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Q9Y371

- SHLB1_HUMAN

UniProt

Q9Y371 - SHLB1_HUMAN

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Protein
Endophilin-B1
Gene
SH3GLB1, KIAA0491, CGI-61
Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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
Complete GO annotation...

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

GO - Cellular componenti

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

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-B1
PRO_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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 261235BAR
Add
BLAST
Domaini305 – 36561SH3
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili155 – 19541 Reviewed prediction
Add
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.
Contains 1 BAR domain.
Contains 1 SH3 domain.

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.
VSP_044895Add
BLAST
Alternative sequencei190 – 1901S → SQLNSARLEGDNIMIWAEEV TK in isoform 2.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 127 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

Similar proteinsi