Q99961 (SH3G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endophilin-A2

Alternative name(s):
EEN fusion partner of MLL
Endophilin-2
Extra eleven-nineteen leukemia fusion gene protein
Short name=EEN
SH3 domain protein 2B
SH3 domain-containing GRB2-like protein 1

Gene names

Name:	SH3GL1
Synonyms:	CNSA1, SH3D2B

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	368 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Implicated in endocytosis. May recruit other proteins to membranes with high curvature By similarity.
Subunit structure	Interacts with ARC By similarity. Interacts with SYNJ1 and DNM1. Interacts with PDCD6IP. Ref.6 Ref.8
Subcellular location	Cytoplasm By similarity. Early endosome membrane; Peripheral membrane protein By similarity. Note: Associated with postsynaptic endosomes in hippocampal neurons By similarity.
Tissue specificity	Ubiquitous. Higher expression in pancreas, placenta, prostate, testis and uterus.
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.
Involvement in disease	Note=In some cases of acute leukemia, a translocation results in the formation of a MLL-EEN fusion gene.
Sequence similarities	Belongs to the endophilin family. Contains 1 BAR domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm Endosome Membrane
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	central nervous system development Traceable author statement. Source: ProtInc endocytosis Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement. Source: ProtInc
Cellular component	early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DPPA4	Q7L190	3	EBI-697911,EBI-710457
SH2D4A	Q9H788	3	EBI-697911,EBI-747035
SH3GL3	Q99963	3	EBI-697911,EBI-473910

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 368	368	Endophilin-A2		PRO_0000146744
Regions
	Domain	18 – 249	232	BAR
	Domain	306 – 365	60	SH3
	Region	1 – 21	21	Membrane-binding amphipathic helix By similarity
	Region	60 – 87	28	Required for dimerization upon membrane association By similarity
	Region	218 – 254	37	Interaction with ARC By similarity
	Coiled coil	145 – 250	106	Potential
Sites
	Site	15 – 16	2	Breakpoint for translocation to form MLL-EEN oncogene
Amino acid modifications
	Modified residue	287	1	Phosphoserine Ref.11 Ref.12
	Modified residue	288	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q99961 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 6E5BE978BC955077	FASTA	368	41,490
	10 20 30 40 50 60 MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKEMEKKV DVTSKAVTEV LARTIEYLQP 70 80 90 100 110 120 NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMIRH GKELGGESNF GDALLDAGES 130 140 150 160 170 180 MKRLAEVKDS LDIEVKQNFI DPLQNLCEKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD 190 200 210 220 230 240 EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILDELAEKL 250 260 270 280 290 300 KRRMREASSR PKREYKPKPR EPFDLGEPEQ SNGGFPCTTA PKIAASSSFR SSDKPIRTPS 310 320 330 340 350 360 RSMPPLDQPS CKALYDFEPE NDGELGFHEG DVITLTNQID ENWYEGMLDG QSGFFPLSYV EVLVPLPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel SH3-containing human gene family preferentially expressed in the central nervous system." Giachino C., Lantelme E., Lanzetti L., Saccone S., Della Valle G., Migone N. Genomics 41:427-434(1997) [PubMed: 9169142] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukemia." So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J., Sham M.H., Wiedemann L.M., Chan L.C. Proc. Natl. Acad. Sci. U.S.A. 94:2563-2568(1997) [PubMed: 9122235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION. Tissue: Fetal brain.
[3]	So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J., Sham M.H., Wiedemann L.M., Chan L.C. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Homo sapiens SH3-containing protein EEN gene." Chen S., Xiong H., Dong H., Lin W., Zhang C., Fu G., Qi Z., Huang G.M. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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]. Tissue: Cervix.
[6]	"The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity." Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A., Migone N., Hoffmueller U., Schneider-Mergener J., Cesareni G. J. Biol. Chem. 274:32001-32007(1999) [PubMed: 10542231] [Abstract] Cited for: INTERACTION WITH SYNJ1.
[7]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding." Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., Hill C.P. Cell 128:841-852(2007) [PubMed: 17350572] [Abstract] Cited for: INTERACTION WITH PDCD6IP.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-288, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, MASS SPECTROMETRY.
[13]	"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].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	X99656 mRNA. Translation: CAA67970.1. U65999 mRNA. Translation: AAB86800.1. AF190465 Genomic DNA. Translation: AAF04290.1. BC001270 mRNA. Translation: AAH01270.1.
RefSeq	NP_001186872.1. NM_001199943.1. NP_003016.1. NM_003025.3.
UniGene	Hs.97616.
3D structure databases
ProteinModelPortal	Q99961.
SMR	Q99961. Positions 26-247, 305-368.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99961. 14 interactions.
MINT	MINT-128645.
STRING	Q99961.
PTM databases
PhosphoSite	Q99961.
Polymorphism databases
DMDM	12643797.
2D gel databases
OGP	Q99961.
Proteomic databases
PeptideAtlas	Q99961.
PRIDE	Q99961.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000269886; ENSP00000269886; ENSG00000141985.
GeneID	6455.
KEGG	hsa:6455.
UCSC	uc002maj.1. human.
Organism-specific databases
CTD	6455.
GeneCards	GC19M004360.
H-InvDB	HIX0014664. HIX0202593.
HGNC	HGNC:10830. SH3GL1.
HPA	HPA021485.
MIM	601768. gene.
neXtProt	NX_Q99961.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG447412.
HOVERGEN	HBG052866.
InParanoid	Q99961.
OMA	IRGQVKN.
OrthoDB	EOG4C2H9V.
PhylomeDB	Q99961.
Gene expression databases
ArrayExpress	Q99961.
Bgee	Q99961.
CleanEx	HS_SH3GL1.
Genevestigator	Q99961.
GermOnline	ENSG00000141985. Homo sapiens.
Family and domain databases
InterPro	IPR004148. BAR_dom. IPR000108. p67phox. IPR001452. SH3_domain. [Graphical view]
KO	K11247.
Pfam	PF03114. BAR. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00499. P67PHOX. PR00452. SH3DOMAIN.
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	25089.
SOURCE	Search...

Entry information

Entry name

SH3G1_HUMAN

Accession

Primary (citable) accession number: Q99961
Secondary accession number(s): Q99668

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 123 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.