Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enhancer of filamentation 1

Gene

Nedd9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Cell cycle, Cell division, Growth regulation, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of filamentation 1
Short name:
mEF1
Alternative name(s):
CRK-associated substrate-related protein
Short name:
CAS-L
Neural precursor cell expressed developmentally down-regulated protein 9
Short name:
NEDD-9
p105
Gene namesi
Name:Nedd9
Synonyms:Casl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:97302. Nedd9.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • nucleus Source: MGI
  • spindle pole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833Enhancer of filamentation 1PRO_0000089329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei368 – 3681PhosphoserineBy similarity

Post-translational modificationi

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-368 induces proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35177.
MaxQBiO35177.
PaxDbiO35177.
PRIDEiO35177.

PTM databases

iPTMnetiO35177.
PhosphoSiteiO35177.

Expressioni

Gene expression databases

BgeeiO35177.
GenevisibleiO35177. MM.

Interactioni

Subunit structurei

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 (By similarity). Interacts with BCAR3 and SH2D3C.By similarity2 Publications

Protein-protein interaction databases

BioGridi201726. 3 interactions.
DIPiDIP-57058N.
IntActiO35177. 5 interactions.
STRINGi10090.ENSMUSP00000021794.

Structurei

3D structure databases

ProteinModelPortaliO35177.
SMRiO35177. Positions 5-71, 398-562, 703-831.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6563SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni709 – 75951Divergent helix-loop-helix motifAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi359 – 3624Caspase cleavage related siteBy similarity

Sequence similaritiesi

Belongs to the CAS family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410IEDD. Eukaryota.
ENOG410ZSUM. LUCA.
GeneTreeiENSGT00490000043324.
HOVERGENiHBG004354.
InParanoidiO35177.
KOiK16832.
OrthoDBiEOG7QRQTD.
PhylomeDBiO35177.
TreeFamiTF328782.

Family and domain databases

InterProiIPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWARNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG
60 70 80 90 100
RQGIVPGNRV KLLIGPVQET PGHEQPTPGP MHQTFGQQKL YQVPNSQAAS
110 120 130 140 150
RDTIYQVPPS YQNQGIYQVP TGHGTPEQDV YQVPPSVQRN IGGTNGPLLS
160 170 180 190 200
KKVITPVRTG HGYVYEYPSR YQKDVYDVPP SHSTQGVYDI PPSSVKGPVF
210 220 230 240 250
SVPVGEIKPQ GVYDIPPTQG VYAIPPSACR DEAGLREKEY DFPPPMKQDG
260 270 280 290 300
KPDTRPEGVY DIPPTSTKTA GKDLHIKFPC DAPGGVEPMA RRHQSFSLHH
310 320 330 340 350
APSQLGQSGD TQSDAYDVPR GVQFLEVPTE TSEKANPEER DGVYDVPLHN
360 370 380 390 400
PADAKGSRDV VDGINRLSFS STGSTRSNMS TSSTSSKESS LSASPSQDKR
410 420 430 440 450
LRLDPDTAIE KLYRLQQTLE MGVCSLMSLV TTDWRCYGYM ERHINEIRTA
460 470 480 490 500
VDKVELFLRE YLHFAKGALA NASCLPELVL HNKMKRELQR VEDSHQILSQ
510 520 530 540 550
TSHDLNECSW SLNILAINKP QNKCDDLDRF VMVAKTVPDD AKQLTTTIST
560 570 580 590 600
YAETLFRADP ANSHLKNGPN SIMNSSEYTH PGSQMQPLHP GDYKAQVHSK
610 620 630 640 650
PLPPSLSKDQ PPDCGSSDGS ERSWMDDYDY VHLQGKEEFE RQQKELLEKE
660 670 680 690 700
NIMKQSKAQL EHHQLSQFQL LEQEITKPVE NDISKWKPSQ SLPTTNNSVG
710 720 730 740 750
AQDRQLLCFY YDQCETHFIS LLNAIDALFS CVSSAQPPRI FVAHSKFVIL
760 770 780 790 800
SAHKLVFIGD TLTRQVAAQD IRNKVRNSSN QLCEQLKTIV MATKMAALHY
810 820 830
PSTTALQEMV HQVTDLSRNA QLFKRSLLEM ATF
Length:833
Mass (Da):93,052
Last modified:June 20, 2003 - v2
Checksum:i78AA1B042775DC01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 43WAR → KYK in BAC35682 (PubMed:16141072).Curated
Sequence conflicti2 – 43WAR → KYK in BAC32689 (PubMed:16141072).Curated
Sequence conflicti2 – 43WAR → KYK in BAC28451 (PubMed:16141072).Curated
Sequence conflicti55 – 551V → A in BAC32689 (PubMed:16141072).Curated
Sequence conflicti126 – 1272PE → QN in AAB71663 (Ref. 1) Curated
Sequence conflicti137 – 1371V → F in AAB71663 (Ref. 1) Curated
Sequence conflicti149 – 1491L → V in BAC32689 (PubMed:16141072).Curated
Sequence conflicti161 – 1611H → L in AAB71663 (Ref. 1) Curated
Sequence conflicti313 – 3131S → N in BAC27203 (PubMed:16141072).Curated
Sequence conflicti485 – 4851K → S in AAB71663 (Ref. 1) Curated
Sequence conflicti504 – 5063DLN → ELD in AAB71663 (Ref. 1) Curated
Sequence conflicti526 – 5261D → G in AAB71663 (Ref. 1) Curated
Sequence conflicti604 – 6041P → A in BAC35682 (PubMed:16141072).Curated
Sequence conflicti612 – 6121P → Q in BAC32689 (PubMed:16141072).Curated
Sequence conflicti650 – 6501E → A in AAB71663 (Ref. 1) Curated
Sequence conflicti685 – 6851K → R in BAC32689 (PubMed:16141072).Curated
Sequence conflicti733 – 7342SS → TP in AAB71663 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009366 mRNA. Translation: AAB71663.1.
AK030985 mRNA. Translation: BAC27203.1.
AK033729 mRNA. Translation: BAC28451.1.
AK046357 mRNA. Translation: BAC32689.1.
AK054179 mRNA. Translation: BAC35682.1.
AK083374 mRNA. Translation: BAC38890.1.
BC004696 mRNA. Translation: AAH04696.1.
BC053713 mRNA. Translation: AAH53713.1.
CCDSiCCDS49247.1.
RefSeqiNP_001104794.1. NM_001111324.2.
NP_059492.3. NM_017464.5.
UniGeneiMm.288980.

Genome annotation databases

EnsembliENSMUST00000021794; ENSMUSP00000021794; ENSMUSG00000021365.
GeneIDi18003.
KEGGimmu:18003.
UCSCiuc007qfd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009366 mRNA. Translation: AAB71663.1.
AK030985 mRNA. Translation: BAC27203.1.
AK033729 mRNA. Translation: BAC28451.1.
AK046357 mRNA. Translation: BAC32689.1.
AK054179 mRNA. Translation: BAC35682.1.
AK083374 mRNA. Translation: BAC38890.1.
BC004696 mRNA. Translation: AAH04696.1.
BC053713 mRNA. Translation: AAH53713.1.
CCDSiCCDS49247.1.
RefSeqiNP_001104794.1. NM_001111324.2.
NP_059492.3. NM_017464.5.
UniGeneiMm.288980.

3D structure databases

ProteinModelPortaliO35177.
SMRiO35177. Positions 5-71, 398-562, 703-831.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201726. 3 interactions.
DIPiDIP-57058N.
IntActiO35177. 5 interactions.
STRINGi10090.ENSMUSP00000021794.

PTM databases

iPTMnetiO35177.
PhosphoSiteiO35177.

Proteomic databases

EPDiO35177.
MaxQBiO35177.
PaxDbiO35177.
PRIDEiO35177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021794; ENSMUSP00000021794; ENSMUSG00000021365.
GeneIDi18003.
KEGGimmu:18003.
UCSCiuc007qfd.2. mouse.

Organism-specific databases

CTDi4739.
MGIiMGI:97302. Nedd9.

Phylogenomic databases

eggNOGiENOG410IEDD. Eukaryota.
ENOG410ZSUM. LUCA.
GeneTreeiENSGT00490000043324.
HOVERGENiHBG004354.
InParanoidiO35177.
KOiK16832.
OrthoDBiEOG7QRQTD.
PhylomeDBiO35177.
TreeFamiTF328782.

Miscellaneous databases

ChiTaRSiNedd9. mouse.
NextBioi293007.
PROiO35177.
SOURCEiSearch...

Gene expression databases

BgeeiO35177.
GenevisibleiO35177. MM.

Family and domain databases

InterProiIPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Harvey K.F., Fitter S., Kumar S.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.
  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].
    Strain: C57BL/6J.
    Tissue: Cecum, Corpora quadrigemina, Oviduct and Thymus.
  3. "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].
    Tissue: Hematopoietic and Mammary gland.
  4. "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways."
    Sakakibara A., Hattori S.
    J. Biol. Chem. 275:6404-6410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D3C.
  5. "The GDP exchange factor AND-34 is expressed in B cells, associates with HEF1, and activates Cdc42."
    Cai D., Felekkis K.N., Near R.I., O'Neill G.M., van Seventer J.M., Golemis E.A., Lerner A.
    J. Immunol. 170:969-978(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCAR3.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiCASL_MOUSE
AccessioniPrimary (citable) accession number: O35177
Secondary accession number(s): Q8BJL8
, Q8BK90, Q8BL52, Q8BM94, Q8BMI9, Q99KE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 20, 2003
Last modified: March 16, 2016
This is version 135 of the entry and version 2 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

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 one 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.