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Q96JJ3

- ELMO2_HUMAN

UniProt

Q96JJ3 - ELMO2_HUMAN

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Protein
Engulfment and cell motility protein 2
Gene
ELMO2, CED12A, KIAA1834
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 DOCK1.3 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. receptor tyrosine kinase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. apoptotic process Source: UniProtKB-KW
  3. cell chemotaxis Source: UniProtKB
  4. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Phagocytosis

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Engulfment and cell motility protein 2
Alternative name(s):
Protein ced-12 homolog A
Short name:
hCed-12A
Gene namesi
Name:ELMO2
Synonyms:CED12A, KIAA1834
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:17233. ELMO2.

Subcellular locationi

Cytoplasm. Cytoplasmcytosol. Membrane 1 Publication

GO - Cellular componenti

  1. cytoskeleton Source: InterPro
  2. cytosol Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Engulfment and cell motility protein 2
PRO_0000153714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphotyrosine By similarity
Modified residuei717 – 7171Phosphotyrosine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96JJ3.
PaxDbiQ96JJ3.
PRIDEiQ96JJ3.

PTM databases

PhosphoSiteiQ96JJ3.

Expressioni

Tissue specificityi

Widely expressed, with a higher expression in skeletal muscle, kidney and placenta.1 Publication

Gene expression databases

ArrayExpressiQ96JJ3.
BgeeiQ96JJ3.
GenevestigatoriQ96JJ3.

Organism-specific databases

HPAiHPA018811.

Interactioni

Subunit structurei

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 EPHA2.2 Publications

Protein-protein interaction databases

BioGridi121987. 3 interactions.
IntActiQ96JJ3. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ96JJ3.
SMRiQ96JJ3. Positions 523-717.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini311 – 485175ELMO
Add
BLAST
Domaini553 – 674122PH
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi700 – 7078SH3-binding

Sequence similaritiesi

Contains 1 ELMO domain.
Contains 1 PH domain.

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG295208.
HOVERGENiHBG051463.
InParanoidiQ96JJ3.
OrthoDBiEOG7D85VW.
PhylomeDBiQ96JJ3.
TreeFamiTF312966.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR006816. Engulfment_cell_motility_ELMO.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51335. ELMO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96JJ3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT    50
LRYADGPQLY ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSNMETR 100
LDAMKELAKL SADVTFATEF INMDGIIVLT RLVESGTKLL SHYSEMLAFT 150
LTAFLELMDH GIVSWDMVSI TFIKQIAGYV SQPMVDVSIL QRSLAILESM 200
VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN ALFLKAPEDK 250
RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER 300
MMTKMDPNDQ AQRDIIFELR RIAFDAESDP SNAPGSGTEK RKAMYTKDYK 350
MLGFTNHINP AMDFTQTPPG MLALDNMLYL AKVHQDTYIR IVLENSSRED 400
KHECPFGRSA IELTKMLCEI LQVGELPNEG RNDYHPMFFT HDRAFEELFG 450
ICIQLLNKTW KEMRATAEDF NKVMQVVREQ ITRALPSKPN SLDQFKSKLR 500
SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL IKQQRLNRLC 550
EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLDDNPQG EVTFESLQEK 600
IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP 650
NKYEYCIWID GLSALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP 700
EAPPPIPKEP SSYDFVYHYG 720
Length:720
Mass (Da):82,615
Last modified:May 16, 2003 - v2
Checksum:iA67377E3B26F2937
GO
Isoform 2 (identifier: Q96JJ3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.

Note: No experimental confirmation available.

Show »
Length:632
Mass (Da):72,798
Checksum:i066EE50A3A2B358A
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti695 – 6951E → D.
Corresponds to variant rs34630674 [ dbSNP | Ensembl ].
VAR_048928

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8888Missing in isoform 2.
VSP_055477Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081Y → C in BAB71350. 1 Publication
Sequence conflicti299 – 2991E → G in BAB13879. 1 Publication
Sequence conflicti509 – 5091R → P in BAB13879. 1 Publication
Sequence conflicti586 – 5861D → N in BAB14210. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
AL031686 Genomic DNA. No translation available.
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.
BC000143 mRNA. Translation: AAH00143.2.
CCDSiCCDS13398.1.
RefSeqiNP_573403.1. NM_133171.3.
NP_877496.1. NM_182764.1.
XP_005260553.1. XM_005260496.1.
XP_006723917.1. XM_006723854.1.
UniGeneiHs.210469.

Genome annotation databases

EnsembliENST00000290246; ENSP00000290246; ENSG00000062598.
ENST00000372176; ENSP00000361249; ENSG00000062598.
ENST00000396391; ENSP00000379673; ENSG00000062598.
GeneIDi63916.
KEGGihsa:63916.
UCSCiuc002xrs.1. human.

Polymorphism databases

DMDMi30913107.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
AL031686 Genomic DNA. No translation available.
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 .
BC000143 mRNA. Translation: AAH00143.2 .
CCDSi CCDS13398.1.
RefSeqi NP_573403.1. NM_133171.3.
NP_877496.1. NM_182764.1.
XP_005260553.1. XM_005260496.1.
XP_006723917.1. XM_006723854.1.
UniGenei Hs.210469.

3D structure databases

ProteinModelPortali Q96JJ3.
SMRi Q96JJ3. Positions 523-717.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121987. 3 interactions.
IntActi Q96JJ3. 1 interaction.

PTM databases

PhosphoSitei Q96JJ3.

Polymorphism databases

DMDMi 30913107.

Proteomic databases

MaxQBi Q96JJ3.
PaxDbi Q96JJ3.
PRIDEi Q96JJ3.

Protocols and materials databases

DNASUi 63916.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290246 ; ENSP00000290246 ; ENSG00000062598 .
ENST00000372176 ; ENSP00000361249 ; ENSG00000062598 .
ENST00000396391 ; ENSP00000379673 ; ENSG00000062598 .
GeneIDi 63916.
KEGGi hsa:63916.
UCSCi uc002xrs.1. human.

Organism-specific databases

CTDi 63916.
GeneCardsi GC20M044994.
HGNCi HGNC:17233. ELMO2.
HPAi HPA018811.
MIMi 606421. gene.
neXtProti NX_Q96JJ3.
PharmGKBi PA27755.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295208.
HOVERGENi HBG051463.
InParanoidi Q96JJ3.
OrthoDBi EOG7D85VW.
PhylomeDBi Q96JJ3.
TreeFami TF312966.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

GeneWikii ELMO2.
GenomeRNAii 63916.
NextBioi 65636.
PROi Q96JJ3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96JJ3.
Bgeei Q96JJ3.
Genevestigatori Q96JJ3.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR006816. Engulfment_cell_motility_ELMO.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS51335. ELMO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORM 1).
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cervix.
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiELMO2_HUMAN
AccessioniPrimary (citable) accession number: Q96JJ3
Secondary accession number(s): E1P5T3
, Q5JVZ6, Q7Z5G9, Q96CJ2, Q96ME5, Q96PA9, Q9H938, Q9H9L5, Q9HAH0, Q9NQQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: September 3, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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