawrence P., Qian S.B., Brenna J.T.
    J. Lipid Res. 53:1502-1512(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INDUCTION.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFADS1_HUMAN
AccessioniPrimary (citable) accession number: O60427
Secondary accession number(s): A8K0I7
, B2RAI0, Q53GM5, Q8N3A6, Q8NCC7, Q8NCG0, Q96I39, Q96SV3, Q96T10, Q9NRP8, Q9NYX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 11, 2013
Last modified: September 3, 2014
This is version 122 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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