Q9JK48 (SHLB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endophilin-B1

Alternative name(s):
SH3 domain-containing GRB2-like protein B1

Gene names

Name:	Sh3glb1
Synonyms:	Kiaa0491

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.5
Subunit structure	Homodimer, and heterodimer with SH3GLB2. Binds BAX By similarity. Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1.
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein By similarity. Note: Association with the Golgi apparatus depends on the cell type. Ref.1 Ref.5
Tissue specificity	Isoform 1 is widely expressed. Isoform 2 is brain specific.
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 By similarity.
Post-translational modification	Phosphorylated at Thr-145 by CDK5; this phosphorylation is required for autophagy induction in starved neurons and facilitates homodimerization By similarity.
Miscellaneous	Fibroblasts with a reduced level of Sh3glb1 show a defect in retrograde transport between the Golgi apparatus and the endoplasmic reticulum.
Sequence similarities	Belongs to the endophilin family. Contains 1 BAR domain. Contains 1 SH3 domain.
Caution	Was originally (Ref.1) thought to have lysophosphatidic acid acyltransferase activity, but by homology with SH3GL2/endophilin A1 is unlikely to have this activity.
Sequence caution	The sequence BAD32237.1 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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Inferred from direct assay. Source: MGI filopodium assembly Inferred from electronic annotation. Source: InterPro phosphatidic acid biosynthetic process Inferred from direct assay Ref.1. Source: MGI protein insertion into mitochondrial membrane involved in induction of apoptosis Inferred from mutant phenotype. Source: MGI signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred by curator Ref.1. Source: MGI microsome Inferred from direct assay Ref.1. Source: MGI mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from direct assay. Source: MGI
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: InterPro cytoskeletal adaptor activity Inferred from electronic annotation. Source: InterPro fatty acid binding Inferred from direct assay Ref.1. Source: MGI lysophosphatidic acid acyltransferase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9JK48-1)

Also known as: Endophilin B1a;

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: Q9JK48-2)

Also known as: Endophilin B1b;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 365

365

Endophilin-B1

PRO_0000146754

Regions

Domain

27 – 261

235

BAR

Domain

305 – 365

61

SH3

Region

1 – 30

30

Membrane-binding amphipathic helix By similarity

Coiled coil

155 – 186

32

Potential

Amino acid modifications

Modified residue

145

1

Phosphothreonine; by CDK5 By similarity

Natural variations

Alternative sequence

190

1

S → SQLNSARPEGDNIMIWAEEV TK in isoform 2.

VSP_009277

Experimental info

Sequence conflict

159

1

A → T in BAB27575. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

365

Helix Strand Turn

Details...

Beta strand

308 – 314

7

Beta strand

331 – 335

5

Beta strand

344 – 349

6

Beta strand

352 – 357

6

Helix

358 – 360

3

Beta strand

361 – 363

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Endophilin B1a) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1FC02795693142FB	FASTA	365	40,855
	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 KAKAAETKSS SEQELRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ 250 260 270 280 290 300 CYQYMLDLQK QLGSFPSNYL SNNNQTSGTP VPYALSNAIG PSAQASTGSL VITCPSNLND 310 320 330 340 350 360 LKESSNNRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG NQKGKVPITY LELLN
	Isoform 2 (Endophilin B1b) [UniParc]. Checksum: EB57B8AB5DE6F627	FASTA	386	43,239
	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 KAKAAETKSS QLNSARPEGD NIMIWAEEVT KSEQELRITQ SEFDRQAEIT RLLLEGISST 250 260 270 280 290 300 HAHHLRCLND FVEAQMTYYA QCYQYMLDLQ KQLGSFPSNY LSNNNQTSGT PVPYALSNAI 310 320 330 340 350 360 GPSAQASTGS LVITCPSNLN DLKESSNNRK ARVLYDYDAA NSTELSLLAD EVITVFSVVG 370 380 MDSDWLMGER GNQKGKVPIT YLELLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12456676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH DNM1; HTT; BIN1 AND AMPH, SUBCELLULAR LOCATION. Strain: BALB/c. Tissue: Embryo.
[2]	"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: 15368895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Natural killer cell.
[3]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryo and Testis.
[4]	"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: Mammary gland.
[5]	"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: 17086176] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARFGAP1.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF263364 mRNA. Translation: AAF73438.1.
AF272946 mRNA. Translation: AAL59846.1.
AK172959 mRNA. Translation: BAD32237.1. Different initiation.
AK029647 mRNA. Translation: BAC26545.1.
AK011371 mRNA. Translation: BAB27575.3.
BC024362 mRNA. Translation: AAH24362.1.

IPI

IPI00122267.
IPI00128778.

RefSeq

NP_062337.1. NM_019464.2.

UniGene

Mm.271775.
Mm.440295.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X43	NMR	-	A	298-365	[»]

ProteinModelPortal

Q9JK48.

SMR

Q9JK48. Positions 19-255, 296-365.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9JK48. 1 interaction.

STRING

Q9JK48.

PTM databases

PhosphoSite

Q9JK48.

2D gel databases

REPRODUCTION-2DPAGE

Q9JK48.

Proteomic databases

PRIDE

Q9JK48.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000106210; ENSMUSP00000101816; ENSMUSG00000037062.
ENSMUST00000163279; ENSMUSP00000129800; ENSMUSG00000037062.

GeneID

54673.

KEGG

mmu:54673.

UCSC

uc008rpv.1. mouse.
uc008rpw.1. mouse.

Organism-specific databases

CTD

51100.

MGI

MGI:1859730. Sh3glb1.

Rouge

Search...

Phylogenomic databases

GeneTree

ENSGT00550000074464.

HOVERGEN

HBG054448.

OMA

YLCNNNQ.

OrthoDB

EOG4NGGMZ.

Gene expression databases

ArrayExpress

Q9JK48.

Bgee

Q9JK48.

CleanEx

MM_SH3GLB1.

Genevestigator

Q9JK48.

GermOnline

ENSMUSG00000037062. Mus musculus.

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

311528.

SOURCE

Search...

Entry information

Entry name

SHLB1_MOUSE

Accession

Primary (citable) accession number: Q9JK48
Secondary accession number(s): Q6A059 , Q8CDS9, Q8VI52, Q9CT31

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program