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Q9Y371 (SHLB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endophilin-B1
Alternative name(s):
Bax-interacting factor 1
Short name=Bif-1
SH3 domain-containing GRB2-like protein B1
Gene names
Name:SH3GLB1
Synonyms:KIAA0491
ORF Names:CGI-61
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.9 Ref.10

Subunit structure

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

Subcellular location

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. Ref.10

Tissue specificity

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. Ref.1 Ref.2

Domain

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. Ref.9

Post-translational modification

Phosphorylated at Thr-145 by CDK5; this phosphorylation is required for autophagy induction in starved neurons and facilitates homodimerization. Ref.12

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.

Sequence similarities

Belongs to the endophilin family.

Contains 1 BAR domain.

Contains 1 SH3 domain.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Was originally (Ref.3) thought to have lysophosphatidic acid acyltransferase activity, but by homology with SH3GL2/endophilin A1 is unlikely to have this activity.

Sequence caution

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

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

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Golgi apparatus
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidic acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein oligomerization

Inferred from direct assay PubMed 19074440. Source: UniProtKB

protein oligomerization

Inferred from direct assay PubMed 19805544. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.1. Source: HGNC

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionfatty acid binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 20562859PubMed 23414517PubMed 19805544. Source: IntAct

lysophosphatidic acid acyltransferase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 19074440. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9Y371-1)

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.
Isoform 2 (identifier: Q9Y371-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: S → SQLNSARLEGDNIMIWAEEVTK
Isoform 3 (identifier: Q9Y371-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Endophilin-B1
PRO_0000146753

Regions

Domain27 – 261235BAR
Domain305 – 36561SH3
Region1 – 3030Membrane-binding amphipathic helix
Coiled coil155 – 19541 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13
Modified residue1451Phosphothreonine; by CDK5 Ref.12

Natural variations

Alternative sequence1 – 100100Missing in isoform 3.
VSP_044895
Alternative sequence1901S → SQLNSARLEGDNIMIWAEEV TK in isoform 2.
VSP_009276

Experimental info

Mutagenesis81V → M: Abolishes interaction with BAX. Ref.1
Mutagenesis1451T → A: Reduced CDK5-mediated phosphorylation and impaired dimerization. Ref.12
Mutagenesis1451T → E: Spontaneous dimerization. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 42C2AEA57A0B350E

FASTA36540,796
        10         20         30         40         50         60 
MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE CTKIWTEKIM 

        70         80         90        100        110        120 
KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY MIDAGTEFGP GTAYGNALIK 

       130        140        150        160        170        180 
CGETQKRIGT ADRELIQTSA LNFLTPLRNF IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK 

       190        200        210        220        230        240 
KAKAAETRNS SEQELRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ 

       250        260        270        280        290        300 
CYQYMLDLQK QLGSFPSNYL SNNNQTSVTP VPSVLPNAIG SSAMASTSGL VITSPSNLSD 

       310        320        330        340        350        360 
LKECSGSRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG NQKGKVPITY 


LELLN 

« Hide

Isoform 2 [UniParc].

Checksum: 37C3D1F9338BCC5A
Show »

FASTA38643,196
Isoform 3 [UniParc].

Checksum: 200A8BB41A8ED20B
Show »

FASTA26529,318

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS55612.1. [Q9Y371-2]
CCDS55613.1. [Q9Y371-3]
CCDS710.1. [Q9Y371-1]
RefSeqNP_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]
UniGeneHs.136309.

3D structure databases

ProteinModelPortalQ9Y371.
SMRQ9Y371. Positions 21-252, 293-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119289. 44 interactions.
IntActQ9Y371. 38 interactions.
MINTMINT-192077.
STRING9606.ENSP00000212369.

PTM databases

PhosphoSiteQ9Y371.

Polymorphism databases

DMDM41018158.

2D gel databases

REPRODUCTION-2DPAGEIPI00006558.

Proteomic databases

MaxQBQ9Y371.
PaxDbQ9Y371.
PRIDEQ9Y371.

Protocols and materials databases

DNASU51100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370558; ENSP00000473267; ENSG00000097033. [Q9Y371-1]
ENST00000482504; ENSP00000418744; ENSG00000097033. [Q9Y371-2]
ENST00000535010; ENSP00000441355; ENSG00000097033. [Q9Y371-3]
GeneID51100.
KEGGhsa:51100.
UCSCuc001dlw.3. human. [Q9Y371-1]
uc001dlx.3. human. [Q9Y371-2]

Organism-specific databases

CTD51100.
GeneCardsGC01P087170.
HGNCHGNC:10833. SH3GLB1.
HPACAB004650.
HPA015608.
HPA019900.
MIM609287. gene.
neXtProtNX_Q9Y371.
PharmGKBPA35739.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309804.
HOGENOMHOG000232056.
HOVERGENHBG054448.
KOK11248.
OMARITQSEF.
OrthoDBEOG744T9N.
PhylomeDBQ9Y371.
TreeFamTF313281.

Enzyme and pathway databases

SignaLinkQ9Y371.

Gene expression databases

BgeeQ9Y371.
CleanExHS_SH3GLB1.
GenevestigatorQ9Y371.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
IPR028503. SH3GLB1.
[Graphical view]
PANTHERPTHR10661:SF15. PTHR10661:SF15. 1 hit.
PfamPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
PROSITEPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSH3GLB1. human.
GeneWikiSH3GLB1.
GenomeRNAi51100.
NextBio53809.
PROQ9Y371.
SOURCESearch...

Entry information

Entry nameSHLB1_HUMAN
AccessionPrimary (citable) accession number: Q9Y371
Secondary accession number(s): B4E182 expand/collapse secondary AC list , Q5H8U5, Q9H3Z0, Q9NR47, Q9NYA9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM