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O14975

- S27A2_HUMAN

UniProt

O14975 - S27A2_HUMAN

Protein

Very long-chain acyl-CoA synthetase

Gene

SLC27A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes By similarity.By similarity

    Catalytic activityi

    ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication
    ATP + a very-long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi222 – 23312AMPSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: UniProtKB
    3. fatty acid transporter activity Source: Ensembl
    4. long-chain fatty acid-CoA ligase activity Source: UniProtKB
    5. phytanate-CoA ligase activity Source: UniProtKB
    6. pristanate-CoA ligase activity Source: UniProtKB
    7. receptor binding Source: UniProtKB
    8. very long-chain fatty acid-CoA ligase activity Source: UniProtKB

    GO - Biological processi

    1. bile acid biosynthetic process Source: UniProtKB
    2. bile acid metabolic process Source: Reactome
    3. cellular lipid metabolic process Source: Reactome
    4. fatty acid alpha-oxidation Source: UniProtKB
    5. fatty acid beta-oxidation Source: UniProtKB
    6. long-chain fatty acid import Source: UniProtKB
    7. long-chain fatty acid metabolic process Source: UniProtKB
    8. methyl-branched fatty acid metabolic process Source: UniProtKB
    9. small molecule metabolic process Source: Reactome
    10. very long-chain fatty acid catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06695-MONOMER.
    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_17003. Alpha-oxidation of phytanate.

    Protein family/group databases

    TCDBi4.C.1.1.5. the proposed fatty acid transporter (fat) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Very long-chain acyl-CoA synthetase (EC:6.2.1.-)
    Short name:
    VLACS
    Short name:
    VLCS
    Alternative name(s):
    Fatty acid transport protein 2
    Short name:
    FATP-2
    Fatty-acid-coenzyme A ligase, very long-chain 1
    Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3)
    Solute carrier family 27 member 2
    THCA-CoA ligase
    Very long-chain-fatty-acid-CoA ligase
    Gene namesi
    Name:SLC27A2
    Synonyms:ACSVL1, FACVL1, FATP2, VLACS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:10996. SLC27A2.

    Subcellular locationi

    Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Multi-pass membrane protein
    Note: Peripheral membrane associated with the lumenal side of peroxisomes.

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of endoplasmic reticulum membrane Source: UniProtKB
    5. integral component of peroxisomal membrane Source: UniProtKB
    6. mitochondrion Source: Ensembl
    7. peroxisomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27971.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 620620Very long-chain acyl-CoA synthetasePRO_0000193204Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei291 – 2911N6-acetyllysineBy similarity
    Modified residuei577 – 5771Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14975.
    PaxDbiO14975.
    PRIDEiO14975.

    PTM databases

    PhosphoSiteiO14975.

    Expressioni

    Tissue specificityi

    Expressed in liver, kidney, placenta and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiO14975.
    BgeeiO14975.
    CleanExiHS_SLC27A2.
    GenevestigatoriO14975.

    Organism-specific databases

    HPAiHPA026089.

    Interactioni

    Protein-protein interaction databases

    BioGridi116194. 8 interactions.
    IntActiO14975. 2 interactions.
    MINTiMINT-2998454.
    STRINGi9606.ENSP00000267842.

    Structurei

    3D structure databases

    ProteinModelPortaliO14975.
    SMRiO14975. Positions 60-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44Lumenal1 Publication
    Topological domaini28 – 10679CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini128 – 261134LumenalSequence AnalysisAdd
    BLAST
    Topological domaini283 – 620338CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723HelicalSequence AnalysisAdd
    BLAST
    Transmembranei107 – 12721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei262 – 28221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000044189.
    HOVERGENiHBG005642.
    InParanoidiO14975.
    KOiK08746.
    OMAiIPMTEDI.
    OrthoDBiEOG7W6WKB.
    PhylomeDBiO14975.
    TreeFamiTF313430.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14975-1) [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

    MLSAIYTVLA GLLFLPLLVN LCCPYFFQDI GYFLKVAAVG RRVRSYGKRR    50
    PARTILRAFL EKARQTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG 100
    LRQGDCVALL MGNEPAYVWL WLGLVKLGCA MACLNYNIRA KSLLHCFQCC 150
    GAKVLLVSPE LQAAVEEILP SLKKDDVSIY YVSRTSNTDG IDSFLDKVDE 200
    VSTEPIPESW RSEVTFSTPA LYIYTSGTTG LPKAAMITHQ RIWYGTGLTF 250
    VSGLKADDVI YITLPFYHSA ALLIGIHGCI VAGATLALRT KFSASQFWDD 300
    CRKYNVTVIQ YIGELLRYLC NSPQKPNDRD HKVRLALGNG LRGDVWRQFV 350
    KRFGDICIYE FYAATEGNIG FMNYARKVGA VGRVNYLQKK IITYDLIKYD 400
    VEKDEPVRDE NGYCVRVPKG EVGLLVCKIT QLTPFNGYAG AKAQTEKKKL 450
    RDVFKKGDLY FNSGDLLMVD HENFIYFHDR VGDTFRWKGE NVATTEVADT 500
    VGLVDFVQEV NVYGVHVPDH EGRIGMASIK MKENHEFDGK KLFQHIADYL 550
    PSYARPRFLR IQDTIEITGT FKHRKMTLVE EGFNPAVIKD ALYFLDDTAK 600
    MYVPMTEDIY NAISAKTLKL 620
    Length:620
    Mass (Da):70,312
    Last modified:October 5, 2010 - v2
    Checksum:i752E2FFBB2E47C26
    GO
    Isoform 2 (identifier: O14975-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         230-282: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:567
    Mass (Da):64,616
    Checksum:iFF3A2B0FD68177B0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481K → Q.4 Publications
    Corresponds to variant rs1648348 [ dbSNP | Ensembl ].
    VAR_046533

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei230 – 28253Missing in isoform 2. 1 PublicationVSP_042726Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88308 mRNA. Translation: BAA23644.1.
    AF096290 mRNA. Translation: AAC64973.1.
    AK223145 mRNA. Translation: BAD96865.1.
    AK290262 mRNA. Translation: BAF82951.1.
    AC009753 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77386.1.
    BC057770 mRNA. Translation: AAH57770.1.
    CCDSiCCDS10133.1. [O14975-1]
    CCDS53943.1. [O14975-2]
    RefSeqiNP_001153101.1. NM_001159629.1. [O14975-2]
    NP_003636.2. NM_003645.3. [O14975-1]
    UniGeneiHs.11729.

    Genome annotation databases

    EnsembliENST00000267842; ENSP00000267842; ENSG00000140284. [O14975-1]
    ENST00000380902; ENSP00000370289; ENSG00000140284. [O14975-2]
    GeneIDi11001.
    KEGGihsa:11001.
    UCSCiuc001zxw.3. human. [O14975-1]
    uc010bes.3. human. [O14975-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88308 mRNA. Translation: BAA23644.1 .
    AF096290 mRNA. Translation: AAC64973.1 .
    AK223145 mRNA. Translation: BAD96865.1 .
    AK290262 mRNA. Translation: BAF82951.1 .
    AC009753 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77386.1 .
    BC057770 mRNA. Translation: AAH57770.1 .
    CCDSi CCDS10133.1. [O14975-1 ]
    CCDS53943.1. [O14975-2 ]
    RefSeqi NP_001153101.1. NM_001159629.1. [O14975-2 ]
    NP_003636.2. NM_003645.3. [O14975-1 ]
    UniGenei Hs.11729.

    3D structure databases

    ProteinModelPortali O14975.
    SMRi O14975. Positions 60-555.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116194. 8 interactions.
    IntActi O14975. 2 interactions.
    MINTi MINT-2998454.
    STRINGi 9606.ENSP00000267842.

    Chemistry

    ChEMBLi CHEMBL4326.

    Protein family/group databases

    TCDBi 4.C.1.1.5. the proposed fatty acid transporter (fat) family.

    PTM databases

    PhosphoSitei O14975.

    Proteomic databases

    MaxQBi O14975.
    PaxDbi O14975.
    PRIDEi O14975.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267842 ; ENSP00000267842 ; ENSG00000140284 . [O14975-1 ]
    ENST00000380902 ; ENSP00000370289 ; ENSG00000140284 . [O14975-2 ]
    GeneIDi 11001.
    KEGGi hsa:11001.
    UCSCi uc001zxw.3. human. [O14975-1 ]
    uc010bes.3. human. [O14975-2 ]

    Organism-specific databases

    CTDi 11001.
    GeneCardsi GC15P050474.
    HGNCi HGNC:10996. SLC27A2.
    HPAi HPA026089.
    MIMi 603247. gene.
    neXtProti NX_O14975.
    PharmGKBi PA27971.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000044189.
    HOVERGENi HBG005642.
    InParanoidi O14975.
    KOi K08746.
    OMAi IPMTEDI.
    OrthoDBi EOG7W6WKB.
    PhylomeDBi O14975.
    TreeFami TF313430.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06695-MONOMER.
    Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_17003. Alpha-oxidation of phytanate.

    Miscellaneous databases

    ChiTaRSi SLC27A2. human.
    GeneWikii SLC27A2.
    GenomeRNAii 11001.
    NextBioi 41795.
    PROi O14975.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14975.
    Bgeei O14975.
    CleanExi HS_SLC27A2.
    Genevestigatori O14975.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a possible human homolog of the rat very-long-chain acyl-CoA synthetase cDNA and its chromosomal localization."
      Uchiyama A., Aoyama T., Kamijo K., Wakui K., Fukushima Y., Shimozawa N., Suzuki Y., Kondo N., Orii T., Hashimoto T.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-48.
      Tissue: Liver.
    2. "Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism."
      Steinberg S.J., Wang S.J., Kim D.G., Mihalik S.J., Watkins P.A.
      Biochem. Biophys. Res. Commun. 257:615-621(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT GLN-48.
    3. "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] (ISOFORM 1), VARIANT GLN-48.
      Tissue: Colon.
    4. 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.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-48.
    7. "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 2).
      Tissue: Placenta.
    8. "Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling."
      Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G., Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D., Watkins P.A.
      J. Biol. Chem. 277:24771-24779(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiS27A2_HUMAN
    AccessioniPrimary (citable) accession number: O14975
    Secondary accession number(s): A8K2J7, Q53FY6, Q6PF09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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 15
      Human chromosome 15: 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