Q9Y371 (SHLB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis
Cellular component	Cytoplasm Golgi apparatus Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from direct assay Ref.1. Source: HGNC filopodium assembly Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: InterPro cytoskeletal adaptor activity Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from physical interaction Ref.1. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GADD45A	P24522	2	EBI-2623095,EBI-448167

Alternative products

This entry describes 2 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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 365	365	Endophilin-B1		PRO_0000146753
Regions
	Domain	27 – 261	235	BAR
	Domain	305 – 365	61	SH3
	Region	1 – 30	30	Membrane-binding amphipathic helix
	Coiled coil	155 – 195	41	Potential
Amino acid modifications
	Modified residue	145	1	Phosphothreonine; by CDK5 Ref.12
Natural variations
	Alternative sequence	190	1	S → SQLNSARLEGDNIMIWAEEV TK in isoform 2.		VSP_009276
Experimental info
	Mutagenesis	8	1	V → M: Abolishes interaction with BAX. Ref.1
	Mutagenesis	145	1	T → A: Reduced CDK5-mediated phosphorylation and impaired dimerization. Ref.12
	Mutagenesis	145	1	T → E: Spontaneous dimerization. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 42C2AEA57A0B350E	FASTA	365	40,796
	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
	Isoform 2 [UniParc]. Checksum: 37C3D1F9338BCC5A	FASTA	386	43,196
	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 QLNSARLEGD NIMIWAEEVT KSEQELRITQ SEFDRQAEIT RLLLEGISST 250 260 270 280 290 300 HAHHLRCLND FVEAQMTYYA QCYQYMLDLQ KQLGSFPSNY LSNNNQTSVT PVPSVLPNAI 310 320 330 340 350 360 GSSAMASTSG LVITSPSNLS DLKECSGSRK ARVLYDYDAA NSTELSLLAD EVITVFSVVG 370 380 MDSDWLMGER GNQKGKVPIT YLELLN

References

	« Hide 'large scale' referencesShow '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: 11161816] [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: 11259440] [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: 12456676] [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: 9455484] [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: 10810093] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: 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: 16710414] [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: 15489334] [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: 11604418] [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: 15452144] [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: 21269460] [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: 21499257] [Abstract] Cited for: PHOSPHORYLATION AT THR-145, MUTAGENESIS OF THR-145.
+	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. AL049597 Genomic DNA. Translation: CAC10394.1. AL049597 Genomic DNA. Translation: CAC10395.1. BC007455 mRNA. Translation: AAH07455.1.
IPI	IPI00006558. IPI00022824.
RefSeq	NP_001193580.1. NM_001206651.1. NP_001193581.1. NM_001206652.1. NP_057093.1. NM_016009.4.
UniGene	Hs.136309.
3D structure databases
ProteinModelPortal	Q9Y371.
SMR	Q9Y371. Positions 18-256, 293-365.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y371. 29 interactions.
MINT	MINT-192077.
STRING	Q9Y371.
PTM databases
PhosphoSite	Q9Y371.
Polymorphism databases
DMDM	41018158.
2D gel databases
REPRODUCTION-2DPAGE	IPI00006558.
Proteomic databases
PRIDE	Q9Y371.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000212369; ENSP00000212369; ENSG00000097033.
GeneID	51100.
KEGG	hsa:51100.
UCSC	uc001dlw.1. human. uc001dlx.1. human.
Organism-specific databases
CTD	51100.
GeneCards	GC01P087170.
H-InvDB	HIX0000753.
HGNC	HGNC:10833. SH3GLB1.
HPA	CAB004650. HPA015608. HPA019900.
MIM	609287. gene.
neXtProt	NX_Q9Y371.
PharmGKB	PA35739.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16487.
GeneTree	ENSGT00550000074464.
HOVERGEN	HBG054448.
OMA	YLCNNNQ.
OrthoDB	EOG4NGGMZ.
Gene expression databases
ArrayExpress	Q9Y371.
Bgee	Q9Y371.
CleanEx	HS_SH3GLB1.
Genevestigator	Q9Y371.
GermOnline	ENSG00000097033. Homo sapiens.
Family and domain databases
InterPro	IPR004148. BAR_dom. IPR013606. IRSp53/MIM_homology_IMD. IPR001452. SH3_domain. [Graphical view]
Gene3D	G3DSA:1.20.1270.80. IRSp53/MIM_homology_IMD. 1 hit.
KO	K11248.
Pfam	PF03114. BAR. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00721. BAR. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS51021. BAR. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	53809.
SOURCE	Search...

Entry information

Entry name

SHLB1_HUMAN

Accession

Primary (citable) accession number: Q9Y371
Secondary accession number(s): Q5H8U5 , Q9H3Z0, Q9NR47, Q9NYA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.