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Q9BQE5

- APOL2_HUMAN

UniProt

Q9BQE5 - APOL2_HUMAN

Protein

Apolipoprotein L2

Gene

APOL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.

    GO - Molecular functioni

    1. high-density lipoprotein particle binding Source: UniProtKB
    2. lipid binding Source: UniProtKB
    3. receptor binding Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: UniProtKB
    2. cholesterol metabolic process Source: UniProtKB
    3. lipid metabolic process Source: UniProtKB
    4. lipid transport Source: UniProtKB
    5. lipoprotein metabolic process Source: InterPro
    6. maternal process involved in female pregnancy Source: UniProtKB
    7. multicellular organismal development Source: UniProtKB

    Keywords - Biological processi

    Lipid transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apolipoprotein L2
    Alternative name(s):
    Apolipoprotein L-II
    Short name:
    ApoL-II
    Gene namesi
    Name:APOL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:619. APOL2.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. extracellular region Source: InterPro
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337Apolipoprotein L2PRO_0000137601Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei250 – 2501Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BQE5.
    PaxDbiQ9BQE5.
    PRIDEiQ9BQE5.

    PTM databases

    PhosphoSiteiQ9BQE5.

    Expressioni

    Tissue specificityi

    Widely expressed; the highest levels are found in lung, thymus, pancreas, placenta, adult brain and prostate; also detected in spleen, liver, kidney, colon, small intestine, uterus, spinal cord, adrenal gland, salivary gland, trachea, mammary gland, skeletal muscle, testis and fetal brain and liver.

    Gene expression databases

    ArrayExpressiQ9BQE5.
    BgeeiQ9BQE5.
    GenevestigatoriQ9BQE5.

    Organism-specific databases

    HPAiHPA001078.

    Interactioni

    Protein-protein interaction databases

    BioGridi117279. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BQE5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi157 – 1626Poly-Ala

    Sequence similaritiesi

    Belongs to the apolipoprotein L family.Curated

    Phylogenomic databases

    eggNOGiNOG125779.
    HOVERGENiHBG074468.
    InParanoidiQ9BQE5.
    KOiK14480.
    OrthoDBiEOG7K9K41.
    PhylomeDBiQ9BQE5.
    TreeFamiTF334681.

    Family and domain databases

    InterProiIPR008405. ApoL.
    [Graphical view]
    PANTHERiPTHR14096. PTHR14096. 1 hit.
    PfamiPF05461. ApoL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BQE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPESSIFIE DYLKYFQDQV SRENLLQLLT DDEAWNGFVA AAELPRDEAD    50
    ELRKALNKLA SHMVMKDKNR HDKDQQHRQW FLKEFPRLKR ELEDHIRKLR 100
    ALAEEVEQVH RGTTIANVVS NSVGTTSGIL TLLGLGLAPF TEGISFVLLD 150
    TGMGLGAAAA VAGITCSVVE LVNKLRARAQ ARNLDQSGTN VAKVMKEFVG 200
    GNTPNVLTLV DNWYQVTQGI GRNIRAIRRA RANPQLGAYA PPPHIIGRIS 250
    AEGGEQVERV VEGPAQAMSR GTMIVGAATG GILLLLDVVS LAYESKHLLE 300
    GAKSESAEEL KKRAQELEGK LNFLTKIHEM LQPGQDQ 337
    Length:337
    Mass (Da):37,092
    Last modified:June 1, 2001 - v1
    Checksum:i0A54640FCC029400
    GO

    Sequence cautioni

    The sequence BAD92227.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861Q → R in BAD92227. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti182 – 1821R → C.
    Corresponds to variant rs7285167 [ dbSNP | Ensembl ].
    VAR_024366
    Natural varianti245 – 2451I → V.1 Publication
    Corresponds to variant rs132760 [ dbSNP | Ensembl ].
    VAR_012978

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305225 mRNA. Translation: AAK20211.1.
    AF324223 mRNA. Translation: AAK11592.1.
    AF324224 mRNA. Translation: AAK11593.1.
    AF324230, AF324228, AF324229 Genomic DNA. Translation: AAK11598.1.
    AF305429 mRNA. Translation: AAL09359.1.
    AK056938 mRNA. Translation: BAB71315.1.
    AB208990 mRNA. Translation: BAD92227.1. Different initiation.
    AL031426, Z82215, Z95114 Genomic DNA. Translation: CAQ10954.1.
    Z82215, AL031426, Z95114 Genomic DNA. Translation: CAQ09084.1.
    Z95114, AL031426, Z82215 Genomic DNA. Translation: CAQ08516.1.
    BC004395 mRNA. Translation: AAH04395.1.
    CCDSiCCDS43014.1.
    RefSeqiNP_112092.1. NM_030882.2.
    NP_663612.1. NM_145637.1.
    XP_006724281.1. XM_006724218.1.
    UniGeneiHs.474740.

    Genome annotation databases

    EnsembliENST00000249066; ENSP00000249066; ENSG00000128335.
    ENST00000358502; ENSP00000351292; ENSG00000128335.
    GeneIDi23780.
    KEGGihsa:23780.
    UCSCiuc003aoz.3. human.

    Polymorphism databases

    DMDMi17433285.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305225 mRNA. Translation: AAK20211.1 .
    AF324223 mRNA. Translation: AAK11592.1 .
    AF324224 mRNA. Translation: AAK11593.1 .
    AF324230 , AF324228 , AF324229 Genomic DNA. Translation: AAK11598.1 .
    AF305429 mRNA. Translation: AAL09359.1 .
    AK056938 mRNA. Translation: BAB71315.1 .
    AB208990 mRNA. Translation: BAD92227.1 . Different initiation.
    AL031426 , Z82215 , Z95114 Genomic DNA. Translation: CAQ10954.1 .
    Z82215 , AL031426 , Z95114 Genomic DNA. Translation: CAQ09084.1 .
    Z95114 , AL031426 , Z82215 Genomic DNA. Translation: CAQ08516.1 .
    BC004395 mRNA. Translation: AAH04395.1 .
    CCDSi CCDS43014.1.
    RefSeqi NP_112092.1. NM_030882.2.
    NP_663612.1. NM_145637.1.
    XP_006724281.1. XM_006724218.1.
    UniGenei Hs.474740.

    3D structure databases

    ProteinModelPortali Q9BQE5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117279. 1 interaction.

    PTM databases

    PhosphoSitei Q9BQE5.

    Polymorphism databases

    DMDMi 17433285.

    Proteomic databases

    MaxQBi Q9BQE5.
    PaxDbi Q9BQE5.
    PRIDEi Q9BQE5.

    Protocols and materials databases

    DNASUi 23780.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249066 ; ENSP00000249066 ; ENSG00000128335 .
    ENST00000358502 ; ENSP00000351292 ; ENSG00000128335 .
    GeneIDi 23780.
    KEGGi hsa:23780.
    UCSCi uc003aoz.3. human.

    Organism-specific databases

    CTDi 23780.
    GeneCardsi GC22M036622.
    HGNCi HGNC:619. APOL2.
    HPAi HPA001078.
    MIMi 607252. gene.
    neXtProti NX_Q9BQE5.
    PharmGKBi PA24905.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG125779.
    HOVERGENi HBG074468.
    InParanoidi Q9BQE5.
    KOi K14480.
    OrthoDBi EOG7K9K41.
    PhylomeDBi Q9BQE5.
    TreeFami TF334681.

    Miscellaneous databases

    ChiTaRSi APOL2. human.
    GeneWikii APOL2.
    GenomeRNAii 23780.
    NextBioi 46771.
    PROi Q9BQE5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BQE5.
    Bgeei Q9BQE5.
    Genevestigatori Q9BQE5.

    Family and domain databases

    InterProi IPR008405. ApoL.
    [Graphical view ]
    PANTHERi PTHR14096. PTHR14096. 1 hit.
    Pfami PF05461. ApoL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human apolipoprotein L gene cluster: identification, classification, and sites of distribution."
      Page N.M., Butlin D.J., Lomthaisong K., Lowry P.J.
      Genomics 74:71-78(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Apolipoprotein L gene family: tissue-specific expression, splicing, promoter regions; discovery of a new gene."
      Duchateau P.N., Pullinger C.R., Cho M.H., Eng C., Kane J.P.
      J. Lipid Res. 42:620-630(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Pancreas.
    3. "The apolipoprotein L gene cluster has emerged recently in evolution and is expressed in human vascular tissue."
      Monajemi H., Fontijn R.D., Pannekoek H., Horrevoets A.J.G.
      Genomics 79:539-546(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL LOCATION.
      Tissue: Endothelial cell.
    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].
      Tissue: Salivary gland.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-245.
      Tissue: Brain.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Placenta.
    8. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-14; 249-259 AND 271-296, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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 SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAPOL2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQE5
    Secondary accession number(s): B0QYK7
    , O95915, Q59GW9, Q5TH96, Q969T6, Q9BT28, Q9UGT1, Q9UH10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 116 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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