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Protein

Endophilin-B1

Gene

Sh3glb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells (PubMed:17086176). May recruit other proteins to membranes with high curvature. May promote membrane fusion (By similarity). Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation (PubMed:16227588). Isoform 1 acts proapoptotic in fibroblasts (PubMed:24523556). Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance of mitochondrial morphology and promotes neuronal viability (PubMed:24523556).By similarity2 Publications

GO - Molecular functioni

  • fatty acid binding Source: MGI
  • identical protein binding Source: MGI
  • lysophosphatidic acid acyltransferase activity Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • 'de novo' posttranslational protein folding Source: MGI
  • apoptotic process Source: MGI
  • autophagic cell death Source: UniProtKB
  • cellular response to amino acid starvation Source: MGI
  • cellular response to glucose starvation Source: MGI
  • membrane fission Source: MGI
  • mitochondrion organization Source: UniProtKB
  • negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • phosphatidic acid biosynthetic process Source: MGI
  • phospholipid biosynthetic process Source: MGI
  • positive regulation of autophagosome assembly Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • positive regulation of membrane tubulation Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: MGI
  • positive regulation of protein oligomerization Source: MGI
  • positive regulation of protein targeting to mitochondrion Source: MGI
  • protein localization to vacuolar membrane Source: UniProtKB
  • protein oligomerization Source: MGI
  • receptor catabolic process Source: MGI
  • regulation of cytokinesis Source: MGI
  • regulation of protein stability Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Endophilin-B1
Alternative name(s):
SH3 domain-containing GRB2-like protein B1
Gene namesi
Name:Sh3glb1
Synonyms:Kiaa0491
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1859730. Sh3glb1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Golgi apparatus membrane 1 Publication; Peripheral membrane protein By similarity
  • Mitochondrion outer membrane By similarity; Peripheral membrane protein By similarity
  • Cytoplasmic vesicleautophagosome membrane By similarity
  • Midbody By similarity

  • Note: Association with the Golgi apparatus depends on the cell type. Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes.By similarity

GO - Cellular componenti

  • autophagosome membrane Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic vesicle Source: UniProtKB-KW
  • cytosol Source: MGI
  • endoplasmic reticulum Source: MGI
  • extracellular exosome Source: MGI
  • Golgi membrane Source: UniProtKB-SubCell
  • membrane Source: MGI
  • midbody Source: MGI
  • mitochondrial envelope Source: MGI
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Endophilin-B1PRO_0000146754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei145 – 1451Phosphothreonine; by CDK5By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JK48.
MaxQBiQ9JK48.
PaxDbiQ9JK48.
PeptideAtlasiQ9JK48.
PRIDEiQ9JK48.

2D gel databases

REPRODUCTION-2DPAGEQ9JK48.

PTM databases

iPTMnetiQ9JK48.
PhosphoSiteiQ9JK48.
SwissPalmiQ9JK48.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed. Isoform 2 is brain-specific. Isoform 3 is predominantly expressed in testis, but it is also detected in liver and, at much lower levels, in skin, stomach and ovary.1 Publication

Gene expression databases

BgeeiQ9JK48.
CleanExiMM_SH3GLB1.
ExpressionAtlasiQ9JK48. baseline and differential.
GenevisibleiQ9JK48. MM.

Interactioni

Subunit structurei

Homodimer, and heterodimer with SH3GLB2 (By similarity). Binds BAX; induction of apoptosis augments BAX binding (PubMed:16227588, PubMed:17381077). Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1 (PubMed:12456676, PubMed:17086176). Interacts with UVRAG; UVRAG bridges the interaction to BECN1 indicative for an association with the PI3K complex II (PI3KC3-C2) (By similarity). Isoform 3 interacts with PPP1CC; this interaction leads to the inhibition of phosphatase activity (PubMed:17381077).By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207716. 4 interactions.
IntActiQ9JK48. 4 interactions.
MINTiMINT-4134582.
STRINGi10090.ENSMUSP00000129800.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi308 – 3147Combined sources
Beta strandi331 – 3355Combined sources
Beta strandi344 – 3496Combined sources
Beta strandi352 – 3576Combined sources
Helixi358 – 3603Combined sources
Beta strandi361 – 3633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X43NMR-A298-365[»]
ProteinModelPortaliQ9JK48.
SMRiQ9JK48. Positions 21-252, 296-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JK48.

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 – 3737Required for membrane bindingBy similarityAdd
BLAST
Regioni1 – 3030Membrane-binding amphipathic helixBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili155 – 18632Sequence 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.By similarity
The SH3 domain is required and sufficient for the interaction with UVRAG.By similarity

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

eggNOGiKOG3725. Eukaryota.
ENOG410XPA6. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000232056.
HOVERGENiHBG054448.
InParanoidiQ9JK48.
KOiK11248.
OrthoDBiEOG744T9N.
PhylomeDBiQ9JK48.
TreeFamiTF313281.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
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. AlignAdd to basket

Isoform 1 (identifier: Q9JK48-1) [UniParc]FASTAAdd to basket

Also known as: Endophilin B1a, Bif-11 Publication

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

        10         20         30         40         50
MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE
60 70 80 90 100
CTKIWTEKIM KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY
110 120 130 140 150
MIDAGTEFGP GTAYGNALIK CGETQKRIGT ADRELIQTSA LNFLTPLRNF
160 170 180 190 200
IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK KAKAAETKSS SEQELRITQS
210 220 230 240 250
EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ CYQYMLDLQK
260 270 280 290 300
QLGSFPSNYL SNNNQTSGTP VPYALSNAIG PSAQASTGSL VITCPSNLND
310 320 330 340 350
LKESSNNRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG
360
NQKGKVPITY LELLN
Length:365
Mass (Da):40,855
Last modified:October 1, 2000 - v1
Checksum:i1FC02795693142FB
GO
Isoform 2 (identifier: Q9JK48-2) [UniParc]FASTAAdd to basket

Also known as: Endophilin B1b

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

Show »
Length:386
Mass (Da):43,239
Checksum:iEB57B8AB5DE6F627
GO
Isoform 3 (identifier: Q9JK48-3) [UniParc]FASTAAdd to basket

Also known as: Endophilin-B1t1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     356-365: Missing.

Show »
Length:355
Mass (Da):39,699
Checksum:i89E97B600228F592
GO

Sequence cautioni

The sequence BAD32237.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591A → T in BAB27575 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei190 – 1901S → SQLNSARPEGDNIMIWAEEV TK in isoform 2. 1 PublicationVSP_009277
Alternative sequencei356 – 36510Missing in isoform 3. VSP_058266

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263364 mRNA. Translation: AAF73438.1.
AF272946 mRNA. Translation: AAL59846.1.
DQ205686 mRNA. Translation: ABA54268.1.
AK172959 mRNA. Translation: BAD32237.1. Different initiation.
AK029647 mRNA. Translation: BAC26545.1.
AK011371 mRNA. Translation: BAB27575.3.
AK158415 mRNA. Translation: BAE34495.1.
AC134404 Genomic DNA. No translation available.
BC024362 mRNA. Translation: AAH24362.1.
CCDSiCCDS17885.1. [Q9JK48-1]
CCDS80042.1. [Q9JK48-3]
CCDS80043.1. [Q9JK48-2]
RefSeqiNP_001268966.1. NM_001282037.1. [Q9JK48-2]
NP_001268971.1. NM_001282042.1. [Q9JK48-3]
NP_062337.1. NM_019464.3. [Q9JK48-1]
UniGeneiMm.271775.
Mm.440295.

Genome annotation databases

EnsembliENSMUST00000163279; ENSMUSP00000129800; ENSMUSG00000037062. [Q9JK48-1]
ENSMUST00000198254; ENSMUSP00000143312; ENSMUSG00000037062. [Q9JK48-2]
ENSMUST00000199531; ENSMUSP00000143433; ENSMUSG00000037062. [Q9JK48-3]
GeneIDi54673.
KEGGimmu:54673.
UCSCiuc008rpt.2. mouse. [Q9JK48-1]
uc008rpw.2. mouse. [Q9JK48-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263364 mRNA. Translation: AAF73438.1.
AF272946 mRNA. Translation: AAL59846.1.
DQ205686 mRNA. Translation: ABA54268.1.
AK172959 mRNA. Translation: BAD32237.1. Different initiation.
AK029647 mRNA. Translation: BAC26545.1.
AK011371 mRNA. Translation: BAB27575.3.
AK158415 mRNA. Translation: BAE34495.1.
AC134404 Genomic DNA. No translation available.
BC024362 mRNA. Translation: AAH24362.1.
CCDSiCCDS17885.1. [Q9JK48-1]
CCDS80042.1. [Q9JK48-3]
CCDS80043.1. [Q9JK48-2]
RefSeqiNP_001268966.1. NM_001282037.1. [Q9JK48-2]
NP_001268971.1. NM_001282042.1. [Q9JK48-3]
NP_062337.1. NM_019464.3. [Q9JK48-1]
UniGeneiMm.271775.
Mm.440295.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X43NMR-A298-365[»]
ProteinModelPortaliQ9JK48.
SMRiQ9JK48. Positions 21-252, 296-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207716. 4 interactions.
IntActiQ9JK48. 4 interactions.
MINTiMINT-4134582.
STRINGi10090.ENSMUSP00000129800.

PTM databases

iPTMnetiQ9JK48.
PhosphoSiteiQ9JK48.
SwissPalmiQ9JK48.

2D gel databases

REPRODUCTION-2DPAGEQ9JK48.

Proteomic databases

EPDiQ9JK48.
MaxQBiQ9JK48.
PaxDbiQ9JK48.
PeptideAtlasiQ9JK48.
PRIDEiQ9JK48.

Protocols and materials databases

DNASUi54673.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163279; ENSMUSP00000129800; ENSMUSG00000037062. [Q9JK48-1]
ENSMUST00000198254; ENSMUSP00000143312; ENSMUSG00000037062. [Q9JK48-2]
ENSMUST00000199531; ENSMUSP00000143433; ENSMUSG00000037062. [Q9JK48-3]
GeneIDi54673.
KEGGimmu:54673.
UCSCiuc008rpt.2. mouse. [Q9JK48-1]
uc008rpw.2. mouse. [Q9JK48-2]

Organism-specific databases

CTDi51100.
MGIiMGI:1859730. Sh3glb1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3725. Eukaryota.
ENOG410XPA6. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000232056.
HOVERGENiHBG054448.
InParanoidiQ9JK48.
KOiK11248.
OrthoDBiEOG744T9N.
PhylomeDBiQ9JK48.
TreeFamiTF313281.

Miscellaneous databases

ChiTaRSiSh3glb1. mouse.
EvolutionaryTraceiQ9JK48.
PROiQ9JK48.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JK48.
CleanExiMM_SH3GLB1.
ExpressionAtlasiQ9JK48. baseline and differential.
GenevisibleiQ9JK48. MM.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2), INTERACTION WITH DNM1; HTT; BIN1 AND AMPH, SUBCELLULAR LOCATION.
    Strain: BALB/cJ.
    Tissue: Embryo.
  2. "A testis specific isoform of endophilin B1, endophilin B1t, interacts specifically with protein phosphatase-1c gamma2 in mouse testis and is abnormally expressed in PP1c gamma null mice."
    Hrabchak C., Henderson H., Varmuza S.
    Biochemistry 46:4635-4644(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH BAX AND PPP1CC, SUBCELLULAR LOCATION.
    Strain: CD-1.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Natural killer cell.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Embryo, Inner ear and Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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: Mammary gland.
  7. "Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis."
    Takahashi Y., Karbowski M., Yamaguchi H., Kazi A., Wu J., Sebti S.M., Youle R.J., Wang H.G.
    Mol. Cell. Biol. 25:9369-9382(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BAX.
  8. "Key components of the fission machinery are interchangeable."
    Yang J.S., Zhang L., Lee S.Y., Gad H., Luini A., Hsu V.W.
    Nat. Cell Biol. 8:1376-1382(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARFGAP1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  10. "Bax interacting factor-1 promotes survival and mitochondrial elongation in neurons."
    Wang D.B., Uo T., Kinoshita C., Sopher B.L., Lee R.J., Murphy S.P., Kinoshita Y., Garden G.A., Wang H.G., Morrison R.S.
    J. Neurosci. 34:2674-2683(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, FUNCTION (ISOFORM 2).
  11. "Solution structure of the SH3 domain of endophilin B1 (SH3G1B1)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 296-365.

Entry informationi

Entry nameiSHLB1_MOUSE
AccessioniPrimary (citable) accession number: Q9JK48
Secondary accession number(s): Q3TYR7
, Q6A059, Q8CDS9, Q8VI52, Q9CT31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2000
Last modified: July 6, 2016
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

Miscellaneousi

Miscellaneous

Fibroblasts with a reduced level of Sh3glb1 show a defect in retrograde transport between the Golgi apparatus and the endoplasmic reticulum.

Caution

Was originally thought to have lysophosphatidic acid acyltransferase activity, but by homology with SH3GL2/endophilin A1 is unlikely to have this activity.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.