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Protein

Fatty acid desaturase 2

Gene

FADS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum.2 Publications

Pathwayi

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. stearoyl-CoA 9-desaturase activity Source: Ensembl

GO - Biological processi

  1. alpha-linolenic acid metabolic process Source: Reactome
  2. linoleic acid metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. unsaturated fatty acid biosynthetic process Source: ProtInc
  5. 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:HS05918-MONOMER.
BRENDAi1.14.19.3. 2681.
ReactomeiREACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
UniPathwayiUPA00658.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid desaturase 2 (EC:1.14.19.-)
Alternative name(s):
Delta(6) fatty acid desaturase
Short name:
D6D
Short name:
Delta(6) desaturase
Short name:
Delta-6 desaturase
Gene namesi
Name:FADS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3575. FADS2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 131131CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence AnalysisAdd
BLAST
Topological domaini153 – 1575LumenalSequence Analysis
Transmembranei158 – 17821HelicalSequence AnalysisAdd
BLAST
Topological domaini179 – 26486CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei265 – 28521HelicalSequence AnalysisAdd
BLAST
Topological domaini286 – 30520LumenalSequence AnalysisAdd
BLAST
Transmembranei306 – 32621HelicalSequence AnalysisAdd
BLAST
Topological domaini327 – 444118CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27974.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Fatty acid desaturase 2PRO_0000307101Add
BLAST

Proteomic databases

MaxQBiO95864.
PaxDbiO95864.
PeptideAtlasiO95864.
PRIDEiO95864.

PTM databases

PhosphoSiteiO95864.

Expressioni

Tissue specificityi

Expressed in a wide array of tissues, highest expression is found in liver followed by brain, lung, heart, and retina. A lower level is found in breast tumor when compared with normal tissues; lowest levels were found in patients with poor prognostic index.3 Publications

Developmental stagei

Found in fetal heart.

Inductioni

Repressed by dietary highly unsaturated fatty acids.2 Publications

Gene expression databases

BgeeiO95864.
CleanExiHS_FADS2.
ExpressionAtlasiO95864. baseline and differential.
GenevestigatoriO95864.

Organism-specific databases

HPAiHPA006741.

Interactioni

Protein-protein interaction databases

BioGridi114810. 6 interactions.
MINTiMINT-2866355.
STRINGi9606.ENSP00000278840.

Structurei

3D structure databases

ProteinModelPortaliO95864.
SMRiO95864. Positions 17-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 9578Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1845Histidine box-1
Motifi217 – 2215Histidine 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

Belongs to the fatty acid desaturase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5274.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiO95864.
KOiK10226.
OMAiAWFTIFY.
PhylomeDBiO95864.
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.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95864-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MGKGGNQGEG AAEREVSVPT FSWEEIQKHN LRTDRWLVID RKVYNITKWS
60 70 80 90 100
IQHPGGQRVI GHYAGEDATD AFRAFHPDLE FVGKFLKPLL IGELAPEEPS
110 120 130 140 150
QDHGKNSKIT EDFRALRKTA EDMNLFKTNH VFFLLLLAHI IALESIAWFT
160 170 180 190 200
VFYFGNGWIP TLITAFVLAT SQAQAGWLQH DYGHLSVYRK PKWNHLVHKF
210 220 230 240 250
VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDVNMLHVFV LGEWQPIEYG
260 270 280 290 300
KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIVH KNWVDLAWAV
310 320 330 340 350
SYYIRFFITY IPFYGILGAL LFLNFIRFLE SHWFVWVTQM NHIVMEIDQE
360 370 380 390 400
AYRDWFSSQL TATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA
410 420 430 440
PLVKSLCAKH GIEYQEKPLL RALLDIIRSL KKSGKLWLDA YLHK
Length:444
Mass (Da):52,259
Last modified:April 30, 1999 - v1
Checksum:iF65CE58076961A7A
GO
Isoform 2 (identifier: O95864-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MGKGGNQGEG...IGHYAGEDAT → MHGREAGPFV...SAGHPITGQQ

Show »
Length:422
Mass (Da):49,326
Checksum:iA4A7EB76FBF1FFA4
GO
Isoform 3 (identifier: O95864-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     386-444: HLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK → Q

Note: No experimental confirmation available.

Show »
Length:386
Mass (Da):45,524
Checksum:i2A18FA9CBFBFE432
GO
Isoform 4 (identifier: O95864-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MGKGGNQGEG...IGHYAGEDAT → MTREPPGCRR...HPERWATSSQ

Show »
Length:413
Mass (Da):48,883
Checksum:i3A9CD17C669AE834
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1374LLLL → RTRG in CAB43280 (PubMed:17974005).Curated
Sequence conflicti380 – 3812NF → SL in BAB55167 (PubMed:14702039).Curated
Sequence conflicti429 – 4313SLK → DLM in CAB43280 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969MGKGG…GEDAT → MHGREAGPFVCVCVLLASIP TPQTPLLQASLPPFHPASAG HPITGQQ in isoform 2. 2 PublicationsVSP_028568Add
BLAST
Alternative sequencei1 – 6969MGKGG…GEDAT → MTREPPGCRRVNSLMLYTLR SITSHRSSHPERWATSSQ in isoform 4. 1 PublicationVSP_054809Add
BLAST
Alternative sequencei386 – 44459HLFPT…AYLHK → Q in isoform 3. 1 PublicationVSP_028569Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126799 mRNA. Translation: AAD20018.1.
AF084559 mRNA. Translation: AAG23121.1.
AF108658 mRNA. Translation: AAG43192.1.
AK027513 mRNA. Translation: BAB55167.1.
AK290291 mRNA. Translation: BAF82980.1.
AK299762 mRNA. Translation: BAH13120.1.
AK074939 mRNA. Translation: BAC11305.1.
AP002380 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73975.1.
BC009011 mRNA. Translation: AAH09011.1.
AL050118 mRNA. Translation: CAB43280.1.
BX640945 mRNA. Translation: CAE45971.1.
CCDSiCCDS60807.1. [O95864-2]
CCDS60808.1. [O95864-4]
CCDS8012.1. [O95864-1]
PIRiT13155.
RefSeqiNP_001268430.1. NM_001281501.1. [O95864-2]
NP_001268431.1. NM_001281502.1. [O95864-4]
NP_004256.1. NM_004265.3. [O95864-1]
UniGeneiHs.502745.

Genome annotation databases

EnsembliENST00000257261; ENSP00000257261; ENSG00000134824. [O95864-2]
ENST00000278840; ENSP00000278840; ENSG00000134824. [O95864-1]
ENST00000521849; ENSP00000431091; ENSG00000134824. [O95864-3]
ENST00000522056; ENSP00000429500; ENSG00000134824. [O95864-4]
GeneIDi9415.
KEGGihsa:9415.
UCSCiuc001nsj.2. human. [O95864-2]
uc001nsk.3. human. [O95864-3]
uc001nsl.1. human. [O95864-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126799 mRNA. Translation: AAD20018.1.
AF084559 mRNA. Translation: AAG23121.1.
AF108658 mRNA. Translation: AAG43192.1.
AK027513 mRNA. Translation: BAB55167.1.
AK290291 mRNA. Translation: BAF82980.1.
AK299762 mRNA. Translation: BAH13120.1.
AK074939 mRNA. Translation: BAC11305.1.
AP002380 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73975.1.
BC009011 mRNA. Translation: AAH09011.1.
AL050118 mRNA. Translation: CAB43280.1.
BX640945 mRNA. Translation: CAE45971.1.
CCDSiCCDS60807.1. [O95864-2]
CCDS60808.1. [O95864-4]
CCDS8012.1. [O95864-1]
PIRiT13155.
RefSeqiNP_001268430.1. NM_001281501.1. [O95864-2]
NP_001268431.1. NM_001281502.1. [O95864-4]
NP_004256.1. NM_004265.3. [O95864-1]
UniGeneiHs.502745.

3D structure databases

ProteinModelPortaliO95864.
SMRiO95864. Positions 17-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114810. 6 interactions.
MINTiMINT-2866355.
STRINGi9606.ENSP00000278840.

Chemistry

BindingDBiO95864.
ChEMBLiCHEMBL6097.
DrugBankiDB00132. Alpha-Linolenic Acid.

PTM databases

PhosphoSiteiO95864.

Proteomic databases

MaxQBiO95864.
PaxDbiO95864.
PeptideAtlasiO95864.
PRIDEiO95864.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257261; ENSP00000257261; ENSG00000134824. [O95864-2]
ENST00000278840; ENSP00000278840; ENSG00000134824. [O95864-1]
ENST00000521849; ENSP00000431091; ENSG00000134824. [O95864-3]
ENST00000522056; ENSP00000429500; ENSG00000134824. [O95864-4]
GeneIDi9415.
KEGGihsa:9415.
UCSCiuc001nsj.2. human. [O95864-2]
uc001nsk.3. human. [O95864-3]
uc001nsl.1. human. [O95864-1]

Organism-specific databases

CTDi9415.
GeneCardsiGC11P061583.
HGNCiHGNC:3575. FADS2.
HPAiHPA006741.
MIMi606149. gene.
neXtProtiNX_O95864.
PharmGKBiPA27974.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5274.
GeneTreeiENSGT00510000046574.
HOGENOMiHOG000012997.
HOVERGENiHBG002839.
InParanoidiO95864.
KOiK10226.
OMAiAWFTIFY.
PhylomeDBiO95864.
TreeFamiTF313604.

Enzyme and pathway databases

UniPathwayiUPA00658.
BioCyciMetaCyc:HS05918-MONOMER.
BRENDAi1.14.19.3. 2681.
ReactomeiREACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.

Miscellaneous databases

ChiTaRSiFADS2. human.
GeneWikiiFADS2.
GenomeRNAii9415.
NextBioi35274.
PROiO95864.
SOURCEiSearch...

Gene expression databases

BgeeiO95864.
CleanExiHS_FADS2.
ExpressionAtlasiO95864. baseline and differential.
GenevestigatoriO95864.

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.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and nutritional regulation of the mammalian Delta-6 desaturase."
    Cho H.P., Nakamura M.T., Clarke S.D.
    J. Biol. Chem. 274:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. Zhang J.S.S., Reddel R.R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Mesothelium.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-444 (ISOFORMS 1/2).
    Tissue: Tongue.
  5. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-444 (ISOFORMS 1/2).
    Tissue: Uterus.
  10. "The E-box like sterol regulatory element mediates the suppression of human Delta-6 desaturase gene by highly unsaturated fatty acids."
    Nara T.Y., He W.S., Tang C., Clarke S.D., Nakamura M.T.
    Biochem. Biophys. Res. Commun. 296:111-117(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Identification of the delta-6 desaturase of human sebaceous glands: expression and enzyme activity."
    Ge L., Gordon J.S., Hsuan C., Stenn K., Prouty S.M.
    J. Invest. Dermatol. 120:707-714(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Erratum
    Ge L., Gordon J.S., Hsuan C., Stenn K., Prouty S.M.
    J. Invest. Dermatol. 121:434-434(2002)
  13. "Regulation of human delta-6 desaturase gene transcription: identification of a functional direct repeat-1 element."
    Tang C., Cho H.P., Nakamura M.T., Clarke S.D.
    J. Lipid Res. 44:686-695(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Expression of human delta-6-desaturase is associated with aggressiveness of human breast cancer."
    Lane J., Mansel R.E., Jiang W.G.
    Int. J. Mol. Med. 12:253-257(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFADS2_HUMAN
AccessioniPrimary (citable) accession number: O95864
Secondary accession number(s): A8K2M6
, B7Z634, Q6MZQ7, Q96H07, Q96SV8, Q9H3G3, Q9Y3X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 2007
Last sequence update: April 30, 1999
Last modified: March 31, 2015
This is version 118 of the entry and version 1 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.