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O60238

- BNI3L_HUMAN

UniProt

O60238 - BNI3L_HUMAN

Protein

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like

Gene

BNIP3L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.2 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. lamin binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. defense response to virus Source: UniProtKB
    2. mitochondrial outer membrane permeabilization Source: RefGenome
    3. mitochondrial protein catabolic process Source: UniProtKB
    4. negative regulation of apoptotic process Source: UniProtKB
    5. positive regulation of apoptotic process Source: UniProtKB
    6. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, Host-virus interaction

    Protein family/group databases

    TCDBi1.A.20.1.2. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
    Alternative name(s):
    Adenovirus E1B19K-binding protein B5
    BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A
    NIP3-like protein X
    Short name:
    NIP3L
    Gene namesi
    Name:BNIP3L
    Synonyms:BNIP3A, BNIP3H, NIX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1085. BNIP3L.

    Subcellular locationi

    Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane Curated; Single-pass membrane protein Curated
    Note: Colocalizes with SPATA18 at the mitochondrion outer membrane.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. intrinsic component of membrane Source: UniProtKB
    4. mitochondrial outer membrane Source: UniProtKB
    5. mitochondrion Source: UniProtKB
    6. nuclear envelope Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25395.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 219219BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-likePRO_0000064957Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621PhosphoserineBy similarity
    Modified residuei117 – 1171PhosphoserineBy similarity
    Modified residuei118 – 1181PhosphoserineBy similarity
    Modified residuei120 – 1201Phosphoserine1 Publication

    Post-translational modificationi

    Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO60238.
    PaxDbiO60238.
    PRIDEiO60238.

    PTM databases

    PhosphoSiteiO60238.

    Expressioni

    Gene expression databases

    ArrayExpressiO60238.
    BgeeiO60238.
    CleanExiHS_BNIP3L.
    GenevestigatoriO60238.

    Organism-specific databases

    HPAiCAB025371.
    HPA015652.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with BNIP3 and STEAP3. Interacts with human adenovirus-2 E1B 19 kDa protein. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself8EBI-849893,EBI-849893
    ATP13A2Q9NQ112EBI-849893,EBI-6308763
    BADQ929342EBI-849893,EBI-700771
    BCL2P104152EBI-849893,EBI-77694
    BNIP3Q129839EBI-849893,EBI-749464
    E1BP032477EBI-849893,EBI-849856From a different organism.

    Protein-protein interaction databases

    BioGridi107133. 26 interactions.
    DIPiDIP-35187N.
    IntActiO60238. 28 interactions.
    MINTiMINT-1429960.
    STRINGi9606.ENSP00000370003.

    Structurei

    3D structure databases

    ProteinModelPortaliO60238.
    SMRiO60238. Positions 178-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei188 – 20821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi126 – 14823BH3Add
    BLAST

    Sequence similaritiesi

    Belongs to the NIP3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG83470.
    HOVERGENiHBG050707.
    InParanoidiO60238.
    KOiK15465.
    OMAiMVGGLEH.
    OrthoDBiEOG74N5J4.
    PhylomeDBiO60238.
    TreeFamiTF315424.

    Family and domain databases

    InterProiIPR010548. BNIP3.
    [Graphical view]
    PfamiPF06553. BNIP3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60238-1) [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

    MSSHLVEPPP PLHNNNNNCE ENEQSLPPPA GLNSSWVELP MNSSNGNDNG    50
    NGKNGGLEHV PSSSSIHNGD MEKILLDAQH ESGQSSSRGS SHCDSPSPQE 100
    DGQIMFDVEM HTSRDHSSQS EEEVVEGEKE VEALKKSADW VSDWSSRPEN 150
    IPPKEFHFRH PKRSVSLSMR KSGAMKKGGI FSAEFLKVFI PSLFLSHVLA 200
    LGLGIYIGKR LSTPSASTY 219
    Length:219
    Mass (Da):23,930
    Last modified:August 1, 1998 - v1
    Checksum:i19372E897BC63609
    GO
    Isoform 2 (identifier: O60238-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:179
    Mass (Da):19,559
    Checksum:i3C5A4AA97F65D467
    GO

    Sequence cautioni

    The sequence CAI46217.1 differs from that shown. Reason: Erroneous termination at position 122. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071D → E in AAN04051. (PubMed:10381623)Curated
    Sequence conflicti150 – 1501N → S in CAI46217. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040Missing in isoform 2. 1 PublicationVSP_056248Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004788 mRNA. Translation: BAA28692.1.
    AF079221 mRNA. Translation: AAC27723.1.
    AF067396 mRNA. Translation: AAD03589.1.
    AF536326 mRNA. Translation: AAN04051.1.
    AF452712 mRNA. Translation: AAL50978.1.
    AF255051 Genomic DNA. Translation: AAF70290.1.
    AK315870 mRNA. Translation: BAF98761.1.
    AK316315 mRNA. Translation: BAH14686.1.
    BT019501 mRNA. Translation: AAV38308.1.
    AL132665 mRNA. Translation: CAI46217.1. Sequence problems.
    AC011726 Genomic DNA. No translation available.
    AC015743 Genomic DNA. No translation available.
    AC022911 Genomic DNA. No translation available.
    BC001559 mRNA. Translation: AAH01559.1.
    BC009603 mRNA. Translation: AAH09603.1.
    CCDSiCCDS6050.1.
    PIRiT34523.
    RefSeqiNP_004322.1. NM_004331.2.
    XP_005273674.1. XM_005273617.1.
    UniGeneiHs.131226.

    Genome annotation databases

    EnsembliENST00000380629; ENSP00000370003; ENSG00000104765.
    ENST00000518611; ENSP00000429851; ENSG00000104765.
    GeneIDi665.
    KEGGihsa:665.
    UCSCiuc003xex.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004788 mRNA. Translation: BAA28692.1 .
    AF079221 mRNA. Translation: AAC27723.1 .
    AF067396 mRNA. Translation: AAD03589.1 .
    AF536326 mRNA. Translation: AAN04051.1 .
    AF452712 mRNA. Translation: AAL50978.1 .
    AF255051 Genomic DNA. Translation: AAF70290.1 .
    AK315870 mRNA. Translation: BAF98761.1 .
    AK316315 mRNA. Translation: BAH14686.1 .
    BT019501 mRNA. Translation: AAV38308.1 .
    AL132665 mRNA. Translation: CAI46217.1 . Sequence problems.
    AC011726 Genomic DNA. No translation available.
    AC015743 Genomic DNA. No translation available.
    AC022911 Genomic DNA. No translation available.
    BC001559 mRNA. Translation: AAH01559.1 .
    BC009603 mRNA. Translation: AAH09603.1 .
    CCDSi CCDS6050.1.
    PIRi T34523.
    RefSeqi NP_004322.1. NM_004331.2.
    XP_005273674.1. XM_005273617.1.
    UniGenei Hs.131226.

    3D structure databases

    ProteinModelPortali O60238.
    SMRi O60238. Positions 178-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107133. 26 interactions.
    DIPi DIP-35187N.
    IntActi O60238. 28 interactions.
    MINTi MINT-1429960.
    STRINGi 9606.ENSP00000370003.

    Protein family/group databases

    TCDBi 1.A.20.1.2. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

    PTM databases

    PhosphoSitei O60238.

    Proteomic databases

    MaxQBi O60238.
    PaxDbi O60238.
    PRIDEi O60238.

    Protocols and materials databases

    DNASUi 665.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380629 ; ENSP00000370003 ; ENSG00000104765 .
    ENST00000518611 ; ENSP00000429851 ; ENSG00000104765 .
    GeneIDi 665.
    KEGGi hsa:665.
    UCSCi uc003xex.1. human.

    Organism-specific databases

    CTDi 665.
    GeneCardsi GC08P026240.
    HGNCi HGNC:1085. BNIP3L.
    HPAi CAB025371.
    HPA015652.
    MIMi 605368. gene.
    neXtProti NX_O60238.
    PharmGKBi PA25395.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83470.
    HOVERGENi HBG050707.
    InParanoidi O60238.
    KOi K15465.
    OMAi MVGGLEH.
    OrthoDBi EOG74N5J4.
    PhylomeDBi O60238.
    TreeFami TF315424.

    Miscellaneous databases

    ChiTaRSi BNIP3L. human.
    GeneWikii BNIP3L.
    GenomeRNAii 665.
    NextBioi 2712.
    PROi O60238.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60238.
    Bgeei O60238.
    CleanExi HS_BNIP3L.
    Genevestigatori O60238.

    Family and domain databases

    InterProi IPR010548. BNIP3.
    [Graphical view ]
    Pfami PF06553. BNIP3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3."
      Matsushima M., Fujiwara T., Takahashi E., Minaguchi T., Eguchi Y., Tsujimoto Y., Suzumori K., Nakamura Y.
      Genes Chromosomes Cancer 21:230-235(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "BNIP3a, a human homolog of pro-apoptotic protein BNIP3, promotes apoptosis and interacts with viral and cellular anti-apoptosis proteins."
      Yasuda M., Han J.-W., Dionne C.A., Boyd J.M., Chinnadurai G.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins."
      Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J., Shi L., Dubik D., Greenberg A.
      J. Biol. Chem. 274:7-10(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    4. "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region."
      Ohi N., Tokunaga A., Tsunoda H., Nakano K., Haraguchi K., Oda K., Motoyama N., Nakajima T.
      Cell Death Differ. 6:314-325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, INTERACTION WITH BNIP3 AND HUMAN ADENOVIRUS-2 E1B 19 KDA PROTEIN.
    5. "The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation."
      Aerbajinai W., Giattina M., Lee Y.T., Raffeld M., Miller J.L.
      Blood 102:712-717(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "A catalog of genes in the human dermal papilla cells as identified by expressed sequence tags."
      Farooq M., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Sohn M.Y., Hwang S.Y., Chung H.J., Im S.U., Jung E.J., Kim J.C.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Hair follicle dermal papilla.
    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 2).
      Tissue: Brain.
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney.
    10. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Bone marrow and Cervix.
    12. Cited for: INTERACTION WITH STEAP3.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Mieap, a p53-inducible protein, controls mitochondrial quality by repairing or eliminating unhealthy mitochondria."
      Kitamura N., Nakamura Y., Miyamoto Y., Miyamoto T., Kabu K., Yoshida M., Futamura M., Ichinose S., Arakawa H.
      PLoS ONE 6:E16060-E16060(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SPATA18, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBNI3L_HUMAN
    AccessioniPrimary (citable) accession number: O60238
    Secondary accession number(s): B0AZS9, Q5JW63, Q8NF87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 132 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3