Q96JJ3 (ELMO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Engulfment and cell motility protein 2

Alternative name(s):
Protein ced-12 homolog A
Short name=hCed-12A

Gene names

Name:	ELMO2
Synonyms:	CED12A, KIAA1834

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	720 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. Ref.1 Ref.2 Ref.7
Subunit structure	Interacts with the SH3-domain of DOCK1 via its SH3-binding site. Probably part of a complex with DOCK1 and RAC1. Probably part of a complex with DOCK1 and CRK isoform CRK-II. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates activation of RAC1 by EPHA2. Ref.1 Ref.7
Subcellular location	Cytoplasm. Cytoplasm › cytosol. Membrane Ref.7.
Tissue specificity	Widely expressed, with a higher expression in skeletal muscle, kidney and placenta. Ref.1
Sequence similarities	Contains 1 ELMO domain. Contains 1 PH domain.
Sequence caution	The sequence BAB13879.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB47463.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis Phagocytosis
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	SH3-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell chemotaxis Inferred from mutant phenotype Ref.7. Source: UniProtKB phagocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: InterPro cytosol Inferred from direct assay Ref.7. Source: UniProtKB membrane Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 720	720	Engulfment and cell motility protein 2		PRO_0000153714
Regions
	Domain	311 – 485	175	ELMO
	Domain	553 – 674	122	PH
	Motif	700 – 707	8	SH3-binding
Amino acid modifications
	Modified residue	48	1	Phosphotyrosine By similarity
	Modified residue	717	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	695	1	E → D. Corresponds to variant rs34630674 [ dbSNP | Ensembl ].		VAR_048928
Experimental info
	Sequence conflict	208	1	Y → C in BAB71350. Ref.4
	Sequence conflict	299	1	E → G in BAB13879. Ref.4
	Sequence conflict	509	1	R → P in BAB13879. Ref.4
	Sequence conflict	586	1	D → N in BAB14210. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q96JJ3 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: A67377E3B26F2937	FASTA	720	82,615
	10 20 30 40 50 60 MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY 70 80 90 100 110 120 ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSNMETR LDAMKELAKL SADVTFATEF 130 140 150 160 170 180 INMDGIIVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSI TFIKQIAGYV 190 200 210 220 230 240 SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN 250 260 270 280 290 300 ALFLKAPEDK RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER 310 320 330 340 350 360 MMTKMDPNDQ AQRDIIFELR RIAFDAESDP SNAPGSGTEK RKAMYTKDYK MLGFTNHINP 370 380 390 400 410 420 AMDFTQTPPG MLALDNMLYL AKVHQDTYIR IVLENSSRED KHECPFGRSA IELTKMLCEI 430 440 450 460 470 480 LQVGELPNEG RNDYHPMFFT HDRAFEELFG ICIQLLNKTW KEMRATAEDF NKVMQVVREQ 490 500 510 520 530 540 ITRALPSKPN SLDQFKSKLR SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL 550 560 570 580 590 600 IKQQRLNRLC EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLDDNPQG EVTFESLQEK 610 620 630 640 650 660 IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP NKYEYCIWID 670 680 690 700 710 720 GLSALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP EAPPPIPKEP SSYDFVYHYG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration." Gumienny T.L., Brugnera E., Tosello-Trampont A.-C., Kinchen J.M., Haney L.B., Nishiwaki K., Walk S.F., Nemergut M.E., Macara I.G., Francis R., Schedl T., Qin Y., Van Aelst L., Hengartner M.O., Ravichandran K.S. Cell 107:27-41(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH DOCK1.
[2]	"The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway." Zhou Z., Caron E., Hartwieg E., Hall A., Horvitz H.R. Dev. Cell 1:477-489(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Testis.
[3]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"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]. Tissue: Embryo, Neuroepithelioma and Teratocarcinoma.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism." Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H. J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARHGEF16; DOCK4 AND EPHA2, SUBCELLULAR LOCATION.
[8]	"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF398886 Transcribed RNA. Translation: AAL14467.1. AF417861 mRNA. Translation: AAL38512.1. AB058737 mRNA. Translation: BAB47463.1. Different initiation. AK021718 mRNA. Translation: BAB13879.1. Different initiation. AK022731 mRNA. Translation: BAB14210.1. Different initiation. AK023103 mRNA. Translation: BAB14405.1. Different initiation. AK057032 mRNA. Translation: BAB71350.1. AL133227 Genomic DNA. Translation: CAI40561.1. CH471077 Genomic DNA. Translation: EAW75739.1. CH471077 Genomic DNA. Translation: EAW75743.1. CH471077 Genomic DNA. Translation: EAW75745.1. CH471077 Genomic DNA. Translation: EAW75746.1.
IPI	IPI00940537.
RefSeq	NP_573403.1. NM_133171.3. NP_877496.1. NM_182764.1.
UniGene	Hs.210469.
3D structure databases
ProteinModelPortal	Q96JJ3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96JJ3. 1 interaction.
PTM databases
PhosphoSite	Q96JJ3.
Polymorphism databases
DMDM	30913107.
Proteomic databases
PaxDb	Q96JJ3.
PRIDE	Q96JJ3.
Protocols and materials databases
DNASU	63916.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000290246; ENSP00000290246; ENSG00000062598. ENST00000396391; ENSP00000379673; ENSG00000062598.
GeneID	63916.
KEGG	hsa:63916.
UCSC	uc002xrs.1. human.
Organism-specific databases
CTD	63916.
GeneCards	GC20M044994.
HGNC	HGNC:17233. ELMO2.
HPA	HPA018811.
MIM	606421. gene.
neXtProt	NX_Q96JJ3.
PharmGKB	PA27755.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG295208.
HOVERGEN	HBG051463.
InParanoid	Q96JJ3.
OrthoDB	EOG42RD6S.
PhylomeDB	Q96JJ3.
Gene expression databases
ArrayExpress	Q96JJ3.
Bgee	Q96JJ3.
Genevestigator	Q96JJ3.
GermOnline	ENSG00000062598. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR024574. DUF3361. IPR006816. Engulfment_cell_motility_ELMO. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
Pfam	PF11841. DUF3361. 1 hit. PF04727. ELMO_CED12. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS51335. ELMO. 1 hit. PS50003. PH_DOMAIN. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	63916.
NextBio	65636.
SOURCE	Search...

Entry information

Entry name

ELMO2_HUMAN

Accession

Primary (citable) accession number: Q96JJ3
Secondary accession number(s): E1P5T3 , Q5JVZ6, Q96CJ2, Q96ME5, Q96PA9, Q9H938, Q9H9L5, Q9HAH0, Q9NQQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 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.