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Enhancer of filamentation 1 (hEF1) (CRK-associated substrate-related protein) (CAS-L) (CasL) (Cas scaffolding protein family member 2) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (Renal carcinoma antigen NY-REN-12) (p105) [Cleaved into: Enhancer of filamentation 1 p55]

 CASL_HUMAN              Reviewed;         834 AA.
Q14511; A8K9G7; A8MSJ9; G5E9Y9; Q5T9R4; Q5XKI0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 194.
RecName: Full=Enhancer of filamentation 1;
Short=hEF1;
AltName: Full=CRK-associated substrate-related protein;
Short=CAS-L;
Short=CasL;
AltName: Full=Cas scaffolding protein family member 2;
AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 9;
Short=NEDD-9;
AltName: Full=Renal carcinoma antigen NY-REN-12;
AltName: Full=p105;
Contains:
RecName: Full=Enhancer of filamentation 1 p55;
Name=NEDD9; Synonyms=CASL, CASS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8668148; DOI=10.1128/MCB.16.7.3327;
Law S.F., Estojak J., Wang B., Mysliwiec T., Kruh G., Golemis E.A.;
"Human enhancer of filamentation 1, a novel p130cas-like docking
protein, associates with focal adhesion kinase and induces
pseudohyphal growth in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:3327-3337(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphoma;
PubMed=8879209; DOI=10.1084/jem.184.4.1365;
Minegishi M., Tachibana K., Sato T., Iwata S., Nojima Y., Morimoto C.;
"Structure and function of Cas-L, a 105-kD Crk-associated substrate-
related protein that is involved in beta 1 integrin-mediated signaling
in lymphocytes.";
J. Exp. Med. 184:1365-1375(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INCREASED TYROSINE PHOSPHORYLATION BY LIGATION OF INTEGRIN-B1 AND BCR.
PubMed=9020138; DOI=10.1074/jbc.272.7.4230;
Manie S.N., Beck A.R.P., Astier A., Law S.F., Canty T., Hirai H.,
Druker B.J., Avraham H., Haghayeghi N., Sattler M., Salgia R.,
Griffin J.D., Golemis E.A., Freedman A.S.;
"Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking
protein, in a cytoskeleton-dependent signaling pathway initiated by
ligation of integrin or antigen receptor on human B cells.";
J. Biol. Chem. 272:4230-4236(1997).
[8]
PHOSPHORYLATION AT TYROSINE RESIDUES BY PTK2/FAK1.
PubMed=9360983; DOI=10.1074/jbc.272.46.29083;
Tachibana K., Urano T., Fujita H., Ohashi Y., Kamiguchi K., Iwata S.,
Hirai H., Morimoto C.;
"Tyrosine phosphorylation of Crk-associated substrates by focal
adhesion kinase. A putative mechanism for the integrin-mediated
tyrosine phosphorylation of Crk-associated substrates.";
J. Biol. Chem. 272:29083-29090(1997).
[9]
PROTEOLYTIC PROCESSING.
PubMed=9584194; DOI=10.1128/MCB.18.6.3540;
Law S.F., Zhang Y.-Z., Klein-Szanto A.J.P., Golemis E.A.;
"Cell cycle-regulated processing of HEF1 to multiple protein forms
differentially targeted to multiple subcellular compartments.";
Mol. Cell. Biol. 18:3540-3551(1998).
[10]
PHOSPHORYLATION AT TYROSINE RESIDUES UPON CD3 CROSS-LINKING.
PubMed=9497377; DOI=10.1074/jbc.273.11.6446;
Ohashi Y., Tachibana K., Kamiguchi K., Fujita H., Morimoto C.;
"T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa
Crk-associated substrate-related protein, and its association of Crk
and C3G.";
J. Biol. Chem. 273:6446-6451(1998).
[11]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[12]
CHARACTERIZATION OF CARBOXY-TERMINAL DOMAIN.
PubMed=10502414; DOI=10.1006/excr.1999.4609;
Law S.F., Zhang Y.-Z., Fashena S.J., Toby G., Estojak J.,
Golemis E.A.;
"Dimerization of the docking/adaptor protein HEF1 via a carboxy-
terminal helix-loop-helix domain.";
Exp. Cell Res. 252:224-235(1999).
[13]
INTERACTION WITH TXNL4.
PubMed=11054566; DOI=10.1016/S0378-1119(00)00372-3;
Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E.,
Golemis E.A.;
"Evidence that Dim1 associates with proteins involved in pre-mRNA
splicing, and delineation of residues essential for Dim1 interactions
with hnRNP F and Npw38/PQBP-1.";
Gene 257:33-43(2000).
[14]
INTERACTION WITH MICAL.
PubMed=11827972; DOI=10.1074/jbc.M111842200;
Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K.,
Morimoto C., Hirai H.;
"MICAL, a novel CasL interacting molecule, associates with vimentin.";
J. Biol. Chem. 277:14933-14941(2002).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[17]
PHOSPHORYLATION AT SER-296 AND SER-369.
PubMed=19539609; DOI=10.1016/j.bcp.2009.06.005;
Hivert V., Pierre J., Raingeaud J.;
"Phosphorylation of human enhancer of filamentation (HEF1) on serine
369 induces its proteasomal degradation.";
Biochem. Pharmacol. 78:1017-1025(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
STRUCTURE BY NMR OF 399-563.
Northeast structural genomics consortium (NESG);
"Northeast structural genomics consortium target HR5554A.";
Submitted (FEB-2011) to the PDB data bank.
-!- FUNCTION: Docking protein which plays a central coordinating role
for tyrosine-kinase-based signaling related to cell adhesion. May
function in transmitting growth control signals between focal
adhesions at the cell periphery and the mitotic spindle in
response to adhesion or growth factor signals initiating cell
proliferation. May play an important role in integrin beta-1 or B
cell antigen receptor (BCR) mediated signaling in B- and T-cells.
Integrin beta-1 stimulation leads to recruitment of various
proteins including CRK, NCK and SHPTP2 to the tyrosine
phosphorylated form.
-!- SUBUNIT: Interacts with BCAR3 and SH2D3C (By similarity).
Homodimer. Can heterodimerize with HLH proteins ID2, E12, E47 and
also with p130cas. Forms complexes in vivo with related adhesion
focal tyrosine kinase (RAFTK), adapter protein CRKL and LYN
kinase. Interacts with MICAL and TXNL4/DIM1. {ECO:0000250,
ECO:0000269|PubMed:11054566, ECO:0000269|PubMed:11827972}.
-!- INTERACTION:
Q49AR9:ANKS1A; NbExp=4; IntAct=EBI-11746523, EBI-11954519;
Q8N9N5:BANP; NbExp=4; IntAct=EBI-2108053, EBI-744695;
O75815:BCAR3; NbExp=3; IntAct=EBI-2108053, EBI-702336;
Q15742:NAB2; NbExp=4; IntAct=EBI-2108053, EBI-8641936;
P25963:NFKBIA; NbExp=3; IntAct=EBI-2108053, EBI-307386;
P86479:PRR20C; NbExp=3; IntAct=EBI-2108053, EBI-10172814;
Q93062:RBPMS; NbExp=3; IntAct=EBI-2108053, EBI-740322;
Q04864:REL; NbExp=3; IntAct=EBI-2108053, EBI-307352;
Q8HWS3:RFX6; NbExp=3; IntAct=EBI-2108053, EBI-746118;
P14373:TRIM27; NbExp=4; IntAct=EBI-2108053, EBI-719493;
Q15654:TRIP6; NbExp=3; IntAct=EBI-2108053, EBI-742327;
P36508:ZNF76; NbExp=4; IntAct=EBI-11746523, EBI-7254550;
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Nucleus. Golgi
apparatus. Cell projection, lamellipodium. Cytoplasm. Cell
junction, focal adhesion. Note=Localizes to both the cell nucleus
and the cell periphery and is differently localized in fibroblasts
and epithelial cells. In fibroblasts is predominantly nuclear and
in some cells is present in the Golgi apparatus. In epithelial
cells localized predominantly in the cell periphery with
particular concentration in lamellipodia but is also found in the
nucleus. Isoforms p105 and p115 are predominantly cytoplasmic and
associate with focal adhesions while p55 associates with mitotic
spindle.
-!- SUBCELLULAR LOCATION: Enhancer of filamentation 1 p55: Cytoplasm,
cytoskeleton, spindle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14511-1; Sequence=Displayed;
Name=2;
IsoId=Q14511-2; Sequence=VSP_042835, VSP_042836;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q14511-3; Sequence=VSP_044579;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Higher levels detected in
kidney, lung, and placenta. Also detected in T-cells, B-cells and
diverse cell lines. The protein has been detected in lymphocytes,
in diverse cell lines, and in lung tissues.
-!- INDUCTION: Activated upon induction of cell growth.
-!- DOMAIN: Contains a central domain containing multiple potential
SH2-binding sites and a C-terminal domain containing a divergent
helix-loop-helix (HLH) motif. The SH2-binding sites putatively
bind CRK, NCK and ABL SH2 domains. The HLH motif confers specific
interaction with the HLH proteins ID2, E12 and E47. It is
absolutely required for the induction of pseudohyphal growth in
yeast and mediates homodimerization and heterodimerization with
p130cas.
-!- DOMAIN: The SH3 domain interacts with two proline-rich regions of
PTK2/FAK1.
-!- PTM: Cell cycle-regulated processing produces four isoforms: p115,
p105, p65, and p55. Isoform p115 arises from p105 phosphorylation
and appears later in the cell cycle. Isoform p55 arises from p105
as a result of cleavage at a caspase cleavage-related site and it
appears specifically at mitosis. The p65 isoform is poorly
detected. {ECO:0000269|PubMed:9584194}.
-!- PTM: PTK2/FAK1 phosphorylates the protein at the YDYVHL motif
(conserved among all cas proteins). The SRC family kinases (FYN,
SRC, LCK and CRK) are recruited to the phosphorylated sites and
can phosphorylate other tyrosine residues. Ligation of either
integrin beta-1 or B-cell antigen receptor on tonsillar B-cells
and B-cell lines promotes tyrosine phosphorylation and both
integrin and BCR-mediated tyrosine phosphorylation requires an
intact actin network. In fibroblasts transformation with oncogene
v-ABL results in an increase in tyrosine phosphorylation.
Transiently phosphorylated following CD3 cross-linking and this
phosphorylated form binds to CRK and C3G. A mutant lacking the SH3
domain is phosphorylated upon CD3 cross-linking but not upon
integrin beta-1 cross-linking. Tyrosine phosphorylation occurs
upon stimulation of the G-protein coupled C1a calcitonin receptor.
Calcitonin-stimulated tyrosine phosphorylation is mediated by
calcium- and protein kinase C-dependent mechanisms and requires
the integrity of the actin cytoskeleton. Phosphorylation at Ser-
369 induces proteasomal degradation.
{ECO:0000269|PubMed:19539609}.
-!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
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EMBL; L43821; AAA98770.1; -; mRNA.
EMBL; U64317; AAB53696.1; -; mRNA.
EMBL; AK292682; BAF85371.1; -; mRNA.
EMBL; AL022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL139807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471087; EAW55299.1; -; Genomic_DNA.
EMBL; CH471087; EAW55301.1; -; Genomic_DNA.
EMBL; BC020686; AAH20686.1; -; mRNA.
EMBL; BC040207; AAH40207.1; -; mRNA.
CCDS; CCDS34340.1; -. [Q14511-2]
CCDS; CCDS4520.1; -. [Q14511-1]
CCDS; CCDS47373.1; -. [Q14511-3]
RefSeq; NP_001135865.1; NM_001142393.1. [Q14511-3]
RefSeq; NP_001257962.1; NM_001271033.1.
RefSeq; NP_006394.1; NM_006403.3. [Q14511-1]
RefSeq; NP_892011.2; NM_182966.3. [Q14511-2]
UniGene; Hs.37982; -.
PDB; 2L81; NMR; -; A=399-563.
PDB; 5X3S; X-ray; 2.90 A; C/D=799-809.
PDBsum; 2L81; -.
PDBsum; 5X3S; -.
ProteinModelPortal; Q14511; -.
SMR; Q14511; -.
BioGrid; 110816; 45.
CORUM; Q14511; -.
ELM; Q14511; -.
IntAct; Q14511; 48.
MINT; Q14511; -.
STRING; 9606.ENSP00000368759; -.
iPTMnet; Q14511; -.
PhosphoSitePlus; Q14511; -.
BioMuta; NEDD9; -.
DMDM; 8134360; -.
MaxQB; Q14511; -.
PaxDb; Q14511; -.
PeptideAtlas; Q14511; -.
PRIDE; Q14511; -.
ProteomicsDB; 60015; -.
ProteomicsDB; 60016; -. [Q14511-2]
DNASU; 4739; -.
Ensembl; ENST00000379433; ENSP00000368745; ENSG00000111859. [Q14511-2]
Ensembl; ENST00000379446; ENSP00000368759; ENSG00000111859. [Q14511-1]
Ensembl; ENST00000504387; ENSP00000422871; ENSG00000111859. [Q14511-3]
GeneID; 4739; -.
KEGG; hsa:4739; -.
UCSC; uc003mzv.2; human. [Q14511-1]
CTD; 4739; -.
DisGeNET; 4739; -.
EuPathDB; HostDB:ENSG00000111859.16; -.
GeneCards; NEDD9; -.
HGNC; HGNC:7733; NEDD9.
HPA; CAB009720; -.
HPA; HPA038768; -.
HPA; HPA039270; -.
MIM; 602265; gene.
neXtProt; NX_Q14511; -.
OpenTargets; ENSG00000111859; -.
PharmGKB; PA31538; -.
eggNOG; ENOG410IEDD; Eukaryota.
eggNOG; ENOG410ZSUM; LUCA.
GeneTree; ENSGT00490000043324; -.
HOGENOM; HOG000261698; -.
HOVERGEN; HBG004354; -.
InParanoid; Q14511; -.
KO; K16832; -.
OMA; YEYPSRY; -.
PhylomeDB; Q14511; -.
TreeFam; TF328782; -.
SignaLink; Q14511; -.
ChiTaRS; NEDD9; human.
GeneWiki; NEDD9; -.
GenomeRNAi; 4739; -.
PMAP-CutDB; Q14511; -.
PRO; PR:Q14511; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000111859; Expressed in 210 organ(s), highest expression level in metanephric glomerulus.
CleanEx; HS_NEDD9; -.
ExpressionAtlas; Q14511; baseline and differential.
Genevisible; Q14511; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005819; C:spindle; TAS:ProtInc.
GO; GO:0000922; C:spindle pole; IEA:Ensembl.
GO; GO:0051017; P:actin filament bundle assembly; NAS:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd12002; SH3_NEDD9; 1.
Gene3D; 1.20.120.830; -; 1.
InterPro; IPR021901; CAS_C.
InterPro; IPR037362; CAS_fam.
InterPro; IPR035746; NEDD9_SH3.
InterPro; IPR014928; Serine_rich_dom.
InterPro; IPR038319; Serine_rich_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10654; PTHR10654; 1.
Pfam; PF12026; DUF3513; 1.
Pfam; PF08824; Serine_rich; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell cycle;
Cell division; Cell junction; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Golgi apparatus; Growth regulation; Mitosis;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; SH3 domain.
CHAIN 1 834 Enhancer of filamentation 1.
/FTId=PRO_0000089328.
CHAIN 1 ? Enhancer of filamentation 1 p55.
/FTId=PRO_0000296242.
DOMAIN 3 65 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 102 229 Interacts strongly with spindle-
regulatory protein D1M1.
REGION 710 760 Divergent helix-loop-helix motif.
MOTIF 360 363 Caspase cleavage related site.
MOD_RES 296 296 Phosphoserine.
{ECO:0000269|PubMed:19539609}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000269|PubMed:19539609}.
VAR_SEQ 1 4 MKYK -> MWTR (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044579.
VAR_SEQ 155 174 ITPVRTGHGYVYEYPSRYQK -> FQRDGQVSYFLVRASKQ
TSL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042835.
VAR_SEQ 175 834 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042836.
VARIANT 178 178 D -> N (in dbSNP:rs11546959).
/FTId=VAR_054082.
VARIANT 304 304 P -> L (in dbSNP:rs34184473).
/FTId=VAR_054083.
VARIANT 577 577 T -> M (in dbSNP:rs3734401).
/FTId=VAR_021857.
CONFLICT 139 139 Q -> R (in Ref. 3; BAF85371).
{ECO:0000305}.
HELIX 406 430 {ECO:0000244|PDB:2L81}.
HELIX 438 442 {ECO:0000244|PDB:2L81}.
TURN 443 446 {ECO:0000244|PDB:2L81}.
HELIX 447 473 {ECO:0000244|PDB:2L81}.
HELIX 480 508 {ECO:0000244|PDB:2L81}.
TURN 509 511 {ECO:0000244|PDB:2L81}.
HELIX 513 516 {ECO:0000244|PDB:2L81}.
HELIX 527 535 {ECO:0000244|PDB:2L81}.
HELIX 538 551 {ECO:0000244|PDB:2L81}.
HELIX 553 556 {ECO:0000244|PDB:2L81}.
SEQUENCE 834 AA; 92861 MW; C54DEC36C8C8E9E6 CRC64;
MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG RQGIVPGNRV
KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA PRDTIYQVPP SYQNQGIYQV
PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV GKKVITPVRT GHGYVYEYPS RYQKDVYDIP
PSHTTQGVYD IPPSSAKGPV FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGLREKD
YDFPPPMRQA GRPDLRPEGV YDIPPTCTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN
HPPPQLGQSV GSQNDAYDVP RGVQFLEPPA ETSEKANPQE RDGVYDVPLH NPPDAKGSRD
LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK RLFLDPDTAI ERLQRLQQAL
EMGVSSLMAL VTTDWRCYGY MERHINEIRT AVDKVELFLK EYLHFVKGAV ANAACLPELI
LHNKMKRELQ RVEDSHQILS QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD
DAKQLTTTIN TNAEALFRPG PGSLHLKNGP ESIMNSTEYP HGGSQGQLLH PGDHKAQAHN
KALPPGLSKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK ENIMKQNKMQ
LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV SAQDRQLLCF YYDQCETHFI
SLLNAIDALF SCVSSAQPPR IFVAHSKFVI LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS
NQLCEQLKTI VMATKMAALH YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF


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