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Q92556

- ELMO1_HUMAN

UniProt

Q92556 - ELMO1_HUMAN

Protein

Engulfment and cell motility protein 1

Gene

ELMO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
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    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 DOCK1.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. cellular component movement Source: UniProtKB
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. innate immune response Source: Reactome
    6. phagocytosis, engulfment Source: UniProtKB
    7. Rac protein signal transduction Source: UniProtKB
    8. regulation of defense response to virus by virus Source: Reactome
    9. viral process Source: Reactome

    Keywords - Biological processi

    Apoptosis, Phagocytosis

    Enzyme and pathway databases

    ReactomeiREACT_11068. Nef and signal transduction.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Engulfment and cell motility protein 1
    Alternative name(s):
    Protein ced-12 homolog
    Gene namesi
    Name:ELMO1
    Synonyms:KIAA0281
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:16286. ELMO1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: InterPro
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27754.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 727727Engulfment and cell motility protein 1PRO_0000153712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphotyrosine; by HCK2 Publications
    Modified residuei100 – 1001N6-acetyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei216 – 2161Phosphotyrosine; by HCK2 Publications
    Modified residuei395 – 3951Phosphotyrosine; by HCK2 Publications
    Modified residuei511 – 5111Phosphotyrosine; by HCK2 Publications
    Modified residuei720 – 7201Phosphotyrosine; by HCK2 Publications

    Post-translational modificationi

    Phosphorylated by HCK.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92556.
    PaxDbiQ92556.
    PeptideAtlasiQ92556.
    PRIDEiQ92556.

    PTM databases

    PhosphoSiteiQ92556.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ92556.
    BgeeiQ92556.
    CleanExiHS_ELMO1.
    GenevestigatoriQ92556.

    Organism-specific databases

    HPAiHPA017941.

    Interactioni

    Subunit structurei

    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).By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DOCK1Q1418516EBI-346417,EBI-446740
    HCKP086314EBI-346417,EBI-346340
    RHOGP840953EBI-346417,EBI-446579

    Protein-protein interaction databases

    BioGridi115180. 5 interactions.
    DIPiDIP-31095N.
    IntActiQ92556. 5 interactions.
    MINTiMINT-238417.
    STRINGi9606.ENSP00000312185.

    Structurei

    Secondary structure

    1
    727
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi532 – 55827
    Beta strandi560 – 5634
    Beta strandi569 – 5713
    Beta strandi573 – 5797
    Beta strandi583 – 5908
    Beta strandi607 – 6093
    Helixi610 – 6123
    Beta strandi613 – 6186
    Helixi619 – 6213
    Helixi623 – 6253
    Helixi638 – 6403
    Beta strandi641 – 6466
    Turni647 – 6493
    Beta strandi650 – 6556
    Helixi659 – 67214
    Helixi680 – 69718
    Helixi699 – 7013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RQRNMR-A697-722[»]
    2VSZX-ray2.30A/B532-675[»]
    3A98X-ray2.10B/D532-727[»]
    ProteinModelPortaliQ92556.
    SMRiQ92556. Positions 530-727.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92556.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini319 – 492174ELMOPROSITE-ProRule annotationAdd
    BLAST
    Domaini555 – 676122PHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi707 – 7148SH3-binding

    Sequence similaritiesi

    Contains 1 ELMO domain.PROSITE-ProRule annotation
    Contains 1 PH domain.Curated

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG295208.
    HOGENOMiHOG000230985.
    HOVERGENiHBG055277.
    InParanoidiQ92556.
    KOiK12366.
    OMAiKPAICIF.
    OrthoDBiEOG7D85VW.
    PhylomeDBiQ92556.
    TreeFamiTF312966.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    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. 2 hits.
    PROSITEiPS51335. ELMO. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92556-1) [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

    MPPPADIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA    50
    LQHADSSNFY ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK 100
    LEALKDLASL SRDVTFAQEF INLDGISLLT QMVESGTERY QKLQKIMKPC 150
    FGDMLSFTLT AFVELMDHGI VSWDTFSVAF IKKIASFVNK SAIDISILQR 200
    SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGSDQEIQ TYTIAVINAL 250
    FLKAPDERRQ EMANILAQKQ LRSIILTHVI RAQRAINNEM AHQLYVLQVL 300
    TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS 350
    MYTRDYKKLG FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL 400
    ENSSREDKHE CPFGRSSIEL TKMLCEILKV GELPSETCND FHPMFFTHDR 450
    SFEEFFCICI QLLNKTWKEM RATSEDFNKV MQVVKEQVMR ALTTKPSSLD 500
    QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI QPEILELIKQ 550
    QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP 600
    HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC 650
    QLNFIAPDKH EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD 700
    LENIQIPDAP PPIPKEPSNY DFVYDCN 727
    Length:727
    Mass (Da):83,829
    Last modified:May 16, 2003 - v2
    Checksum:i053DCA73D2B0A4C6
    GO
    Isoform 2 (identifier: Q92556-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-480: Missing.

    Show »
    Length:247
    Mass (Da):28,742
    Checksum:iD02BCEC8D8A4383F
    GO
    Isoform 3 (identifier: Q92556-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:429
    Mass (Da):49,915
    Checksum:i36C411CBBE5CA12B
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti716 – 7161E → A in CAB66721. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti362 – 3621I → S.1 Publication
    VAR_065824

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 480480Missing in isoform 2. 2 PublicationsVSP_007480Add
    BLAST
    Alternative sequencei1 – 298298Missing in isoform 3. 1 PublicationVSP_038550Add
    BLAST
    Alternative sequencei299 – 36264VLTFN…KLGFI → MSEHQKEQTLDTPSLRTVTL TVRVHGFILEVSKTKNPPIP DTFWPPRWDHRPSPGGETNA YCQM in isoform 3. 1 PublicationVSP_038551Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS5449.1. [Q92556-1]
    CCDS5450.1. [Q92556-2]
    RefSeqiNP_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]
    UniGeneiHs.434989.
    Hs.656638.

    Genome annotation databases

    EnsembliENST00000310758; ENSP00000312185; ENSG00000155849. [Q92556-1]
    ENST00000396040; ENSP00000379355; ENSG00000155849. [Q92556-2]
    ENST00000396045; ENSP00000379360; ENSG00000155849. [Q92556-2]
    ENST00000442504; ENSP00000406952; ENSG00000155849. [Q92556-1]
    ENST00000448602; ENSP00000394458; ENSG00000155849. [Q92556-1]
    GeneIDi9844.
    KEGGihsa:9844.
    UCSCiuc003tfi.2. human. [Q92556-2]
    uc003tfk.2. human. [Q92556-1]

    Polymorphism databases

    DMDMi30923321.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS5449.1. [Q92556-1 ]
    CCDS5450.1. [Q92556-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.434989.
    Hs.656638.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RQR NMR - A 697-722 [» ]
    2VSZ X-ray 2.30 A/B 532-675 [» ]
    3A98 X-ray 2.10 B/D 532-727 [» ]
    ProteinModelPortali Q92556.
    SMRi Q92556. Positions 530-727.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115180. 5 interactions.
    DIPi DIP-31095N.
    IntActi Q92556. 5 interactions.
    MINTi MINT-238417.
    STRINGi 9606.ENSP00000312185.

    PTM databases

    PhosphoSitei Q92556.

    Polymorphism databases

    DMDMi 30923321.

    Proteomic databases

    MaxQBi Q92556.
    PaxDbi Q92556.
    PeptideAtlasi Q92556.
    PRIDEi Q92556.

    Protocols and materials databases

    DNASUi 9844.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310758 ; ENSP00000312185 ; ENSG00000155849 . [Q92556-1 ]
    ENST00000396040 ; ENSP00000379355 ; ENSG00000155849 . [Q92556-2 ]
    ENST00000396045 ; ENSP00000379360 ; ENSG00000155849 . [Q92556-2 ]
    ENST00000442504 ; ENSP00000406952 ; ENSG00000155849 . [Q92556-1 ]
    ENST00000448602 ; ENSP00000394458 ; ENSG00000155849 . [Q92556-1 ]
    GeneIDi 9844.
    KEGGi hsa:9844.
    UCSCi uc003tfi.2. human. [Q92556-2 ]
    uc003tfk.2. human. [Q92556-1 ]

    Organism-specific databases

    CTDi 9844.
    GeneCardsi GC07M036860.
    HGNCi HGNC:16286. ELMO1.
    HPAi HPA017941.
    MIMi 606420. gene.
    neXtProti NX_Q92556.
    PharmGKBi PA27754.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295208.
    HOGENOMi HOG000230985.
    HOVERGENi HBG055277.
    InParanoidi Q92556.
    KOi K12366.
    OMAi KPAICIF.
    OrthoDBi EOG7D85VW.
    PhylomeDBi Q92556.
    TreeFami TF312966.

    Enzyme and pathway databases

    Reactomei REACT_11068. Nef and signal transduction.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi ELMO1. human.
    EvolutionaryTracei Q92556.
    GeneWikii ELMO1.
    GenomeRNAii 9844.
    NextBioi 37098.
    PROi Q92556.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92556.
    Bgeei Q92556.
    CleanExi HS_ELMO1.
    Genevestigatori Q92556.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    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. 2 hits.
    PROSITEi PS51335. ELMO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. 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.
      , 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. 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiELMO1_HUMAN
    AccessioniPrimary (citable) accession number: Q92556
    Secondary accession number(s): A4D1X6
    , Q29R79, Q6ZTJ0, Q96PB0, Q9H0I1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 140 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3