NEDD9
entrez
4739
canonical
uniprot
Q14511
canonical
ensembl
ENSG00000111859
resolver
ensp
ENSP00000368745
resolver
ensp
ENSP00000368759
resolver
ensp
ENSP00000422871
resolver
ensp
ENSP00000478563
resolver
enst
ENST00000620854
resolver
genesymbol
NEDD9
resolver
genesymbol_syn
CASL
resolver
hgnc
HGNC:7733
resolver
uniprot
A0A087WUD2
resolver
uniprot
A8K9G7
resolver
uniprot
A8MSJ9
resolver
uniprot
G5E9Y9
resolver
uniprot
Q5T9R4
resolver
uniprot
Q5XKI0
resolver
uniprot_entry
A0A087WUD2_HUMAN
resolver
uniprot_entry
CASL_HUMAN
resolver
uniprot_sec
A8K9G7
resolver
uniprot_sec
A8MSJ9
resolver
uniprot_sec
G5E9Y9
resolver
uniprot_sec
Q5T9R4
resolver
uniprot_sec
Q5XKI0
resolver
amino_acid_sequence
MKYKNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPMQETASSHEQPASGLMQQTFGQQKLYQVPNPQAAPRDTIYQVPPSYQNQGIYQVPTGHGTQEQEVYQVPPSVQRSIGGTSGPHVGKKVITPVRTGHGYVYEYPSRYQKDVYDIPPSHTTQGVYDIPPSSAKGPVFSVPVGEIKPQGVYDIPPTKGVYAIPPSACRDEAGLREKDYDFPPPMRQAGRPDLRPEGVYDIPPTCTKPAGKDLHVKYNCDIPGAAEPVARRHQSLSPNHPPPQLGQSVGSQNDAYDVPRGVQFLEPPAETSEKANPQERDGVYDVPLHNPPDAKGSRDLVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPAQDKRLFLDPDTAIERLQRLQQALEMGVSSLMALVTTDWRCYGYMERHINEIRTAVDKVELFLKEYLHFVKGAVANAACLPELILHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSLHLKNGPESIMNSTEYPHGGSQGQLLHPGDHKAQAHNKALPPGLSKEQAPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQNKMQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSGVSAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVTAQDIRNKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF
uniprot
proteins
function
FUNCTION: Scaffolding protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion (PubMed:24574519). As a focal adhesion protein, plays a role in embryonic fibroblast migration (By similarity). 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 CRKL and SHPTP2 to the tyrosine phosphorylated form (PubMed:9020138). Promotes adhesion and migration of lymphocytes; as a result required for the correct migration of lymphocytes to the spleen and other secondary lymphoid organs (PubMed:17174122). Plays a role in the organization of T-cell F-actin cortical cytoskeleton and the centralization of T-cell receptor microclusters at the immunological synapse (By similarity). Negatively regulates cilia outgrowth in polarized cysts (By similarity). Modulates cilia disassembly via activation of AURKA-mediated phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723). Positively regulates RANKL-induced osteoclastogenesis (By similarity). Required for the maintenance of hippocampal dendritic spines in the dentate gyrus and CA1 regions, thereby involved in spatial learning and memory (By similarity). {ECO:0000250|UniProtKB:A0A8I3PDQ1, ECO:0000250|UniProtKB:O35177, ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:24574519, ECO:0000269|PubMed:9020138}.
uniprot
proteins
mass_dalton
92861
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="C->A: Abolishes the oxidation-mediated reduction in interaction with SMAD3."; /evidence="ECO:0000269|PubMed:29899023"; MUTAGEN 735; /note="S->A: No effect on interaction with PLK1."; /evidence="ECO:0000269|PubMed:29191835"; MUTAGEN 751; /note="L->D: Abolishes interaction with BCAR3."; /evidence="ECO:0000269|PubMed:19103205"; MUTAGEN 754; /note="H->D: No effect on interaction with BCAR3."; /evidence="ECO:0000269|PubMed:19103205"; MUTAGEN 758; /note="F->D: No effect on interaction with BCAR3."; /evidence="ECO:0000269|PubMed:19103205"; MUTAGEN 780; /note="S->A: Reduces interaction with PLK1. Reduces protein phosphorylation by CSNK1D; when associated with A-804."; /evidence="ECO:0000269|PubMed:29191835"; MUTAGEN 780; /note="S->D: Reduces interaction with PLK1. Abolishes interaction with PLK1; when associated with D-804."; /evidence="ECO:0000269|PubMed:29191835"; MUTAGEN 780; /note="S->E: Abolishes interaction with PLK1."; /evidence="ECO:0000269|PubMed:29191835"; MUTAGEN 796; /note="M->D: No effect on interaction with BCAR3."; /evidence="ECO:0000269|PubMed:19103205"; MUTAGEN 804; /note="T->A: Reduces interaction with PLK1. Reduces protein phosphorylation by CSNK1D; when associated with A-780."; /evidence="ECO:0000269|PubMed:29191835"; MUTAGEN 804; /note="T->D: Reduces interaction with PLK1. Abolishes interaction with PLK1; when associated with D-780."; /evidence="ECO:0000269|PubMed:29191835"; MUTAGEN 804; /note="T->E: No effect on interaction with PLK1."; /evidence="ECO:0000269|PubMed:29191835
uniprot
proteins
post_translational_modification
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: Polyubiquitinated by ITCH/AIP4, leading to proteasomal degradation. {ECO:0000269|PubMed:15051726}.; PTM: PTK2/FAK1 phosphorylates the protein at the YDYVHL motif (conserved among all cas proteins) following integrin stimulation (PubMed:9360983). The SRC family kinases (FYN, SRC, LCK and CRK) are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues (PubMed:9020138). 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 (PubMed:9020138). Phosphorylation is required to recruit NEDD9 to T-cell receptor microclusters at the periphery of newly formed immunological synapses (By similarity). 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 CRKL and C3G (PubMed:9497377). A mutant lacking the SH3 domain is phosphorylated upon CD3 cross-linking but not upon integrin beta-1 cross-linking (PubMed:9497377). 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 (PubMed:19539609). Phosphorylated by LYN (PubMed:9020138). Phosphorylation at Ser-780 by CSNK1D or CSNK1E, or phosphorylation of Thr-804 by CSNK1E enhances the interaction of NEDD9 with PLK1 (PubMed:29191835). {ECO:0000250|UniProtKB:O35177, ECO:0000269|PubMed:19539609, ECO:0000269|PubMed:29191835, ECO:0000269|PubMed:9020138, ECO:0000269|PubMed:9360983, ECO:0000269|PubMed:9497377}.
uniprot
proteins
protein_family
CAS family
uniprot
proteins
pubmed
10502414
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
11054566
uniprot
proteins
pubmed
11827972
uniprot
proteins
pubmed
12522270
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15051726
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16394104
uniprot
proteins
pubmed
17174122
uniprot
proteins
pubmed
17604723
uniprot
proteins
pubmed
19103205
uniprot
proteins
pubmed
19275884
uniprot
proteins
pubmed
19539609
uniprot
proteins
pubmed
22810897
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24574519
uniprot
proteins
pubmed
29191835
uniprot
proteins
pubmed
29899023
uniprot
proteins
pubmed
8668148
uniprot
proteins
pubmed
8879209
uniprot
proteins
pubmed
9020138
uniprot
proteins
pubmed
9360983
uniprot
proteins
pubmed
9497377
uniprot
proteins
pubmed
9584194
uniprot
proteins
sequence_length
834
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:11827972}. Nucleus {ECO:0000269|PubMed:29899023, ECO:0000269|PubMed:8668148, ECO:0000269|PubMed:9584194}. Golgi apparatus {ECO:0000269|PubMed:8668148}. Cell projection, lamellipodium {ECO:0000269|PubMed:24574519, ECO:0000269|PubMed:8668148}. Cytoplasm {ECO:0000269|PubMed:11827972, ECO:0000269|PubMed:9584194}. Cell junction, focal adhesion {ECO:0000269|PubMed:19103205, ECO:0000269|PubMed:19275884, ECO:0000269|PubMed:29191835, ECO:0000269|PubMed:8668148}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11827972}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16394104, ECO:0000269|PubMed:9584194}. Cell projection, cilium {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane {ECO:0000250|UniProtKB:A0A8I3PDQ1}.; SUBCELLULAR LOCATION: [Enhancer of filamentation 1 p55]: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9584194}.
uniprot
proteins