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Q8BHL5

- ELMO2_MOUSE

UniProt

Q8BHL5 - ELMO2_MOUSE

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Protein

Engulfment and cell motility protein 2

Gene

Elmo2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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 (By similarity).By similarity

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell chemotaxis Source: UniProtKB
  3. phagocytosis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Phagocytosis

Enzyme and pathway databases

ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_257088. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Engulfment and cell motility protein 2
Alternative name(s):
Protein ced-12 homolog A
Gene namesi
Name:Elmo2
Synonyms:Kiaa1834
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2153045. Elmo2.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytosol By similarity. Membrane By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Engulfment and cell motility protein 2PRO_0000153715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphotyrosine2 Publications
Modified residuei729 – 7291Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BHL5.
PaxDbiQ8BHL5.
PRIDEiQ8BHL5.

PTM databases

PhosphoSiteiQ8BHL5.

Expressioni

Gene expression databases

BgeeiQ8BHL5.
ExpressionAtlasiQ8BHL5. baseline and differential.
GenevestigatoriQ8BHL5.

Interactioni

Subunit structurei

Interacts directly with the SH3-domain of DOCK1 via its SH3-binding site. Probably forms a heterotrimeric complex with DOCK1 and RAC1. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates activation of RAC1 by EPHA2 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8BHL5. 2 interactions.
MINTiMINT-270694.

Structurei

3D structure databases

ProteinModelPortaliQ8BHL5.
SMRiQ8BHL5. Positions 189-238, 535-729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini323 – 497175ELMOPROSITE-ProRule annotationAdd
BLAST
Domaini565 – 686122PHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi712 – 7198SH3-binding

Sequence similaritiesi

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

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG295208.
GeneTreeiENSGT00390000014155.
HOVERGENiHBG051463.
InParanoidiQ8BHL5.
OMAiYLAKFHQ.
OrthoDBiEOG7D85VW.
PhylomeDBiQ8BHL5.
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.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
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: Q8BHL5-1) [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

        10         20         30         40         50
MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT
60 70 80 90 100
LRYADGPQLY VTEQTRNDIK NGTILQLAVS PSRAARQLME RTQSSSMETR
110 120 130 140 150
LDAMKELAKL SADVTFATEF INMDGIIVLT RLVESGTKLL SHYSEMLAFT
160 170 180 190 200
LTAFLELMDH GIVSWDMVSV TFIKQIAGYV SQPMVDVSIL QRSLAILESM
210 220 230 240 250
VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN ALFLKAPEDK
260 270 280 290 300
RQDKHLNPLD LPVTDMANAF AQKHLRSIIL NHVIRGNRPI KTEMAHQLYV
310 320 330 340 350
LQVLTFNLLE ERMMTKMDPN DQAQRDIIFE LRRIAFDAES DPSNVPGSGT
360 370 380 390 400
EKRKAMYTKD YKMLGFTNHI NPALDFTQTP PGMLALDNML YLAKVHQDTY
410 420 430 440 450
IRIVLENSSR EDKHECPFGR SAIELTKMLC EILQVGELPN EGRNDYHPMF
460 470 480 490 500
FTHDRAFEEL FGICIQLLNK TWKEMRATAE DFNKVMQVVR EQITRALPSK
510 520 530 540 550
PNSLDQFKSK LRSLSYSEIL RLRQSERMSQ DDFQSPPIVE LREKIQPEIL
560 570 580 590 600
ELIKQQRLNR LCEGSSFRKI GNRRRQERFW HCRLALNHKV LHYGDLDDNP
610 620 630 640 650
QGEVTFESLQ EKIPVADIKA IVTGKDCPHM KEKSALKQNK EVLELAFSIL
660 670 680 690 700
YDPDETLNFI APNKYEYCIW IDGLSALLGK DMSSELTKSD LDTLLSMEMK
710 720 730
LRLLDLENIQ IPEAPPPVPK EPSSYDFVYH YG
Length:732
Mass (Da):83,887
Last modified:March 1, 2003 - v1
Checksum:i087A80728DC43A23
GO
Isoform 2 (identifier: Q8BHL5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     253-264: Missing.

Show »
Length:720
Mass (Da):82,543
Checksum:i04C6F4357F82F1F9
GO
Isoform 3 (identifier: Q8BHL5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     253-264: Missing.
     667-732: YCIWIDGLSA...SSYDFVYHYG → VSSVPHCLEH...PLLTRDSQFT

Note: No experimental confirmation available.

Show »
Length:798
Mass (Da):91,251
Checksum:i93E26AA789067C39
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021D → G in BAC28514. (PubMed:16141072)Curated
Sequence conflicti143 – 1442Missing in AAL14465. (PubMed:11595183)Curated
Sequence conflicti519 – 5235ILRLR → NSAVA in BAC29162. (PubMed:16141072)Curated
Sequence conflicti613 – 6131I → V in BAC41483. (PubMed:12465718)Curated
Sequence conflicti682 – 6821M → I in BAC34424. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei253 – 26412Missing in isoform 2 and isoform 3. 2 PublicationsVSP_007488Add
BLAST
Alternative sequencei667 – 73266YCIWI…VYHYG → VSSVPHCLEHQCPHCEEVSV PHCLEHQCSHCEEVWPAQRY PHKPGSQNGSLSLWTFYHWA GLPTSHRGLSSSAFRGLGLE LCATTPNLSLCALEQLAWHR EGFPLCNLAVTFPRRVESQL PGANLVRLWSQMDLPLLTRD SQFT in isoform 3. 1 PublicationVSP_007489Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398884 mRNA. Translation: AAL14465.1.
AK004448 mRNA. Translation: BAB23307.1.
AK032033 mRNA. Translation: BAC27662.1.
AK033918 mRNA. Translation: BAC28514.1.
AK035710 mRNA. Translation: BAC29162.1.
AK038455 mRNA. Translation: BAC30007.1.
AK045428 mRNA. Translation: BAC32361.1.
AK047040 mRNA. Translation: BAC32945.1.
AK050823 mRNA. Translation: BAC34424.1.
AK053574 mRNA. Translation: BAC35433.1.
AL591430 Genomic DNA. Translation: CAI51618.2.
AL591430 Genomic DNA. Translation: CAM23849.1.
BC023954 mRNA. Translation: AAH23954.1.
AB093301 Transcribed RNA. Translation: BAC41483.3.
CCDSiCCDS17075.1. [Q8BHL5-2]
CCDS17076.1. [Q8BHL5-1]
CCDS17077.1. [Q8BHL5-3]
RefSeqiNP_525026.2. NM_080287.2. [Q8BHL5-2]
NP_997588.1. NM_207705.1. [Q8BHL5-3]
NP_997589.1. NM_207706.1. [Q8BHL5-1]
XP_006498804.1. XM_006498741.1. [Q8BHL5-3]
XP_006498805.1. XM_006498742.1. [Q8BHL5-3]
XP_006498808.1. XM_006498745.1. [Q8BHL5-2]
UniGeneiMm.35064.

Genome annotation databases

EnsembliENSMUST00000071699; ENSMUSP00000071619; ENSMUSG00000017670. [Q8BHL5-3]
ENSMUST00000074046; ENSMUSP00000073691; ENSMUSG00000017670. [Q8BHL5-1]
ENSMUST00000094329; ENSMUSP00000091887; ENSMUSG00000017670. [Q8BHL5-2]
ENSMUST00000103088; ENSMUSP00000099377; ENSMUSG00000017670. [Q8BHL5-3]
ENSMUST00000103091; ENSMUSP00000099380; ENSMUSG00000017670. [Q8BHL5-2]
GeneIDi140579.
KEGGimmu:140579.
UCSCiuc008nxj.1. mouse. [Q8BHL5-2]
uc008nxk.1. mouse. [Q8BHL5-1]
uc008nxm.1. mouse. [Q8BHL5-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398884 mRNA. Translation: AAL14465.1 .
AK004448 mRNA. Translation: BAB23307.1 .
AK032033 mRNA. Translation: BAC27662.1 .
AK033918 mRNA. Translation: BAC28514.1 .
AK035710 mRNA. Translation: BAC29162.1 .
AK038455 mRNA. Translation: BAC30007.1 .
AK045428 mRNA. Translation: BAC32361.1 .
AK047040 mRNA. Translation: BAC32945.1 .
AK050823 mRNA. Translation: BAC34424.1 .
AK053574 mRNA. Translation: BAC35433.1 .
AL591430 Genomic DNA. Translation: CAI51618.2 .
AL591430 Genomic DNA. Translation: CAM23849.1 .
BC023954 mRNA. Translation: AAH23954.1 .
AB093301 Transcribed RNA. Translation: BAC41483.3 .
CCDSi CCDS17075.1. [Q8BHL5-2 ]
CCDS17076.1. [Q8BHL5-1 ]
CCDS17077.1. [Q8BHL5-3 ]
RefSeqi NP_525026.2. NM_080287.2. [Q8BHL5-2 ]
NP_997588.1. NM_207705.1. [Q8BHL5-3 ]
NP_997589.1. NM_207706.1. [Q8BHL5-1 ]
XP_006498804.1. XM_006498741.1. [Q8BHL5-3 ]
XP_006498805.1. XM_006498742.1. [Q8BHL5-3 ]
XP_006498808.1. XM_006498745.1. [Q8BHL5-2 ]
UniGenei Mm.35064.

3D structure databases

ProteinModelPortali Q8BHL5.
SMRi Q8BHL5. Positions 189-238, 535-729.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BHL5. 2 interactions.
MINTi MINT-270694.

PTM databases

PhosphoSitei Q8BHL5.

Proteomic databases

MaxQBi Q8BHL5.
PaxDbi Q8BHL5.
PRIDEi Q8BHL5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071699 ; ENSMUSP00000071619 ; ENSMUSG00000017670 . [Q8BHL5-3 ]
ENSMUST00000074046 ; ENSMUSP00000073691 ; ENSMUSG00000017670 . [Q8BHL5-1 ]
ENSMUST00000094329 ; ENSMUSP00000091887 ; ENSMUSG00000017670 . [Q8BHL5-2 ]
ENSMUST00000103088 ; ENSMUSP00000099377 ; ENSMUSG00000017670 . [Q8BHL5-3 ]
ENSMUST00000103091 ; ENSMUSP00000099380 ; ENSMUSG00000017670 . [Q8BHL5-2 ]
GeneIDi 140579.
KEGGi mmu:140579.
UCSCi uc008nxj.1. mouse. [Q8BHL5-2 ]
uc008nxk.1. mouse. [Q8BHL5-1 ]
uc008nxm.1. mouse. [Q8BHL5-3 ]

Organism-specific databases

CTDi 63916.
MGIi MGI:2153045. Elmo2.
Rougei Search...

Phylogenomic databases

eggNOGi NOG295208.
GeneTreei ENSGT00390000014155.
HOVERGENi HBG051463.
InParanoidi Q8BHL5.
OMAi YLAKFHQ.
OrthoDBi EOG7D85VW.
PhylomeDBi Q8BHL5.
TreeFami TF312966.

Enzyme and pathway databases

Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_257088. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

ChiTaRSi Elmo2. mouse.
NextBioi 369891.
PROi Q8BHL5.
SOURCEi Search...

Gene expression databases

Bgeei Q8BHL5.
ExpressionAtlasi Q8BHL5. baseline and differential.
Genevestigatori Q8BHL5.

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.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 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 2).
    Strain: C3H.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Brain, Cerebellum, Diencephalon, Embryo, Eye, Hypothalamus, Medulla oblongata and Urinary bladder.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
    DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-732.
    Tissue: Brain.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48 AND TYR-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiELMO2_MOUSE
AccessioniPrimary (citable) accession number: Q8BHL5
Secondary accession number(s): A2A5A6
, Q5GMG3, Q8BHL9, Q8BQG1, Q8CBM8, Q8CC50, Q8CH98, Q91ZU2, Q9CT75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3