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O76054

- S14L2_HUMAN

UniProt

O76054 - S14L2_HUMAN

Protein

SEC14-like protein 2

Gene

SEC14L2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.

    GO - Molecular functioni

    1. phospholipid binding Source: UniProtKB
    2. transporter activity Source: InterPro
    3. vitamin E binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: UniProtKB
    2. regulation of cholesterol biosynthetic process Source: UniProtKB
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SEC14-like protein 2
    Alternative name(s):
    Alpha-tocopherol-associated protein
    Short name:
    TAP
    Short name:
    hTAP
    Squalene transfer protein
    Supernatant protein factor
    Short name:
    SPF
    Gene namesi
    Name:SEC14L2
    Synonyms:C22orf6, KIAA1186, KIAA1658
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:10699. SEC14L2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. integral component of membrane Source: InterPro
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35622.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 403403SEC14-like protein 2PRO_0000210755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-succinyllysineBy similarity
    Modified residuei253 – 2531N6-succinyllysineBy similarity
    Modified residuei257 – 2571N6-succinyllysineBy similarity
    Modified residuei393 – 3931N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiO76054.
    PaxDbiO76054.
    PeptideAtlasiO76054.
    PRIDEiO76054.

    PTM databases

    PhosphoSiteiO76054.

    Expressioni

    Tissue specificityi

    Widely expressed. Strong expression in liver, brain and prostate.1 Publication

    Developmental stagei

    Low expression in fetal tissues.

    Gene expression databases

    ArrayExpressiO76054.
    BgeeiO76054.
    CleanExiHS_SEC14L2.
    GenevestigatoriO76054.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi117085. 1 interaction.
    IntActiO76054. 1 interaction.
    MINTiMINT-3002196.
    STRINGi9606.ENSP00000316203.

    Structurei

    Secondary structure

    1
    403
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2314
    Helixi24 – 296
    Helixi35 – 4410
    Turni45 – 473
    Helixi49 – 6517
    Helixi68 – 736
    Helixi78 – 836
    Beta strandi86 – 916
    Beta strandi97 – 1026
    Helixi108 – 1125
    Helixi117 – 14226
    Beta strandi149 – 1546
    Helixi160 – 1634
    Helixi165 – 18117
    Beta strandi186 – 1938
    Helixi198 – 2058
    Helixi206 – 2083
    Helixi211 – 2155
    Beta strandi217 – 2193
    Helixi224 – 2285
    Turni229 – 2313
    Helixi234 – 2363
    Helixi239 – 2413
    Beta strandi243 – 2453
    Turni255 – 2573
    Helixi266 – 2683
    Beta strandi279 – 2846
    Beta strandi289 – 2968
    Beta strandi302 – 31211
    Beta strandi314 – 3207
    Beta strandi323 – 3264
    Helixi330 – 3323
    Beta strandi333 – 34210
    Turni344 – 3463
    Beta strandi349 – 3546
    Beta strandi359 – 3668
    Beta strandi374 – 38411
    Helixi388 – 3958

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O6UX-ray2.05A/C/E1-403[»]
    1OLMX-ray1.95A/C/E1-403[»]
    ProteinModelPortaliO76054.
    SMRiO76054. Positions 1-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO76054.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 249174CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST
    Domaini275 – 383109GOLDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
    Contains 1 GOLD domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG309458.
    HOGENOMiHOG000232201.
    HOVERGENiHBG055336.
    InParanoidiO76054.
    OMAiKXPKLFP.
    OrthoDBiEOG7N8ZVD.
    PhylomeDBiO76054.
    TreeFamiTF313988.

    Family and domain databases

    Gene3Di3.40.525.10. 1 hit.
    InterProiIPR001071. CRAL-bd_toc_tran.
    IPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    IPR009038. GOLD.
    [Graphical view]
    PfamiPF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    [Graphical view]
    PRINTSiPR00180. CRETINALDHBP.
    SMARTiSM01100. CRAL_TRIO_N. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view]
    SUPFAMiSSF101576. SSF101576. 1 hit.
    SSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    PS50866. GOLD. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O76054-1) [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

    MSGRVGDLSP RQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARSFDLQ    50
    KSEAMLRKHV EFRKQKDIDN IISWQPPEVI QQYLSGGMCG YDLDGCPVWY 100
    DIIGPLDAKG LLFSASKQDL LRTKMRECEL LLQECAHQTT KLGRKVETIT 150
    IIYDCEGLGL KHLWKPAVEA YGEFLCMFEE NYPETLKRLF VVKAPKLFPV 200
    AYNLIKPFLS EDTRKKIMVL GANWKEVLLK HISPDQVPVE YGGTMTDPDG 250
    NPKCKSKINY GGDIPRKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG 300
    CVLRWQFMSD GADVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHLVPED 350
    GTLTCSDPGI YVLRFDNTYS FIHAKKVNFT VEVLLPDKAS EEKMKQLGAG 400
    TPK 403
    Length:403
    Mass (Da):46,145
    Last modified:November 1, 1998 - v1
    Checksum:iD846747EC8D1513E
    GO
    Isoform 2 (identifier: O76054-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         361-403: YVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK → CKYLCLGNALKPHVQLSACEVPLPPWIFGSEC

    Note: No experimental confirmation available.

    Show »
    Length:392
    Mass (Da):44,748
    Checksum:i11A833345968FE5A
    GO
    Isoform 3 (identifier: O76054-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-140: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:320
    Mass (Da):36,636
    Checksum:i64CCC92D4A8149C7
    GO

    Sequence cautioni

    The sequence BAA86500.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361Y → H(PubMed:11444841)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111R → K.2 Publications
    Corresponds to variant rs757660 [ dbSNP | Ensembl ].
    VAR_024626

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei58 – 14083Missing in isoform 3. 1 PublicationVSP_045880Add
    BLAST
    Alternative sequencei361 – 40343YVLRF…AGTPK → CKYLCLGNALKPHVQLSACE VPLPPWIFGSEC in isoform 2. 1 PublicationVSP_042021Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL096881 mRNA. Translation: CAB51405.1.
    AB033012 mRNA. Translation: BAA86500.2. Different initiation.
    CR456571 mRNA. Translation: CAG30457.1.
    AK303751 mRNA. Translation: BAH14037.1.
    AK223587 mRNA. Translation: BAD97307.1.
    AC004832 Genomic DNA. Translation: AAF19256.1.
    BC058915 mRNA. Translation: AAH58915.1.
    CCDSiCCDS13876.1. [O76054-1]
    CCDS46685.1. [O76054-4]
    CCDS56228.1. [O76054-5]
    PIRiJC7708.
    RefSeqiNP_001191133.1. NM_001204204.2. [O76054-5]
    NP_036561.1. NM_012429.4. [O76054-1]
    NP_203740.1. NM_033382.2. [O76054-4]
    UniGeneiHs.335614.

    Genome annotation databases

    EnsembliENST00000402592; ENSP00000383882; ENSG00000100003. [O76054-5]
    ENST00000405717; ENSP00000385186; ENSG00000100003. [O76054-4]
    GeneIDi23541.
    KEGGihsa:23541.
    UCSCiuc003ahq.3. human. [O76054-4]
    uc003ahr.3. human. [O76054-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL096881 mRNA. Translation: CAB51405.1 .
    AB033012 mRNA. Translation: BAA86500.2 . Different initiation.
    CR456571 mRNA. Translation: CAG30457.1 .
    AK303751 mRNA. Translation: BAH14037.1 .
    AK223587 mRNA. Translation: BAD97307.1 .
    AC004832 Genomic DNA. Translation: AAF19256.1 .
    BC058915 mRNA. Translation: AAH58915.1 .
    CCDSi CCDS13876.1. [O76054-1 ]
    CCDS46685.1. [O76054-4 ]
    CCDS56228.1. [O76054-5 ]
    PIRi JC7708.
    RefSeqi NP_001191133.1. NM_001204204.2. [O76054-5 ]
    NP_036561.1. NM_012429.4. [O76054-1 ]
    NP_203740.1. NM_033382.2. [O76054-4 ]
    UniGenei Hs.335614.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O6U X-ray 2.05 A/C/E 1-403 [» ]
    1OLM X-ray 1.95 A/C/E 1-403 [» ]
    ProteinModelPortali O76054.
    SMRi O76054. Positions 1-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117085. 1 interaction.
    IntActi O76054. 1 interaction.
    MINTi MINT-3002196.
    STRINGi 9606.ENSP00000316203.

    Chemistry

    DrugBanki DB00163. Vitamin E.

    PTM databases

    PhosphoSitei O76054.

    Proteomic databases

    MaxQBi O76054.
    PaxDbi O76054.
    PeptideAtlasi O76054.
    PRIDEi O76054.

    Protocols and materials databases

    DNASUi 23541.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000402592 ; ENSP00000383882 ; ENSG00000100003 . [O76054-5 ]
    ENST00000405717 ; ENSP00000385186 ; ENSG00000100003 . [O76054-4 ]
    GeneIDi 23541.
    KEGGi hsa:23541.
    UCSCi uc003ahq.3. human. [O76054-4 ]
    uc003ahr.3. human. [O76054-1 ]

    Organism-specific databases

    CTDi 23541.
    GeneCardsi GC22P030792.
    HGNCi HGNC:10699. SEC14L2.
    MIMi 607558. gene.
    neXtProti NX_O76054.
    PharmGKBi PA35622.
    HUGEi Search...
    Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309458.
    HOGENOMi HOG000232201.
    HOVERGENi HBG055336.
    InParanoidi O76054.
    OMAi KXPKLFP.
    OrthoDBi EOG7N8ZVD.
    PhylomeDBi O76054.
    TreeFami TF313988.

    Miscellaneous databases

    ChiTaRSi SEC14L2. human.
    EvolutionaryTracei O76054.
    GeneWikii SEC14L2.
    GenomeRNAii 23541.
    NextBioi 46048.
    PROi O76054.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O76054.
    Bgeei O76054.
    CleanExi HS_SEC14L2.
    Genevestigatori O76054.

    Family and domain databases

    Gene3Di 3.40.525.10. 1 hit.
    InterProi IPR001071. CRAL-bd_toc_tran.
    IPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    IPR009038. GOLD.
    [Graphical view ]
    Pfami PF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00180. CRETINALDHBP.
    SMARTi SM01100. CRAL_TRIO_N. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101576. SSF101576. 1 hit.
    SSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    PS50866. GOLD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization."
      Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J., Azzi A.
      J. Biol. Chem. 275:25672-25680(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHARACTERIZATION.
    2. "Tocopherol-associated protein is a ligand-dependent transcriptional activator."
      Yamauchi J., Iwamoto T., Kida S., Masushige S., Yamada K., Esashi T.
      Biochem. Biophys. Res. Commun. 285:295-299(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Liver.
    3. "Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis."
      Shibata N., Arita M., Misaki Y., Dohmae N., Takio K., Ono T., Inoue K., Arai H.
      Proc. Natl. Acad. Sci. U.S.A. 98:2244-2249(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Liver.
    4. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
      Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
      DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. Ohara O., Nagase T., Kikuno R.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "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 3), VARIANT LYS-11.
      Tissue: Liver.
    8. 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), VARIANT LYS-11.
      Tissue: Kidney.
    9. "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].
    10. "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: Brain.
    11. "Crystal structure of the human supernatant protein factor."
      Stocker A., Tomizaki T., Schulze-Briese C., Baumann U.
      Structure 10:1533-1540(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

    Entry informationi

    Entry nameiS14L2_HUMAN
    AccessioniPrimary (citable) accession number: O76054
    Secondary accession number(s): B7Z8Q1
    , F5H3U4, Q53EQ2, Q6PD61, Q9ULN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 137 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

    3D-structure, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3