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Q14511

- CASL_HUMAN

UniProt

Q14511 - CASL_HUMAN

Protein

Enhancer of filamentation 1

Gene

NEDD9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin filament bundle assembly Source: UniProtKB
    2. cell adhesion Source: ProtInc
    3. cytoskeleton organization Source: UniProtKB
    4. integrin-mediated signaling pathway Source: UniProtKB
    5. mitotic nuclear division Source: UniProtKB-KW
    6. regulation of growth Source: UniProtKB-KW
    7. signal transduction Source: ProtInc

    Keywords - Biological processi

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

    Enzyme and pathway databases

    SignaLinkiQ14511.

    Names & Taxonomyi

    Protein namesi
    Recommended 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:
    Gene namesi
    Name:NEDD9
    Synonyms:CASL, CASS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7733. NEDD9.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cytoplasm Source: ProtInc
    3. focal adhesion Source: UniProtKB-SubCell
    4. Golgi apparatus Source: UniProtKB-SubCell
    5. lamellipodium Source: UniProtKB-SubCell
    6. nucleus Source: ProtInc
    7. spindle Source: ProtInc
    8. spindle pole Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31538.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 834834Enhancer of filamentation 1PRO_0000089328Add
    BLAST
    Chaini1 – ?Enhancer of filamentation 1 p55PRO_0000296242

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei296 – 2961Phosphoserine1 Publication
    Modified residuei369 – 3691Phosphoserine1 Publication

    Post-translational modificationi

    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.1 Publication
    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.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14511.
    PaxDbiQ14511.
    PRIDEiQ14511.

    PTM databases

    PhosphoSiteiQ14511.

    Miscellaneous databases

    PMAP-CutDBQ14511.

    Expressioni

    Tissue specificityi

    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.

    Inductioni

    Activated upon induction of cell growth.

    Gene expression databases

    ArrayExpressiQ14511.
    BgeeiQ14511.
    CleanExiHS_NEDD9.
    GenevestigatoriQ14511.

    Organism-specific databases

    HPAiCAB009720.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi110816. 29 interactions.
    IntActiQ14511. 16 interactions.
    MINTiMINT-1175514.
    STRINGi9606.ENSP00000368759.

    Structurei

    Secondary structure

    1
    834
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi406 – 43025
    Helixi438 – 4425
    Turni443 – 4464
    Helixi447 – 47327
    Helixi480 – 50829
    Turni509 – 5113
    Helixi513 – 5164
    Helixi527 – 5359
    Helixi538 – 55114
    Helixi553 – 5564

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L81NMR-A399-563[»]
    ProteinModelPortaliQ14511.
    SMRiQ14511. Positions 5-65, 399-563, 704-832.
    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
    Regioni102 – 229128Interacts strongly with spindle-regulatory protein D1M1Add
    BLAST
    Regioni710 – 76051Divergent helix-loop-helix motifAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi360 – 3634Caspase cleavage related site

    Domaini

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

    Sequence similaritiesi

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

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG82196.
    HOGENOMiHOG000261698.
    HOVERGENiHBG004354.
    InParanoidiQ14511.
    KOiK16832.
    OMAiYEYPSRY.
    OrthoDBiEOG7QRQTD.
    PhylomeDBiQ14511.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14511-1) [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

    MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG    50
    RQGIVPGNRV KLLIGPMQET ASSHEQPASG LMQQTFGQQK LYQVPNPQAA 100
    PRDTIYQVPP SYQNQGIYQV PTGHGTQEQE VYQVPPSVQR SIGGTSGPHV 150
    GKKVITPVRT GHGYVYEYPS RYQKDVYDIP PSHTTQGVYD IPPSSAKGPV 200
    FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGLREKD YDFPPPMRQA 250
    GRPDLRPEGV YDIPPTCTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN 300
    HPPPQLGQSV GSQNDAYDVP RGVQFLEPPA ETSEKANPQE RDGVYDVPLH 350
    NPPDAKGSRD LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK 400
    RLFLDPDTAI ERLQRLQQAL EMGVSSLMAL VTTDWRCYGY MERHINEIRT 450
    AVDKVELFLK EYLHFVKGAV ANAACLPELI LHNKMKRELQ RVEDSHQILS 500
    QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD DAKQLTTTIN 550
    TNAEALFRPG PGSLHLKNGP ESIMNSTEYP HGGSQGQLLH PGDHKAQAHN 600
    KALPPGLSKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK 650
    ENIMKQNKMQ LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV 700
    SAQDRQLLCF YYDQCETHFI SLLNAIDALF SCVSSAQPPR IFVAHSKFVI 750
    LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS NQLCEQLKTI VMATKMAALH 800
    YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF 834
    Length:834
    Mass (Da):92,861
    Last modified:November 1, 1996 - v1
    Checksum:iC54DEC36C8C8E9E6
    GO
    Isoform 2 (identifier: Q14511-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-174: ITPVRTGHGYVYEYPSRYQK → FQRDGQVSYFLVRASKQTSL
         175-834: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:174
    Mass (Da):19,285
    Checksum:iD7C42D0C07FCECC0
    GO
    Isoform 3 (identifier: Q14511-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MKYK → MWTR

    Note: No experimental confirmation available.

    Show »
    Length:834
    Mass (Da):92,885
    Checksum:iC6895E14FA35AE86
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391Q → R in BAF85371. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti178 – 1781D → N.
    Corresponds to variant rs11546959 [ dbSNP | Ensembl ].
    VAR_054082
    Natural varianti304 – 3041P → L.
    Corresponds to variant rs34184473 [ dbSNP | Ensembl ].
    VAR_054083
    Natural varianti577 – 5771T → M.
    Corresponds to variant rs3734401 [ dbSNP | Ensembl ].
    VAR_021857

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MKYK → MWTR in isoform 3. 1 PublicationVSP_044579
    Alternative sequencei155 – 17420ITPVR…SRYQK → FQRDGQVSYFLVRASKQTSL in isoform 2. 1 PublicationVSP_042835Add
    BLAST
    Alternative sequencei175 – 834660Missing in isoform 2. 1 PublicationVSP_042836Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS34340.1. [Q14511-2]
    CCDS4520.1. [Q14511-1]
    CCDS47373.1. [Q14511-3]
    RefSeqiNP_001135865.1. NM_001142393.1. [Q14511-3]
    NP_001257962.1. NM_001271033.1.
    NP_006394.1. NM_006403.3. [Q14511-1]
    NP_892011.2. NM_182966.3. [Q14511-2]
    UniGeneiHs.37982.

    Genome annotation databases

    EnsembliENST00000379433; ENSP00000368745; ENSG00000111859. [Q14511-2]
    ENST00000379446; ENSP00000368759; ENSG00000111859. [Q14511-1]
    ENST00000504387; ENSP00000422871; ENSG00000111859. [Q14511-3]
    GeneIDi4739.
    KEGGihsa:4739.
    UCSCiuc003mzv.2. human. [Q14511-1]
    uc003mzx.3. human. [Q14511-2]
    uc010joz.2. human.

    Polymorphism databases

    DMDMi8134360.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS34340.1. [Q14511-2 ]
    CCDS4520.1. [Q14511-1 ]
    CCDS47373.1. [Q14511-3 ]
    RefSeqi NP_001135865.1. NM_001142393.1. [Q14511-3 ]
    NP_001257962.1. NM_001271033.1.
    NP_006394.1. NM_006403.3. [Q14511-1 ]
    NP_892011.2. NM_182966.3. [Q14511-2 ]
    UniGenei Hs.37982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L81 NMR - A 399-563 [» ]
    ProteinModelPortali Q14511.
    SMRi Q14511. Positions 5-65, 399-563, 704-832.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110816. 29 interactions.
    IntActi Q14511. 16 interactions.
    MINTi MINT-1175514.
    STRINGi 9606.ENSP00000368759.

    PTM databases

    PhosphoSitei Q14511.

    Polymorphism databases

    DMDMi 8134360.

    Proteomic databases

    MaxQBi Q14511.
    PaxDbi Q14511.
    PRIDEi Q14511.

    Protocols and materials databases

    DNASUi 4739.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379433 ; ENSP00000368745 ; ENSG00000111859 . [Q14511-2 ]
    ENST00000379446 ; ENSP00000368759 ; ENSG00000111859 . [Q14511-1 ]
    ENST00000504387 ; ENSP00000422871 ; ENSG00000111859 . [Q14511-3 ]
    GeneIDi 4739.
    KEGGi hsa:4739.
    UCSCi uc003mzv.2. human. [Q14511-1 ]
    uc003mzx.3. human. [Q14511-2 ]
    uc010joz.2. human.

    Organism-specific databases

    CTDi 4739.
    GeneCardsi GC06M011183.
    HGNCi HGNC:7733. NEDD9.
    HPAi CAB009720.
    MIMi 602265. gene.
    neXtProti NX_Q14511.
    PharmGKBi PA31538.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82196.
    HOGENOMi HOG000261698.
    HOVERGENi HBG004354.
    InParanoidi Q14511.
    KOi K16832.
    OMAi YEYPSRY.
    OrthoDBi EOG7QRQTD.
    PhylomeDBi Q14511.
    TreeFami TF328782.

    Enzyme and pathway databases

    SignaLinki Q14511.

    Miscellaneous databases

    GeneWikii NEDD9.
    GenomeRNAii 4739.
    NextBioi 18276.
    PMAP-CutDB Q14511.
    PROi Q14511.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14511.
    Bgeei Q14511.
    CleanExi HS_NEDD9.
    Genevestigatori Q14511.

    Family and domain databases

    InterProi IPR021901. CAS_DUF3513.
    IPR014928. Serine_rich.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF12026. DUF3513. 1 hit.
    PF08824. Serine_rich. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiCASL_HUMAN
    AccessioniPrimary (citable) accession number: Q14511
    Secondary accession number(s): A8K9G7
    , A8MSJ9, G5E9Y9, Q5T9R4, Q5XKI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3