SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q92556

- ELMO1_HUMAN

UniProt

Q92556 - ELMO1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Engulfment and cell motility protein 1
Gene
ELMO1, KIAA0281
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 DOCK1.2 Publications

GO - Molecular functioni

  1. SH3 domain binding Source: UniProtKB
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

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

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. plasma membrane Source: UniProtKB
Complete GO annotation...

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 1
PRO_0000153712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphotyrosine; by HCK1 Publication
Modified residuei100 – 1001N6-acetyllysine1 Publication
Modified residuei105 – 1051N6-acetyllysine1 Publication
Modified residuei216 – 2161Phosphotyrosine; by HCK1 Publication
Modified residuei395 – 3951Phosphotyrosine; by HCK1 Publication
Modified residuei511 – 5111Phosphotyrosine; by HCK1 Publication
Modified residuei720 – 7201Phosphotyrosine; by HCK1 Publication

Post-translational modificationi

Phosphorylated by HCK Inferred.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).4 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

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.

Miscellaneous databases

EvolutionaryTraceiQ92556.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini319 – 492174ELMO
Add
BLAST
Domaini555 – 676122PH
Add
BLAST

Motif

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

Sequence similaritiesi

Contains 1 ELMO domain.
Contains 1 PH domain.

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.

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.
VSP_007480Add
BLAST
Alternative sequencei1 – 298298Missing in isoform 3.
VSP_038550Add
BLAST
Alternative sequencei299 – 36264VLTFN…KLGFI → MSEHQKEQTLDTPSLRTVTL TVRVHGFILEVSKTKNPPIP DTFWPPRWDHRPSPGGETNA YCQM in isoform 3.
VSP_038551Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti716 – 7161E → A in CAB66721. 1 Publication

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]
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]
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...

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 ]
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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

Similar proteinsi