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Q14511 (CASL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enhancer of filamentation 1

Short name=hEF1
Alternative name(s):
CRK-associated substrate-related protein
Short name=CAS-L
Short name=CasL
Cas scaffolding protein family member 2
Neural precursor cell expressed developmentally down-regulated protein 9
Short name=NEDD-9
Renal carcinoma antigen NY-REN-12
p105

Cleaved into the following chain:

  1. Enhancer of filamentation 1 p55
Gene names
Name:NEDD9
Synonyms:CASL, CASS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length834 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

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. Ref.13 Ref.14

Subcellular location

Cytoplasmcell cortex. Nucleus. Golgi apparatus. Cell projectionlamellipodium. Cytoplasm. Cell junctionfocal 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.

Enhancer of filamentation 1 p55: Cytoplasmcytoskeletonspindle.

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. Ref.12

The SH3 domain interacts with two proline-rich regions of PTK2/FAK1. Ref.12

Post-translational modification

Cell cycle-regulated processing produces four isoforms: p115, p105, p65, and p55. Isoform p115arises from p105 phosphorylation and appears later in the cell cycle. Isoform p55arises from p105 as a result of cleavage at a caspase cleavage-related site and it appears specifically at mitosis. The p65 isoform ispoorly detected.

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. Ref.7 Ref.8 Ref.10 Ref.17

Sequence similarities

Belongs to the CAS family.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processCell adhesion
Cell cycle
Cell division
Growth regulation
Mitosis
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoskeleton
Golgi apparatus
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Non-traceable author statement Ref.14. Source: UniProtKB

cell adhesion

Non-traceable author statement Ref.9. Source: ProtInc

cytoskeleton organization

Non-traceable author statement Ref.14. Source: UniProtKB

integrin-mediated signaling pathway

Non-traceable author statement Ref.14. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Traceable author statement Ref.9. Source: ProtInc

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement Ref.1. Source: ProtInc

spindle

Traceable author statement Ref.9. Source: ProtInc

spindle pole

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14511-1)

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.
Isoform 2 (identifier: Q14511-2)

The sequence of this isoform differs from the canonical sequence as follows:
     155-174: ITPVRTGHGYVYEYPSRYQK → FQRDGQVSYFLVRASKQTSL
     175-834: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q14511-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MKYK → MWTR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 834834Enhancer of filamentation 1
PRO_0000089328
Chain1 – ?Enhancer of filamentation 1 p55PRO_0000296242

Regions

Domain3 – 6563SH3
Region102 – 229128Interacts strongly with spindle-regulatory protein D1M1
Region710 – 76051Divergent helix-loop-helix motif
Motif360 – 3634Caspase cleavage related site

Amino acid modifications

Modified residue2961Phosphoserine Ref.8 Ref.10 Ref.17
Modified residue3691Phosphoserine Ref.8 Ref.10 Ref.17

Natural variations

Alternative sequence1 – 44MKYK → MWTR in isoform 3.
VSP_044579
Alternative sequence155 – 17420ITPVR…SRYQK → FQRDGQVSYFLVRASKQTSL in isoform 2.
VSP_042835
Alternative sequence175 – 834660Missing in isoform 2.
VSP_042836
Natural variant1781D → N.
Corresponds to variant rs11546959 [ dbSNP | Ensembl ].
VAR_054082
Natural variant3041P → L.
Corresponds to variant rs34184473 [ dbSNP | Ensembl ].
VAR_054083
Natural variant5771T → M.
Corresponds to variant rs3734401 [ dbSNP | Ensembl ].
VAR_021857

Experimental info

Sequence conflict1391Q → R in BAF85371. Ref.3

Secondary structure

.................. 834
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C54DEC36C8C8E9E6

FASTA83492,861
        10         20         30         40         50         60 
MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG RQGIVPGNRV 

        70         80         90        100        110        120 
KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA PRDTIYQVPP SYQNQGIYQV 

       130        140        150        160        170        180 
PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV GKKVITPVRT GHGYVYEYPS RYQKDVYDIP 

       190        200        210        220        230        240 
PSHTTQGVYD IPPSSAKGPV FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGLREKD 

       250        260        270        280        290        300 
YDFPPPMRQA GRPDLRPEGV YDIPPTCTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN 

       310        320        330        340        350        360 
HPPPQLGQSV GSQNDAYDVP RGVQFLEPPA ETSEKANPQE RDGVYDVPLH NPPDAKGSRD 

       370        380        390        400        410        420 
LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK RLFLDPDTAI ERLQRLQQAL 

       430        440        450        460        470        480 
EMGVSSLMAL VTTDWRCYGY MERHINEIRT AVDKVELFLK EYLHFVKGAV ANAACLPELI 

       490        500        510        520        530        540 
LHNKMKRELQ RVEDSHQILS QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD 

       550        560        570        580        590        600 
DAKQLTTTIN TNAEALFRPG PGSLHLKNGP ESIMNSTEYP HGGSQGQLLH PGDHKAQAHN 

       610        620        630        640        650        660 
KALPPGLSKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK ENIMKQNKMQ 

       670        680        690        700        710        720 
LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV SAQDRQLLCF YYDQCETHFI 

       730        740        750        760        770        780 
SLLNAIDALF SCVSSAQPPR IFVAHSKFVI LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS 

       790        800        810        820        830 
NQLCEQLKTI VMATKMAALH YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF 

« Hide

Isoform 2 [UniParc].

Checksum: D7C42D0C07FCECC0
Show »

FASTA17419,285
Isoform 3 [UniParc].

Checksum: C6895E14FA35AE86
Show »

FASTA83492,885

References

« Hide 'large scale' references
[1]"Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae."
Law S.F., Estojak J., Wang B., Mysliwiec T., Kruh G., Golemis E.A.
Mol. Cell. Biol. 16:3327-3337(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"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."
Minegishi M., Tachibana K., Sato T., Iwata S., Nojima Y., Morimoto C.
J. Exp. Med. 184:1365-1375(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lymphoma.
[3]"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. expand/collapse author list , 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 3).
Tissue: Thymus.
[4]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
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: Brain and Lung.
[7]"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."
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.
J. Biol. Chem. 272:4230-4236(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INCREASED TYROSINE PHOSPHORYLATION BY LIGATION OF INTEGRIN-B1 AND BCR.
[8]"Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates."
Tachibana K., Urano T., Fujita H., Ohashi Y., Kamiguchi K., Iwata S., Hirai H., Morimoto C.
J. Biol. Chem. 272:29083-29090(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES BY PTK2/FAK1.
[9]"Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments."
Law S.F., Zhang Y.-Z., Klein-Szanto A.J.P., Golemis E.A.
Mol. Cell. Biol. 18:3540-3551(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[10]"T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G."
Ohashi Y., Tachibana K., Kamiguchi K., Fujita H., Morimoto C.
J. Biol. Chem. 273:6446-6451(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES UPON CD3 CROSS-LINKING.
[11]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
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.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[12]"Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain."
Law S.F., Zhang Y.-Z., Fashena S.J., Toby G., Estojak J., Golemis E.A.
Exp. Cell Res. 252:224-235(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF CARBOXY-TERMINAL DOMAIN.
[13]"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."
Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A.
Gene 257:33-43(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNL4.
[14]"MICAL, a novel CasL interacting molecule, associates with vimentin."
Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K., Morimoto C., Hirai H.
J. Biol. Chem. 277:14933-14941(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICAL.
[15]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Phosphorylation of human enhancer of filamentation (HEF1) on serine 369 induces its proteasomal degradation."
Hivert V., Pierre J., Raingeaud J.
Biochem. Pharmacol. 78:1017-1025(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-296 AND SER-369.
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Northeast structural genomics consortium target HR5554A."
Northeast structural genomics consortium (NESG)
Submitted (FEB-2011) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 399-563.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43821 mRNA. Translation: AAA98770.1.
U64317 mRNA. Translation: AAB53696.1.
AK292682 mRNA. Translation: BAF85371.1.
AL022098 Genomic DNA. No translation available.
AL136139, AL139807 Genomic DNA. Translation: CAI22676.1.
AL136139, AL139807 Genomic DNA. Translation: CAI22677.1.
AL139807, AL136139 Genomic DNA. Translation: CAI21579.1.
AL139807, AL136139 Genomic DNA. Translation: CAI21580.1.
AL512382 Genomic DNA. No translation available.
CH471087 Genomic DNA. Translation: EAW55299.1.
CH471087 Genomic DNA. Translation: EAW55301.1.
BC020686 mRNA. Translation: AAH20686.1.
BC040207 mRNA. Translation: AAH40207.1.
RefSeqNP_001135865.1. NM_001142393.1.
NP_001257962.1. NM_001271033.1.
NP_006394.1. NM_006403.3.
NP_892011.2. NM_182966.3.
UniGeneHs.37982.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L81NMR-A399-563[»]
ProteinModelPortalQ14511.
SMRQ14511. Positions 5-65, 399-563, 704-832.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110816. 29 interactions.
IntActQ14511. 16 interactions.
MINTMINT-1175514.
STRING9606.ENSP00000368759.

PTM databases

PhosphoSiteQ14511.

Polymorphism databases

DMDM8134360.

Proteomic databases

PaxDbQ14511.
PRIDEQ14511.

Protocols and materials databases

DNASU4739.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379433; ENSP00000368745; ENSG00000111859. [Q14511-2]
ENST00000379446; ENSP00000368759; ENSG00000111859. [Q14511-1]
ENST00000504387; ENSP00000422871; ENSG00000111859. [Q14511-3]
GeneID4739.
KEGGhsa:4739.
UCSCuc003mzv.2. human. [Q14511-1]
uc003mzx.3. human. [Q14511-2]
uc010joz.2. human.

Organism-specific databases

CTD4739.
GeneCardsGC06M011183.
HGNCHGNC:7733. NEDD9.
HPACAB009720.
MIM602265. gene.
neXtProtNX_Q14511.
PharmGKBPA31538.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82196.
HOGENOMHOG000261698.
HOVERGENHBG004354.
InParanoidQ14511.
KOK16832.
OMAYEYPSRY.
OrthoDBEOG7QRQTD.
PhylomeDBQ14511.
TreeFamTF328782.

Enzyme and pathway databases

SignaLinkQ14511.

Gene expression databases

ArrayExpressQ14511.
BgeeQ14511.
CleanExHS_NEDD9.
GenevestigatorQ14511.

Family and domain databases

InterProIPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
[Graphical view]
PfamPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNEDD9.
GenomeRNAi4739.
NextBio18276.
PMAP-CutDBQ14511.
PROQ14511.
SOURCESearch...

Entry information

Entry nameCASL_HUMAN
AccessionPrimary (citable) accession number: Q14511
Secondary accession number(s): A8K9G7 expand/collapse secondary AC list , A8MSJ9, G5E9Y9, Q5T9R4, Q5XKI0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM