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Q9Y371

- SHLB1_HUMAN

UniProt

Q9Y371 - SHLB1_HUMAN

Protein

Endophilin-B1

Gene

SH3GLB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells. May recruit other proteins to membranes with high curvature. May promote membrane fusion.3 Publications

    GO - Molecular functioni

    1. fatty acid binding Source: Ensembl
    2. identical protein binding Source: IntAct
    3. lysophosphatidic acid acyltransferase activity Source: Ensembl
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: HGNC

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Ensembl
    2. apoptotic process Source: UniProtKB-KW
    3. phosphatidic acid biosynthetic process Source: Ensembl
    4. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Ensembl
    5. positive regulation of protein oligomerization Source: UniProtKB
    6. protein oligomerization Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    SignaLinkiQ9Y371.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endophilin-B1
    Alternative name(s):
    Bax-interacting factor 1
    Short name:
    Bif-1
    SH3 domain-containing GRB2-like protein B1
    Gene namesi
    Name:SH3GLB1
    Synonyms:KIAA0491
    ORF Names:CGI-61
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10833. SH3GLB1.

    Subcellular locationi

    Cytoplasm 1 Publication. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity. Mitochondrion outer membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Association with the Golgi apparatus depends on the cell type.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi membrane Source: UniProtKB-SubCell
    4. mitochondrial outer membrane Source: UniProtKB-SubCell
    5. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81V → M: Abolishes interaction with BAX. 1 Publication
    Mutagenesisi145 – 1451T → A: Reduced CDK5-mediated phosphorylation and impaired dimerization. 1 Publication
    Mutagenesisi145 – 1451T → E: Spontaneous dimerization. 1 Publication

    Organism-specific databases

    PharmGKBiPA35739.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 365365Endophilin-B1PRO_0000146753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei145 – 1451Phosphothreonine; by CDK51 Publication

    Post-translational modificationi

    Phosphorylated at Thr-145 by CDK5; this phosphorylation is required for autophagy induction in starved neurons and facilitates homodimerization.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y371.
    PaxDbiQ9Y371.
    PRIDEiQ9Y371.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00006558.

    PTM databases

    PhosphoSiteiQ9Y371.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, skeletal muscle, kidney and placenta. Detected at lower levels in brain, colon, thymus, spleen, liver, small intestine, lung and peripheral blood leukocytes.2 Publications

    Gene expression databases

    BgeeiQ9Y371.
    CleanExiHS_SH3GLB1.
    GenevestigatoriQ9Y371.

    Organism-specific databases

    HPAiCAB004650.
    HPA015608.
    HPA019900.

    Interactioni

    Subunit structurei

    Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1 By similarity. Homodimer, and heterodimer with SH3GLB2. Binds BAX. Induction of apoptosis augments BAX binding.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-2623095,EBI-2623095
    BAXQ078122EBI-5291808,EBI-516580
    GADD45AP245222EBI-2623095,EBI-448167
    SH3GLB2Q9NR465EBI-2623095,EBI-749607
    UVRAGQ9P2Y52EBI-2623095,EBI-2952704

    Protein-protein interaction databases

    BioGridi119289. 44 interactions.
    IntActiQ9Y371. 38 interactions.
    MINTiMINT-192077.
    STRINGi9606.ENSP00000212369.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y371.
    SMRiQ9Y371. Positions 21-252, 293-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 261235BARPROSITE-ProRule annotationAdd
    BLAST
    Domaini305 – 36561SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 3030Membrane-binding amphipathic helixAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili155 – 19541Sequence AnalysisAdd
    BLAST

    Domaini

    An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes.1 Publication

    Sequence similaritiesi

    Belongs to the endophilin family.Curated
    Contains 1 BAR domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG309804.
    HOGENOMiHOG000232056.
    HOVERGENiHBG054448.
    KOiK11248.
    OMAiRITQSEF.
    OrthoDBiEOG744T9N.
    PhylomeDBiQ9Y371.
    TreeFamiTF313281.

    Family and domain databases

    Gene3Di1.20.1270.60. 1 hit.
    InterProiIPR027267. AH/BAR-dom.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    IPR028503. SH3GLB1.
    [Graphical view]
    PANTHERiPTHR10661:SF15. PTHR10661:SF15. 1 hit.
    PfamiPF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    SMARTiSM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 2 hits.
    PROSITEiPS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9Y371-1) [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

    MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE    50
    CTKIWTEKIM KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY 100
    MIDAGTEFGP GTAYGNALIK CGETQKRIGT ADRELIQTSA LNFLTPLRNF 150
    IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK KAKAAETRNS SEQELRITQS 200
    EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ CYQYMLDLQK 250
    QLGSFPSNYL SNNNQTSVTP VPSVLPNAIG SSAMASTSGL VITSPSNLSD 300
    LKECSGSRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG 350
    NQKGKVPITY LELLN 365
    Length:365
    Mass (Da):40,796
    Last modified:November 1, 1999 - v1
    Checksum:i42C2AEA57A0B350E
    GO
    Isoform 2 (identifier: Q9Y371-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         190-190: S → SQLNSARLEGDNIMIWAEEVTK

    Show »
    Length:386
    Mass (Da):43,196
    Checksum:i37C3D1F9338BCC5A
    GO
    Isoform 3 (identifier: Q9Y371-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:265
    Mass (Da):29,318
    Checksum:i200A8BB41A8ED20B
    GO

    Sequence cautioni

    The sequence AAF81225.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD88797.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 3. 1 PublicationVSP_044895Add
    BLAST
    Alternative sequencei190 – 1901S → SQLNSARLEGDNIMIWAEEV TK in isoform 2. 1 PublicationVSP_009276

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257318 mRNA. Translation: AAF81225.1. Different initiation.
    AF350371 mRNA. Translation: AAK27365.1.
    AF263293 mRNA. Translation: AAF73017.1.
    AB007960 mRNA. Translation: BAD88797.1. Different initiation.
    AF151819 mRNA. Translation: AAD34056.1.
    AK001954 mRNA. Translation: BAA91999.1.
    AK303710 mRNA. Translation: BAG64694.1.
    AL049597 Genomic DNA. Translation: CAC10394.1.
    AL049597 Genomic DNA. Translation: CAC10395.1.
    BC007455 mRNA. Translation: AAH07455.1.
    CCDSiCCDS55612.1. [Q9Y371-2]
    CCDS55613.1. [Q9Y371-3]
    CCDS710.1. [Q9Y371-1]
    RefSeqiNP_001193580.1. NM_001206651.1.
    NP_001193581.1. NM_001206652.1. [Q9Y371-2]
    NP_001193582.1. NM_001206653.1. [Q9Y371-3]
    NP_057093.1. NM_016009.4. [Q9Y371-1]
    UniGeneiHs.136309.

    Genome annotation databases

    EnsembliENST00000370558; ENSP00000473267; ENSG00000097033. [Q9Y371-1]
    ENST00000482504; ENSP00000418744; ENSG00000097033. [Q9Y371-2]
    ENST00000535010; ENSP00000441355; ENSG00000097033. [Q9Y371-3]
    GeneIDi51100.
    KEGGihsa:51100.
    UCSCiuc001dlw.3. human. [Q9Y371-1]
    uc001dlx.3. human. [Q9Y371-2]

    Polymorphism databases

    DMDMi41018158.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257318 mRNA. Translation: AAF81225.1 . Different initiation.
    AF350371 mRNA. Translation: AAK27365.1 .
    AF263293 mRNA. Translation: AAF73017.1 .
    AB007960 mRNA. Translation: BAD88797.1 . Different initiation.
    AF151819 mRNA. Translation: AAD34056.1 .
    AK001954 mRNA. Translation: BAA91999.1 .
    AK303710 mRNA. Translation: BAG64694.1 .
    AL049597 Genomic DNA. Translation: CAC10394.1 .
    AL049597 Genomic DNA. Translation: CAC10395.1 .
    BC007455 mRNA. Translation: AAH07455.1 .
    CCDSi CCDS55612.1. [Q9Y371-2 ]
    CCDS55613.1. [Q9Y371-3 ]
    CCDS710.1. [Q9Y371-1 ]
    RefSeqi NP_001193580.1. NM_001206651.1.
    NP_001193581.1. NM_001206652.1. [Q9Y371-2 ]
    NP_001193582.1. NM_001206653.1. [Q9Y371-3 ]
    NP_057093.1. NM_016009.4. [Q9Y371-1 ]
    UniGenei Hs.136309.

    3D structure databases

    ProteinModelPortali Q9Y371.
    SMRi Q9Y371. Positions 21-252, 293-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119289. 44 interactions.
    IntActi Q9Y371. 38 interactions.
    MINTi MINT-192077.
    STRINGi 9606.ENSP00000212369.

    PTM databases

    PhosphoSitei Q9Y371.

    Polymorphism databases

    DMDMi 41018158.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00006558.

    Proteomic databases

    MaxQBi Q9Y371.
    PaxDbi Q9Y371.
    PRIDEi Q9Y371.

    Protocols and materials databases

    DNASUi 51100.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370558 ; ENSP00000473267 ; ENSG00000097033 . [Q9Y371-1 ]
    ENST00000482504 ; ENSP00000418744 ; ENSG00000097033 . [Q9Y371-2 ]
    ENST00000535010 ; ENSP00000441355 ; ENSG00000097033 . [Q9Y371-3 ]
    GeneIDi 51100.
    KEGGi hsa:51100.
    UCSCi uc001dlw.3. human. [Q9Y371-1 ]
    uc001dlx.3. human. [Q9Y371-2 ]

    Organism-specific databases

    CTDi 51100.
    GeneCardsi GC01P087170.
    HGNCi HGNC:10833. SH3GLB1.
    HPAi CAB004650.
    HPA015608.
    HPA019900.
    MIMi 609287. gene.
    neXtProti NX_Q9Y371.
    PharmGKBi PA35739.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309804.
    HOGENOMi HOG000232056.
    HOVERGENi HBG054448.
    KOi K11248.
    OMAi RITQSEF.
    OrthoDBi EOG744T9N.
    PhylomeDBi Q9Y371.
    TreeFami TF313281.

    Enzyme and pathway databases

    SignaLinki Q9Y371.

    Miscellaneous databases

    ChiTaRSi SH3GLB1. human.
    GeneWikii SH3GLB1.
    GenomeRNAii 51100.
    NextBioi 53809.
    PROi Q9Y371.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y371.
    CleanExi HS_SH3GLB1.
    Genevestigatori Q9Y371.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    InterProi IPR027267. AH/BAR-dom.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    IPR028503. SH3GLB1.
    [Graphical view ]
    PANTHERi PTHR10661:SF15. PTHR10661:SF15. 1 hit.
    Pfami PF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 2 hits.
    PROSITEi PS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SH3GLB, a new endophilin-related protein family featuring an SH3 domain."
      Pierrat B., Simonen M., Cueto M., Mestan J., Ferrigno P., Heim J.
      Genomics 71:222-234(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF VAL-8, INTERACTION WITH BAX AND SH3GLB2, TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    2. "Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax."
      Cuddeback S.M., Yamaguchi H., Komatsu K., Miyashita T., Yamada M., Wu C., Singh S., Wang H.-G.
      J. Biol. Chem. 276:20559-20565(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BAX, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    3. "Characterization of endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1."
      Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.
      J. Biol. Chem. 278:4160-4167(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Lung.
    4. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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 3).
      Tissue: Kidney and Placenta.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Skin.
    9. "Generation of high curvature membranes mediated by direct endophilin bilayer interactions."
      Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P.
      J. Cell Biol. 155:193-200(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    10. "Endophilin B1 is required for the maintenance of mitochondrial morphology."
      Karbowski M., Jeong S.-Y., Youle R.J.
      J. Cell Biol. 166:1027-1039(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson's disease."
      Wong A.S., Lee R.H., Cheung A.Y., Yeung P.K., Chung S.K., Cheung Z.H., Ip N.Y.
      Nat. Cell Biol. 13:568-579(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-145, MUTAGENESIS OF THR-145.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSHLB1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y371
    Secondary accession number(s): B4E182
    , Q5H8U5, Q9H3Z0, Q9NR47, Q9NYA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 128 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

    Miscellaneous

    HeLa cells lacking SH3GLB1 show dissociation of outer and inner mitochondrial membrane as well as abnormal mitochondrial morphology. Cells overexpressing SH3GLB1 lacking an N-terminal amphipathic helix show a similar phenotype.
    SH3GLB1 binds liposomes and induces formation of tubules from liposomes. SH3GLB1 lacking the N-terminal amphipathic helix fails to induce liposome tubulation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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