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UniProtKB/Swiss-Prot entry Q92556


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ELMO1_HUMAN
Primary accession number Q92556
Secondary accession numbers Q29R79 Q96PB0 Q9H0I1
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 16, 2003 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 80)
Name and origin of the protein
Protein name Engulfment and cell motility protein 1
Synonym CED-12 homolog
Gene name
Name: ELMO1
Synonyms: KIAA0281
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH DOCK1, AND SUBUNIT OF A COMPLEX WITH DOCK1 AND CRK.
DOI=10.1016/S0092-8674(01)00520-7; PubMed=11595183 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration.";
Cell 107:27-41(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1093/dnares/4.1.53; PubMed=9179496 [NCBI, ExPASy, EBI, Israel, Japan]
Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.;
"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins.";
DNA Res. 4:53-59(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Lung, and Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION.
DOI=10.1074/jbc.M202783200; PubMed=12029088 [NCBI, ExPASy, EBI, Israel, Japan]
Scott M.P., Zappacosta F., Kim E.Y., Annan R.S., Miller W.T.;
"Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1.";
J. Biol. Chem. 277:28238-28246(2002).
[6]
FUNCTION, INTERACTION WITH DOCK1, AND SUBUNIT OF A COMPLEX CONTAINING RAC1 AND DOCK1.
DOI=10.1038/ncb824; PubMed=12134158 [NCBI, ExPASy, EBI, Israel, Japan]
Brugnera E., Haney L., Grimsley C., Lu M., Walk S.F., Tosello-Trampont A.-C., Macara I.G., Madhani H., Fink G.R., Ravichandran K.S.;
"Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex.";
Nat. Cell Biol. 4:574-582(2002).
[7]
INTERACTION WITH PLEKHG6.
DOI=10.1091/mbc.E06-12-1144; PubMed=17881735 [NCBI, ExPASy, EBI, Israel, Japan]
D'Angelo R., Aresta S., Blangy A., Del Maestro L., Louvard D., Arpin M.;
"Interaction of ezrin with the novel guanine nucleotide exchange factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in epithelial cells.";
Mol. Biol. Cell 18:4780-4793(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF398885; AAL14466.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D87457; BAA13397.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136787; CAB66721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003051; AAH03051.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064635; AAH64635.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC077074; AAH77074.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114341; AAI14342.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001034548.1; -.
NP_055615.8; -.
NP_569709.1; -.
UniGene Hs.656638
3D structure databases
ModBase Q92556.
Protein-protein interaction databases
IntAct Q92556; -.
PTM databases
PhosphoSite Q92556; -.
Enzyme and pathway databases
Reactome REACT_6185; HIV Infection.
Organism-specific databases
H-InvDB HIX0020858; -.
HGNC HGNC:16286; ELMO1.
GeneLynx ELMO1; Homo sapiens.
GenAtlas ELMO1.
MIM 606420; gene. [NCBI / EBI]
PharmGKB PA27754; -.
GeneCards Q92556.
HUGE KIAA0281.
Gene expression databases
ArrayExpress Q92556; -.
CleanEx HS_ELMO1; -.
GermOnline ENSG00000155849; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0017124; Molecular function: SH3 domain binding (inferred from physical interaction from UniProtKB).
GO:0030036; Biological process: actin cytoskeleton organization and biogenesis (inferred from genetic interaction from UniProtKB).
GO:0006915; Biological process: apoptosis (non-traceable author statement from UniProtKB).
GO:0006928; Biological process: cell motility (inferred from genetic interaction from UniProtKB).
GO:0006911; Biological process: phagocytosis, engulfment (inferred from genetic interaction from UniProtKB).
GO:0016601; Biological process: Rac protein signal transduction (inferred from genetic interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006816; ELM.
IPR001849; PH.
IPR011993; PH_type.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
Pfam PF04727; ELMO_CED12; 1.
Pfam graphical view of domain structure.
SMART SM00233; PH; 1.
SMART graphical view of domain structure.
PROSITE PS51335; ELMO; 1.
PS50003; PH_DOMAIN; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q92556.
Proteomic databases
PeptideAtlas Q92556; -.
Genome annotation databases
Ensembl ENSG00000155849; Homo sapiens. [Contig view]
GeneID 9844; -.
KEGG hsa:9844; -.
Phylogenomic databases
HOGENOM Q92556; -.
HOVERGEN Q92556; -.
Other
SOURCE ELMO1; Homo sapiens.
ProtoNet Q92556.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Apoptosis; Cytoplasm; Membrane; Phagocytosis; Phosphoprotein; SH3-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   727  727     Engulfment and cell motility protein 1. PRO_0000153712
DOMAIN   319   492  174     ELMO. 
DOMAIN   555   676  122     PH. 
MOTIF   707   714  8     SH3-binding. 
VAR_SEQ   1   480        Missing (in isoform 2). VSP_007480
CONFLICT   716   716        E -> A (in Ref. 3; CAB66721). 
Sequence information
Length: 727 AA [This is the length of the unprocessed precursor] Molecular weight: 83829 Da [This is the MW of the unprocessed precursor] CRC64: 053DCA73D2B0A4C6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPPPADIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY 

        70         80         90        100        110        120 
ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF 

       130        140        150        160        170        180 
INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF 

       190        200        210        220        230        240 
IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGSDQEIQ 

       250        260        270        280        290        300 
TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRSIILTHVI RAQRAINNEM AHQLYVLQVL 

       310        320        330        340        350        360 
TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG 

       370        380        390        400        410        420 
FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL 

       430        440        450        460        470        480 
TKMLCEILKV GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV 

       490        500        510        520        530        540 
MQVVKEQVMR ALTTKPSSLD QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI 

       550        560        570        580        590        600 
QPEILELIKQ QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP 

       610        620        630        640        650        660 
HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH 

       670        680        690        700        710        720 
EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY 


DFVYDCN 

Q92556 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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