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Q96JJ3 (ELMO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Cytoplasmcytosol. 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Engulfment and cell motility protein 2
PRO_0000153714

Regions

Domain311 – 485175ELMO
Domain553 – 674122PH
Motif700 – 7078SH3-binding

Amino acid modifications

Modified residue481Phosphotyrosine By similarity
Modified residue7171Phosphotyrosine By similarity

Natural variations

Natural variant6951E → D.
Corresponds to variant rs34630674 [ dbSNP | Ensembl ].
VAR_048928

Experimental info

Sequence conflict2081Y → C in BAB71350. Ref.4
Sequence conflict2991E → G in BAB13879. Ref.4
Sequence conflict5091R → P in BAB13879. Ref.4
Sequence conflict5861D → N in BAB14210. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q96JJ3 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: A67377E3B26F2937

FASTA72082,615
        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 

« Hide

References

« Hide '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. 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].
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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_573403.1. NM_133171.3.
NP_877496.1. NM_182764.1.
XP_005260553.1. XM_005260496.1.
UniGeneHs.210469.

3D structure databases

ProteinModelPortalQ96JJ3.
SMRQ96JJ3. Positions 523-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121987. 3 interactions.
IntActQ96JJ3. 1 interaction.

PTM databases

PhosphoSiteQ96JJ3.

Polymorphism databases

DMDM30913107.

Proteomic databases

PaxDbQ96JJ3.
PRIDEQ96JJ3.

Protocols and materials databases

DNASU63916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290246; ENSP00000290246; ENSG00000062598.
ENST00000396391; ENSP00000379673; ENSG00000062598.
GeneID63916.
KEGGhsa:63916.
UCSCuc002xrs.1. human.

Organism-specific databases

CTD63916.
GeneCardsGC20M044994.
HGNCHGNC:17233. ELMO2.
HPAHPA018811.
MIM606421. gene.
neXtProtNX_Q96JJ3.
PharmGKBPA27755.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295208.
HOVERGENHBG051463.
InParanoidQ96JJ3.
OrthoDBEOG7D85VW.
PhylomeDBQ96JJ3.
TreeFamTF312966.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ96JJ3.
BgeeQ96JJ3.
GenevestigatorQ96JJ3.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR006816. Engulfment_cell_motility_ELMO.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS51335. ELMO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiELMO2.
GenomeRNAi63916.
NextBio65636.
PROQ96JJ3.
SOURCESearch...

Entry information

Entry nameELMO2_HUMAN
AccessionPrimary (citable) accession number: Q96JJ3
Secondary accession number(s): E1P5T3 expand/collapse secondary AC list , 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: April 16, 2014
This is version 118 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM