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Protein

Engulfment and cell motility protein 2

Gene

ELMO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 DOCK1.3 Publications

GO - Molecular functioni

  1. receptor tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell chemotaxis Source: UniProtKB
  3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  4. innate immune response Source: Reactome
  5. vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Phagocytosis

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_264464. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Engulfment and cell motility protein 2
Alternative name(s):
Protein ced-12 homolog A
Short name:
hCed-12A
Gene namesi
Name:ELMO2
Synonyms:CED12A, KIAA1834
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:17233. ELMO2.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Cytoplasmcytosol 1 Publication
  3. Membrane 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27755.

Polymorphism and mutation databases

BioMutaiELMO2.
DMDMi30913107.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Engulfment and cell motility protein 2PRO_0000153714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphotyrosineBy similarity
Modified residuei717 – 7171PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96JJ3.
PaxDbiQ96JJ3.
PRIDEiQ96JJ3.

PTM databases

PhosphoSiteiQ96JJ3.

Expressioni

Tissue specificityi

Widely expressed, with a higher expression in skeletal muscle, kidney and placenta.1 Publication

Gene expression databases

BgeeiQ96JJ3.
ExpressionAtlasiQ96JJ3. baseline and differential.
GenevestigatoriQ96JJ3.

Organism-specific databases

HPAiHPA018811.

Interactioni

Subunit structurei

Interacts with the SH3-domain of DOCK1 via its SH3-binding site. Probably part of a complex with DOCK1 and RAC1. Probably part of a complex with DOCK1 and CRK isoform CRK-II. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates activation of RAC1 by EPHA2.2 Publications

Protein-protein interaction databases

BioGridi121987. 7 interactions.
IntActiQ96JJ3. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ96JJ3.
SMRiQ96JJ3. Positions 523-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini311 – 485175ELMOPROSITE-ProRule annotationAdd
BLAST
Domaini553 – 674122PHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi700 – 7078SH3-binding

Sequence similaritiesi

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

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG295208.
GeneTreeiENSGT00390000014155.
HOGENOMiHOG000230985.
HOVERGENiHBG051463.
InParanoidiQ96JJ3.
KOiK18985.
OrthoDBiEOG7D85VW.
PhylomeDBiQ96JJ3.
TreeFamiTF312966.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR030713. ELMO2.
IPR006816. Engulfment_cell_motility_ELMO.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR12771:SF8. PTHR12771:SF8. 1 hit.
PfamiPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51335. ELMO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96JJ3-1) [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 ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSNMETR
110 120 130 140 150
LDAMKELAKL SADVTFATEF INMDGIIVLT RLVESGTKLL SHYSEMLAFT
160 170 180 190 200
LTAFLELMDH GIVSWDMVSI TFIKQIAGYV SQPMVDVSIL QRSLAILESM
210 220 230 240 250
VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN ALFLKAPEDK
260 270 280 290 300
RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER
310 320 330 340 350
MMTKMDPNDQ AQRDIIFELR RIAFDAESDP SNAPGSGTEK RKAMYTKDYK
360 370 380 390 400
MLGFTNHINP AMDFTQTPPG MLALDNMLYL AKVHQDTYIR IVLENSSRED
410 420 430 440 450
KHECPFGRSA IELTKMLCEI LQVGELPNEG RNDYHPMFFT HDRAFEELFG
460 470 480 490 500
ICIQLLNKTW KEMRATAEDF NKVMQVVREQ ITRALPSKPN SLDQFKSKLR
510 520 530 540 550
SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL IKQQRLNRLC
560 570 580 590 600
EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLDDNPQG EVTFESLQEK
610 620 630 640 650
IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP
660 670 680 690 700
NKYEYCIWID GLSALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP
710 720
EAPPPIPKEP SSYDFVYHYG
Length:720
Mass (Da):82,615
Last modified:May 16, 2003 - v2
Checksum:iA67377E3B26F2937
GO
Isoform 2 (identifier: Q96JJ3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.

Note: No experimental confirmation available.

Show »
Length:632
Mass (Da):72,798
Checksum:i066EE50A3A2B358A
GO

Sequence cautioni

The sequence BAB13879.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB47463.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081Y → C in BAB71350 (PubMed:14702039).Curated
Sequence conflicti299 – 2991E → G in BAB13879 (PubMed:14702039).Curated
Sequence conflicti509 – 5091R → P in BAB13879 (PubMed:14702039).Curated
Sequence conflicti586 – 5861D → N in BAB14210 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti695 – 6951E → D.
Corresponds to variant rs34630674 [ dbSNP | Ensembl ].
VAR_048928

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8888Missing in isoform 2. 1 PublicationVSP_055477Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398886 Transcribed RNA. Translation: AAL14467.1.
AF417861 mRNA. Translation: AAL38512.1.
AB058737 mRNA. Translation: BAB47463.1. Different initiation.
AK021718 mRNA. Translation: BAB13879.1. Different initiation.
AK022731 mRNA. Translation: BAB14210.1. Different initiation.
AK023103 mRNA. Translation: BAB14405.1. Different initiation.
AK057032 mRNA. Translation: BAB71350.1.
AL031686 Genomic DNA. No translation available.
AL133227 Genomic DNA. Translation: CAI40561.1.
CH471077 Genomic DNA. Translation: EAW75739.1.
CH471077 Genomic DNA. Translation: EAW75743.1.
CH471077 Genomic DNA. Translation: EAW75745.1.
CH471077 Genomic DNA. Translation: EAW75746.1.
BC000143 mRNA. Translation: AAH00143.2.
CCDSiCCDS13398.1. [Q96JJ3-1]
RefSeqiNP_573403.1. NM_133171.3. [Q96JJ3-1]
NP_877496.1. NM_182764.1. [Q96JJ3-1]
XP_005260553.1. XM_005260496.2. [Q96JJ3-1]
XP_005260554.1. XM_005260497.2. [Q96JJ3-3]
XP_005260555.1. XM_005260498.2. [Q96JJ3-3]
XP_005260556.1. XM_005260499.2. [Q96JJ3-3]
XP_005260557.1. XM_005260500.2. [Q96JJ3-3]
XP_006723917.1. XM_006723854.2. [Q96JJ3-1]
UniGeneiHs.210469.

Genome annotation databases

EnsembliENST00000290246; ENSP00000290246; ENSG00000062598. [Q96JJ3-1]
ENST00000372176; ENSP00000361249; ENSG00000062598. [Q96JJ3-3]
ENST00000396391; ENSP00000379673; ENSG00000062598. [Q96JJ3-1]
GeneIDi63916.
KEGGihsa:63916.
UCSCiuc002xrs.1. human. [Q96JJ3-1]

Polymorphism and mutation databases

BioMutaiELMO2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398886 Transcribed RNA. Translation: AAL14467.1.
AF417861 mRNA. Translation: AAL38512.1.
AB058737 mRNA. Translation: BAB47463.1. Different initiation.
AK021718 mRNA. Translation: BAB13879.1. Different initiation.
AK022731 mRNA. Translation: BAB14210.1. Different initiation.
AK023103 mRNA. Translation: BAB14405.1. Different initiation.
AK057032 mRNA. Translation: BAB71350.1.
AL031686 Genomic DNA. No translation available.
AL133227 Genomic DNA. Translation: CAI40561.1.
CH471077 Genomic DNA. Translation: EAW75739.1.
CH471077 Genomic DNA. Translation: EAW75743.1.
CH471077 Genomic DNA. Translation: EAW75745.1.
CH471077 Genomic DNA. Translation: EAW75746.1.
BC000143 mRNA. Translation: AAH00143.2.
CCDSiCCDS13398.1. [Q96JJ3-1]
RefSeqiNP_573403.1. NM_133171.3. [Q96JJ3-1]
NP_877496.1. NM_182764.1. [Q96JJ3-1]
XP_005260553.1. XM_005260496.2. [Q96JJ3-1]
XP_005260554.1. XM_005260497.2. [Q96JJ3-3]
XP_005260555.1. XM_005260498.2. [Q96JJ3-3]
XP_005260556.1. XM_005260499.2. [Q96JJ3-3]
XP_005260557.1. XM_005260500.2. [Q96JJ3-3]
XP_006723917.1. XM_006723854.2. [Q96JJ3-1]
UniGeneiHs.210469.

3D structure databases

ProteinModelPortaliQ96JJ3.
SMRiQ96JJ3. Positions 523-717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121987. 7 interactions.
IntActiQ96JJ3. 1 interaction.

PTM databases

PhosphoSiteiQ96JJ3.

Polymorphism and mutation databases

BioMutaiELMO2.
DMDMi30913107.

Proteomic databases

MaxQBiQ96JJ3.
PaxDbiQ96JJ3.
PRIDEiQ96JJ3.

Protocols and materials databases

DNASUi63916.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290246; ENSP00000290246; ENSG00000062598. [Q96JJ3-1]
ENST00000372176; ENSP00000361249; ENSG00000062598. [Q96JJ3-3]
ENST00000396391; ENSP00000379673; ENSG00000062598. [Q96JJ3-1]
GeneIDi63916.
KEGGihsa:63916.
UCSCiuc002xrs.1. human. [Q96JJ3-1]

Organism-specific databases

CTDi63916.
GeneCardsiGC20M044994.
HGNCiHGNC:17233. ELMO2.
HPAiHPA018811.
MIMi606421. gene.
neXtProtiNX_Q96JJ3.
PharmGKBiPA27755.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295208.
GeneTreeiENSGT00390000014155.
HOGENOMiHOG000230985.
HOVERGENiHBG051463.
InParanoidiQ96JJ3.
KOiK18985.
OrthoDBiEOG7D85VW.
PhylomeDBiQ96JJ3.
TreeFamiTF312966.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_264464. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

ChiTaRSiELMO2. human.
GeneWikiiELMO2.
GenomeRNAii63916.
NextBioi65636.
PROiQ96JJ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ96JJ3.
ExpressionAtlasiQ96JJ3. baseline and differential.
GenevestigatoriQ96JJ3.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024574. DUF3361.
IPR030713. ELMO2.
IPR006816. Engulfment_cell_motility_ELMO.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR12771:SF8. PTHR12771:SF8. 1 hit.
PfamiPF11841. DUF3361. 1 hit.
PF04727. ELMO_CED12. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51335. ELMO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH DOCK1.
  2. "The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway."
    Zhou Z., Caron E., Hartwieg E., Hall A., Horvitz H.R.
    Dev. Cell 1:477-489(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Testis.
  3. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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 1).
    Tissue: Embryo, Neuroepithelioma and Teratocarcinoma.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] (ISOFORM 2).
    Tissue: Cervix.
  8. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
    Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
    J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARHGEF16; DOCK4 AND EPHA2, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiELMO2_HUMAN
AccessioniPrimary (citable) accession number: Q96JJ3
Secondary accession number(s): E1P5T3
, Q5JVZ6, Q7Z5G9, Q96CJ2, Q96ME5, Q96PA9, Q9H938, Q9H9L5, Q9HAH0, Q9NQQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: April 29, 2015
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.