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Q9UI08

- EVL_HUMAN

UniProt

Q9UI08 - EVL_HUMAN

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Protein

Ena/VASP-like protein

Gene

EVL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.

GO - Molecular functioni

  1. profilin binding Source: UniProtKB
  2. SH3 domain binding Source: UniProtKB

GO - Biological processi

  1. actin filament organization Source: ProtInc
  2. actin polymerization or depolymerization Source: UniProtKB
  3. axon guidance Source: Reactome
  4. cell surface receptor signaling pathway Source: UniProtKB
  5. negative regulation of epithelial cell migration Source: UniProt
  6. negative regulation of ruffle assembly Source: UniProt
  7. nervous system development Source: UniProtKB
  8. organ morphogenesis Source: UniProtKB
  9. positive regulation of actin filament polymerization Source: Ensembl
  10. positive regulation of stress fiber assembly Source: UniProt
  11. protein homotetramerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_12623. Generation of second messenger molecules.
REACT_19351. Signaling by Robo receptor.
SignaLinkiQ9UI08.

Names & Taxonomyi

Protein namesi
Recommended name:
Ena/VASP-like protein
Alternative name(s):
Ena/vasodilator-stimulated phosphoprotein-like
Gene namesi
Name:EVL
Synonyms:RNB6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20234. EVL.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity
Note: Targeted to the leading edge of lamellipodia and the dital tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. focal adhesion Source: UniProtKB
  5. lamellipodium Source: UniProtKB
  6. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134890866.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Ena/VASP-like proteinPRO_0000087104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei304 – 3041Phosphoserine2 Publications
Modified residuei306 – 3061Phosphoserine1 Publication
Modified residuei329 – 3291Phosphoserine1 Publication
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei341 – 3411Phosphoserine1 Publication
Modified residuei349 – 3491Phosphoserine2 Publications
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei369 – 3691Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UI08.
PaxDbiQ9UI08.
PRIDEiQ9UI08.

PTM databases

PhosphoSiteiQ9UI08.

Expressioni

Gene expression databases

BgeeiQ9UI08.
CleanExiHS_EVL.
ExpressionAtlasiQ9UI08. baseline and differential.
GenevestigatoriQ9UI08.

Organism-specific databases

HPAiHPA018849.

Interactioni

Subunit structurei

Homotetramer (By similarity). Binds to the SH3 domains of ABL1, LYN and SRC. Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A. Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA (By similarity). Binds, via the EVH1 domain, the Pro-rich domain of ZYX.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428582EBI-6448852,EBI-466029
SPTAN1Q138134EBI-346653,EBI-351450
ZDHHC17Q8IUH52EBI-6448852,EBI-524753

Protein-protein interaction databases

BioGridi119556. 22 interactions.
IntActiQ9UI08. 9 interactions.
MINTiMINT-3080348.
STRINGi9606.ENSP00000376652.

Structurei

3D structure databases

ProteinModelPortaliQ9UI08.
SMRiQ9UI08. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 112112WH1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni222 – 413192EVH2Add
BLAST
Regioni222 – 24221EVH2 block AAdd
BLAST
Regioni265 – 28218EVH2 block BAdd
BLAST
Regioni379 – 41335EVH2 block CAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi231 – 2344KLKR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi162 – 20645Pro-richAdd
BLAST

Domaini

The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.

Sequence similaritiesi

Belongs to the Ena/VASP family.Curated
Contains 1 WH1 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG265043.
GeneTreeiENSGT00730000110272.
HOVERGENiHBG006655.
InParanoidiQ9UI08.
OMAiQHRQESL.
OrthoDBiEOG72JWGQ.
PhylomeDBiQ9UI08.
TreeFamiTF321411.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q9UI08-1) [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
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV
60 70 80 90 100
GVKLQDQQVV INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT
110 120 130 140 150
FSNAMLFALN IMNSQEGGPS SQRQVQNGPS PDEMDIQRRQ VMEQHQQQRQ
160 170 180 190 200
ESLERRTSAT GPILPPGHPS SAASAPVSCS GPPPPPPPPV PPPPTGATPP
210 220 230 240 250
PPPPLPAGGA QGSSHDESSM SGLAAAIAGA KLRRVQRPED ASGGSSPSGT
260 270 280 290 300
SKSDANRASS GGGGGGLMEE MNKLLAKRRK AASQSDKPAE KKEDESQMED
310 320 330 340 350
PSTSPSPGTR AASQPPNSSE AGRKPWERSN SVEKPVSSIL SRTPSVAKSP
360 370 380 390 400
EAKSPLQSQP HSRMKPAGSV NDMALDAFDL DRMKQEILEE VVRELHKVKE
410
EIIDAIRQEL SGISTT
Length:416
Mass (Da):44,620
Last modified:November 15, 2002 - v2
Checksum:iAD5B67458755D659
GO
Isoform 1 (identifier: Q9UI08-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAT

Show »
Length:418
Mass (Da):44,792
Checksum:iBFCCF68CF923720C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011P → S in AAF17197. (PubMed:10931946)Curated
Sequence conflicti329 – 3291S → N in AAP97156. 1 PublicationCurated
Sequence conflicti364 – 3641M → Y in CAB63763. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036464
Natural varianti247 – 2471P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036465

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAT in isoform 1. 3 PublicationsVSP_004044

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052504 mRNA. Translation: AAF21709.1.
AF087843 mRNA. Translation: AAP97156.1.
AF112209 mRNA. Translation: AAF17197.1.
AK289720 mRNA. Translation: BAF82409.1.
CH471061 Genomic DNA. Translation: EAW81684.1.
BC023997 mRNA. Translation: AAH23997.1.
BC032358 mRNA. Translation: AAH32358.1.
AF131766 mRNA. Translation: AAD20040.1.
AL133642 mRNA. Translation: CAB63763.2.
CCDSiCCDS9955.1. [Q9UI08-2]
RefSeqiNP_057421.1. NM_016337.2. [Q9UI08-2]
UniGeneiHs.125867.

Genome annotation databases

EnsembliENST00000392920; ENSP00000376652; ENSG00000196405. [Q9UI08-2]
ENST00000402714; ENSP00000384720; ENSG00000196405. [Q9UI08-1]
GeneIDi51466.
KEGGihsa:51466.
UCSCiuc001ygt.3. human. [Q9UI08-1]
uc001ygu.3. human. [Q9UI08-2]

Polymorphism databases

DMDMi25090276.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052504 mRNA. Translation: AAF21709.1 .
AF087843 mRNA. Translation: AAP97156.1 .
AF112209 mRNA. Translation: AAF17197.1 .
AK289720 mRNA. Translation: BAF82409.1 .
CH471061 Genomic DNA. Translation: EAW81684.1 .
BC023997 mRNA. Translation: AAH23997.1 .
BC032358 mRNA. Translation: AAH32358.1 .
AF131766 mRNA. Translation: AAD20040.1 .
AL133642 mRNA. Translation: CAB63763.2 .
CCDSi CCDS9955.1. [Q9UI08-2 ]
RefSeqi NP_057421.1. NM_016337.2. [Q9UI08-2 ]
UniGenei Hs.125867.

3D structure databases

ProteinModelPortali Q9UI08.
SMRi Q9UI08. Positions 1-113.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119556. 22 interactions.
IntActi Q9UI08. 9 interactions.
MINTi MINT-3080348.
STRINGi 9606.ENSP00000376652.

PTM databases

PhosphoSitei Q9UI08.

Polymorphism databases

DMDMi 25090276.

Proteomic databases

MaxQBi Q9UI08.
PaxDbi Q9UI08.
PRIDEi Q9UI08.

Protocols and materials databases

DNASUi 51466.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392920 ; ENSP00000376652 ; ENSG00000196405 . [Q9UI08-2 ]
ENST00000402714 ; ENSP00000384720 ; ENSG00000196405 . [Q9UI08-1 ]
GeneIDi 51466.
KEGGi hsa:51466.
UCSCi uc001ygt.3. human. [Q9UI08-1 ]
uc001ygu.3. human. [Q9UI08-2 ]

Organism-specific databases

CTDi 51466.
GeneCardsi GC14P101219.
H-InvDB HIX0011964.
HGNCi HGNC:20234. EVL.
HPAi HPA018849.
neXtProti NX_Q9UI08.
PharmGKBi PA134890866.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265043.
GeneTreei ENSGT00730000110272.
HOVERGENi HBG006655.
InParanoidi Q9UI08.
OMAi QHRQESL.
OrthoDBi EOG72JWGQ.
PhylomeDBi Q9UI08.
TreeFami TF321411.

Enzyme and pathway databases

Reactomei REACT_12623. Generation of second messenger molecules.
REACT_19351. Signaling by Robo receptor.
SignaLinki Q9UI08.

Miscellaneous databases

ChiTaRSi EVL. human.
GeneWikii Enah/Vasp-like.
GenomeRNAii 51466.
NextBioi 55097.
PROi Q9UI08.

Gene expression databases

Bgeei Q9UI08.
CleanExi HS_EVL.
ExpressionAtlasi Q9UI08. baseline and differential.
Genevestigatori Q9UI08.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view ]
Pfami PF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view ]
PIRSFi PIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTi SM00461. WH1. 1 hit.
[Graphical view ]
PROSITEi PS50229. WH1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Ohta S., Mineta T., Kimoto M., Tabuchi K.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA."
    Wan Y.Z., Yu L., Yue P., Tu Q., Fu S.N., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  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].
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Lung and Pancreas.
  7. Mei G., Yu W., Gibbs R.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416.
    Tissue: Brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-364.
    Tissue: Uterus.
  9. "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like protein (EVL) via a novel carboxyl-terminal zyxin-like domain."
    Klostermann A., Lutz B., Gertler F., Behl C.
    J. Biol. Chem. 275:39647-39653(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEMA6A.
  10. Cited for: INTERACTION WITH RAPH1.
  11. "Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding."
    Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., McDonald N.Q., Way M.
    Mol. Cell 28:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZYX.
  12. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-304; SER-306; SER-329; SER-331 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-341 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247.

Entry informationi

Entry nameiEVL_HUMAN
AccessioniPrimary (citable) accession number: Q9UI08
Secondary accession number(s): A8K105
, O95884, Q7Z522, Q8TBV1, Q9UF25, Q9UIC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: October 29, 2014
This is version 133 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

Miscellaneous

Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3