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Q7L5A8

- FA2H_HUMAN

UniProt

Q7L5A8 - FA2H_HUMAN

Protein

Fatty acid 2-hydroxylase

Gene

FA2H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

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

    Cofactori

    Iron.By 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: Ensembl
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. central nervous system myelin maintenance Source: Ensembl
    3. fatty acid biosynthetic process Source: UniProtKB-KW
    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

    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: 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

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Spastic paraplegia 35, autosomal recessive (SPG35) [MIM:612319]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.
    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

    ArrayExpressiQ7L5A8.
    BgeeiQ7L5A8.
    CleanExiHS_FA2H.
    GenevestigatoriQ7L5A8.

    Interactioni

    Protein-protein interaction databases

    BioGridi122570. 1 interaction.
    MINTiMINT-2876220.
    STRINGi9606.ENSP00000219368.

    Structurei

    3D structure databases

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

    Transmembrane

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

    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.
    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. Align

    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

    MAPAPPPAAS FSPSEVQRRL AAGACWVRRG ARLYDLSSFV RHHPGGEQLL    50
    RARAGQDISA DLDGPPHRHS ANARRWLEQY YVGELRGEQQ GSMENEPVAL 100
    EETQKTDPAM EPRFKVVDWD KDLVDWRKPL LWQVGHLGEK YDEWVHQPVT 150
    RPIRLFHSDL IEGLSKTVWY SVPIIWVPLV LYLSWSYYRT FAQGNVRLFT 200
    SFTTEYTVAV PKSMFPGLFM LGTFLWSLIE YLIHRFLFHM KPPSDSYYLI 250
    MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IGVFYLCMQL ILPEAVGGTV 300
    FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY SLKAHHVKHH FAHQKSGFGI 350
    STKLWDYCFH TLTPEKPHLK TQ 372
    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.

    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.
    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqiNP_077282.3. NM_024306.4.
    UniGeneiHs.461329.

    Genome annotation databases

    EnsembliENST00000219368; ENSP00000219368; ENSG00000103089.
    ENST00000544337; ENSP00000442334; ENSG00000103089.
    GeneIDi79152.
    KEGGihsa:79152.
    UCSCiuc002fde.2. human.

    Polymorphism databases

    DMDMi74749893.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10911.1.
    RefSeqi NP_077282.3. NM_024306.4.
    UniGenei Hs.461329.

    3D structure databases

    ProteinModelPortali Q7L5A8.
    SMRi Q7L5A8. Positions 12-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122570. 1 interaction.
    MINTi MINT-2876220.
    STRINGi 9606.ENSP00000219368.

    Polymorphism databases

    DMDMi 74749893.

    Proteomic databases

    MaxQBi Q7L5A8.
    PaxDbi Q7L5A8.
    PRIDEi Q7L5A8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219368 ; ENSP00000219368 ; ENSG00000103089 .
    ENST00000544337 ; ENSP00000442334 ; ENSG00000103089 .
    GeneIDi 79152.
    KEGGi hsa:79152.
    UCSCi uc002fde.2. human.

    Organism-specific databases

    CTDi 79152.
    GeneCardsi GC16M074746.
    GeneReviewsi FA2H.
    HGNCi HGNC:21197. FA2H.
    MIMi 611026. gene.
    612319. phenotype.
    neXtProti NX_Q7L5A8.
    Orphaneti 171629. Autosomal recessive spastic paraplegia type 35.
    329308. Fatty acid hydroxylase-associated neurodegeneration.
    PharmGKBi PA145148065.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3000.
    HOGENOMi HOG000023981.
    HOVERGENi HBG054265.
    InParanoidi Q7L5A8.
    OMAi MKAHHVK.
    OrthoDBi EOG71P2BJ.
    PhylomeDBi Q7L5A8.
    TreeFami TF314955.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000103089-MONOMER.

    Miscellaneous databases

    GeneWikii FA2H.
    GenomeRNAii 79152.
    NextBioi 68068.
    PROi Q7L5A8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L5A8.
    Bgeei Q7L5A8.
    CleanExi HS_FA2H.
    Genevestigatori Q7L5A8.

    Family and domain databases

    Gene3Di 3.10.120.10. 1 hit.
    InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR006694. Fatty_acid_hydroxylase.
    IPR014430. Ino-phos-ceramide-B_Hydrxlase.
    [Graphical view ]
    Pfami PF00173. Cyt-b5. 1 hit.
    PF04116. FA_hydroxylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005149. IPC-B_HD. 1 hit.
    PRINTSi PR00363. CYTOCHROMEB5.
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(2004) [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(2004) [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(2004) [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 (MAY-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(2007) [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(2008) [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: October 1, 2014
    This is version 104 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