Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fatty acid 2-hydroxylase

Gene

FA2H

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

Functioni

Required for alpha-hydroxylation of free fatty acids and the formation of alpha-hydroxylated sphingolipids.2 Publications

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi69 – 691Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. fatty acid alpha-hydroxylase activity Source: GO_Central
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. central nervous system myelin maintenance Source: Ensembl
  2. fatty acid biosynthetic process Source: UniProtKB-KW
  3. fatty acid metabolic process Source: GO_Central
  4. lipid modification Source: Ensembl
  5. peripheral nervous system myelin maintenance Source: Ensembl
  6. regulation of cell proliferation Source: Ensembl
  7. regulation of hair cycle Source: Ensembl
  8. sebaceous gland cell differentiation Source: Ensembl
  9. sphingolipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000103089-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid 2-hydroxylase (EC:1.-.-.-)
Alternative name(s):
Fatty acid alpha-hydroxylase
Gene namesi
Name:FA2H
Synonyms:FAAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:21197. FA2H.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Microsome membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei168 – 18821HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 35, autosomal recessive (SPG35)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG35 is a complicated form characterized by childhood onset of gait difficulties. It has a rapid progression and many patients become wheelchair-bound as young adults. Patients manifest cognitive decline associated with leukodystrophy. Other variable neurologic features, such as dystonia, optic atrophy, and seizures may also occur.

See also OMIM:612319
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351D → Y in SPG35; patients present spastic paraparesis associated with leukodystrophy and dystonia. 1 Publication
VAR_054893
Natural varianti53 – 586Missing in SPG35; significantly reduced enzymatic function. 1 Publication
VAR_064620
Natural varianti154 – 1541R → C in SPG35. 1 Publication
VAR_065245
Natural varianti235 – 2351R → C in SPG35; significantly reduced enzymatic function. 1 Publication
VAR_064621

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Leukodystrophy, Neurodegeneration

Organism-specific databases

MIMi612319. phenotype.
Orphaneti171629. Autosomal recessive spastic paraplegia type 35.
329308. Fatty acid hydroxylase-associated neurodegeneration.
PharmGKBiPA145148065.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Fatty acid 2-hydroxylasePRO_0000312349Add
BLAST

Proteomic databases

MaxQBiQ7L5A8.
PaxDbiQ7L5A8.
PRIDEiQ7L5A8.

Expressioni

Tissue specificityi

Detected in differentiating cultured keratinocytes (at protein level). Detected in epidermis and cultured keratinocytes. Highly expressed in brain and colon. Detected at lower levels in testis, prostate, pancreas and kidney.2 Publications

Inductioni

Up-regulated during keratinocyte differentiation.1 Publication

Gene expression databases

BgeeiQ7L5A8.
CleanExiHS_FA2H.
ExpressionAtlasiQ7L5A8. baseline and differential.
GenevestigatoriQ7L5A8.

Organism-specific databases

HPAiHPA056614.

Interactioni

Protein-protein interaction databases

BioGridi122570. 2 interactions.
MINTiMINT-2876220.
STRINGi9606.ENSP00000219368.

Structurei

3D structure databases

ProteinModelPortaliQ7L5A8.
SMRiQ7L5A8. Positions 12-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 8679Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3000.
GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
HOVERGENiHBG054265.
InParanoidiQ7L5A8.
OMAiMKAHHVK.
OrthoDBiEOG71P2BJ.
PhylomeDBiQ7L5A8.
TreeFamiTF314955.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Ino-phos-ceramide-B_Hydrxlase.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7L5A8-1) [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
MAPAPPPAAS FSPSEVQRRL AAGACWVRRG ARLYDLSSFV RHHPGGEQLL
60 70 80 90 100
RARAGQDISA DLDGPPHRHS ANARRWLEQY YVGELRGEQQ GSMENEPVAL
110 120 130 140 150
EETQKTDPAM EPRFKVVDWD KDLVDWRKPL LWQVGHLGEK YDEWVHQPVT
160 170 180 190 200
RPIRLFHSDL IEGLSKTVWY SVPIIWVPLV LYLSWSYYRT FAQGNVRLFT
210 220 230 240 250
SFTTEYTVAV PKSMFPGLFM LGTFLWSLIE YLIHRFLFHM KPPSDSYYLI
260 270 280 290 300
MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IGVFYLCMQL ILPEAVGGTV
310 320 330 340 350
FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY SLKAHHVKHH FAHQKSGFGI
360 370
STKLWDYCFH TLTPEKPHLK TQ
Length:372
Mass (Da):42,791
Last modified:November 23, 2004 - v1
Checksum:i3F56B4C689B317BE
GO
Isoform 2 (identifier: Q7L5A8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: Missing.

Note: No experimental confirmation available.

Show »
Length:159
Mass (Da):18,324
Checksum:i547E5204C9151968
GO

Sequence cautioni

The sequence AAC23496.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841S → G in BAB71632 (PubMed:14702039).Curated
Sequence conflicti356 – 3561D → G in BAB71632 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351D → Y in SPG35; patients present spastic paraparesis associated with leukodystrophy and dystonia. 1 Publication
VAR_054893
Natural varianti53 – 586Missing in SPG35; significantly reduced enzymatic function. 1 Publication
VAR_064620
Natural varianti97 – 971P → A.
Corresponds to variant rs35874850 [ dbSNP | Ensembl ].
VAR_037503
Natural varianti154 – 1541R → C in SPG35. 1 Publication
VAR_065245
Natural varianti235 – 2351R → C in SPG35; significantly reduced enzymatic function. 1 Publication
VAR_064621

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 213213Missing in isoform 2. 1 PublicationVSP_056135Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK058016 mRNA. Translation: BAB71632.1.
AK303878 mRNA. Translation: BAH14072.1.
AC004685 Genomic DNA. Translation: AAC23496.1. Sequence problems.
AC009132 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95678.1.
BC002679 mRNA. Translation: AAH02679.2.
BC004263 mRNA. Translation: AAH04263.2.
BC017049 mRNA. Translation: AAH17049.2.
AJ278219 mRNA. Translation: CAC20436.1.
CCDSiCCDS10911.1. [Q7L5A8-1]
RefSeqiNP_077282.3. NM_024306.4. [Q7L5A8-1]
UniGeneiHs.461329.

Genome annotation databases

EnsembliENST00000219368; ENSP00000219368; ENSG00000103089. [Q7L5A8-1]
GeneIDi79152.
KEGGihsa:79152.
UCSCiuc002fde.2. human. [Q7L5A8-1]

Polymorphism databases

DMDMi74749893.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK058016 mRNA. Translation: BAB71632.1.
AK303878 mRNA. Translation: BAH14072.1.
AC004685 Genomic DNA. Translation: AAC23496.1. Sequence problems.
AC009132 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95678.1.
BC002679 mRNA. Translation: AAH02679.2.
BC004263 mRNA. Translation: AAH04263.2.
BC017049 mRNA. Translation: AAH17049.2.
AJ278219 mRNA. Translation: CAC20436.1.
CCDSiCCDS10911.1. [Q7L5A8-1]
RefSeqiNP_077282.3. NM_024306.4. [Q7L5A8-1]
UniGeneiHs.461329.

3D structure databases

ProteinModelPortaliQ7L5A8.
SMRiQ7L5A8. Positions 12-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122570. 2 interactions.
MINTiMINT-2876220.
STRINGi9606.ENSP00000219368.

Polymorphism databases

DMDMi74749893.

Proteomic databases

MaxQBiQ7L5A8.
PaxDbiQ7L5A8.
PRIDEiQ7L5A8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219368; ENSP00000219368; ENSG00000103089. [Q7L5A8-1]
GeneIDi79152.
KEGGihsa:79152.
UCSCiuc002fde.2. human. [Q7L5A8-1]

Organism-specific databases

CTDi79152.
GeneCardsiGC16M074746.
GeneReviewsiFA2H.
HGNCiHGNC:21197. FA2H.
HPAiHPA056614.
MIMi611026. gene.
612319. phenotype.
neXtProtiNX_Q7L5A8.
Orphaneti171629. Autosomal recessive spastic paraplegia type 35.
329308. Fatty acid hydroxylase-associated neurodegeneration.
PharmGKBiPA145148065.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3000.
GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
HOVERGENiHBG054265.
InParanoidiQ7L5A8.
OMAiMKAHHVK.
OrthoDBiEOG71P2BJ.
PhylomeDBiQ7L5A8.
TreeFamiTF314955.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000103089-MONOMER.

Miscellaneous databases

GeneWikiiFA2H.
GenomeRNAii79152.
NextBioi35480566.
PROiQ7L5A8.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L5A8.
CleanExiHS_FA2H.
ExpressionAtlasiQ7L5A8. baseline and differential.
GenevestigatoriQ7L5A8.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Ino-phos-ceramide-B_Hydrxlase.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 1 AND 2).
    Tissue: Gastric mucosa and Trachea.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 1).
    Tissue: Colon and Pancreas.
  5. "Cloning of human fatty acid hydroxylase."
    Van Veldhoven P.P.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-372 (ISOFORM 1).
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Fatty acid 2-hydroxylase, encoded by FA2H, accounts for differentiation-associated increase in 2-OH ceramides during keratinocyte differentiation."
    Uchida Y., Hama H., Alderson N.L., Douangpanya S., Wang Y., Crumrine D.A., Elias P.M., Holleran W.M.
    J. Biol. Chem. 282:13211-13219(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  8. "Mutations in the fatty acid 2-hydroxylase gene are associated with leukodystrophy with spastic paraparesis and dystonia."
    Edvardson S., Hama H., Shaag A., Gomori J.M., Berger I., Soffer D., Korman S.H., Taustein I., Saada A., Elpeleg O.
    Am. J. Hum. Genet. 83:643-648(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG35 TYR-35.
  9. Cited for: VARIANT SPG35 CYS-154.
  10. Cited for: VARIANTS SPG35 53-ARG--ILE-58 DEL AND CYS-235, CHARACTERIZATION OF VARIANTS SPG35 53-ARG--ILE-58 DEL AND CYS-235.

Entry informationi

Entry nameiFA2H_HUMAN
AccessioniPrimary (citable) accession number: Q7L5A8
Secondary accession number(s): B7Z8T6
, O75213, Q96DK1, Q9H1A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: November 23, 2004
Last modified: March 4, 2015
This is version 109 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 16
    Human chromosome 16: 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. 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.