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Q92556 (ELMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Engulfment and cell motility protein 1
Alternative name(s):
Protein ced-12 homolog
Gene names
Name:ELMO1
Synonyms:KIAA0281
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length727 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.9

Subunit structure

Interacts with BAI1 By similarity. Interacts directly with the SH3-domain of DOCK1 via its SH3-binding site. Part of a complex with DOCK1 and RAC1. Part of a complex with DOCK1 and CRK isoform CRK-II Interacts with PLEKHG6. Interacts with HCK (via SH3 domain). Ref.1 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Cell membrane. Note: Translocation to plasma membrane seems to be mediated by DOCK1 and CRK.

Tissue specificity

Widely expressed, with a higher expression in the spleen and placenta.

Post-translational modification

Phosphorylated by HCK Probable. Ref.8 Ref.10

Sequence similarities

Contains 1 ELMO domain.

Contains 1 PH domain.

Sequence caution

The sequence BAA13397.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Phagocytosis
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

Rac protein signal transduction

Inferred from genetic interaction Ref.1. Source: UniProtKB

actin cytoskeleton organization

Inferred from genetic interaction Ref.1. Source: UniProtKB

apoptotic process

Non-traceable author statement Ref.1. Source: UniProtKB

cellular component movement

Inferred from genetic interaction Ref.1. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

phagocytosis, engulfment

Inferred from genetic interaction Ref.1. Source: UniProtKB

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: InterPro

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9PubMed 12879077PubMed 15247908PubMed 15723800PubMed 18768751. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92556-1)

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.
Isoform 2 (identifier: Q92556-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-480: Missing.
Isoform 3 (identifier: Q92556-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-298: Missing.
     299-362: VLTFNLLEDR...TRDYKKLGFI → MSEHQKEQTL...GGETNAYCQM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 727727Engulfment and cell motility protein 1
PRO_0000153712

Regions

Domain319 – 492174ELMO
Domain555 – 676122PH
Motif707 – 7148SH3-binding

Amino acid modifications

Modified residue181Phosphotyrosine; by HCK Ref.10
Modified residue1001N6-acetyllysine Ref.13
Modified residue1051N6-acetyllysine Ref.13
Modified residue2161Phosphotyrosine; by HCK Ref.10
Modified residue3951Phosphotyrosine; by HCK Ref.10
Modified residue5111Phosphotyrosine; by HCK Ref.10
Modified residue7201Phosphotyrosine; by HCK Ref.10

Natural variations

Alternative sequence1 – 480480Missing in isoform 2.
VSP_007480
Alternative sequence1 – 298298Missing in isoform 3.
VSP_038550
Alternative sequence299 – 36264VLTFN…KLGFI → MSEHQKEQTLDTPSLRTVTL TVRVHGFILEVSKTKNPPIP DTFWPPRWDHRPSPGGETNA YCQM in isoform 3.
VSP_038551
Natural variant3621I → S. Ref.15
VAR_065824

Experimental info

Sequence conflict7161E → A in CAB66721. Ref.3

Secondary structure

............................. 727
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: 053DCA73D2B0A4C6

FASTA72783,829
        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 

« Hide

Isoform 2 [UniParc].

Checksum: D02BCEC8D8A4383F
Show »

FASTA24728,742
Isoform 3 [UniParc].

Checksum: 36C411CBBE5CA12B
Show »

FASTA42949,915

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] (ISOFORM 1), FUNCTION, INTERACTION WITH DOCK1, SUBUNIT OF A COMPLEX WITH DOCK1 AND CRK.
[2]"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[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] (ISOFORM 3).
Tissue: Urinary bladder.
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 2).
Tissue: Brain, Lung and Pancreas.
[8]"Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1."
Scott M.P., Zappacosta F., Kim E.Y., Annan R.S., Miller W.T.
J. Biol. Chem. 277:28238-28246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[9]"Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex."
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.
Nat. Cell Biol. 4:574-582(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DOCK1, SUBUNIT OF A COMPLEX CONTAINING RAC1 AND DOCK1.
[10]"Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck."
Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S., Ravichandran K.S., Miller W.T.
Biochemistry 44:8841-8849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCK, PHOSPHORYLATION AT TYR-18; TYR-216; TYR-395; TYR-511 AND TYR-720.
[11]"Interaction of ezrin with the novel guanine nucleotide exchange factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in epithelial cells."
D'Angelo R., Aresta S., Blangy A., Del Maestro L., Louvard D., Arpin M.
Mol. Biol. Cell 18:4780-4793(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEKHG6.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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].
[15]"BMPER mutation in diaphanospondylodysostosis identified by ancestral autozygosity mapping and targeted high-throughput sequencing."
Funari V.A., Krakow D., Nevarez L., Chen Z., Funari T.L., Vatanavicharn N., Wilcox W.R., Rimoin D.L., Nelson S.F., Cohn D.H.
Am. J. Hum. Genet. 87:532-537(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-362.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF398885 mRNA. Translation: AAL14466.1.
D87457 mRNA. Translation: BAA13397.2. Different initiation.
AL136787 mRNA. Translation: CAB66721.1.
AK126565 mRNA. Translation: BAC86597.1.
CH236951 Genomic DNA. Translation: EAL23979.1.
CH471073 Genomic DNA. Translation: EAW94076.1.
BC003051 mRNA. Translation: AAH03051.1.
BC064635 mRNA. Translation: AAH64635.1.
BC077074 mRNA. Translation: AAH77074.1.
BC114341 mRNA. Translation: AAI14342.1.
CCDSCCDS5449.1. [Q92556-1]
CCDS5450.1. [Q92556-2]
RefSeqNP_001034548.1. NM_001039459.2. [Q92556-2]
NP_001193409.1. NM_001206480.2. [Q92556-1]
NP_001193411.1. NM_001206482.1. [Q92556-1]
NP_055615.8. NM_014800.10. [Q92556-1]
NP_569709.1. NM_130442.3. [Q92556-2]
XP_005249976.1. XM_005249919.1. [Q92556-1]
XP_005249977.1. XM_005249920.1. [Q92556-1]
XP_006715868.1. XM_006715805.1. [Q92556-1]
UniGeneHs.434989.
Hs.656638.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQRNMR-A697-722[»]
2VSZX-ray2.30A/B532-675[»]
3A98X-ray2.10B/D532-727[»]
ProteinModelPortalQ92556.
SMRQ92556. Positions 530-727.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115180. 5 interactions.
DIPDIP-31095N.
IntActQ92556. 5 interactions.
MINTMINT-238417.
STRING9606.ENSP00000312185.

PTM databases

PhosphoSiteQ92556.

Polymorphism databases

DMDM30923321.

Proteomic databases

MaxQBQ92556.
PaxDbQ92556.
PeptideAtlasQ92556.
PRIDEQ92556.

Protocols and materials databases

DNASU9844.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310758; ENSP00000312185; ENSG00000155849. [Q92556-1]
ENST00000341056; ENSP00000342142; ENSG00000155849. [Q92556-3]
ENST00000396040; ENSP00000379355; ENSG00000155849. [Q92556-2]
ENST00000396045; ENSP00000379360; ENSG00000155849. [Q92556-2]
ENST00000442504; ENSP00000406952; ENSG00000155849. [Q92556-1]
ENST00000448602; ENSP00000394458; ENSG00000155849. [Q92556-1]
GeneID9844.
KEGGhsa:9844.
UCSCuc003tfi.2. human. [Q92556-2]
uc003tfk.2. human. [Q92556-1]

Organism-specific databases

CTD9844.
GeneCardsGC07M036860.
HGNCHGNC:16286. ELMO1.
HPAHPA017941.
MIM606420. gene.
neXtProtNX_Q92556.
PharmGKBPA27754.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295208.
HOGENOMHOG000230985.
HOVERGENHBG055277.
InParanoidQ92556.
KOK12366.
OMAKPAICIF.
OrthoDBEOG7D85VW.
PhylomeDBQ92556.
TreeFamTF312966.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ92556.
BgeeQ92556.
CleanExHS_ELMO1.
GenevestigatorQ92556.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
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. 2 hits.
PROSITEPS51335. ELMO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSELMO1. human.
EvolutionaryTraceQ92556.
GeneWikiELMO1.
GenomeRNAi9844.
NextBio37098.
PROQ92556.
SOURCESearch...

Entry information

Entry nameELMO1_HUMAN
AccessionPrimary (citable) accession number: Q92556
Secondary accession number(s): A4D1X6 expand/collapse secondary AC list , Q29R79, Q6ZTJ0, Q96PB0, Q9H0I1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2003
Last modified: July 9, 2014
This is version 138 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 7

Human chromosome 7: entries, gene names and cross-references to MIM